CNRS Nantes University UFIP UFIP
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***  para ti  ***

elNémo ID: 211122221348130179

Job options:

ID        	=	 211122221348130179
JOBID     	=	 para ti
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 para ti

HEADER    HYDROLASE/HYDROLASE INHIBITOR           05-MAY-20   6WUU              
TITLE     CRYSTAL STRUCTURE OF THE SARS COV-2 PAPAIN-LIKE PROTEASE IN COMPLEX   
TITLE    2 WITH PEPTIDE INHIBITOR VIR250                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NON-STRUCTURAL PROTEIN 3;                                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 1563-1879;                                    
COMPND   5 SYNONYM: PP1AB,ORF1AB POLYPROTEIN,NSP3,PL2-PRO,PAPAIN-LIKE PROTEASE, 
COMPND   6 PAPAIN-LIKE PROTEINASE,PL-PRO;                                       
COMPND   7 EC: 3.4.19.121, 3.4.22.-;                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: VIR250;                                                    
COMPND  11 CHAIN: G, H, I, J;                                                   
COMPND  12 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 GENE: REP, 1A-1B;                                                    
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET29B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  14 ORGANISM_TAXID: 32630                                                
KEYWDS    COVID-19, CORONAVIRUS, SARS, COV-2, PAPAIN-LIKE PROTEASE, PLPRO,      
KEYWDS   2 DEUBIQUITINATING ENZYME, UBIQUITIN, ACTIVITY-BASED PROBE, HYDROLASE- 
KEYWDS   3 HYDROLASE INHIBITOR COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.LV,S.K.OLSEN                                                        
REVDAT   4   27-JAN-21 6WUU    1       COMPND                                   
REVDAT   3   02-DEC-20 6WUU    1       JRNL                                     
REVDAT   2   24-JUN-20 6WUU    1       JRNL                                     
REVDAT   1   20-MAY-20 6WUU    0                                                
JRNL        AUTH   W.RUT,Z.LV,M.ZMUDZINSKI,S.PATCHETT,D.NAYAK,S.J.SNIPAS,       
JRNL        AUTH 2 F.EL OUALID,T.T.HUANG,M.BEKES,M.DRAG,S.K.OLSEN               
JRNL        TITL   ACTIVITY PROFILING AND CRYSTAL STRUCTURES OF INHIBITOR-BOUND 
JRNL        TITL 2 SARS-COV-2 PAPAIN-LIKE PROTEASE: A FRAMEWORK FOR             
JRNL        TITL 3 ANTI-COVID-19 DRUG DESIGN.                                   
JRNL        REF    SCI ADV                       V.   6       2020              
JRNL        REFN                   ESSN 2375-2548                               
JRNL        PMID   33067239                                                     
JRNL        DOI    10.1126/SCIADV.ABD4596                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.RUT,Z.LV,M.ZMUDZINSKI,S.PATCHETT,D.NAYAK,S.J.SNIPAS,       
REMARK   1  AUTH 2 F.EL OUALID,T.T.HUANG,M.BEKES,M.DRAG,S.K.OLSEN               
REMARK   1  TITL   ACTIVITY PROFILING AND STRUCTURES OF INHIBITOR-BOUND         
REMARK   1  TITL 2 SARS-COV-2-PLPRO PROTEASE PROVIDES A FRAMEWORK FOR           
REMARK   1  TITL 3 ANTI-COVID-19 DRUG DESIGN.                                   
REMARK   1  REF    BIORXIV                                    2020              
REMARK   1  REFN                                                                
REMARK   1  PMID   32511411                                                     
REMARK   1  DOI    10.1101/2020.04.29.068890                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.79 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.79                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 94.85                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 33481                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.950                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1992                            
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 94.8500 -  6.7200    0.99     2271   150  0.1586 0.1642        
REMARK   3     2  6.7200 -  5.3400    1.00     2265   137  0.1859 0.2126        
REMARK   3     3  5.3400 -  4.6600    1.00     2275   144  0.1480 0.1713        
REMARK   3     4  4.6600 -  4.2400    1.00     2262   138  0.1461 0.1845        
REMARK   3     5  4.2400 -  3.9300    0.99     2220   147  0.1810 0.2261        
REMARK   3     6  3.9300 -  3.7000    1.00     2254   139  0.2016 0.2680        
REMARK   3     7  3.7000 -  3.5200    1.00     2264   146  0.2216 0.2807        
REMARK   3     8  3.5200 -  3.3600    1.00     2269   131  0.2417 0.2858        
REMARK   3     9  3.3600 -  3.2300    1.00     2234   163  0.2598 0.3080        
REMARK   3    10  3.2300 -  3.1200    1.00     2259   135  0.2710 0.3405        
REMARK   3    11  3.1200 -  3.0200    1.00     2280   138  0.2943 0.3423        
REMARK   3    12  3.0200 -  2.9400    1.00     2227   145  0.3023 0.3645        
REMARK   3    13  2.9400 -  2.8600    0.98     2200   150  0.2993 0.3394        
REMARK   3    14  2.8600 -  2.7900    0.98     2209   129  0.3000 0.3332        
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.730           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.91                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 16                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 120 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8860  96.4850   5.8221              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6627 T22:   0.6280                                     
REMARK   3      T33:   0.4492 T12:   0.0135                                     
REMARK   3      T13:  -0.0641 T23:   0.1459                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0740 L22:   2.1166                                     
REMARK   3      L33:  -1.5780 L12:   0.7623                                     
REMARK   3      L13:  -0.3939 L23:   1.1991                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1364 S12:   0.2081 S13:   0.2549                       
REMARK   3      S21:   0.1639 S22:   0.2460 S23:   0.1894                       
REMARK   3      S31:   0.1818 S32:  -0.0657 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 121 THROUGH 175 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  36.4871  79.7690   2.7157              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7163 T22:   0.6133                                     
REMARK   3      T33:   0.5956 T12:  -0.0499                                     
REMARK   3      T13:  -0.0005 T23:   0.0169                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1267 L22:   0.9617                                     
REMARK   3      L33:   0.3373 L12:   0.0021                                     
REMARK   3      L13:   0.4246 L23:  -0.1728                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0814 S12:   0.0353 S13:  -0.3771                       
REMARK   3      S21:   0.2082 S22:   0.0540 S23:   0.1069                       
REMARK   3      S31:  -0.3027 S32:   0.0547 S33:  -0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 176 THROUGH 253 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  38.7608  57.4777  -9.2645              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4213 T22:   0.4899                                     
REMARK   3      T33:   0.5767 T12:   0.0183                                     
REMARK   3      T13:  -0.0397 T23:  -0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.4135 L22:   1.5744                                     
REMARK   3      L33:   1.4483 L12:  -0.9710                                     
REMARK   3      L13:  -0.1548 L23:   0.2501                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0372 S12:   0.1369 S13:  -0.0326                       
REMARK   3      S21:  -0.0616 S22:  -0.1112 S23:   0.1533                       
REMARK   3      S31:   0.0679 S32:   0.1224 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 254 THROUGH 316 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  34.6971  61.3048   8.0518              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5767 T22:   0.5311                                     
REMARK   3      T33:   0.6276 T12:   0.0217                                     
REMARK   3      T13:   0.0446 T23:   0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.4119 L22:   1.3398                                     
REMARK   3      L33:   0.4371 L12:  -1.4942                                     
REMARK   3      L13:   0.3179 L23:  -0.6224                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2361 S12:   0.2094 S13:  -0.1891                       
REMARK   3      S21:   0.3327 S22:   0.0422 S23:   0.0612                       
REMARK   3      S31:  -0.0398 S32:  -0.0745 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 62 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  57.4637   8.0007  -7.1631              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4324 T22:   0.5031                                     
REMARK   3      T33:   0.4755 T12:  -0.0434                                     
REMARK   3      T13:  -0.0033 T23:   0.0668                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6469 L22:   1.5218                                     
REMARK   3      L33:   0.2679 L12:   0.1217                                     
REMARK   3      L13:  -0.1042 L23:  -0.0207                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2761 S12:   0.0803 S13:   0.4327                       
REMARK   3      S21:  -0.0862 S22:   0.1197 S23:   0.2129                       
REMARK   3      S31:   0.0310 S32:  -0.2510 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 63 THROUGH 181 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  57.2927  31.2342   5.2611              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6022 T22:   0.4046                                     
REMARK   3      T33:   0.4010 T12:   0.0002                                     
REMARK   3      T13:  -0.0446 T23:   0.0488                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0513 L22:   1.1428                                     
REMARK   3      L33:   1.1403 L12:  -1.2325                                     
REMARK   3      L13:  -0.8758 L23:   1.0890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0601 S12:   0.0515 S13:   0.1110                       
REMARK   3      S21:  -0.0059 S22:  -0.0361 S23:   0.0458                       
REMARK   3      S31:   0.3404 S32:   0.0323 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 182 THROUGH 238 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  62.3855  46.3851  31.9179              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4778 T22:   0.5945                                     
REMARK   3      T33:   0.4942 T12:  -0.0135                                     
REMARK   3      T13:  -0.0246 T23:  -0.1208                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4511 L22:   0.3297                                     
REMARK   3      L33:   0.7278 L12:   0.6716                                     
REMARK   3      L13:   0.2091 L23:   0.8693                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1562 S12:  -0.1509 S13:   0.1032                       
REMARK   3      S21:   0.1111 S22:  -0.0539 S23:   0.0446                       
REMARK   3      S31:   0.0210 S32:   0.1960 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 239 THROUGH 319 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  57.3224  51.0102  14.0400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5452 T22:   0.5091                                     
REMARK   3      T33:   0.5988 T12:   0.0054                                     
REMARK   3      T13:  -0.0060 T23:   0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1848 L22:   0.4475                                     
REMARK   3      L33:   0.8377 L12:  -0.0153                                     
REMARK   3      L13:   0.6909 L23:   0.2777                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0539 S12:   0.0054 S13:   0.1709                       
REMARK   3      S21:  -0.0212 S22:   0.0642 S23:  -0.0719                       
REMARK   3      S31:  -0.0575 S32:   0.0349 S33:  -0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 3 THROUGH 61 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  53.1443  84.7443 -30.7822              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4597 T22:   0.5427                                     
REMARK   3      T33:   0.5790 T12:   0.1012                                     
REMARK   3      T13:  -0.0234 T23:  -0.0816                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0300 L22:   0.0881                                     
REMARK   3      L33:   0.2208 L12:  -0.0876                                     
REMARK   3      L13:  -0.4350 L23:  -0.5968                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0113 S12:   0.0255 S13:  -0.3223                       
REMARK   3      S21:  -0.1462 S22:  -0.1995 S23:  -0.0189                       
REMARK   3      S31:  -0.1427 S32:   0.0564 S33:   0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 62 THROUGH 174 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  30.4308  76.9435 -22.1187              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5191 T22:   0.4541                                     
REMARK   3      T33:   0.5155 T12:  -0.0120                                     
REMARK   3      T13:  -0.0083 T23:  -0.0582                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9151 L22:   1.5542                                     
REMARK   3      L33:   0.7264 L12:   0.3938                                     
REMARK   3      L13:   0.0058 L23:  -1.0725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0203 S12:   0.0396 S13:  -0.1434                       
REMARK   3      S21:  -0.0849 S22:   0.0313 S23:   0.2241                       
REMARK   3      S31:  -0.1217 S32:   0.1969 S33:  -0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 175 THROUGH 253 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.7769  78.2374  -1.8650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6009 T22:   0.5339                                     
REMARK   3      T33:   0.6985 T12:   0.1479                                     
REMARK   3      T13:   0.1279 T23:   0.1980                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7768 L22:  -0.1284                                     
REMARK   3      L33:   1.4204 L12:  -0.5686                                     
REMARK   3      L13:   1.2035 L23:   0.1524                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0589 S12:  -0.1051 S13:  -0.0985                       
REMARK   3      S21:  -0.0166 S22:   0.3134 S23:   0.0006                       
REMARK   3      S31:  -0.1977 S32:  -0.5370 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 254 THROUGH 313 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.3654  68.3419 -18.7406              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4938 T22:   0.5571                                     
REMARK   3      T33:   0.9029 T12:   0.0219                                     
REMARK   3      T13:  -0.0632 T23:   0.0786                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5701 L22:   0.0926                                     
REMARK   3      L33:   1.5322 L12:  -0.4563                                     
REMARK   3      L13:  -0.3080 L23:  -0.3901                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0006 S12:   0.1214 S13:  -0.1876                       
REMARK   3      S21:  -0.0102 S22:   0.1078 S23:   0.3366                       
REMARK   3      S31:   0.1661 S32:  -0.0552 S33:  -0.0000                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 3 THROUGH 77 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  75.1759  10.9058  32.4781              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4157 T22:   0.5280                                     
REMARK   3      T33:   0.4954 T12:  -0.0151                                     
REMARK   3      T13:   0.0720 T23:  -0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5215 L22:   1.1624                                     
REMARK   3      L33:   0.2113 L12:  -1.3487                                     
REMARK   3      L13:  -0.1980 L23:   1.3747                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4500 S12:  -0.1833 S13:   0.2911                       
REMARK   3      S21:  -0.2813 S22:   0.0601 S23:  -0.2067                       
REMARK   3      S31:   0.1588 S32:   0.0875 S33:   0.0000                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 78 THROUGH 175 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  53.1765  23.1532  32.2408              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4821 T22:   0.5890                                     
REMARK   3      T33:   0.4212 T12:   0.0286                                     
REMARK   3      T13:   0.0109 T23:   0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9749 L22:   1.1129                                     
REMARK   3      L33:   0.7682 L12:  -0.5197                                     
REMARK   3      L13:  -0.7920 L23:   0.6128                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1732 S12:  -0.1571 S13:  -0.1138                       
REMARK   3      S21:   0.0007 S22:   0.1109 S23:   0.0917                       
REMARK   3      S31:   0.1323 S32:   0.2141 S33:   0.0000                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 176 THROUGH 253 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  34.2161  29.3423  12.5216              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5185 T22:   0.7813                                     
REMARK   3      T33:   0.5121 T12:   0.0307                                     
REMARK   3      T13:  -0.0219 T23:  -0.1214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5747 L22:   0.0853                                     
REMARK   3      L33:   1.1915 L12:   0.5567                                     
REMARK   3      L13:   0.6648 L23:   0.0439                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1557 S12:   0.2509 S13:  -0.2563                       
REMARK   3      S21:   0.0389 S22:  -0.0400 S23:   0.0755                       
REMARK   3      S31:  -0.1129 S32:  -0.4118 S33:   0.0000                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 254 THROUGH 315 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  35.2964  29.9755  31.2419              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4218 T22:   0.6507                                     
REMARK   3      T33:   0.5171 T12:  -0.0655                                     
REMARK   3      T13:   0.0731 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9892 L22:  -0.2572                                     
REMARK   3      L33:   1.1736 L12:  -0.4485                                     
REMARK   3      L13:   0.2385 L23:   0.1223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0670 S12:   0.1191 S13:   0.0080                       
REMARK   3      S21:   0.1848 S22:   0.0410 S23:   0.0497                       
REMARK   3      S31:   0.0567 S32:  -0.2441 S33:   0.0000                       
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 1 THROUGH 501)           
REMARK   3     SELECTION          : (CHAIN B AND (RESID 1 THROUGH 316 OR        
REMARK   3                          RESID 401 THROUGH 501))                     
REMARK   3     ATOM PAIRS NUMBER  : 6127                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND RESID 1 THROUGH 501)           
REMARK   3     SELECTION          : (CHAIN C AND (RESID 1 THROUGH 316 OR        
REMARK   3                          RESID 401 THROUGH 501))                     
REMARK   3     ATOM PAIRS NUMBER  : 6127                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND RESID 1 THROUGH 501)           
REMARK   3     SELECTION          : (CHAIN D AND (RESID 1 THROUGH 316 OR        
REMARK   3                          RESID 401 THROUGH 501))                     
REMARK   3     ATOM PAIRS NUMBER  : 6127                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6WUU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000249023.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-APR-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER2 X 16M               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.32                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33589                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.790                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 94.850                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.15800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.79                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.78800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6W9C                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE 291K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       94.84650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1330 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, J                                  
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 PEPTIDE COVALENTLY LINKED TO ACTIVE SITE CYS                         
REMARK 400                                                                      
REMARK 400 THE PAPAIN-LIKE PROTEASE PEPTIDE INHIBITOR IS PEPTIDE-LIKE, A        
REMARK 400 MEMBER OF ENZYME INHIBITOR CLASS.                                    
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: PAPAIN-LIKE PROTEASE PEPTIDE INHIBITOR                       
REMARK 400   CHAIN: G, H, I, J                                                  
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   DESCRIPTION: NULL                                                  
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     LEU A   317                                                      
REMARK 465     GLU A   318                                                      
REMARK 465     HIS A   319                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS B   320                                                      
REMARK 465     HIS B   321                                                      
REMARK 465     HIS B   322                                                      
REMARK 465     HIS B   323                                                      
REMARK 465     HIS B   324                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     ARG C     0                                                      
REMARK 465     GLU C   318                                                      
REMARK 465     HIS C   319                                                      
REMARK 465     HIS C   320                                                      
REMARK 465     HIS C   321                                                      
REMARK 465     HIS C   322                                                      
REMARK 465     HIS C   323                                                      
REMARK 465     HIS C   324                                                      
REMARK 465     MET D    -1                                                      
REMARK 465     ARG D     0                                                      
REMARK 465     HIS D   319                                                      
REMARK 465     HIS D   320                                                      
REMARK 465     HIS D   321                                                      
REMARK 465     HIS D   322                                                      
REMARK 465     HIS D   323                                                      
REMARK 465     HIS D   324                                                      
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   OD2  ASP B    61     OG1  THR B    63              2.16            
REMARK 500   OD1  ASN D   267     N    CYS D   270              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   NH1  ARG B     3     OE2  GLU C     1     2744     2.00            
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    ASN A  13       18.44     59.29                                   
REMARK 500    GLU A  51      109.90    -52.19                                   
REMARK 500    PRO A  59       90.13    -67.00                                   
REMARK 500    ALA A 107      132.47   -170.23                                   
REMARK 500    LYS A 279     -118.11   -128.11                                   
REMARK 500    ASN A 308      -63.72   -134.93                                   
REMARK 500    LYS A 315      159.32     87.62                                   
REMARK 500    ASN B  13       19.08     58.88                                   
REMARK 500    PRO B  59       87.47    -67.25                                   
REMARK 500    ALA B 107      133.18   -170.05                                   
REMARK 500    LYS B 279     -117.88   -128.69                                   
REMARK 500    ASP B 286       79.81   -117.95                                   
REMARK 500    ASN B 308      -64.17   -134.45                                   
REMARK 500    ASN C  13       16.71     59.18                                   
REMARK 500    PRO C  59       86.35    -68.70                                   
REMARK 500    ASN C  60       38.71    -99.64                                   
REMARK 500    LYS C 279     -118.09   -129.05                                   
REMARK 500    ASN C 308      -65.95   -132.96                                   
REMARK 500    PRO D  59       88.22    -67.60                                   
REMARK 500    LYS D 279     -116.77   -131.01                                   
REMARK 500    ASN D 308      -64.19   -132.68                                   
REMARK 500    LYS D 315       87.50     48.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 189   SG                                                     
REMARK 620 2 CYS A 192   SG  112.0                                              
REMARK 620 3 CYS A 224   SG  127.0 109.1                                        
REMARK 620 4 CYS A 226   SG  104.3  97.5 102.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 189   SG                                                     
REMARK 620 2 CYS B 192   SG  122.8                                              
REMARK 620 3 CYS B 224   SG  119.5  91.3                                        
REMARK 620 4 CYS B 226   SG  108.6 113.0  98.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 189   SG                                                     
REMARK 620 2 CYS C 192   SG  123.2                                              
REMARK 620 3 CYS C 224   SG  115.7 100.8                                        
REMARK 620 4 CYS C 226   SG  112.1  99.7 102.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 189   SG                                                     
REMARK 620 2 CYS D 192   SG  108.2                                              
REMARK 620 3 CYS D 224   SG  138.4  99.5                                        
REMARK 620 4 CYS D 226   SG  119.4  93.3  88.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG D 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE G 1 and UB4 G 2      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues UB4 G 2 and DPP G 3      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DPP G 3 and GLY G 4    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY G 4 and GVE G 5    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE H 1 and UB4 H 2      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues UB4 H 2 and DPP H 3      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DPP H 3 and GLY H 4    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY H 4 and GVE H 5    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE I 1 and UB4 I 2      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues UB4 I 2 and DPP I 3      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DPP I 3 and GLY I 4    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY I 4 and GVE I 5    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GVE I 5 and CYS C      
REMARK 800  111                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACE J 1 and UB4 J 2      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues UB4 J 2 and DPP J 3      
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DPP J 3 and GLY J 4    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY J 4 and GVE J 5    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GVE J 5 and CYS D      
REMARK 800  111                                                                 
DBREF  6WUU A    0   316  UNP    P0DTD1   R1AB_SARS2    1563   1879             
DBREF  6WUU B    0   316  UNP    P0DTD1   R1AB_SARS2    1563   1879             
DBREF  6WUU C    0   316  UNP    P0DTD1   R1AB_SARS2    1563   1879             
DBREF  6WUU D    0   316  UNP    P0DTD1   R1AB_SARS2    1563   1879             
DBREF  6WUU G    1     5  PDB    6WUU     6WUU             1      5             
DBREF  6WUU H    1     5  PDB    6WUU     6WUU             1      5             
DBREF  6WUU I    1     5  PDB    6WUU     6WUU             1      5             
DBREF  6WUU J    1     5  PDB    6WUU     6WUU             1      5             
SEQADV 6WUU MET A   -1  UNP  P0DTD1              INITIATING METHIONINE          
SEQADV 6WUU LEU A  317  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU GLU A  318  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS A  319  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS A  320  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS A  321  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS A  322  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS A  323  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS A  324  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU MET B   -1  UNP  P0DTD1              INITIATING METHIONINE          
SEQADV 6WUU LEU B  317  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU GLU B  318  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS B  319  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS B  320  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS B  321  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS B  322  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS B  323  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS B  324  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU MET C   -1  UNP  P0DTD1              INITIATING METHIONINE          
SEQADV 6WUU LEU C  317  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU GLU C  318  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS C  319  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS C  320  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS C  321  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS C  322  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS C  323  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS C  324  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU MET D   -1  UNP  P0DTD1              INITIATING METHIONINE          
SEQADV 6WUU LEU D  317  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU GLU D  318  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS D  319  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS D  320  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS D  321  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS D  322  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS D  323  UNP  P0DTD1              EXPRESSION TAG                 
SEQADV 6WUU HIS D  324  UNP  P0DTD1              EXPRESSION TAG                 
SEQRES   1 A  326  MET ARG GLU VAL ARG THR ILE LYS VAL PHE THR THR VAL          
SEQRES   2 A  326  ASP ASN ILE ASN LEU HIS THR GLN VAL VAL ASP MET SER          
SEQRES   3 A  326  MET THR TYR GLY GLN GLN PHE GLY PRO THR TYR LEU ASP          
SEQRES   4 A  326  GLY ALA ASP VAL THR LYS ILE LYS PRO HIS ASN SER HIS          
SEQRES   5 A  326  GLU GLY LYS THR PHE TYR VAL LEU PRO ASN ASP ASP THR          
SEQRES   6 A  326  LEU ARG VAL GLU ALA PHE GLU TYR TYR HIS THR THR ASP          
SEQRES   7 A  326  PRO SER PHE LEU GLY ARG TYR MET SER ALA LEU ASN HIS          
SEQRES   8 A  326  THR LYS LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU THR          
SEQRES   9 A  326  SER ILE LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA THR          
SEQRES  10 A  326  ALA LEU LEU THR LEU GLN GLN ILE GLU LEU LYS PHE ASN          
SEQRES  11 A  326  PRO PRO ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG ALA          
SEQRES  12 A  326  GLY GLU ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA TYR          
SEQRES  13 A  326  CYS ASN LYS THR VAL GLY GLU LEU GLY ASP VAL ARG GLU          
SEQRES  14 A  326  THR MET SER TYR LEU PHE GLN HIS ALA ASN LEU ASP SER          
SEQRES  15 A  326  CYS LYS ARG VAL LEU ASN VAL VAL CYS LYS THR CYS GLY          
SEQRES  16 A  326  GLN GLN GLN THR THR LEU LYS GLY VAL GLU ALA VAL MET          
SEQRES  17 A  326  TYR MET GLY THR LEU SER TYR GLU GLN PHE LYS LYS GLY          
SEQRES  18 A  326  VAL GLN ILE PRO CYS THR CYS GLY LYS GLN ALA THR LYS          
SEQRES  19 A  326  TYR LEU VAL GLN GLN GLU SER PRO PHE VAL MET MET SER          
SEQRES  20 A  326  ALA PRO PRO ALA GLN TYR GLU LEU LYS HIS GLY THR PHE          
SEQRES  21 A  326  THR CYS ALA SER GLU TYR THR GLY ASN TYR GLN CYS GLY          
SEQRES  22 A  326  HIS TYR LYS HIS ILE THR SER LYS GLU THR LEU TYR CYS          
SEQRES  23 A  326  ILE ASP GLY ALA LEU LEU THR LYS SER SER GLU TYR LYS          
SEQRES  24 A  326  GLY PRO ILE THR ASP VAL PHE TYR LYS GLU ASN SER TYR          
SEQRES  25 A  326  THR THR THR ILE LYS PRO LEU GLU HIS HIS HIS HIS HIS          
SEQRES  26 A  326  HIS                                                          
SEQRES   1 B  326  MET ARG GLU VAL ARG THR ILE LYS VAL PHE THR THR VAL          
SEQRES   2 B  326  ASP ASN ILE ASN LEU HIS THR GLN VAL VAL ASP MET SER          
SEQRES   3 B  326  MET THR TYR GLY GLN GLN PHE GLY PRO THR TYR LEU ASP          
SEQRES   4 B  326  GLY ALA ASP VAL THR LYS ILE LYS PRO HIS ASN SER HIS          
SEQRES   5 B  326  GLU GLY LYS THR PHE TYR VAL LEU PRO ASN ASP ASP THR          
SEQRES   6 B  326  LEU ARG VAL GLU ALA PHE GLU TYR TYR HIS THR THR ASP          
SEQRES   7 B  326  PRO SER PHE LEU GLY ARG TYR MET SER ALA LEU ASN HIS          
SEQRES   8 B  326  THR LYS LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU THR          
SEQRES   9 B  326  SER ILE LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA THR          
SEQRES  10 B  326  ALA LEU LEU THR LEU GLN GLN ILE GLU LEU LYS PHE ASN          
SEQRES  11 B  326  PRO PRO ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG ALA          
SEQRES  12 B  326  GLY GLU ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA TYR          
SEQRES  13 B  326  CYS ASN LYS THR VAL GLY GLU LEU GLY ASP VAL ARG GLU          
SEQRES  14 B  326  THR MET SER TYR LEU PHE GLN HIS ALA ASN LEU ASP SER          
SEQRES  15 B  326  CYS LYS ARG VAL LEU ASN VAL VAL CYS LYS THR CYS GLY          
SEQRES  16 B  326  GLN GLN GLN THR THR LEU LYS GLY VAL GLU ALA VAL MET          
SEQRES  17 B  326  TYR MET GLY THR LEU SER TYR GLU GLN PHE LYS LYS GLY          
SEQRES  18 B  326  VAL GLN ILE PRO CYS THR CYS GLY LYS GLN ALA THR LYS          
SEQRES  19 B  326  TYR LEU VAL GLN GLN GLU SER PRO PHE VAL MET MET SER          
SEQRES  20 B  326  ALA PRO PRO ALA GLN TYR GLU LEU LYS HIS GLY THR PHE          
SEQRES  21 B  326  THR CYS ALA SER GLU TYR THR GLY ASN TYR GLN CYS GLY          
SEQRES  22 B  326  HIS TYR LYS HIS ILE THR SER LYS GLU THR LEU TYR CYS          
SEQRES  23 B  326  ILE ASP GLY ALA LEU LEU THR LYS SER SER GLU TYR LYS          
SEQRES  24 B  326  GLY PRO ILE THR ASP VAL PHE TYR LYS GLU ASN SER TYR          
SEQRES  25 B  326  THR THR THR ILE LYS PRO LEU GLU HIS HIS HIS HIS HIS          
SEQRES  26 B  326  HIS                                                          
SEQRES   1 C  326  MET ARG GLU VAL ARG THR ILE LYS VAL PHE THR THR VAL          
SEQRES   2 C  326  ASP ASN ILE ASN LEU HIS THR GLN VAL VAL ASP MET SER          
SEQRES   3 C  326  MET THR TYR GLY GLN GLN PHE GLY PRO THR TYR LEU ASP          
SEQRES   4 C  326  GLY ALA ASP VAL THR LYS ILE LYS PRO HIS ASN SER HIS          
SEQRES   5 C  326  GLU GLY LYS THR PHE TYR VAL LEU PRO ASN ASP ASP THR          
SEQRES   6 C  326  LEU ARG VAL GLU ALA PHE GLU TYR TYR HIS THR THR ASP          
SEQRES   7 C  326  PRO SER PHE LEU GLY ARG TYR MET SER ALA LEU ASN HIS          
SEQRES   8 C  326  THR LYS LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU THR          
SEQRES   9 C  326  SER ILE LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA THR          
SEQRES  10 C  326  ALA LEU LEU THR LEU GLN GLN ILE GLU LEU LYS PHE ASN          
SEQRES  11 C  326  PRO PRO ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG ALA          
SEQRES  12 C  326  GLY GLU ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA TYR          
SEQRES  13 C  326  CYS ASN LYS THR VAL GLY GLU LEU GLY ASP VAL ARG GLU          
SEQRES  14 C  326  THR MET SER TYR LEU PHE GLN HIS ALA ASN LEU ASP SER          
SEQRES  15 C  326  CYS LYS ARG VAL LEU ASN VAL VAL CYS LYS THR CYS GLY          
SEQRES  16 C  326  GLN GLN GLN THR THR LEU LYS GLY VAL GLU ALA VAL MET          
SEQRES  17 C  326  TYR MET GLY THR LEU SER TYR GLU GLN PHE LYS LYS GLY          
SEQRES  18 C  326  VAL GLN ILE PRO CYS THR CYS GLY LYS GLN ALA THR LYS          
SEQRES  19 C  326  TYR LEU VAL GLN GLN GLU SER PRO PHE VAL MET MET SER          
SEQRES  20 C  326  ALA PRO PRO ALA GLN TYR GLU LEU LYS HIS GLY THR PHE          
SEQRES  21 C  326  THR CYS ALA SER GLU TYR THR GLY ASN TYR GLN CYS GLY          
SEQRES  22 C  326  HIS TYR LYS HIS ILE THR SER LYS GLU THR LEU TYR CYS          
SEQRES  23 C  326  ILE ASP GLY ALA LEU LEU THR LYS SER SER GLU TYR LYS          
SEQRES  24 C  326  GLY PRO ILE THR ASP VAL PHE TYR LYS GLU ASN SER TYR          
SEQRES  25 C  326  THR THR THR ILE LYS PRO LEU GLU HIS HIS HIS HIS HIS          
SEQRES  26 C  326  HIS                                                          
SEQRES   1 D  326  MET ARG GLU VAL ARG THR ILE LYS VAL PHE THR THR VAL          
SEQRES   2 D  326  ASP ASN ILE ASN LEU HIS THR GLN VAL VAL ASP MET SER          
SEQRES   3 D  326  MET THR TYR GLY GLN GLN PHE GLY PRO THR TYR LEU ASP          
SEQRES   4 D  326  GLY ALA ASP VAL THR LYS ILE LYS PRO HIS ASN SER HIS          
SEQRES   5 D  326  GLU GLY LYS THR PHE TYR VAL LEU PRO ASN ASP ASP THR          
SEQRES   6 D  326  LEU ARG VAL GLU ALA PHE GLU TYR TYR HIS THR THR ASP          
SEQRES   7 D  326  PRO SER PHE LEU GLY ARG TYR MET SER ALA LEU ASN HIS          
SEQRES   8 D  326  THR LYS LYS TRP LYS TYR PRO GLN VAL ASN GLY LEU THR          
SEQRES   9 D  326  SER ILE LYS TRP ALA ASP ASN ASN CYS TYR LEU ALA THR          
SEQRES  10 D  326  ALA LEU LEU THR LEU GLN GLN ILE GLU LEU LYS PHE ASN          
SEQRES  11 D  326  PRO PRO ALA LEU GLN ASP ALA TYR TYR ARG ALA ARG ALA          
SEQRES  12 D  326  GLY GLU ALA ALA ASN PHE CYS ALA LEU ILE LEU ALA TYR          
SEQRES  13 D  326  CYS ASN LYS THR VAL GLY GLU LEU GLY ASP VAL ARG GLU          
SEQRES  14 D  326  THR MET SER TYR LEU PHE GLN HIS ALA ASN LEU ASP SER          
SEQRES  15 D  326  CYS LYS ARG VAL LEU ASN VAL VAL CYS LYS THR CYS GLY          
SEQRES  16 D  326  GLN GLN GLN THR THR LEU LYS GLY VAL GLU ALA VAL MET          
SEQRES  17 D  326  TYR MET GLY THR LEU SER TYR GLU GLN PHE LYS LYS GLY          
SEQRES  18 D  326  VAL GLN ILE PRO CYS THR CYS GLY LYS GLN ALA THR LYS          
SEQRES  19 D  326  TYR LEU VAL GLN GLN GLU SER PRO PHE VAL MET MET SER          
SEQRES  20 D  326  ALA PRO PRO ALA GLN TYR GLU LEU LYS HIS GLY THR PHE          
SEQRES  21 D  326  THR CYS ALA SER GLU TYR THR GLY ASN TYR GLN CYS GLY          
SEQRES  22 D  326  HIS TYR LYS HIS ILE THR SER LYS GLU THR LEU TYR CYS          
SEQRES  23 D  326  ILE ASP GLY ALA LEU LEU THR LYS SER SER GLU TYR LYS          
SEQRES  24 D  326  GLY PRO ILE THR ASP VAL PHE TYR LYS GLU ASN SER TYR          
SEQRES  25 D  326  THR THR THR ILE LYS PRO LEU GLU HIS HIS HIS HIS HIS          
SEQRES  26 D  326  HIS                                                          
SEQRES   1 G    5  ACE UB4 DPP GLY GVE                                          
SEQRES   1 H    5  ACE UB4 DPP GLY GVE                                          
SEQRES   1 I    5  ACE UB4 DPP GLY GVE                                          
SEQRES   1 J    5  ACE UB4 DPP GLY GVE                                          
HET    ACE  G   1       3                                                       
HET    UB4  G   2      15                                                       
HET    DPP  G   3       6                                                       
HET    GVE  G   5       8                                                       
HET    ACE  H   1       3                                                       
HET    UB4  H   2      15                                                       
HET    DPP  H   3       6                                                       
HET    GVE  H   5       8                                                       
HET    ACE  I   1       3                                                       
HET    UB4  I   2      15                                                       
HET    DPP  I   3       6                                                       
HET    GVE  I   5       8                                                       
HET    ACE  J   1       3                                                       
HET    UB4  J   2      15                                                       
HET    DPP  J   3       6                                                       
HET    GVE  J   5       8                                                       
HET     ZN  A 501       1                                                       
HET     ZN  B 501       1                                                       
HET     MG  B 502       1                                                       
HET     ZN  C 501       1                                                       
HET     MG  C 502       1                                                       
HET     ZN  D 501       1                                                       
HET     MG  D 502       1                                                       
HET     MG  D 503       1                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     UB4 (2S)-2-AMINO-4-(1,3-BENZOTHIAZOL-2-YL)BUTANOIC ACID              
HETNAM     DPP DIAMINOPROPANOIC ACID                                            
HETNAM     GVE METHYL 4-AMINOBUTANOATE                                          
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   5  ACE    4(C2 H4 O)                                                   
FORMUL   5  UB4    4(C11 H12 N2 O2 S)                                           
FORMUL   5  DPP    4(C3 H8 N2 O2)                                               
FORMUL   5  GVE    4(C5 H11 N O2)                                               
FORMUL   9   ZN    4(ZN 2+)                                                     
FORMUL  11   MG    4(MG 2+)                                                     
FORMUL  17  HOH   *18(H2 O)                                                     
HELIX    1 AA1 TYR A   27  GLY A   32  1                                   6    
HELIX    2 AA2 HIS A   47  GLU A   51  5                                   5    
HELIX    3 AA3 ASP A   61  HIS A   73  1                                  13    
HELIX    4 AA4 PRO A   77  LYS A   91  1                                  15    
HELIX    5 AA5 ASN A  110  GLN A  121  1                                  12    
HELIX    6 AA6 PRO A  129  GLY A  142  1                                  14    
HELIX    7 AA7 ALA A  144  CYS A  155  1                                  12    
HELIX    8 AA8 ASP A  164  HIS A  175  1                                  12    
HELIX    9 AA9 VAL A  202  ALA A  204  5                                   3    
HELIX   10 AB1 SER A  212  GLY A  219  1                                   8    
HELIX   11 AB2 HIS B   47  GLU B   51  5                                   5    
HELIX   12 AB3 ASP B   61  HIS B   73  1                                  13    
HELIX   13 AB4 SER B   78  LYS B   91  1                                  14    
HELIX   14 AB5 ASN B  110  GLN B  121  1                                  12    
HELIX   15 AB6 PRO B  129  GLY B  142  1                                  14    
HELIX   16 AB7 ALA B  144  CYS B  155  1                                  12    
HELIX   17 AB8 ASP B  164  HIS B  175  1                                  12    
HELIX   18 AB9 VAL B  202  ALA B  204  5                                   3    
HELIX   19 AC1 SER B  212  GLY B  219  1                                   8    
HELIX   20 AC2 THR C   26  GLY C   32  1                                   7    
HELIX   21 AC3 HIS C   47  GLU C   51  5                                   5    
HELIX   22 AC4 ASP C   61  HIS C   73  1                                  13    
HELIX   23 AC5 SER C   78  LYS C   91  1                                  14    
HELIX   24 AC6 ASN C  110  GLN C  121  1                                  12    
HELIX   25 AC7 PRO C  129  GLY C  142  1                                  14    
HELIX   26 AC8 ALA C  144  CYS C  155  1                                  12    
HELIX   27 AC9 ASP C  164  HIS C  175  1                                  12    
HELIX   28 AD1 VAL C  202  ALA C  204  5                                   3    
HELIX   29 AD2 SER C  212  GLY C  219  1                                   8    
HELIX   30 AD3 THR D   26  PHE D   31  1                                   6    
HELIX   31 AD4 HIS D   47  GLU D   51  5                                   5    
HELIX   32 AD5 ASP D   61  HIS D   73  1                                  13    
HELIX   33 AD6 PRO D   77  LYS D   91  1                                  15    
HELIX   34 AD7 ASN D  110  GLN D  121  1                                  12    
HELIX   35 AD8 PRO D  129  GLY D  142  1                                  14    
HELIX   36 AD9 ALA D  144  CYS D  155  1                                  12    
HELIX   37 AE1 ASP D  164  HIS D  175  1                                  12    
HELIX   38 AE2 VAL D  202  ALA D  204  5                                   3    
HELIX   39 AE3 SER D  212  GLY D  219  1                                   8    
SHEET    1 AA1 5 HIS A  17  ASP A  22  0                                        
SHEET    2 AA1 5 THR A   4  THR A  10 -1  N  VAL A   7   O  GLN A  19           
SHEET    3 AA1 5 THR A  54  VAL A  57  1  O  PHE A  55   N  PHE A   8           
SHEET    4 AA1 5 THR A  34  LEU A  36 -1  N  TYR A  35   O  TYR A  56           
SHEET    5 AA1 5 ALA A  39  ASP A  40 -1  O  ALA A  39   N  LEU A  36           
SHEET    1 AA2 2 GLN A  97  VAL A  98  0                                        
SHEET    2 AA2 2 LEU A 101  THR A 102 -1  O  LEU A 101   N  VAL A  98           
SHEET    1 AA3 4 GLN A 194  LYS A 200  0                                        
SHEET    2 AA3 4 LYS A 182  VAL A 188 -1  N  ARG A 183   O  LEU A 199           
SHEET    3 AA3 4 GLN A 229  GLU A 238 -1  O  GLN A 236   N  VAL A 184           
SHEET    4 AA3 4 VAL A 220  PRO A 223 -1  N  VAL A 220   O  LYS A 232           
SHEET    1 AA411 GLN A 194  LYS A 200  0                                        
SHEET    2 AA411 LYS A 182  VAL A 188 -1  N  ARG A 183   O  LEU A 199           
SHEET    3 AA411 GLN A 229  GLU A 238 -1  O  GLN A 236   N  VAL A 184           
SHEET    4 AA411 SER A 309  THR A 312 -1  O  TYR A 310   N  GLN A 237           
SHEET    5 AA411 LEU B 289  SER B 293 -1  O  LYS B 292   N  SER A 309           
SHEET    6 AA411 LEU B 282  ASP B 286 -1  N  ASP B 286   O  LEU B 289           
SHEET    7 AA411 GLY B 271  SER B 278 -1  N  HIS B 275   O  ILE B 285           
SHEET    8 AA411 CYS B 260  GLY B 266 -1  N  GLU B 263   O  LYS B 274           
SHEET    9 AA411 TYR B 296  LYS B 306 -1  O  PHE B 304   N  CYS B 260           
SHEET   10 AA411 PHE B 241  LEU B 253 -1  N  MET B 244   O  VAL B 303           
SHEET   11 AA411 MET B 206  MET B 208  1  N  TYR B 207   O  SER B 245           
SHEET    1 AA5 7 MET A 206  MET A 208  0                                        
SHEET    2 AA5 7 PHE A 241  LEU A 253  1  O  SER A 245   N  TYR A 207           
SHEET    3 AA5 7 TYR A 296  LYS A 306 -1  O  VAL A 303   N  MET A 244           
SHEET    4 AA5 7 CYS A 260  GLY A 266 -1  N  CYS A 260   O  PHE A 304           
SHEET    5 AA5 7 GLY A 271  SER A 278 -1  O  LYS A 274   N  GLU A 263           
SHEET    6 AA5 7 LEU A 282  ASP A 286 -1  O  ILE A 285   N  HIS A 275           
SHEET    7 AA5 7 LEU A 289  SER A 293 -1  O  LEU A 289   N  ASP A 286           
SHEET    1 AA6 5 HIS B  17  ASP B  22  0                                        
SHEET    2 AA6 5 THR B   4  THR B  10 -1  N  VAL B   7   O  GLN B  19           
SHEET    3 AA6 5 THR B  54  VAL B  57  1  O  PHE B  55   N  PHE B   8           
SHEET    4 AA6 5 THR B  34  LEU B  36 -1  N  TYR B  35   O  TYR B  56           
SHEET    5 AA6 5 ALA B  39  ASP B  40 -1  O  ALA B  39   N  LEU B  36           
SHEET    1 AA7 2 GLN B  97  VAL B  98  0                                        
SHEET    2 AA7 2 LEU B 101  THR B 102 -1  O  LEU B 101   N  VAL B  98           
SHEET    1 AA8 4 GLY B 193  LYS B 200  0                                        
SHEET    2 AA8 4 LYS B 182  CYS B 189 -1  N  CYS B 189   O  GLY B 193           
SHEET    3 AA8 4 GLN B 229  GLU B 238 -1  O  GLN B 236   N  VAL B 184           
SHEET    4 AA8 4 VAL B 220  PRO B 223 -1  N  ILE B 222   O  ALA B 230           
SHEET    1 AA9 4 GLY B 193  LYS B 200  0                                        
SHEET    2 AA9 4 LYS B 182  CYS B 189 -1  N  CYS B 189   O  GLY B 193           
SHEET    3 AA9 4 GLN B 229  GLU B 238 -1  O  GLN B 236   N  VAL B 184           
SHEET    4 AA9 4 SER B 309  THR B 311 -1  O  TYR B 310   N  GLN B 237           
SHEET    1 AB1 5 HIS C  17  ASP C  22  0                                        
SHEET    2 AB1 5 THR C   4  THR C  10 -1  N  VAL C   7   O  GLN C  19           
SHEET    3 AB1 5 THR C  54  VAL C  57  1  O  PHE C  55   N  PHE C   8           
SHEET    4 AB1 5 THR C  34  LEU C  36 -1  N  TYR C  35   O  TYR C  56           
SHEET    5 AB1 5 ALA C  39  ASP C  40 -1  O  ALA C  39   N  LEU C  36           
SHEET    1 AB2 2 GLN C  97  VAL C  98  0                                        
SHEET    2 AB2 2 LEU C 101  THR C 102 -1  O  LEU C 101   N  VAL C  98           
SHEET    1 AB3 4 GLY C 193  LYS C 200  0                                        
SHEET    2 AB3 4 LYS C 182  CYS C 189 -1  N  VAL C 187   O  GLN C 195           
SHEET    3 AB3 4 GLN C 229  GLU C 238 -1  O  GLN C 236   N  VAL C 184           
SHEET    4 AB3 4 VAL C 220  PRO C 223 -1  N  VAL C 220   O  LYS C 232           
SHEET    1 AB4 4 GLY C 193  LYS C 200  0                                        
SHEET    2 AB4 4 LYS C 182  CYS C 189 -1  N  VAL C 187   O  GLN C 195           
SHEET    3 AB4 4 GLN C 229  GLU C 238 -1  O  GLN C 236   N  VAL C 184           
SHEET    4 AB4 4 TYR C 310  THR C 311 -1  O  TYR C 310   N  GLN C 237           
SHEET    1 AB5 7 MET C 206  MET C 208  0                                        
SHEET    2 AB5 7 PHE C 241  LEU C 253  1  O  SER C 245   N  TYR C 207           
SHEET    3 AB5 7 TYR C 296  LYS C 306 -1  O  VAL C 303   N  MET C 244           
SHEET    4 AB5 7 CYS C 260  GLY C 266 -1  N  CYS C 260   O  PHE C 304           
SHEET    5 AB5 7 GLY C 271  SER C 278 -1  O  LYS C 274   N  GLU C 263           
SHEET    6 AB5 7 LEU C 282  ASP C 286 -1  O  ILE C 285   N  HIS C 275           
SHEET    7 AB5 7 LEU C 289  SER C 293 -1  O  THR C 291   N  CYS C 284           
SHEET    1 AB6 5 HIS D  17  ASP D  22  0                                        
SHEET    2 AB6 5 THR D   4  THR D  10 -1  N  VAL D   7   O  GLN D  19           
SHEET    3 AB6 5 THR D  54  VAL D  57  1  O  PHE D  55   N  PHE D   8           
SHEET    4 AB6 5 THR D  34  LEU D  36 -1  N  TYR D  35   O  TYR D  56           
SHEET    5 AB6 5 ALA D  39  ASP D  40 -1  O  ALA D  39   N  LEU D  36           
SHEET    1 AB7 2 GLN D  97  VAL D  98  0                                        
SHEET    2 AB7 2 LEU D 101  THR D 102 -1  O  LEU D 101   N  VAL D  98           
SHEET    1 AB8 4 GLY D 193  LYS D 200  0                                        
SHEET    2 AB8 4 LYS D 182  CYS D 189 -1  N  ARG D 183   O  LEU D 199           
SHEET    3 AB8 4 GLN D 229  GLU D 238 -1  O  VAL D 235   N  VAL D 184           
SHEET    4 AB8 4 VAL D 220  PRO D 223 -1  N  VAL D 220   O  LYS D 232           
SHEET    1 AB9 4 GLY D 193  LYS D 200  0                                        
SHEET    2 AB9 4 LYS D 182  CYS D 189 -1  N  ARG D 183   O  LEU D 199           
SHEET    3 AB9 4 GLN D 229  GLU D 238 -1  O  VAL D 235   N  VAL D 184           
SHEET    4 AB9 4 TYR D 310  THR D 311 -1  O  TYR D 310   N  GLN D 237           
SHEET    1 AC1 7 MET D 206  MET D 208  0                                        
SHEET    2 AC1 7 PHE D 241  LEU D 253  1  O  SER D 245   N  TYR D 207           
SHEET    3 AC1 7 TYR D 296  LYS D 306 -1  O  VAL D 303   N  MET D 244           
SHEET    4 AC1 7 CYS D 260  GLY D 266 -1  N  CYS D 260   O  PHE D 304           
SHEET    5 AC1 7 GLY D 271  SER D 278 -1  O  LYS D 274   N  GLU D 263           
SHEET    6 AC1 7 LEU D 282  ASP D 286 -1  O  ILE D 285   N  HIS D 275           
SHEET    7 AC1 7 LEU D 289  SER D 293 -1  O  THR D 291   N  CYS D 284           
LINK         SG  CYS A 111                 CB  GVE G   5     1555   1555  1.81  
LINK         SG  CYS B 111                 CB  GVE H   5     1555   1555  1.79  
LINK         SG  CYS C 111                 CB  GVE I   5     1555   1555  1.80  
LINK         SG  CYS D 111                 CB  GVE J   5     1555   1555  1.80  
LINK         C   ACE G   1                 N   UB4 G   2     1555   1555  1.44  
LINK         C   UB4 G   2                 N   DPP G   3     1555   1555  1.45  
LINK         C   DPP G   3                 N   GLY G   4     1555   1555  1.44  
LINK         C   GLY G   4                 N   GVE G   5     1555   1555  1.45  
LINK         C   ACE H   1                 N   UB4 H   2     1555   1555  1.45  
LINK         C   UB4 H   2                 N   DPP H   3     1555   1555  1.44  
LINK         C   DPP H   3                 N   GLY H   4     1555   1555  1.45  
LINK         C   GLY H   4                 N   GVE H   5     1555   1555  1.45  
LINK         C   ACE I   1                 N   UB4 I   2     1555   1555  1.45  
LINK         C   UB4 I   2                 N   DPP I   3     1555   1555  1.45  
LINK         C   DPP I   3                 N   GLY I   4     1555   1555  1.45  
LINK         C   GLY I   4                 N   GVE I   5     1555   1555  1.46  
LINK         C   ACE J   1                 N   UB4 J   2     1555   1555  1.45  
LINK         C   UB4 J   2                 N   DPP J   3     1555   1555  1.45  
LINK         C   DPP J   3                 N   GLY J   4     1555   1555  1.44  
LINK         C   GLY J   4                 N   GVE J   5     1555   1555  1.45  
LINK         SG  CYS A 189                ZN    ZN A 501     1555   1555  2.27  
LINK         SG  CYS A 192                ZN    ZN A 501     1555   1555  2.32  
LINK         SG  CYS A 224                ZN    ZN A 501     1555   1555  2.40  
LINK         SG  CYS A 226                ZN    ZN A 501     1555   1555  2.30  
LINK         SG  CYS B 189                ZN    ZN B 501     1555   1555  2.36  
LINK         SG  CYS B 192                ZN    ZN B 501     1555   1555  2.07  
LINK         SG  CYS B 224                ZN    ZN B 501     1555   1555  2.43  
LINK         SG  CYS B 226                ZN    ZN B 501     1555   1555  2.38  
LINK         SG  CYS C 189                ZN    ZN C 501     1555   1555  2.25  
LINK         SG  CYS C 192                ZN    ZN C 501     1555   1555  2.23  
LINK         SG  CYS C 224                ZN    ZN C 501     1555   1555  2.44  
LINK         SG  CYS C 226                ZN    ZN C 501     1555   1555  2.28  
LINK         SG  CYS D 189                ZN    ZN D 501     1555   1555  2.37  
LINK         SG  CYS D 192                ZN    ZN D 501     1555   1555  2.28  
LINK         SG  CYS D 224                ZN    ZN D 501     1555   1555  2.39  
LINK         SG  CYS D 226                ZN    ZN D 501     1555   1555  2.30  
SITE     1 AC1  4 CYS A 189  CYS A 192  CYS A 224  CYS A 226                    
SITE     1 AC2  4 CYS B 189  CYS B 192  CYS B 224  CYS B 226                    
SITE     1 AC3  3 GLN B 174  CYS D 155  ASN D 156                               
SITE     1 AC4  4 CYS C 189  CYS C 192  CYS C 224  CYS C 226                    
SITE     1 AC5  4 CYS D 189  CYS D 192  CYS D 224  CYS D 226                    
SITE     1 AC6  2 ILE D 285  GLY D 287                                          
SITE     1 AC7  1 ASP D  61                                                     
SITE     1 AC8 11 GLY A 163  ASP A 164  MET A 208  PRO A 247                    
SITE     2 AC8 11 PRO A 248  TYR A 264  TYR A 268  TYR A 273                    
SITE     3 AC8 11 THR A 301  DPP G   3  ACE I   1                               
SITE     1 AC9 16 LEU A 162  GLY A 163  ASP A 164  MET A 208                    
SITE     2 AC9 16 PRO A 247  PRO A 248  TYR A 264  TYR A 268                    
SITE     3 AC9 16 GLN A 269  CYS A 270  GLY A 271  TYR A 273                    
SITE     4 AC9 16 THR A 301  ACE G   1  GLY G   4  ACE I   1                    
SITE     1 AD1 10 CYS A 111  LEU A 162  GLY A 163  TYR A 264                    
SITE     2 AD1 10 TYR A 268  GLN A 269  CYS A 270  GLY A 271                    
SITE     3 AD1 10 UB4 G   2  GVE G   5                                          
SITE     1 AD2  8 TRP A 106  ASN A 109  CYS A 111  LEU A 162                    
SITE     2 AD2  8 GLY A 163  GLY A 271  HIS A 272  DPP G   3                    
SITE     1 AD3  8 GLY B 163  ASP B 164  MET B 208  TYR B 264                    
SITE     2 AD3  8 TYR B 273  MET D 208  DPP H   3  UB4 J   2                    
SITE     1 AD4 13 LEU B 162  GLY B 163  ASP B 164  MET B 208                    
SITE     2 AD4 13 TYR B 264  TYR B 268  GLN B 269  CYS B 270                    
SITE     3 AD4 13 GLY B 271  TYR B 273  MET D 208  ACE H   1                    
SITE     4 AD4 13 GLY H   4                                                     
SITE     1 AD5 10 CYS B 111  LEU B 162  GLY B 163  TYR B 268                    
SITE     2 AD5 10 GLN B 269  CYS B 270  GLY B 271  MET D 208                    
SITE     3 AD5 10 UB4 H   2  GVE H   5                                          
SITE     1 AD6  8 TRP B 106  ASN B 109  CYS B 111  LEU B 162                    
SITE     2 AD6  8 GLY B 163  GLY B 271  HIS B 272  DPP H   3                    
SITE     1 AD7 10 MET A 208  GLY C 163  ASP C 164  MET C 208                    
SITE     2 AD7 10 PRO C 247  TYR C 264  TYR C 268  TYR C 273                    
SITE     3 AD7 10 UB4 G   2  DPP I   3                                          
SITE     1 AD8 14 MET A 208  LEU C 162  GLY C 163  ASP C 164                    
SITE     2 AD8 14 MET C 208  PRO C 247  TYR C 264  TYR C 268                    
SITE     3 AD8 14 GLN C 269  CYS C 270  GLY C 271  TYR C 273                    
SITE     4 AD8 14 ACE I   1  GLY I   4                                          
SITE     1 AD9 11 MET A 208  CYS C 111  LEU C 162  GLY C 163                    
SITE     2 AD9 11 TYR C 264  TYR C 268  GLN C 269  CYS C 270                    
SITE     3 AD9 11 GLY C 271  UB4 I   2  GVE I   5                               
SITE     1 AE1  8 LEU B 317  ASN C 109  CYS C 111  LEU C 162                    
SITE     2 AE1  8 GLY C 163  GLY C 271  HIS C 272  DPP I   3                    
SITE     1 AE2 17 LEU B 317  THR C   4  LYS C   6  VAL C  20                    
SITE     2 AE2 17 VAL C  21  HIS C  47  GLU C  51  ASN C 109                    
SITE     3 AE2 17 ASN C 110  TYR C 112  LEU C 113  ALA C 114                    
SITE     4 AE2 17 THR C 115  GLY C 271  HIS C 272  TYR C 273                    
SITE     5 AE2 17 GLY I   4                                                     
SITE     1 AE3 10 GLY D 163  ASP D 164  MET D 208  PRO D 247                    
SITE     2 AE3 10 PRO D 248  TYR D 264  TYR D 273  THR D 301                    
SITE     3 AE3 10 ACE H   1  DPP J   3                                          
SITE     1 AE4 16 LEU D 162  GLY D 163  ASP D 164  MET D 208                    
SITE     2 AE4 16 PRO D 247  PRO D 248  TYR D 264  TYR D 268                    
SITE     3 AE4 16 GLN D 269  CYS D 270  GLY D 271  TYR D 273                    
SITE     4 AE4 16 THR D 301  ACE H   1  ACE J   1  GLY J   4                    
SITE     1 AE5 10 CYS D 111  LEU D 162  GLY D 163  TYR D 264                    
SITE     2 AE5 10 TYR D 268  GLN D 269  CYS D 270  GLY D 271                    
SITE     3 AE5 10 UB4 J   2  GVE J   5                                          
SITE     1 AE6  7 ASN D 109  CYS D 111  LEU D 162  GLY D 163                    
SITE     2 AE6  7 GLY D 271  HIS D 272  DPP J   3                               
SITE     1 AE7 17 THR D   4  LYS D   6  VAL D  20  VAL D  21                    
SITE     2 AE7 17 MET D  23  HIS D  47  GLU D  51  ASN D 109                    
SITE     3 AE7 17 ASN D 110  TYR D 112  LEU D 113  ALA D 114                    
SITE     4 AE7 17 THR D 115  GLY D 271  HIS D 272  TYR D 273                    
SITE     5 AE7 17 GLY J   4                                                     
CRYST1   58.425  189.693   63.118  90.00  98.66  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017116  0.000000  0.002608        0.00000                         
SCALE2      0.000000  0.005272  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016026        0.00000                         
ATOM      1  N   MET A  -1      23.940 128.572   3.487  1.00141.21           N  
ATOM      2  CA  MET A  -1      24.766 129.636   4.042  1.00142.02           C  
ATOM      3  C   MET A  -1      25.335 129.217   5.395  1.00139.22           C  
ATOM      4  O   MET A  -1      25.444 130.028   6.315  1.00139.00           O  
ATOM      5  CB  MET A  -1      23.957 130.934   4.169  1.00144.78           C  
ATOM      6  CG  MET A  -1      22.630 130.774   4.910  1.00147.00           C  
ATOM      7  SD  MET A  -1      21.726 132.322   5.154  1.00146.58           S  
ATOM      8  CE  MET A  -1      20.753 131.920   6.606  1.00144.73           C  
ATOM      9  N   ARG A   0      25.706 127.942   5.507  1.00135.18           N  
ATOM     10  CA  ARG A   0      26.216 127.382   6.748  1.00132.16           C  
ATOM     11  C   ARG A   0      27.702 127.057   6.633  1.00130.12           C  
ATOM     12  O   ARG A   0      28.181 126.597   5.591  1.00131.31           O  
ATOM     13  CB  ARG A   0      25.431 126.130   7.148  1.00131.70           C  
ATOM     14  CG  ARG A   0      24.053 126.439   7.723  1.00130.72           C  
ATOM     15  CD  ARG A   0      23.652 125.431   8.791  1.00129.30           C  
ATOM     16  NE  ARG A   0      24.727 125.212   9.758  1.00127.72           N  
ATOM     17  CZ  ARG A   0      25.462 124.105   9.822  1.00123.94           C  
ATOM     18  NH1 ARG A   0      25.230 123.105   8.982  1.00124.08           N  
ATOM     19  NH2 ARG A   0      26.425 123.996  10.729  1.00120.83           N  
ATOM     20  N   GLU A   1      28.422 127.308   7.729  1.00126.52           N  
ATOM     21  CA  GLU A   1      29.870 127.175   7.787  1.00123.33           C  
ATOM     22  C   GLU A   1      30.300 125.737   7.493  1.00115.92           C  
ATOM     23  O   GLU A   1      29.503 124.795   7.540  1.00116.40           O  
ATOM     24  CB  GLU A   1      30.379 127.583   9.166  1.00127.99           C  
ATOM     25  CG  GLU A   1      30.078 129.024   9.518  1.00130.65           C  
ATOM     26  CD  GLU A   1      30.406 129.326  10.956  1.00128.81           C  
ATOM     27  OE1 GLU A   1      30.612 128.363  11.727  1.00128.77           O  
ATOM     28  OE2 GLU A   1      30.441 130.519  11.317  1.00126.12           O  
ATOM     29  N   VAL A   2      31.587 125.570   7.182  1.00109.72           N  
ATOM     30  CA  VAL A   2      32.156 124.251   6.949  1.00103.98           C  
ATOM     31  C   VAL A   2      33.084 123.895   8.107  1.00101.22           C  
ATOM     32  O   VAL A   2      33.899 124.716   8.543  1.00100.32           O  
ATOM     33  CB  VAL A   2      32.902 124.173   5.607  1.00 96.21           C  
ATOM     34  CG1 VAL A   2      31.909 124.173   4.447  1.00 89.56           C  
ATOM     35  CG2 VAL A   2      33.889 125.324   5.477  1.00 93.91           C  
ATOM     36  N   ARG A   3      32.956 122.660   8.581  1.00136.34           N  
ANISOU   36  N   ARG A   3    14052  17611  20140    271    215   1722       N  
ATOM     37  CA  ARG A   3      33.827 122.057   9.572  1.00116.86           C  
ANISOU   37  CA  ARG A   3    11633  15210  17558    408    298   1569       C  
ATOM     38  C   ARG A   3      34.410 120.797   8.958  1.00101.70           C  
ANISOU   38  C   ARG A   3     9737  13360  15543    518    232   1722       C  
ATOM     39  O   ARG A   3      33.696 120.037   8.293  1.00 95.07           O  
ANISOU   39  O   ARG A   3     8858  12524  14739    429    120   1945       O  
ATOM     40  CB  ARG A   3      33.078 121.731  10.870  1.00116.54           C  
ANISOU   40  CB  ARG A   3    11571  15130  17581    327    359   1482       C  
ATOM     41  CG  ARG A   3      32.605 122.956  11.641  1.00117.28           C  
ANISOU   41  CG  ARG A   3    11661  15180  17721    240    426   1303       C  
ATOM     42  CD  ARG A   3      31.840 122.586  12.918  1.00119.61           C  
ANISOU   42  CD  ARG A   3    11938  15429  18079    144    496   1220       C  
ATOM     43  NE  ARG A   3      30.658 121.764  12.651  1.00124.60           N  
ANISOU   43  NE  ARG A   3    12531  15962  18848     -1    443   1382       N  
ATOM     44  CZ  ARG A   3      29.941 121.138  13.583  1.00127.43           C  
ANISOU   44  CZ  ARG A   3    12882  16258  19277   -103    506   1343       C  
ATOM     45  NH1 ARG A   3      30.272 121.234  14.864  1.00131.31           N  
ANISOU   45  NH1 ARG A   3    13391  16781  19721    -74    626   1166       N  
ATOM     46  NH2 ARG A   3      28.881 120.420  13.230  1.00125.16           N  
ANISOU   46  NH2 ARG A   3    12579  15868  19106   -245    449   1474       N  
ATOM     47  N   THR A   4      35.708 120.573   9.143  1.00 98.13           N  
ANISOU   47  N   THR A   4     9369  12964  14953    713    279   1595       N  
ATOM     48  CA  THR A   4      36.361 119.462   8.470  1.00 90.39           C  
ANISOU   48  CA  THR A   4     8446  12043  13854    848    206   1724       C  
ATOM     49  C   THR A   4      37.175 118.636   9.445  1.00 85.76           C  
ANISOU   49  C   THR A   4     8060  11452  13073   1003    246   1536       C  
ATOM     50  O   THR A   4      37.748 119.151  10.406  1.00 85.92           O  
ANISOU   50  O   THR A   4     8022  11472  13153   1107    348   1344       O  
ATOM     51  CB  THR A   4      37.290 119.953   7.365  1.00 83.69           C  
ANISOU   51  CB  THR A   4     7643  11208  12947    927    200   1722       C  
ATOM     52  OG1 THR A   4      38.235 120.871   7.929  1.00 77.51           O  
ANISOU   52  OG1 THR A   4     6922  10398  12132   1018    309   1438       O  
ATOM     53  CG2 THR A   4      36.495 120.644   6.270  1.00 83.09           C  
ANISOU   53  CG2 THR A   4     7478  11116  12976    758    131   1910       C  
ATOM     54  N   ILE A   5      37.207 117.328   9.170  1.00 84.17           N  
ANISOU   54  N   ILE A   5     8217  11218  12545    967    142   1535       N  
ATOM     55  CA  ILE A   5      38.114 116.393   9.820  1.00 79.39           C  
ANISOU   55  CA  ILE A   5     7892  10583  11688   1098    136   1354       C  
ATOM     56  C   ILE A   5      38.738 115.519   8.740  1.00 71.08           C  
ANISOU   56  C   ILE A   5     7105   9517  10384   1112     38   1373       C  
ATOM     57  O   ILE A   5      38.168 115.303   7.668  1.00 64.01           O  
ANISOU   57  O   ILE A   5     6252   8637   9433    977    -41   1535       O  
ATOM     58  CB  ILE A   5      37.418 115.515  10.884  1.00 75.28           C  
ANISOU   58  CB  ILE A   5     7553  10021  11028   1017    125   1306       C  
ATOM     59  CG1 ILE A   5      36.369 114.612  10.236  1.00 65.35           C  
ANISOU   59  CG1 ILE A   5     6467   8739   9623    832     23   1454       C  
ATOM     60  CG2 ILE A   5      36.807 116.369  11.985  1.00 77.53           C  
ANISOU   60  CG2 ILE A   5     7585  10310  11564    977    241   1265       C  
ATOM     61  CD1 ILE A   5      35.834 113.553  11.164  1.00 56.76           C  
ANISOU   61  CD1 ILE A   5     5616   7597   8354    772     16   1392       C  
ATOM     62  N   LYS A   6      39.910 114.985   9.054  1.00 68.76           N  
ANISOU   62  N   LYS A   6     6995   9185   9947   1265     38   1196       N  
ATOM     63  CA  LYS A   6      40.650 114.114   8.154  1.00 67.62           C  
ANISOU   63  CA  LYS A   6     7098   9007   9587   1277    -37   1167       C  
ATOM     64  C   LYS A   6      40.419 112.660   8.552  1.00 68.71           C  
ANISOU   64  C   LYS A   6     7541   9111   9456   1213   -126   1133       C  
ATOM     65  O   LYS A   6      40.536 112.305   9.729  1.00 70.99           O  
ANISOU   65  O   LYS A   6     7912   9365   9697   1280   -115   1017       O  
ATOM     66  CB  LYS A   6      42.129 114.502   8.190  1.00 72.42           C  
ANISOU   66  CB  LYS A   6     7689   9563  10266   1483     23    975       C  
ATOM     67  CG  LYS A   6      43.149 113.400   8.004  1.00 85.13           C  
ANISOU   67  CG  LYS A   6     9589  11086  11671   1541    -42    826       C  
ATOM     68  CD  LYS A   6      44.535 113.959   8.329  1.00 88.67           C  
ANISOU   68  CD  LYS A   6     9972  11451  12267   1766     31    602       C  
ATOM     69  CE  LYS A   6      45.647 113.037   7.884  1.00 87.25           C  
ANISOU   69  CE  LYS A   6    10041  11153  11956   1809    -24    444       C  
ATOM     70  NZ  LYS A   6      46.742 113.834   7.264  1.00 88.15           N  
ANISOU   70  NZ  LYS A   6    10047  11192  12255   1943     72    316       N  
ATOM     71  N   VAL A   7      40.053 111.832   7.578  1.00 67.08           N  
ANISOU   71  N   VAL A   7     7495   8915   9077   1079   -210   1240       N  
ATOM     72  CA  VAL A   7      39.807 110.414   7.784  1.00 64.06           C  
ANISOU   72  CA  VAL A   7     7381   8507   8451   1011   -288   1220       C  
ATOM     73  C   VAL A   7      40.512 109.638   6.677  1.00 64.37           C  
ANISOU   73  C   VAL A   7     7594   8533   8331    978   -348   1198       C  
ATOM     74  O   VAL A   7      41.099 110.221   5.767  1.00 70.70           O  
ANISOU   74  O   VAL A   7     8322   9339   9202    994   -324   1205       O  
ATOM     75  CB  VAL A   7      38.299 110.076   7.815  1.00 59.58           C  
ANISOU   75  CB  VAL A   7     6814   7970   7856    843   -318   1378       C  
ATOM     76  CG1 VAL A   7      37.593 110.825   8.931  1.00 58.30           C  
ANISOU   76  CG1 VAL A   7     6479   7799   7874    847   -241   1378       C  
ATOM     77  CG2 VAL A   7      37.658 110.395   6.483  1.00 57.94           C  
ANISOU   77  CG2 VAL A   7     6514   7811   7688    708   -363   1561       C  
ATOM     78  N   PHE A   8      40.445 108.310   6.760  1.00 57.91           N  
ANISOU   78  N   PHE A   8     7004   7693   7306    922   -416   1167       N  
ATOM     79  CA  PHE A   8      41.057 107.423   5.780  1.00 55.66           C  
ANISOU   79  CA  PHE A   8     6882   7394   6873    862   -468   1131       C  
ATOM     80  C   PHE A   8      40.006 106.501   5.181  1.00 63.13           C  
ANISOU   80  C   PHE A   8     7923   8399   7665    689   -529   1273       C  
ATOM     81  O   PHE A   8      39.187 105.934   5.912  1.00 68.58           O  
ANISOU   81  O   PHE A   8     8670   9091   8296    659   -545   1304       O  
ATOM     82  CB  PHE A   8      42.176 106.599   6.412  1.00 49.92           C  
ANISOU   82  CB  PHE A   8     6326   6570   6072    967   -495    925       C  
ATOM     83  CG  PHE A   8      43.315 107.427   6.902  1.00 53.83           C  
ANISOU   83  CG  PHE A   8     6740   6986   6728   1148   -444    759       C  
ATOM     84  CD1 PHE A   8      44.276 107.892   6.020  1.00 53.61           C  
ANISOU   84  CD1 PHE A   8     6669   6910   6788   1183   -404    680       C  
ATOM     85  CD2 PHE A   8      43.406 107.778   8.238  1.00 49.76           C  
ANISOU   85  CD2 PHE A   8     6187   6438   6283   1283   -425    675       C  
ATOM     86  CE1 PHE A   8      45.322 108.671   6.466  1.00 48.55           C  
ANISOU   86  CE1 PHE A   8     5943   6182   6323   1367   -346    509       C  
ATOM     87  CE2 PHE A   8      44.443 108.558   8.689  1.00 47.75           C  
ANISOU   87  CE2 PHE A   8     5842   6111   6189   1463   -379    511       C  
ATOM     88  CZ  PHE A   8      45.404 109.006   7.801  1.00 49.91           C  
ANISOU   88  CZ  PHE A   8     6064   6330   6571   1514   -338    425       C  
ATOM     89  N   THR A   9      40.020 106.371   3.854  1.00 58.40           N  
ANISOU   89  N   THR A   9     7342   7842   7004    574   -556   1350       N  
ATOM     90  CA  THR A   9      39.173 105.429   3.141  1.00 56.19           C  
ANISOU   90  CA  THR A   9     7155   7621   6573    414   -618   1461       C  
ATOM     91  C   THR A   9      40.032 104.295   2.598  1.00 59.55           C  
ANISOU   91  C   THR A   9     7752   8025   6848    369   -642   1345       C  
ATOM     92  O   THR A   9      41.218 104.481   2.311  1.00 58.25           O  
ANISOU   92  O   THR A   9     7612   7803   6718    418   -613   1216       O  
ATOM     93  CB  THR A   9      38.400 106.103   1.994  1.00 56.15           C  
ANISOU   93  CB  THR A   9     7040   7687   6606    289   -646   1652       C  
ATOM     94  OG1 THR A   9      39.310 106.719   1.070  1.00 58.17           O  
ANISOU   94  OG1 THR A   9     7273   7941   6888    286   -619   1630       O  
ATOM     95  CG2 THR A   9      37.446 107.155   2.539  1.00 49.49           C  
ANISOU   95  CG2 THR A   9     6005   6848   5949    309   -632   1767       C  
ATOM     96  N   THR A  10      39.424 103.116   2.466  1.00 63.37           N  
ANISOU   96  N   THR A  10     8342   8546   7191    272   -686   1379       N  
ATOM     97  CA  THR A  10      40.141 101.923   2.034  1.00 57.30           C  
ANISOU   97  CA  THR A  10     7713   7760   6300    212   -706   1265       C  
ATOM     98  C   THR A  10      39.156 100.897   1.493  1.00 58.73           C  
ANISOU   98  C   THR A  10     7944   8024   6349     72   -744   1365       C  
ATOM     99  O   THR A  10      37.953 100.959   1.760  1.00 60.16           O  
ANISOU   99  O   THR A  10     8079   8243   6535     55   -758   1488       O  
ATOM    100  CB  THR A  10      40.938 101.309   3.191  1.00 52.23           C  
ANISOU  100  CB  THR A  10     7165   7018   5663    334   -710   1089       C  
ATOM    101  OG1 THR A  10      41.807 100.284   2.696  1.00 60.43           O  
ANISOU  101  OG1 THR A  10     8306   8015   6637    267   -729    960       O  
ATOM    102  CG2 THR A  10      39.992 100.698   4.207  1.00 46.19           C  
ANISOU  102  CG2 THR A  10     6447   6262   4841    359   -726   1137       C  
ATOM    103  N   VAL A  11      39.688  99.950   0.725  1.00 59.49           N  
ANISOU  103  N   VAL A  11     8120   8136   6346    -31   -754   1293       N  
ATOM    104  CA  VAL A  11      38.940  98.764   0.321  1.00 61.64           C  
ANISOU  104  CA  VAL A  11     8439   8483   6499   -147   -780   1342       C  
ATOM    105  C   VAL A  11      39.588  97.472   0.794  1.00 61.77           C  
ANISOU  105  C   VAL A  11     8550   8451   6468   -138   -780   1188       C  
ATOM    106  O   VAL A  11      38.962  96.406   0.688  1.00 53.64           O  
ANISOU  106  O   VAL A  11     7546   7477   5359   -206   -788   1214       O  
ATOM    107  CB  VAL A  11      38.732  98.712  -1.209  1.00 63.72           C  
ANISOU  107  CB  VAL A  11     8687   8841   6682   -323   -794   1425       C  
ATOM    108  CG1 VAL A  11      37.991  99.941  -1.688  1.00 67.45           C  
ANISOU  108  CG1 VAL A  11     9068   9356   7205   -340   -818   1598       C  
ATOM    109  CG2 VAL A  11      40.066  98.578  -1.916  1.00 72.88           C  
ANISOU  109  CG2 VAL A  11     9898   9961   7833   -393   -760   1282       C  
ATOM    110  N   ASP A  12      40.811  97.527   1.319  1.00 69.54           N  
ANISOU  110  N   ASP A  12     9577   9323   7520    -54   -775   1026       N  
ATOM    111  CA  ASP A  12      41.543  96.338   1.723  1.00 73.88           C  
ANISOU  111  CA  ASP A  12    10209   9804   8060    -57   -795    873       C  
ATOM    112  C   ASP A  12      42.170  96.466   3.104  1.00 72.71           C  
ANISOU  112  C   ASP A  12    10117   9525   7983    116   -823    762       C  
ATOM    113  O   ASP A  12      42.807  95.515   3.565  1.00 76.92           O  
ANISOU  113  O   ASP A  12    10724   9977   8525    127   -862    636       O  
ATOM    114  CB  ASP A  12      42.637  96.012   0.695  1.00 83.40           C  
ANISOU  114  CB  ASP A  12    11423  10971   9294   -182   -779    740       C  
ATOM    115  CG  ASP A  12      43.524  97.205   0.391  1.00 90.85           C  
ANISOU  115  CG  ASP A  12    12343  11834  10344   -135   -745    672       C  
ATOM    116  OD1 ASP A  12      44.730  97.006   0.140  1.00 91.72           O  
ANISOU  116  OD1 ASP A  12    12484  11823  10541   -163   -730    488       O  
ATOM    117  OD2 ASP A  12      43.023  98.348   0.439  1.00 94.91           O  
ANISOU  117  OD2 ASP A  12    12796  12389  10876    -66   -729    792       O  
ATOM    118  N   ASN A  13      42.021  97.613   3.764  1.00 66.94           N  
ANISOU  118  N   ASN A  13     9348   8771   7316    245   -809    802       N  
ATOM    119  CA  ASN A  13      42.621  97.887   5.067  1.00 62.89           C  
ANISOU  119  CA  ASN A  13     8885   8142   6869    413   -835    696       C  
ATOM    120  C   ASN A  13      44.140  97.783   5.040  1.00 65.09           C  
ANISOU  120  C   ASN A  13     9203   8279   7251    458   -866    489       C  
ATOM    121  O   ASN A  13      44.774  97.655   6.089  1.00 64.66           O  
ANISOU  121  O   ASN A  13     9217   8106   7243    583   -919    371       O  
ATOM    122  CB  ASN A  13      42.043  96.971   6.152  1.00 62.62           C  
ANISOU  122  CB  ASN A  13     8952   8094   6746    450   -868    713       C  
ATOM    123  CG  ASN A  13      42.216  97.542   7.544  1.00 67.87           C  
ANISOU  123  CG  ASN A  13     9661   8677   7448    612   -882    667       C  
ATOM    124  OD1 ASN A  13      42.468  98.737   7.707  1.00 69.48           O  
ANISOU  124  OD1 ASN A  13     9782   8866   7750    698   -852    655       O  
ATOM    125  ND2 ASN A  13      42.071  96.695   8.555  1.00 69.97           N  
ANISOU  125  ND2 ASN A  13    10056   8892   7636    652   -922    640       N  
ATOM    126  N   ILE A  14      44.739  97.845   3.849  1.00 71.85           N  
ANISOU  126  N   ILE A  14    10021   9127   8150    350   -835    433       N  
ATOM    127  CA  ILE A  14      46.186  97.886   3.677  1.00 65.87           C  
ANISOU  127  CA  ILE A  14     9286   8207   7534    378   -842    217       C  
ATOM    128  C   ILE A  14      46.631  99.210   3.075  1.00 53.40           C  
ANISOU  128  C   ILE A  14     7623   6606   6061    418   -765    197       C  
ATOM    129  O   ILE A  14      47.599  99.819   3.535  1.00 49.56           O  
ANISOU  129  O   ILE A  14     7127   5976   5725    558   -760     41       O  
ATOM    130  CB  ILE A  14      46.689  96.705   2.818  1.00 64.95           C  
ANISOU  130  CB  ILE A  14     9207   8057   7412    196   -851    116       C  
ATOM    131  CG1 ILE A  14      46.355  95.374   3.486  1.00 64.27           C  
ANISOU  131  CG1 ILE A  14     9188   7978   7254    174   -925    121       C  
ATOM    132  CG2 ILE A  14      48.181  96.827   2.555  1.00 60.48           C  
ANISOU  132  CG2 ILE A  14     8655   7290   7033    204   -843   -128       C  
ATOM    133  CD1 ILE A  14      46.499  94.200   2.562  1.00 68.23           C  
ANISOU  133  CD1 ILE A  14     9681   8505   7738    -31   -916     71       C  
ATOM    134  N   ASN A  15      45.936  99.669   2.032  1.00 52.87           N  
ANISOU  134  N   ASN A  15     7493   6672   5923    300   -707    352       N  
ATOM    135  CA  ASN A  15      46.208 100.953   1.391  1.00 51.66           C  
ANISOU  135  CA  ASN A  15     7257   6514   5855    325   -630    371       C  
ATOM    136  C   ASN A  15      45.195 101.958   1.919  1.00 53.54           C  
ANISOU  136  C   ASN A  15     7393   6859   6092    423   -622    555       C  
ATOM    137  O   ASN A  15      43.996 101.836   1.658  1.00 62.68           O  
ANISOU  137  O   ASN A  15     8524   8153   7139    332   -641    748       O  
ATOM    138  CB  ASN A  15      46.135 100.861  -0.134  1.00 52.11           C  
ANISOU  138  CB  ASN A  15     7322   6638   5839    117   -580    426       C  
ATOM    139  CG  ASN A  15      47.279 100.061  -0.742  1.00 54.61           C  
ANISOU  139  CG  ASN A  15     7718   6823   6207      0   -555    209       C  
ATOM    140  OD1 ASN A  15      47.872  99.206  -0.096  1.00 58.47           O  
ANISOU  140  OD1 ASN A  15     8260   7201   6755     34   -605     53       O  
ATOM    141  ND2 ASN A  15      47.589 100.341  -2.000  1.00 64.27           N  
ANISOU  141  ND2 ASN A  15     8953   8049   7418   -151   -478    197       N  
ATOM    142  N   LEU A  16      45.671 102.932   2.680  1.00 54.27           N  
ANISOU  142  N   LEU A  16     7414   6878   6329    605   -593    483       N  
ATOM    143  CA  LEU A  16      44.810 103.975   3.211  1.00 54.84           C  
ANISOU  143  CA  LEU A  16     7356   7036   6446    690   -570    632       C  
ATOM    144  C   LEU A  16      44.926 105.219   2.340  1.00 57.01           C  
ANISOU  144  C   LEU A  16     7503   7337   6822    685   -492    695       C  
ATOM    145  O   LEU A  16      45.990 105.504   1.779  1.00 54.80           O  
ANISOU  145  O   LEU A  16     7235   6958   6629    705   -436    554       O  
ATOM    146  CB  LEU A  16      45.154 104.291   4.665  1.00 52.12           C  
ANISOU  146  CB  LEU A  16     6992   6613   6196    888   -581    524       C  
ATOM    147  CG  LEU A  16      45.127 103.083   5.607  1.00 52.24           C  
ANISOU  147  CG  LEU A  16     7157   6584   6108    903   -665    459       C  
ATOM    148  CD1 LEU A  16      45.195 103.546   7.043  1.00 49.08           C  
ANISOU  148  CD1 LEU A  16     6738   6137   5772   1077   -675    400       C  
ATOM    149  CD2 LEU A  16      43.899 102.224   5.386  1.00 56.80           C  
ANISOU  149  CD2 LEU A  16     7786   7278   6516    753   -697    628       C  
ATOM    150  N   HIS A  17      43.812 105.932   2.203  1.00 57.77           N  
ANISOU  150  N   HIS A  17     7478   7551   6921    647   -487    903       N  
ATOM    151  CA  HIS A  17      43.722 107.117   1.359  1.00 53.11           C  
ANISOU  151  CA  HIS A  17     6756   7001   6423    625   -429   1007       C  
ATOM    152  C   HIS A  17      43.175 108.261   2.198  1.00 57.12           C  
ANISOU  152  C   HIS A  17     7067   7543   7093    747   -398   1086       C  
ATOM    153  O   HIS A  17      42.021 108.217   2.642  1.00 52.71           O  
ANISOU  153  O   HIS A  17     6458   7058   6513    701   -440   1227       O  
ATOM    154  CB  HIS A  17      42.836 106.848   0.142  1.00 54.26           C  
ANISOU  154  CB  HIS A  17     6934   7254   6427    415   -474   1203       C  
ATOM    155  CG  HIS A  17      43.259 105.649  -0.641  1.00 53.65           C  
ANISOU  155  CG  HIS A  17     7033   7163   6189    272   -498   1126       C  
ATOM    156  ND1 HIS A  17      44.372 105.648  -1.453  1.00 54.80           N  
ANISOU  156  ND1 HIS A  17     7250   7225   6347    228   -435    988       N  
ATOM    157  CD2 HIS A  17      42.748 104.397  -0.701  1.00 55.11           C  
ANISOU  157  CD2 HIS A  17     7325   7396   6219    161   -563   1150       C  
ATOM    158  CE1 HIS A  17      44.516 104.453  -1.998  1.00 55.00           C  
ANISOU  158  CE1 HIS A  17     7410   7254   6233     78   -464    933       C  
ATOM    159  NE2 HIS A  17      43.544 103.675  -1.557  1.00 55.76           N  
ANISOU  159  NE2 HIS A  17     7523   7438   6226     43   -543   1033       N  
ATOM    160  N   THR A  18      44.007 109.277   2.411  1.00 58.78           N  
ANISOU  160  N   THR A  18     7158   7690   7487    897   -312    980       N  
ATOM    161  CA  THR A  18      43.603 110.425   3.210  1.00 56.00           C  
ANISOU  161  CA  THR A  18     6585   7370   7321   1016   -263   1031       C  
ATOM    162  C   THR A  18      42.466 111.172   2.526  1.00 60.48           C  
ANISOU  162  C   THR A  18     7001   8044   7934    891   -275   1279       C  
ATOM    163  O   THR A  18      42.524 111.454   1.326  1.00 64.48           O  
ANISOU  163  O   THR A  18     7513   8571   8415    795   -271   1369       O  
ATOM    164  CB  THR A  18      44.786 111.362   3.414  1.00 51.07           C  
ANISOU  164  CB  THR A  18     5848   6657   6900   1204   -158    857       C  
ATOM    165  OG1 THR A  18      45.855 110.652   4.044  1.00 55.38           O  
ANISOU  165  OG1 THR A  18     6538   7078   7427   1319   -169    616       O  
ATOM    166  CG2 THR A  18      44.382 112.516   4.302  1.00 47.60           C  
ANISOU  166  CG2 THR A  18     5154   6263   6668   1325    -97    895       C  
ATOM    167  N   GLN A  19      41.408 111.447   3.280  1.00 59.76           N  
ANISOU  167  N   GLN A  19     6787   8007   7913    878   -295   1387       N  
ATOM    168  CA  GLN A  19      40.289 112.248   2.807  1.00 63.08           C  
ANISOU  168  CA  GLN A  19     7026   8499   8441    769   -316   1608       C  
ATOM    169  C   GLN A  19      39.968 113.293   3.862  1.00 66.30           C  
ANISOU  169  C   GLN A  19     7180   8914   9098    869   -246   1601       C  
ATOM    170  O   GLN A  19      40.080 113.024   5.062  1.00 67.17           O  
ANISOU  170  O   GLN A  19     7310   8995   9216    960   -217   1476       O  
ATOM    171  CB  GLN A  19      39.041 111.395   2.517  1.00 60.50           C  
ANISOU  171  CB  GLN A  19     6802   8217   7968    590   -424   1760       C  
ATOM    172  CG  GLN A  19      39.274 110.230   1.563  1.00 66.43           C  
ANISOU  172  CG  GLN A  19     7795   8978   8467    480   -491   1756       C  
ATOM    173  CD  GLN A  19      39.516 110.681   0.141  1.00 72.62           C  
ANISOU  173  CD  GLN A  19     8578   9789   9224    387   -503   1855       C  
ATOM    174  OE1 GLN A  19      39.237 111.825  -0.210  1.00 80.36           O  
ANISOU  174  OE1 GLN A  19     9378  10790  10367    382   -490   1977       O  
ATOM    175  NE2 GLN A  19      40.035 109.785  -0.688  1.00 75.28           N  
ANISOU  175  NE2 GLN A  19     9116  10123   9362    301   -526   1804       N  
ATOM    176  N   VAL A  20      39.619 114.496   3.413  1.00 66.79           N  
ANISOU  176  N   VAL A  20     6999   9009   9367    848   -214   1730       N  
ATOM    177  CA  VAL A  20      39.111 115.553   4.284  1.00 68.76           C  
ANISOU  177  CA  VAL A  20     6957   9276   9892    896   -146   1753       C  
ATOM    178  C   VAL A  20      37.623 115.699   3.993  1.00 68.46           C  
ANISOU  178  C   VAL A  20     6817   9265   9929    707   -230   1968       C  
ATOM    179  O   VAL A  20      37.230 115.967   2.851  1.00 73.54           O  
ANISOU  179  O   VAL A  20     7436   9931  10576    593   -303   2138       O  
ATOM    180  CB  VAL A  20      39.858 116.878   4.083  1.00 70.02           C  
ANISOU  180  CB  VAL A  20     6871   9441  10294   1026    -36   1722       C  
ATOM    181  CG1 VAL A  20      39.304 117.939   5.018  1.00 69.99           C  
ANISOU  181  CG1 VAL A  20     6535   9462  10595   1062     42   1737       C  
ATOM    182  CG2 VAL A  20      41.343 116.686   4.330  1.00 68.93           C  
ANISOU  182  CG2 VAL A  20     6845   9243  10102   1219     44   1485       C  
ATOM    183  N   VAL A  21      36.797 115.508   5.019  1.00 61.82           N  
ANISOU  183  N   VAL A  21     5929   8406   9153    667   -224   1952       N  
ATOM    184  CA  VAL A  21      35.351 115.431   4.864  1.00 62.11           C  
ANISOU  184  CA  VAL A  21     5907   8429   9264    483   -304   2113       C  
ATOM    185  C   VAL A  21      34.709 116.631   5.542  1.00 76.76           C  
ANISOU  185  C   VAL A  21     7416  10271  11478    459   -232   2147       C  
ATOM    186  O   VAL A  21      35.265 117.222   6.478  1.00 79.32           O  
ANISOU  186  O   VAL A  21     7594  10604  11941    584   -109   2013       O  
ATOM    187  CB  VAL A  21      34.776 114.120   5.437  1.00 62.37           C  
ANISOU  187  CB  VAL A  21     6181   8423   9092    422   -345   2061       C  
ATOM    188  CG1 VAL A  21      35.443 112.934   4.795  1.00 65.21           C  
ANISOU  188  CG1 VAL A  21     6848   8801   9128    440   -407   2017       C  
ATOM    189  CG2 VAL A  21      34.942 114.081   6.947  1.00 57.32           C  
ANISOU  189  CG2 VAL A  21     5527   7753   8499    513   -239   1894       C  
ATOM    190  N   ASP A  22      33.521 116.988   5.051  1.00 82.21           N  
ANISOU  190  N   ASP A  22     7967  10933  12338    290   -313   2321       N  
ATOM    191  CA  ASP A  22      32.731 118.083   5.599  1.00 84.53           C  
ANISOU  191  CA  ASP A  22     7911  11191  13015    218   -260   2366       C  
ATOM    192  C   ASP A  22      31.776 117.554   6.662  1.00 78.42           C  
ANISOU  192  C   ASP A  22     7172  10337  12286    123   -229   2293       C  
ATOM    193  O   ASP A  22      31.031 116.598   6.417  1.00 70.35           O  
ANISOU  193  O   ASP A  22     6356   9261  11114     18   -319   2336       O  
ATOM    194  CB  ASP A  22      31.950 118.787   4.485  1.00 91.08           C  
ANISOU  194  CB  ASP A  22     8561  12003  14043     74   -381   2590       C  
ATOM    195  CG  ASP A  22      31.154 119.980   4.986  1.00 96.49           C  
ANISOU  195  CG  ASP A  22     8913  12619  15129    -17   -326   2607       C  
ATOM    196  OD1 ASP A  22      31.489 120.534   6.057  1.00 99.05           O  
ANISOU  196  OD1 ASP A  22     9250  12907  15477     55   -162   2380       O  
ATOM    197  OD2 ASP A  22      30.173 120.352   4.309  1.00100.88           O  
ANISOU  197  OD2 ASP A  22     9438  13085  15805   -173   -436   2734       O  
ATOM    198  N   MET A  23      31.807 118.174   7.845  1.00 81.29           N  
ANISOU  198  N   MET A  23     7336  10688  12861    159    -87   2170       N  
ATOM    199  CA  MET A  23      30.999 117.730   8.975  1.00 86.47           C  
ANISOU  199  CA  MET A  23     8035  11259  13559     66    -22   2072       C  
ATOM    200  C   MET A  23      29.513 118.049   8.821  1.00 90.72           C  
ANISOU  200  C   MET A  23     8393  11682  14395   -155    -69   2181       C  
ATOM    201  O   MET A  23      28.735 117.684   9.710  1.00 88.50           O  
ANISOU  201  O   MET A  23     8149  11299  14177   -257     -3   2093       O  
ATOM    202  CB  MET A  23      31.529 118.345  10.273  1.00 89.84           C  
ANISOU  202  CB  MET A  23     8303  11712  14119    160    150   1900       C  
ATOM    203  CG  MET A  23      32.996 118.042  10.552  1.00 96.12           C  
ANISOU  203  CG  MET A  23     9270  12591  14659    388    192   1763       C  
ATOM    204  SD  MET A  23      33.317 117.449  12.228  1.00102.57           S  
ANISOU  204  SD  MET A  23    10266  13384  15323    458    308   1536       S  
ATOM    205  CE  MET A  23      33.272 118.966  13.175  1.00100.83           C  
ANISOU  205  CE  MET A  23     9599  13191  15520    458    484   1450       C  
ATOM    206  N   SER A  24      29.103 118.722   7.739  1.00 97.04           N  
ANISOU  206  N   SER A  24     9005  12475  15391   -238   -182   2361       N  
ATOM    207  CA  SER A  24      27.700 119.055   7.512  1.00 98.60           C  
ANISOU  207  CA  SER A  24     9155  12508  15799   -429   -251   2408       C  
ATOM    208  C   SER A  24      26.971 118.059   6.616  1.00 98.90           C  
ANISOU  208  C   SER A  24     9311  12506  15759   -543   -429   2572       C  
ATOM    209  O   SER A  24      25.738 117.993   6.670  1.00 99.22           O  
ANISOU  209  O   SER A  24     9282  12395  16023   -711   -479   2600       O  
ATOM    210  CB  SER A  24      27.574 120.457   6.901  1.00 98.05           C  
ANISOU  210  CB  SER A  24     9071  12377  15807   -424   -273   2396       C  
ATOM    211  OG  SER A  24      28.190 120.519   5.628  1.00 99.21           O  
ANISOU  211  OG  SER A  24     9209  12622  15866   -379   -389   2580       O  
ATOM    212  N   MET A  25      27.688 117.307   5.786  1.00 97.65           N  
ANISOU  212  N   MET A  25     9430  12446  15225   -443   -516   2619       N  
ATOM    213  CA  MET A  25      27.111 116.268   4.947  1.00 96.79           C  
ANISOU  213  CA  MET A  25     9575  12298  14902   -515   -667   2700       C  
ATOM    214  C   MET A  25      27.309 114.893   5.579  1.00 94.02           C  
ANISOU  214  C   MET A  25     9554  11950  14220   -449   -603   2552       C  
ATOM    215  O   MET A  25      28.173 114.696   6.435  1.00 92.03           O  
ANISOU  215  O   MET A  25     9387  11756  13823   -323   -476   2408       O  
ATOM    216  CB  MET A  25      27.740 116.283   3.553  1.00 98.80           C  
ANISOU  216  CB  MET A  25     9923  12660  14956   -476   -801   2848       C  
ATOM    217  CG  MET A  25      27.672 117.615   2.843  1.00107.04           C  
ANISOU  217  CG  MET A  25    10672  13712  16288   -527   -870   3010       C  
ATOM    218  SD  MET A  25      28.764 117.631   1.410  1.00110.59           S  
ANISOU  218  SD  MET A  25    11281  14300  16438   -450   -961   3133       S  
ATOM    219  CE  MET A  25      28.096 116.273   0.455  1.00111.12           C  
ANISOU  219  CE  MET A  25    11677  14344  16198   -556  -1141   3210       C  
ATOM    220  N   THR A  26      26.491 113.936   5.148  1.00 91.84           N  
ANISOU  220  N   THR A  26     9458  11602  13834   -533   -699   2587       N  
ATOM    221  CA  THR A  26      26.651 112.573   5.622  1.00 92.44           C  
ANISOU  221  CA  THR A  26     9843  11682  13596   -473   -647   2463       C  
ATOM    222  C   THR A  26      27.781 111.881   4.864  1.00 87.71           C  
ANISOU  222  C   THR A  26     9473  11232  12622   -361   -701   2478       C  
ATOM    223  O   THR A  26      28.242 112.349   3.820  1.00 92.34           O  
ANISOU  223  O   THR A  26    10010  11899  13178   -356   -792   2595       O  
ATOM    224  CB  THR A  26      25.356 111.779   5.460  1.00 98.46           C  
ANISOU  224  CB  THR A  26    10700  12307  14404   -593   -709   2476       C  
ATOM    225  OG1 THR A  26      25.154 111.471   4.076  1.00 97.73           O  
ANISOU  225  OG1 THR A  26    10674  12254  14204   -635   -887   2622       O  
ATOM    226  CG2 THR A  26      24.172 112.580   5.979  1.00103.96           C  
ANISOU  226  CG2 THR A  26    11140  12823  15537   -738   -678   2470       C  
ATOM    227  N   TYR A  27      28.227 110.741   5.400  1.00 78.46           N  
ANISOU  227  N   TYR A  27     8556  10083  11171   -281   -640   2352       N  
ATOM    228  CA  TYR A  27      29.262 109.977   4.715  1.00 77.01           C  
ANISOU  228  CA  TYR A  27     8585  10016  10657   -197   -686   2343       C  
ATOM    229  C   TYR A  27      28.770 109.439   3.380  1.00 80.42           C  
ANISOU  229  C   TYR A  27     9101  10472  10982   -290   -831   2472       C  
ATOM    230  O   TYR A  27      29.549 109.351   2.424  1.00 85.43           O  
ANISOU  230  O   TYR A  27     9811  11206  11442   -270   -891   2522       O  
ATOM    231  CB  TYR A  27      29.758 108.825   5.591  1.00 78.81           C  
ANISOU  231  CB  TYR A  27     9055  10247  10643   -108   -604   2184       C  
ATOM    232  CG  TYR A  27      30.706 109.238   6.690  1.00 69.85           C  
ANISOU  232  CG  TYR A  27     7899   9127   9512     19   -490   2050       C  
ATOM    233  CD1 TYR A  27      30.278 109.319   8.003  1.00 73.98           C  
ANISOU  233  CD1 TYR A  27     8402   9569  10140     18   -381   1950       C  
ATOM    234  CD2 TYR A  27      32.031 109.540   6.412  1.00 67.81           C  
ANISOU  234  CD2 TYR A  27     7651   8953   9160    135   -488   2010       C  
ATOM    235  CE1 TYR A  27      31.138 109.693   9.011  1.00 75.70           C  
ANISOU  235  CE1 TYR A  27     8607   9804  10353    132   -288   1825       C  
ATOM    236  CE2 TYR A  27      32.903 109.918   7.414  1.00 70.30           C  
ANISOU  236  CE2 TYR A  27     7943   9272   9495    264   -395   1875       C  
ATOM    237  CZ  TYR A  27      32.447 109.992   8.713  1.00 73.36           C  
ANISOU  237  CZ  TYR A  27     8310   9593   9972    263   -302   1788       C  
ATOM    238  OH  TYR A  27      33.296 110.364   9.726  1.00 73.75           O  
ANISOU  238  OH  TYR A  27     8342   9648  10032    388   -218   1652       O  
ATOM    239  N   GLY A  28      27.490 109.077   3.289  1.00 83.69           N  
ANISOU  239  N   GLY A  28     9507  10786  11504   -397   -883   2515       N  
ATOM    240  CA  GLY A  28      26.964 108.595   2.023  1.00 85.34           C  
ANISOU  240  CA  GLY A  28     9785  11015  11625   -484  -1032   2634       C  
ATOM    241  C   GLY A  28      26.971 109.653   0.941  1.00 81.67           C  
ANISOU  241  C   GLY A  28     9165  10585  11283   -551  -1158   2807       C  
ATOM    242  O   GLY A  28      27.215 109.348  -0.230  1.00 78.45           O  
ANISOU  242  O   GLY A  28     8858  10260  10689   -589  -1266   2898       O  
ATOM    243  N   GLN A  29      26.735 110.911   1.319  1.00 81.90           N  
ANISOU  243  N   GLN A  29     8943  10553  11622   -574  -1138   2851       N  
ATOM    244  CA  GLN A  29      26.733 112.014   0.370  1.00 85.64           C  
ANISOU  244  CA  GLN A  29     9245  11050  12246   -636  -1254   3023       C  
ATOM    245  C   GLN A  29      28.121 112.359  -0.154  1.00 85.85           C  
ANISOU  245  C   GLN A  29     9322  11218  12081   -547  -1222   3038       C  
ATOM    246  O   GLN A  29      28.220 113.111  -1.129  1.00 90.82           O  
ANISOU  246  O   GLN A  29     9868  11879  12761   -600  -1321   3189       O  
ATOM    247  CB  GLN A  29      26.095 113.244   1.021  1.00 92.08           C  
ANISOU  247  CB  GLN A  29     9746  11752  13486   -688  -1223   3050       C  
ATOM    248  CG  GLN A  29      24.648 113.028   1.437  1.00 99.98           C  
ANISOU  248  CG  GLN A  29    10676  12572  14741   -805  -1259   3031       C  
ATOM    249  CD  GLN A  29      24.056 114.221   2.156  1.00101.42           C  
ANISOU  249  CD  GLN A  29    10532  12629  15373   -877  -1207   3029       C  
ATOM    250  OE1 GLN A  29      24.560 115.340   2.044  1.00110.82           O  
ANISOU  250  OE1 GLN A  29    11511  13875  16720   -861  -1196   3098       O  
ATOM    251  NE2 GLN A  29      22.974 113.991   2.895  1.00 95.32           N  
ANISOU  251  NE2 GLN A  29     9707  11678  14831   -965  -1162   2938       N  
ATOM    252  N   GLN A  30      29.185 111.824   0.449  1.00 84.44           N  
ANISOU  252  N   GLN A  30     9283  11106  11694   -419  -1091   2881       N  
ATOM    253  CA  GLN A  30      30.557 112.120   0.044  1.00 75.50           C  
ANISOU  253  CA  GLN A  30     8200  10074  10412   -325  -1040   2852       C  
ATOM    254  C   GLN A  30      31.308 110.903  -0.468  1.00 71.97           C  
ANISOU  254  C   GLN A  30     8038   9700   9609   -303  -1044   2777       C  
ATOM    255  O   GLN A  30      32.095 111.025  -1.411  1.00 69.66           O  
ANISOU  255  O   GLN A  30     7819   9473   9177   -310  -1066   2813       O  
ATOM    256  CB  GLN A  30      31.341 112.746   1.208  1.00 67.57           C  
ANISOU  256  CB  GLN A  30     7072   9067   9533   -182   -881   2711       C  
ATOM    257  CG  GLN A  30      30.658 113.959   1.802  1.00 67.03           C  
ANISOU  257  CG  GLN A  30     6692   8935   9843   -212   -850   2762       C  
ATOM    258  CD  GLN A  30      31.464 114.630   2.900  1.00 65.90           C  
ANISOU  258  CD  GLN A  30     6409   8805   9826    -70   -687   2619       C  
ATOM    259  OE1 GLN A  30      32.516 115.207   2.641  1.00 64.21           O  
ANISOU  259  OE1 GLN A  30     6146   8651   9600     35   -634   2594       O  
ATOM    260  NE2 GLN A  30      30.955 114.589   4.126  1.00 70.67           N  
ANISOU  260  NE2 GLN A  30     6942   9344  10564    -70   -602   2518       N  
ATOM    261  N   PHE A  31      31.079 109.725   0.123  1.00 72.02           N  
ANISOU  261  N   PHE A  31     8202   9688   9475   -287  -1015   2667       N  
ATOM    262  CA  PHE A  31      31.769 108.503  -0.272  1.00 76.08           C  
ANISOU  262  CA  PHE A  31     8958  10264   9683   -274  -1011   2581       C  
ATOM    263  C   PHE A  31      30.864 107.463  -0.908  1.00 78.59           C  
ANISOU  263  C   PHE A  31     9396  10589   9874   -385  -1108   2640       C  
ATOM    264  O   PHE A  31      31.367 106.591  -1.622  1.00 78.24           O  
ANISOU  264  O   PHE A  31     9518  10617   9594   -418  -1128   2610       O  
ATOM    265  CB  PHE A  31      32.443 107.843   0.946  1.00 76.01           C  
ANISOU  265  CB  PHE A  31     9050  10237   9595   -147   -893   2387       C  
ATOM    266  CG  PHE A  31      33.510 108.681   1.589  1.00 72.68           C  
ANISOU  266  CG  PHE A  31     8542   9811   9264    -15   -796   2291       C  
ATOM    267  CD1 PHE A  31      34.248 109.579   0.842  1.00 70.48           C  
ANISOU  267  CD1 PHE A  31     8181   9568   9031      2   -794   2336       C  
ATOM    268  CD2 PHE A  31      33.765 108.570   2.948  1.00 74.03           C  
ANISOU  268  CD2 PHE A  31     8717   9936   9476     95   -702   2149       C  
ATOM    269  CE1 PHE A  31      35.220 110.349   1.430  1.00 77.31           C  
ANISOU  269  CE1 PHE A  31     8952  10420  10003    139   -695   2232       C  
ATOM    270  CE2 PHE A  31      34.739 109.338   3.546  1.00 77.68           C  
ANISOU  270  CE2 PHE A  31     9092  10392  10031    227   -618   2049       C  
ATOM    271  CZ  PHE A  31      35.470 110.229   2.785  1.00 81.89           C  
ANISOU  271  CZ  PHE A  31     9526  10959  10631    256   -611   2085       C  
ATOM    272  N   GLY A  32      29.556 107.532  -0.681  1.00 84.37           N  
ANISOU  272  N   GLY A  32    10038  11241  10777   -448  -1160   2707       N  
ATOM    273  CA  GLY A  32      28.688 106.430  -1.008  1.00 91.01           C  
ANISOU  273  CA  GLY A  32    10990  12067  11522   -517  -1221   2714       C  
ATOM    274  C   GLY A  32      28.554 105.511   0.187  1.00 91.23           C  
ANISOU  274  C   GLY A  32    11108  12043  11513   -441  -1107   2558       C  
ATOM    275  O   GLY A  32      28.663 105.943   1.338  1.00 91.58           O  
ANISOU  275  O   GLY A  32    11088  12025  11685   -369  -1007   2479       O  
ATOM    276  N   PRO A  33      28.300 104.226  -0.059  1.00 91.66           N  
ANISOU  276  N   PRO A  33    11312  12122  11393   -459  -1115   2511       N  
ATOM    277  CA  PRO A  33      28.224 103.262   1.052  1.00 92.09           C  
ANISOU  277  CA  PRO A  33    11472  12128  11391   -385  -1003   2366       C  
ATOM    278  C   PRO A  33      29.529 103.225   1.835  1.00 88.36           C  
ANISOU  278  C   PRO A  33    11071  11692  10807   -274   -907   2245       C  
ATOM    279  O   PRO A  33      30.594 102.923   1.289  1.00 91.80           O  
ANISOU  279  O   PRO A  33    11590  12220  11071   -258   -919   2214       O  
ATOM    280  CB  PRO A  33      27.939 101.932   0.344  1.00 91.27           C  
ANISOU  280  CB  PRO A  33    11495  12079  11104   -427  -1040   2352       C  
ATOM    281  CG  PRO A  33      27.337 102.318  -0.963  1.00 88.91           C  
ANISOU  281  CG  PRO A  33    11126  11810  10845   -539  -1183   2501       C  
ATOM    282  CD  PRO A  33      28.008 103.598  -1.357  1.00 89.41           C  
ANISOU  282  CD  PRO A  33    11097  11910  10966   -554  -1226   2590       C  
ATOM    283  N   THR A  34      29.438 103.545   3.126  1.00 80.89           N  
ANISOU  283  N   THR A  34    10097  10662   9977   -206   -812   2167       N  
ATOM    284  CA  THR A  34      30.602 103.675   3.994  1.00 73.51           C  
ANISOU  284  CA  THR A  34     9214   9741   8976    -92   -735   2051       C  
ATOM    285  C   THR A  34      30.429 102.804   5.229  1.00 71.71           C  
ANISOU  285  C   THR A  34     9121   9442   8683    -35   -645   1929       C  
ATOM    286  O   THR A  34      29.345 102.755   5.820  1.00 71.52           O  
ANISOU  286  O   THR A  34     9075   9320   8779    -74   -597   1927       O  
ATOM    287  CB  THR A  34      30.810 105.128   4.420  1.00 71.98           C  
ANISOU  287  CB  THR A  34     8837   9520   8990    -59   -703   2073       C  
ATOM    288  OG1 THR A  34      30.842 105.966   3.260  1.00 76.66           O  
ANISOU  288  OG1 THR A  34     9301  10166   9660   -120   -787   2204       O  
ATOM    289  CG2 THR A  34      32.124 105.275   5.166  1.00 69.73           C  
ANISOU  289  CG2 THR A  34     8604   9256   8634     72   -638   1945       C  
ATOM    290  N   TYR A  35      31.504 102.122   5.617  1.00 69.39           N  
ANISOU  290  N   TYR A  35     8971   9182   8212     49   -623   1821       N  
ATOM    291  CA  TYR A  35      31.488 101.230   6.767  1.00 70.51           C  
ANISOU  291  CA  TYR A  35     9269   9261   8261    106   -553   1710       C  
ATOM    292  C   TYR A  35      32.613 101.591   7.727  1.00 70.88           C  
ANISOU  292  C   TYR A  35     9361   9292   8279    220   -520   1603       C  
ATOM    293  O   TYR A  35      33.753 101.820   7.308  1.00 69.23           O  
ANISOU  293  O   TYR A  35     9146   9135   8025    273   -562   1569       O  
ATOM    294  CB  TYR A  35      31.624  99.772   6.327  1.00 75.00           C  
ANISOU  294  CB  TYR A  35     9987   9871   8639     93   -578   1678       C  
ATOM    295  CG  TYR A  35      30.541  99.306   5.375  1.00 79.76           C  
ANISOU  295  CG  TYR A  35    10550  10495   9262     -7   -611   1767       C  
ATOM    296  CD1 TYR A  35      29.362  98.744   5.853  1.00 84.19           C  
ANISOU  296  CD1 TYR A  35    11146  10969   9875    -30   -551   1757       C  
ATOM    297  CD2 TYR A  35      30.701  99.418   3.996  1.00 78.35           C  
ANISOU  297  CD2 TYR A  35    10305  10412   9051    -79   -698   1849       C  
ATOM    298  CE1 TYR A  35      28.369  98.307   4.984  1.00 86.38           C  
ANISOU  298  CE1 TYR A  35    11379  11251  10189   -106   -586   1821       C  
ATOM    299  CE2 TYR A  35      29.715  98.984   3.118  1.00 79.49           C  
ANISOU  299  CE2 TYR A  35    10418  10577   9209   -167   -742   1926       C  
ATOM    300  CZ  TYR A  35      28.551  98.428   3.618  1.00 80.65           C  
ANISOU  300  CZ  TYR A  35    10586  10634   9426   -172   -690   1908       C  
ATOM    301  OH  TYR A  35      27.569  97.995   2.756  1.00 73.03           O  
ANISOU  301  OH  TYR A  35     9581   9675   8495   -244   -737   1968       O  
ATOM    302  N   LEU A  36      32.286 101.626   9.017  1.00 70.53           N  
ANISOU  302  N   LEU A  36     9370   9162   8265    255   -441   1537       N  
ATOM    303  CA  LEU A  36      33.247 101.881  10.090  1.00 64.83           C  
ANISOU  303  CA  LEU A  36     8714   8413   7505    365   -413   1425       C  
ATOM    304  C   LEU A  36      33.199 100.695  11.050  1.00 62.81           C  
ANISOU  304  C   LEU A  36     8688   8093   7085    394   -383   1343       C  
ATOM    305  O   LEU A  36      32.266 100.575  11.849  1.00 63.40           O  
ANISOU  305  O   LEU A  36     8811   8088   7191    352   -298   1335       O  
ATOM    306  CB  LEU A  36      32.931 103.194  10.803  1.00 61.27           C  
ANISOU  306  CB  LEU A  36     8104   7924   7253    369   -342   1424       C  
ATOM    307  CG  LEU A  36      33.761 103.475  12.056  1.00 59.05           C  
ANISOU  307  CG  LEU A  36     7890   7608   6939    478   -302   1300       C  
ATOM    308  CD1 LEU A  36      35.246 103.480  11.734  1.00 53.42           C  
ANISOU  308  CD1 LEU A  36     7206   6941   6149    598   -379   1231       C  
ATOM    309  CD2 LEU A  36      33.347 104.794  12.675  1.00 61.38           C  
ANISOU  309  CD2 LEU A  36     7987   7878   7456    458   -215   1299       C  
ATOM    310  N   ASP A  37      34.212  99.828  10.978  1.00 65.86           N  
ANISOU  310  N   ASP A  37     9213   8500   7312    457   -449   1276       N  
ATOM    311  CA  ASP A  37      34.284  98.616  11.802  1.00 73.50           C  
ANISOU  311  CA  ASP A  37    10400   9409   8118    486   -442   1208       C  
ATOM    312  C   ASP A  37      33.080  97.706  11.561  1.00 78.59           C  
ANISOU  312  C   ASP A  37    11093  10037   8729    400   -390   1263       C  
ATOM    313  O   ASP A  37      32.472  97.181  12.495  1.00 79.86           O  
ANISOU  313  O   ASP A  37    11389  10115   8841    396   -315   1232       O  
ATOM    314  CB  ASP A  37      34.412  98.958  13.290  1.00 69.86           C  
ANISOU  314  CB  ASP A  37    10040   8864   7641    548   -391   1130       C  
ATOM    315  CG  ASP A  37      35.686  99.703  13.608  1.00 73.74           C  
ANISOU  315  CG  ASP A  37    10498   9362   8159    657   -449   1049       C  
ATOM    316  OD1 ASP A  37      36.743  99.324  13.057  1.00 76.02           O  
ANISOU  316  OD1 ASP A  37    10811   9672   8399    710   -543   1004       O  
ATOM    317  OD2 ASP A  37      35.626 100.675  14.394  1.00 75.14           O  
ANISOU  317  OD2 ASP A  37    10611   9512   8426    686   -392   1019       O  
ATOM    318  N   GLY A  38      32.741  97.516  10.283  1.00 80.83           N  
ANISOU  318  N   GLY A  38    11272  10395   9043    332   -425   1338       N  
ATOM    319  CA  GLY A  38      31.646  96.652   9.896  1.00 78.90           C  
ANISOU  319  CA  GLY A  38    11049  10142   8787    264   -384   1381       C  
ATOM    320  C   GLY A  38      30.278  97.292   9.919  1.00 81.34           C  
ANISOU  320  C   GLY A  38    11254  10385   9265    193   -313   1441       C  
ATOM    321  O   GLY A  38      29.370  96.802   9.236  1.00 86.76           O  
ANISOU  321  O   GLY A  38    11902  11072   9991    132   -304   1487       O  
ATOM    322  N   ALA A  39      30.094  98.369  10.679  1.00 77.07           N  
ANISOU  322  N   ALA A  39    10655   9780   8850    193   -263   1430       N  
ATOM    323  CA  ALA A  39      28.798  99.014  10.815  1.00 72.74           C  
ANISOU  323  CA  ALA A  39     9996   9136   8507    108   -188   1465       C  
ATOM    324  C   ALA A  39      28.573 100.013   9.691  1.00 78.76           C  
ANISOU  324  C   ALA A  39    10532   9956   9438     49   -267   1571       C  
ATOM    325  O   ALA A  39      29.472 100.778   9.331  1.00 79.30           O  
ANISOU  325  O   ALA A  39    10509  10109   9513     84   -331   1599       O  
ATOM    326  CB  ALA A  39      28.684  99.725  12.165  1.00 67.46           C  
ANISOU  326  CB  ALA A  39     9348   8367   7917    111    -86   1395       C  
ATOM    327  N   ASP A  40      27.362  99.999   9.143  1.00 82.05           N  
ANISOU  327  N   ASP A  40    10863  10311  10000    -39   -263   1627       N  
ATOM    328  CA  ASP A  40      26.998 100.926   8.081  1.00 78.11           C  
ANISOU  328  CA  ASP A  40    10158   9845   9674   -109   -355   1741       C  
ATOM    329  C   ASP A  40      26.850 102.327   8.662  1.00 70.66           C  
ANISOU  329  C   ASP A  40     9048   8838   8961   -141   -315   1749       C  
ATOM    330  O   ASP A  40      26.001 102.561   9.527  1.00 71.45           O  
ANISOU  330  O   ASP A  40     9127   8795   9226   -194   -211   1693       O  
ATOM    331  CB  ASP A  40      25.704 100.468   7.414  1.00 86.90           C  
ANISOU  331  CB  ASP A  40    11235  10884  10899   -190   -374   1784       C  
ATOM    332  CG  ASP A  40      25.455 101.147   6.082  1.00 93.27           C  
ANISOU  332  CG  ASP A  40    11874  11749  11817   -260   -514   1918       C  
ATOM    333  OD1 ASP A  40      26.007 102.242   5.846  1.00 95.97           O  
ANISOU  333  OD1 ASP A  40    12089  12146  12231   -266   -566   1983       O  
ATOM    334  OD2 ASP A  40      24.701 100.580   5.266  1.00 96.40           O  
ANISOU  334  OD2 ASP A  40    12265  12131  12230   -306   -571   1959       O  
ATOM    335  N   VAL A  41      27.686 103.252   8.195  1.00 69.41           N  
ANISOU  335  N   VAL A  41     8764   8780   8829   -113   -383   1807       N  
ATOM    336  CA  VAL A  41      27.675 104.639   8.644  1.00 74.57           C  
ANISOU  336  CA  VAL A  41     9218   9400   9714   -133   -347   1819       C  
ATOM    337  C   VAL A  41      27.276 105.587   7.510  1.00 79.26           C  
ANISOU  337  C   VAL A  41     9590  10018  10508   -212   -451   1961       C  
ATOM    338  O   VAL A  41      27.603 106.774   7.544  1.00 72.95           O  
ANISOU  338  O   VAL A  41     8602   9242   9873   -209   -451   1996       O  
ATOM    339  CB  VAL A  41      29.032 105.036   9.249  1.00 75.77           C  
ANISOU  339  CB  VAL A  41     9395   9632   9762    -15   -317   1747       C  
ATOM    340  CG1 VAL A  41      29.330 104.199  10.485  1.00 77.87           C  
ANISOU  340  CG1 VAL A  41     9880   9851   9856     50   -229   1614       C  
ATOM    341  CG2 VAL A  41      30.139 104.868   8.216  1.00 67.56           C  
ANISOU  341  CG2 VAL A  41     8388   8725   8555     51   -420   1789       C  
ATOM    342  N   THR A  42      26.554 105.073   6.509  1.00 83.98           N  
ANISOU  342  N   THR A  42    10204  10606  11098   -282   -544   2043       N  
ATOM    343  CA  THR A  42      26.180 105.886   5.357  1.00 85.46           C  
ANISOU  343  CA  THR A  42    10212  10814  11446   -363   -672   2192       C  
ATOM    344  C   THR A  42      25.281 107.051   5.753  1.00 85.11           C  
ANISOU  344  C   THR A  42     9928  10635  11773   -455   -650   2222       C  
ATOM    345  O   THR A  42      25.487 108.183   5.301  1.00 85.45           O  
ANISOU  345  O   THR A  42     9775  10715  11979   -481   -710   2318       O  
ATOM    346  CB  THR A  42      25.484 105.014   4.308  1.00 84.71           C  
ANISOU  346  CB  THR A  42    10196  10719  11270   -422   -777   2257       C  
ATOM    347  OG1 THR A  42      26.373 103.980   3.867  1.00 85.42           O  
ANISOU  347  OG1 THR A  42    10474  10944  11039   -356   -793   2228       O  
ATOM    348  CG2 THR A  42      25.061 105.846   3.119  1.00 80.13           C  
ANISOU  348  CG2 THR A  42     9452  10148  10844   -514   -931   2419       C  
ATOM    349  N   LYS A  43      24.289 106.801   6.604  1.00 85.99           N  
ANISOU  349  N   LYS A  43    10047  10581  12043   -513   -556   2133       N  
ATOM    350  CA  LYS A  43      23.259 107.789   6.894  1.00 95.28           C  
ANISOU  350  CA  LYS A  43    10990  11594  13619   -637   -538   2147       C  
ATOM    351  C   LYS A  43      23.602 108.688   8.078  1.00 92.11           C  
ANISOU  351  C   LYS A  43    10459  11166  13371   -633   -396   2060       C  
ATOM    352  O   LYS A  43      22.704 109.328   8.634  1.00 95.83           O  
ANISOU  352  O   LYS A  43    10759  11474  14179   -751   -328   2019       O  
ATOM    353  CB  LYS A  43      21.923 107.086   7.142  1.00106.23           C  
ANISOU  353  CB  LYS A  43    12438  12778  15145   -723   -499   2074       C  
ATOM    354  CG  LYS A  43      21.432 106.258   5.962  1.00113.71           C  
ANISOU  354  CG  LYS A  43    13475  13736  15992   -731   -642   2151       C  
ATOM    355  CD  LYS A  43      20.151 105.510   6.302  1.00118.87           C  
ANISOU  355  CD  LYS A  43    14195  14173  16797   -790   -577   2048       C  
ATOM    356  CE  LYS A  43      19.673 104.669   5.132  1.00121.51           C  
ANISOU  356  CE  LYS A  43    14605  14525  17037   -785   -717   2112       C  
ATOM    357  NZ  LYS A  43      18.436 103.916   5.473  1.00121.61           N  
ANISOU  357  NZ  LYS A  43    14677  14313  17215   -822   -639   1990       N  
ATOM    358  N   ILE A  44      24.874 108.774   8.464  1.00 87.75           N  
ANISOU  358  N   ILE A  44     9973  10763  12606   -508   -348   2022       N  
ATOM    359  CA  ILE A  44      25.273 109.633   9.570  1.00 85.73           C  
ANISOU  359  CA  ILE A  44     9589  10500  12484   -491   -216   1933       C  
ATOM    360  C   ILE A  44      26.364 110.580   9.094  1.00 82.20           C  
ANISOU  360  C   ILE A  44     8985  10207  12039   -403   -267   2004       C  
ATOM    361  O   ILE A  44      26.998 110.369   8.057  1.00 86.14           O  
ANISOU  361  O   ILE A  44     9548  10822  12359   -340   -382   2095       O  
ATOM    362  CB  ILE A  44      25.748 108.835  10.806  1.00 85.29           C  
ANISOU  362  CB  ILE A  44     9775  10440  12191   -411    -81   1774       C  
ATOM    363  CG1 ILE A  44      27.161 108.308  10.593  1.00 88.43           C  
ANISOU  363  CG1 ILE A  44    10350  11006  12245   -244   -131   1764       C  
ATOM    364  CG2 ILE A  44      24.798 107.685  11.118  1.00 84.83           C  
ANISOU  364  CG2 ILE A  44     9923  10243  12065   -472    -32   1709       C  
ATOM    365  CD1 ILE A  44      27.749 107.696  11.830  1.00 91.70           C  
ANISOU  365  CD1 ILE A  44    10977  11415  12450   -160    -26   1619       C  
ATOM    366  N   LYS A  45      26.565 111.642   9.863  1.00 76.78           N  
ANISOU  366  N   LYS A  45     8085   9515  11573   -406   -166   1952       N  
ATOM    367  CA  LYS A  45      27.524 112.697   9.580  1.00 81.01           C  
ANISOU  367  CA  LYS A  45     8422  10174  12182   -319   -176   1996       C  
ATOM    368  C   LYS A  45      28.809 112.494  10.382  1.00 84.01           C  
ANISOU  368  C   LYS A  45     8938  10651  12332   -149    -90   1863       C  
ATOM    369  O   LYS A  45      28.791 111.872  11.449  1.00 86.50           O  
ANISOU  369  O   LYS A  45     9426  10918  12524   -133      2   1733       O  
ATOM    370  CB  LYS A  45      26.917 114.063   9.913  1.00 83.08           C  
ANISOU  370  CB  LYS A  45     8315  10368  12882   -429   -114   2016       C  
ATOM    371  CG  LYS A  45      25.647 114.375   9.126  1.00 86.94           C  
ANISOU  371  CG  LYS A  45     8641  10734  13658   -604   -221   2145       C  
ATOM    372  CD  LYS A  45      25.151 115.785   9.409  1.00 91.42           C  
ANISOU  372  CD  LYS A  45     8808  11234  14694   -719   -169   2167       C  
ATOM    373  CE  LYS A  45      23.855 116.081   8.665  1.00 95.36           C  
ANISOU  373  CE  LYS A  45     9143  11576  15515   -903   -296   2286       C  
ATOM    374  NZ  LYS A  45      23.440 117.507   8.819  1.00 96.32           N  
ANISOU  374  NZ  LYS A  45     9009  11627  15961   -950   -265   2246       N  
ATOM    375  N   PRO A  46      29.944 112.998   9.889  1.00 81.57           N  
ANISOU  375  N   PRO A  46     8565  10464  11964    -19   -122   1887       N  
ATOM    376  CA  PRO A  46      31.213 112.800  10.605  1.00 79.61           C  
ANISOU  376  CA  PRO A  46     8444  10285  11521    154    -59   1746       C  
ATOM    377  C   PRO A  46      31.232 113.537  11.936  1.00 76.15           C  
ANISOU  377  C   PRO A  46     7850   9820  11265    166     88   1621       C  
ATOM    378  O   PRO A  46      30.863 114.708  12.021  1.00 76.66           O  
ANISOU  378  O   PRO A  46     7593   9877  11656    104    146   1652       O  
ATOM    379  CB  PRO A  46      32.261 113.365   9.638  1.00 82.05           C  
ANISOU  379  CB  PRO A  46     8664  10697  11815    267   -116   1801       C  
ATOM    380  CG  PRO A  46      31.608 113.320   8.302  1.00 84.48           C  
ANISOU  380  CG  PRO A  46     8944  11005  12150    152   -239   1979       C  
ATOM    381  CD  PRO A  46      30.158 113.589   8.558  1.00 83.71           C  
ANISOU  381  CD  PRO A  46     8700  10802  12305    -21   -231   2039       C  
ATOM    382  N   HIS A  47      31.681 112.836  12.970  1.00 77.69           N  
ANISOU  382  N   HIS A  47     8271  10000  11248    240    144   1478       N  
ATOM    383  CA  HIS A  47      31.860 113.376  14.306  1.00 80.14           C  
ANISOU  383  CA  HIS A  47     8497  10296  11659    265    280   1338       C  
ATOM    384  C   HIS A  47      33.349 113.521  14.602  1.00 81.78           C  
ANISOU  384  C   HIS A  47     8752  10589  11732    480    278   1230       C  
ATOM    385  O   HIS A  47      34.195 112.938  13.920  1.00 83.79           O  
ANISOU  385  O   HIS A  47     9174  10884  11778    596    178   1240       O  
ATOM    386  CB  HIS A  47      31.189 112.461  15.338  1.00 80.03           C  
ANISOU  386  CB  HIS A  47     8730  10177  11500    175    343   1251       C  
ATOM    387  CG  HIS A  47      31.136 113.032  16.717  1.00 78.93           C  
ANISOU  387  CG  HIS A  47     8507  10007  11477    145    495   1113       C  
ATOM    388  ND1 HIS A  47      31.951 112.589  17.735  1.00 78.67           N  
ANISOU  388  ND1 HIS A  47     8692   9989  11209    260    524    976       N  
ATOM    389  CD2 HIS A  47      30.347 113.992  17.254  1.00 80.50           C  
ANISOU  389  CD2 HIS A  47     8429  10153  12006     -2    623   1086       C  
ATOM    390  CE1 HIS A  47      31.680 113.267  18.836  1.00 82.92           C  
ANISOU  390  CE1 HIS A  47     9100  10498  11907    188    669    872       C  
ATOM    391  NE2 HIS A  47      30.708 114.122  18.572  1.00 81.14           N  
ANISOU  391  NE2 HIS A  47     8566  10232  12033     23    741    930       N  
ATOM    392  N   ASN A  48      33.672 114.307  15.633  1.00 80.80           N  
ANISOU  392  N   ASN A  48     8472  10480  11747    528    393   1110       N  
ATOM    393  CA  ASN A  48      35.072 114.461  16.018  1.00 76.37           C  
ANISOU  393  CA  ASN A  48     7953   9980  11085    745    391    982       C  
ATOM    394  C   ASN A  48      35.708 113.142  16.423  1.00 67.46           C  
ANISOU  394  C   ASN A  48     7226   8816   9591    835    309    898       C  
ATOM    395  O   ASN A  48      36.937 113.028  16.394  1.00 59.70           O  
ANISOU  395  O   ASN A  48     6326   7857   8500   1019    255    808       O  
ATOM    396  CB  ASN A  48      35.230 115.465  17.158  1.00 80.76           C  
ANISOU  396  CB  ASN A  48     8279  10557  11847    774    534    855       C  
ATOM    397  CG  ASN A  48      35.196 116.887  16.674  1.00 85.66           C  
ANISOU  397  CG  ASN A  48     8465  11244  12840    776    605    906       C  
ATOM    398  OD1 ASN A  48      35.878 117.233  15.710  1.00 85.66           O  
ANISOU  398  OD1 ASN A  48     8371  11297  12881    894    549    959       O  
ATOM    399  ND2 ASN A  48      34.423 117.729  17.348  1.00 91.54           N  
ANISOU  399  ND2 ASN A  48     8934  11976  13870    641    737    883       N  
ATOM    400  N   SER A  49      34.906 112.150  16.806  1.00 66.01           N  
ANISOU  400  N   SER A  49     7286   8559   9237    712    300    916       N  
ATOM    401  CA  SER A  49      35.444 110.861  17.205  1.00 62.71           C  
ANISOU  401  CA  SER A  49     7241   8102   8485    785    219    848       C  
ATOM    402  C   SER A  49      35.902 110.039  16.013  1.00 59.74           C  
ANISOU  402  C   SER A  49     7008   7744   7946    834     84    921       C  
ATOM    403  O   SER A  49      36.539 108.999  16.201  1.00 65.27           O  
ANISOU  403  O   SER A  49     7985   8415   8399    910      1    860       O  
ATOM    404  CB  SER A  49      34.387 110.087  17.996  1.00 70.36           C  
ANISOU  404  CB  SER A  49     8414   8980   9342    632    276    843       C  
ATOM    405  OG  SER A  49      33.239 109.828  17.196  1.00 75.91           O  
ANISOU  405  OG  SER A  49     9075   9647  10122    476    273    973       O  
ATOM    406  N   HIS A  50      35.602 110.485  14.800  1.00 58.64           N  
ANISOU  406  N   HIS A  50     6684   7648   7946    783     57   1046       N  
ATOM    407  CA  HIS A  50      36.047 109.812  13.593  1.00 61.15           C  
ANISOU  407  CA  HIS A  50     7116   7993   8124    811    -58   1111       C  
ATOM    408  C   HIS A  50      37.398 110.313  13.102  1.00 62.72           C  
ANISOU  408  C   HIS A  50     7241   8234   8357    974    -90   1046       C  
ATOM    409  O   HIS A  50      37.955 109.730  12.168  1.00 61.06           O  
ANISOU  409  O   HIS A  50     7144   8032   8024    999   -173   1065       O  
ATOM    410  CB  HIS A  50      34.995 109.979  12.495  1.00 60.93           C  
ANISOU  410  CB  HIS A  50     6961   7982   8208    658    -81   1283       C  
ATOM    411  CG  HIS A  50      33.669 109.371  12.833  1.00 65.27           C  
ANISOU  411  CG  HIS A  50     7598   8462   8738    503    -55   1332       C  
ATOM    412  ND1 HIS A  50      32.509 109.699  12.166  1.00 64.78           N  
ANISOU  412  ND1 HIS A  50     7384   8378   8852    353    -60   1462       N  
ATOM    413  CD2 HIS A  50      33.325 108.431  13.745  1.00 66.25           C  
ANISOU  413  CD2 HIS A  50     7956   8517   8699    476    -24   1262       C  
ATOM    414  CE1 HIS A  50      31.504 108.999  12.662  1.00 66.54           C  
ANISOU  414  CE1 HIS A  50     7734   8511   9037    246    -22   1454       C  
ATOM    415  NE2 HIS A  50      31.973 108.219  13.619  1.00 67.26           N  
ANISOU  415  NE2 HIS A  50     8064   8577   8914    316      9   1336       N  
ATOM    416  N   GLU A  51      37.946 111.352  13.733  1.00 65.81           N  
ANISOU  416  N   GLU A  51     7443   8640   8921   1084    -13    952       N  
ATOM    417  CA  GLU A  51      39.223 111.943  13.348  1.00 63.36           C  
ANISOU  417  CA  GLU A  51     7036   8348   8689   1256    -18    864       C  
ATOM    418  C   GLU A  51      40.322 110.893  13.247  1.00 57.02           C  
ANISOU  418  C   GLU A  51     6513   7489   7664   1364   -119    751       C  
ATOM    419  O   GLU A  51      40.756 110.340  14.260  1.00 58.31           O  
ANISOU  419  O   GLU A  51     6855   7597   7703   1439   -148    626       O  
ATOM    420  CB  GLU A  51      39.615 113.019  14.363  1.00 73.41           C  
ANISOU  420  CB  GLU A  51     8099   9634  10158   1372     87    742       C  
ATOM    421  CG  GLU A  51      40.964 113.669  14.131  1.00 83.28           C  
ANISOU  421  CG  GLU A  51     9238  10884  11520   1579    102    614       C  
ATOM    422  CD  GLU A  51      40.889 114.843  13.182  1.00 96.84           C  
ANISOU  422  CD  GLU A  51    10637  12661  13496   1578    172    708       C  
ATOM    423  OE1 GLU A  51      40.356 114.676  12.065  1.00102.45           O  
ANISOU  423  OE1 GLU A  51    11352  13393  14180   1453    126    868       O  
ATOM    424  OE2 GLU A  51      41.361 115.938  13.555  1.00100.72           O  
ANISOU  424  OE2 GLU A  51    10869  13180  14218   1703    272    621       O  
ATOM    425  N   GLY A  52      40.772 110.604  12.029  1.00 55.20           N  
ANISOU  425  N   GLY A  52     6325   7261   7388   1359   -176    791       N  
ATOM    426  CA  GLY A  52      41.869 109.684  11.823  1.00 55.25           C  
ANISOU  426  CA  GLY A  52     6557   7196   7239   1443   -264    669       C  
ATOM    427  C   GLY A  52      41.488 108.224  11.712  1.00 61.11           C  
ANISOU  427  C   GLY A  52     7569   7915   7737   1333   -355    711       C  
ATOM    428  O   GLY A  52      42.377 107.384  11.518  1.00 59.83           O  
ANISOU  428  O   GLY A  52     7584   7685   7462   1382   -434    609       O  
ATOM    429  N   LYS A  53      40.206 107.888  11.824  1.00 65.48           N  
ANISOU  429  N   LYS A  53     8145   8507   8228   1186   -343    845       N  
ATOM    430  CA  LYS A  53      39.810 106.495  11.717  1.00 65.70           C  
ANISOU  430  CA  LYS A  53     8409   8514   8039   1093   -414    881       C  
ATOM    431  C   LYS A  53      39.744 106.070  10.253  1.00 59.05           C  
ANISOU  431  C   LYS A  53     7575   7714   7147    995   -460    975       C  
ATOM    432  O   LYS A  53      39.802 106.890   9.335  1.00 62.04           O  
ANISOU  432  O   LYS A  53     7787   8139   7648    976   -437   1040       O  
ATOM    433  CB  LYS A  53      38.470 106.252  12.406  1.00 69.89           C  
ANISOU  433  CB  LYS A  53     8973   9048   8536    980   -367    965       C  
ATOM    434  CG  LYS A  53      38.524 106.372  13.920  1.00 79.40           C  
ANISOU  434  CG  LYS A  53    10244  10200   9724   1046   -324    861       C  
ATOM    435  CD  LYS A  53      37.291 105.748  14.559  1.00 90.57           C  
ANISOU  435  CD  LYS A  53    11778  11583  11050    919   -279    919       C  
ATOM    436  CE  LYS A  53      37.297 105.915  16.071  1.00 96.38           C  
ANISOU  436  CE  LYS A  53    12595  12265  11758    958   -221    817       C  
ATOM    437  NZ  LYS A  53      38.538 105.362  16.677  1.00 99.22           N  
ANISOU  437  NZ  LYS A  53    13152  12578  11971   1103   -313    683       N  
ATOM    438  N   THR A  54      39.648 104.759  10.049  1.00 55.94           N  
ANISOU  438  N   THR A  54     7381   7304   6570    930   -524    977       N  
ATOM    439  CA  THR A  54      39.665 104.142   8.731  1.00 55.93           C  
ANISOU  439  CA  THR A  54     7416   7343   6492    828   -571   1040       C  
ATOM    440  C   THR A  54      38.272 103.634   8.385  1.00 59.42           C  
ANISOU  440  C   THR A  54     7869   7836   6871    682   -569   1190       C  
ATOM    441  O   THR A  54      37.668 102.890   9.164  1.00 65.94           O  
ANISOU  441  O   THR A  54     8813   8632   7609    663   -563   1186       O  
ATOM    442  CB  THR A  54      40.666 102.992   8.695  1.00 55.90           C  
ANISOU  442  CB  THR A  54     7600   7277   6361    858   -641    910       C  
ATOM    443  OG1 THR A  54      41.976 103.501   8.966  1.00 62.85           O  
ANISOU  443  OG1 THR A  54     8463   8081   7337    999   -648    751       O  
ATOM    444  CG2 THR A  54      40.647 102.308   7.338  1.00 49.17           C  
ANISOU  444  CG2 THR A  54     6777   6473   5432    728   -673    964       C  
ATOM    445  N   PHE A  55      37.768 104.033   7.220  1.00 60.98           N  
ANISOU  445  N   PHE A  55     7953   8100   7118    582   -576   1318       N  
ATOM    446  CA  PHE A  55      36.432 103.674   6.765  1.00 61.48           C  
ANISOU  446  CA  PHE A  55     8001   8199   7158    448   -587   1458       C  
ATOM    447  C   PHE A  55      36.524 102.820   5.514  1.00 62.52           C  
ANISOU  447  C   PHE A  55     8208   8386   7159    351   -646   1498       C  
ATOM    448  O   PHE A  55      37.373 103.058   4.651  1.00 64.62           O  
ANISOU  448  O   PHE A  55     8457   8679   7417    345   -666   1477       O  
ATOM    449  CB  PHE A  55      35.590 104.912   6.475  1.00 58.37           C  
ANISOU  449  CB  PHE A  55     7394   7827   6957    395   -564   1587       C  
ATOM    450  CG  PHE A  55      35.312 105.756   7.684  1.00 62.60           C  
ANISOU  450  CG  PHE A  55     7822   8314   7650    456   -489   1550       C  
ATOM    451  CD1 PHE A  55      34.093 105.673   8.333  1.00 66.42           C  
ANISOU  451  CD1 PHE A  55     8288   8749   8198    384   -448   1591       C  
ATOM    452  CD2 PHE A  55      36.263 106.639   8.166  1.00 66.28           C  
ANISOU  452  CD2 PHE A  55     8196   8773   8214    579   -448   1461       C  
ATOM    453  CE1 PHE A  55      33.827 106.454   9.444  1.00 67.64           C  
ANISOU  453  CE1 PHE A  55     8339   8855   8506    412   -364   1545       C  
ATOM    454  CE2 PHE A  55      36.002 107.425   9.280  1.00 67.90           C  
ANISOU  454  CE2 PHE A  55     8286   8946   8569    624   -369   1420       C  
ATOM    455  CZ  PHE A  55      34.784 107.332   9.918  1.00 64.83           C  
ANISOU  455  CZ  PHE A  55     7883   8514   8235    530   -326   1463       C  
ATOM    456  N   TYR A  56      35.666 101.810   5.432  1.00 63.72           N  
ANISOU  456  N   TYR A  56     8444   8549   7215    272   -661   1541       N  
ATOM    457  CA  TYR A  56      35.533 101.036   4.207  1.00 63.16           C  
ANISOU  457  CA  TYR A  56     8414   8546   7036    161   -711   1593       C  
ATOM    458  C   TYR A  56      34.592 101.741   3.236  1.00 61.63           C  
ANISOU  458  C   TYR A  56     8090   8402   6925     57   -744   1755       C  
ATOM    459  O   TYR A  56      33.625 102.395   3.641  1.00 63.50           O  
ANISOU  459  O   TYR A  56     8226   8603   7299     48   -731   1832       O  
ATOM    460  CB  TYR A  56      35.023  99.628   4.510  1.00 62.32           C  
ANISOU  460  CB  TYR A  56     8435   8435   6810    133   -707   1562       C  
ATOM    461  CG  TYR A  56      36.114  98.600   4.737  1.00 63.40           C  
ANISOU  461  CG  TYR A  56     8705   8554   6830    172   -718   1424       C  
ATOM    462  CD1 TYR A  56      36.512  97.747   3.717  1.00 62.88           C  
ANISOU  462  CD1 TYR A  56     8673   8547   6671     81   -748   1402       C  
ATOM    463  CD2 TYR A  56      36.734  98.471   5.978  1.00 66.26           C  
ANISOU  463  CD2 TYR A  56     9156   8833   7187    287   -703   1311       C  
ATOM    464  CE1 TYR A  56      37.499  96.798   3.920  1.00 65.72           C  
ANISOU  464  CE1 TYR A  56     9131   8874   6967     99   -762   1267       C  
ATOM    465  CE2 TYR A  56      37.725  97.521   6.189  1.00 66.75           C  
ANISOU  465  CE2 TYR A  56     9334   8857   7170    317   -736   1185       C  
ATOM    466  CZ  TYR A  56      38.102  96.688   5.155  1.00 65.73           C  
ANISOU  466  CZ  TYR A  56     9216   8778   6979    220   -764   1162       C  
ATOM    467  OH  TYR A  56      39.081  95.739   5.344  1.00 66.13           O  
ANISOU  467  OH  TYR A  56     9359   8777   6992    231   -799   1030       O  
ATOM    468  N   VAL A  57      34.904 101.634   1.945  1.00 59.48           N  
ANISOU  468  N   VAL A  57     7821   8200   6579    -32   -792   1801       N  
ATOM    469  CA  VAL A  57      34.096 102.229   0.892  1.00 65.29           C  
ANISOU  469  CA  VAL A  57     8458   8983   7365   -142   -852   1962       C  
ATOM    470  C   VAL A  57      33.980 101.227  -0.244  1.00 71.61           C  
ANISOU  470  C   VAL A  57     9342   9861   8003   -263   -901   1987       C  
ATOM    471  O   VAL A  57      34.767 100.285  -0.357  1.00 71.26           O  
ANISOU  471  O   VAL A  57     9403   9840   7831   -270   -878   1874       O  
ATOM    472  CB  VAL A  57      34.695 103.551   0.371  1.00 69.67           C  
ANISOU  472  CB  VAL A  57     8907   9549   8016   -133   -858   2014       C  
ATOM    473  CG1 VAL A  57      34.699 104.607   1.469  1.00 68.01           C  
ANISOU  473  CG1 VAL A  57     8571   9273   7996    -19   -802   1994       C  
ATOM    474  CG2 VAL A  57      36.098 103.313  -0.175  1.00 68.38           C  
ANISOU  474  CG2 VAL A  57     8834   9403   7744   -127   -833   1903       C  
ATOM    475  N   LEU A  58      32.977 101.449  -1.101  1.00 75.01           N  
ANISOU  475  N   LEU A  58     9714  10329   8458   -367   -974   2133       N  
ATOM    476  CA  LEU A  58      32.843 100.627  -2.289  1.00 80.14           C  
ANISOU  476  CA  LEU A  58    10430  11066   8955   -494  -1027   2165       C  
ATOM    477  C   LEU A  58      33.756 101.131  -3.404  1.00 77.90           C  
ANISOU  477  C   LEU A  58    10168  10840   8593   -576  -1048   2190       C  
ATOM    478  O   LEU A  58      33.947 102.340  -3.561  1.00 75.15           O  
ANISOU  478  O   LEU A  58     9744  10468   8341   -561  -1062   2263       O  
ATOM    479  CB  LEU A  58      31.398 100.619  -2.776  1.00 94.01           C  
ANISOU  479  CB  LEU A  58    12127  12825  10769   -570  -1111   2301       C  
ATOM    480  CG  LEU A  58      30.499  99.488  -2.269  1.00102.01           C  
ANISOU  480  CG  LEU A  58    13171  13812  11776   -549  -1085   2251       C  
ATOM    481  CD1 LEU A  58      30.420  99.480  -0.749  1.00105.14           C  
ANISOU  481  CD1 LEU A  58    13570  14105  12273   -422   -993   2161       C  
ATOM    482  CD2 LEU A  58      29.111  99.600  -2.875  1.00100.59           C  
ANISOU  482  CD2 LEU A  58    12923  13611  11686   -624  -1180   2375       C  
ATOM    483  N   PRO A  59      34.309 100.215  -4.217  1.00 81.99           N  
ANISOU  483  N   PRO A  59    10781  11427   8944   -675  -1040   2125       N  
ATOM    484  CA  PRO A  59      35.240 100.624  -5.272  1.00 84.17           C  
ANISOU  484  CA  PRO A  59    11102  11739   9139   -773  -1035   2120       C  
ATOM    485  C   PRO A  59      34.578 101.447  -6.373  1.00 90.32           C  
ANISOU  485  C   PRO A  59    11848  12565   9906   -887  -1131   2311       C  
ATOM    486  O   PRO A  59      34.073 100.900  -7.348  1.00 91.13           O  
ANISOU  486  O   PRO A  59    11995  12746   9885  -1025  -1195   2377       O  
ATOM    487  CB  PRO A  59      35.739  99.282  -5.843  1.00 82.57           C  
ANISOU  487  CB  PRO A  59    10997  11599   8779   -883  -1001   2002       C  
ATOM    488  CG  PRO A  59      35.424  98.275  -4.808  1.00 82.33           C  
ANISOU  488  CG  PRO A  59    10966  11545   8772   -791   -970   1913       C  
ATOM    489  CD  PRO A  59      34.172  98.752  -4.140  1.00 82.66           C  
ANISOU  489  CD  PRO A  59    10929  11551   8925   -705  -1015   2033       C  
ATOM    490  N   ASN A  60      34.565 102.777  -6.200  1.00 99.38           N  
ANISOU  490  N   ASN A  60    12907  13661  11192   -827  -1147   2402       N  
ATOM    491  CA  ASN A  60      34.111 103.693  -7.239  1.00107.96           C  
ANISOU  491  CA  ASN A  60    13962  14776  12283   -932  -1244   2587       C  
ATOM    492  C   ASN A  60      35.254 104.281  -8.058  1.00107.47           C  
ANISOU  492  C   ASN A  60    13967  14721  12145   -994  -1192   2565       C  
ATOM    493  O   ASN A  60      35.138 104.407  -9.282  1.00111.44           O  
ANISOU  493  O   ASN A  60    14542  15280  12522  -1150  -1258   2670       O  
ATOM    494  CB  ASN A  60      33.289 104.836  -6.610  1.00115.78           C  
ANISOU  494  CB  ASN A  60    14785  15698  13507   -849  -1297   2714       C  
ATOM    495  CG  ASN A  60      34.097 105.686  -5.628  1.00124.72           C  
ANISOU  495  CG  ASN A  60    15828  16762  14797   -694  -1189   2626       C  
ATOM    496  OD1 ASN A  60      35.301 105.495  -5.454  1.00130.36           O  
ANISOU  496  OD1 ASN A  60    16613  17466  15451   -639  -1085   2472       O  
ATOM    497  ND2 ASN A  60      33.420 106.621  -4.974  1.00128.58           N  
ANISOU  497  ND2 ASN A  60    16150  17194  15511   -627  -1213   2711       N  
ATOM    498  N   ASP A  61      36.364 104.633  -7.415  1.00108.45           N  
ANISOU  498  N   ASP A  61    14081  14779  12346   -876  -1073   2420       N  
ATOM    499  CA  ASP A  61      37.504 105.230  -8.094  1.00104.35           C  
ANISOU  499  CA  ASP A  61    13621  14233  11794   -914   -996   2366       C  
ATOM    500  C   ASP A  61      38.249 104.184  -8.923  1.00 94.04           C  
ANISOU  500  C   ASP A  61    12483  12958  10291  -1064   -944   2236       C  
ATOM    501  O   ASP A  61      38.083 102.974  -8.753  1.00 91.84           O  
ANISOU  501  O   ASP A  61    12250  12717   9927  -1102   -949   2153       O  
ATOM    502  CB  ASP A  61      38.467 105.860  -7.081  1.00110.77           C  
ANISOU  502  CB  ASP A  61    14361  14946  12779   -724   -880   2219       C  
ATOM    503  CG  ASP A  61      37.856 107.048  -6.348  1.00116.65           C  
ANISOU  503  CG  ASP A  61    14916  15664  13739   -594   -906   2338       C  
ATOM    504  OD1 ASP A  61      36.935 107.685  -6.896  1.00121.29           O  
ANISOU  504  OD1 ASP A  61    15433  16289  14363   -670  -1007   2543       O  
ATOM    505  OD2 ASP A  61      38.306 107.352  -5.223  1.00119.06           O  
ANISOU  505  OD2 ASP A  61    15139  15906  14194   -423   -830   2221       O  
ATOM    506  N   ASP A  62      39.080 104.674  -9.839  1.00 97.58           N  
ANISOU  506  N   ASP A  62    13013  13382  10679  -1159   -883   2211       N  
ATOM    507  CA  ASP A  62      39.893 103.775 -10.645  1.00105.87           C  
ANISOU  507  CA  ASP A  62    14217  14439  11571  -1326   -809   2062       C  
ATOM    508  C   ASP A  62      40.955 103.089  -9.795  1.00 99.40           C  
ANISOU  508  C   ASP A  62    13408  13522  10838  -1228   -695   1797       C  
ATOM    509  O   ASP A  62      41.271 101.911 -10.009  1.00 95.07           O  
ANISOU  509  O   ASP A  62    12932  12991  10201  -1338   -665   1664       O  
ATOM    510  CB  ASP A  62      40.548 104.550 -11.789  1.00120.97           C  
ANISOU  510  CB  ASP A  62    16227  16321  13413  -1456   -751   2087       C  
ATOM    511  CG  ASP A  62      39.537 105.029 -12.819  1.00133.92           C  
ANISOU  511  CG  ASP A  62    17897  18061  14925  -1600   -886   2349       C  
ATOM    512  OD1 ASP A  62      38.618 104.255 -13.169  1.00138.35           O  
ANISOU  512  OD1 ASP A  62    18480  18727  15361  -1705   -997   2440       O  
ATOM    513  OD2 ASP A  62      39.662 106.187 -13.273  1.00135.61           O  
ANISOU  513  OD2 ASP A  62    18110  18242  15175  -1602   -884   2463       O  
ATOM    514  N   THR A  63      41.520 103.815  -8.828  1.00 96.77           N  
ANISOU  514  N   THR A  63    12994  13083  10691  -1025   -637   1714       N  
ATOM    515  CA  THR A  63      42.525 103.230  -7.947  1.00 93.01           C  
ANISOU  515  CA  THR A  63    12529  12494  10316   -915   -556   1465       C  
ATOM    516  C   THR A  63      41.908 102.209  -6.998  1.00 86.53           C  
ANISOU  516  C   THR A  63    11675  11715   9486   -849   -621   1450       C  
ATOM    517  O   THR A  63      42.521 101.174  -6.714  1.00 86.89           O  
ANISOU  517  O   THR A  63    11774  11713   9528   -869   -589   1271       O  
ATOM    518  CB  THR A  63      43.247 104.331  -7.165  1.00 90.37           C  
ANISOU  518  CB  THR A  63    12113  12038  10187   -705   -485   1383       C  
ATOM    519  OG1 THR A  63      42.303 105.054  -6.366  1.00 91.91           O  
ANISOU  519  OG1 THR A  63    12166  12284  10472   -560   -554   1548       O  
ATOM    520  CG2 THR A  63      43.948 105.297  -8.119  1.00 86.54           C  
ANISOU  520  CG2 THR A  63    11665  11492   9724   -765   -395   1374       C  
ATOM    521  N   LEU A  64      40.691 102.471  -6.508  1.00 80.57           N  
ANISOU  521  N   LEU A  64    10833  11037   8745   -778   -710   1631       N  
ATOM    522  CA  LEU A  64      40.043 101.522  -5.605  1.00 77.50           C  
ANISOU  522  CA  LEU A  64    10424  10675   8347   -716   -755   1617       C  
ATOM    523  C   LEU A  64      39.707 100.215  -6.310  1.00 76.09           C  
ANISOU  523  C   LEU A  64    10317  10585   8010   -888   -780   1607       C  
ATOM    524  O   LEU A  64      39.797  99.141  -5.705  1.00 70.29           O  
ANISOU  524  O   LEU A  64     9600   9840   7268   -861   -770   1497       O  
ATOM    525  CB  LEU A  64      38.785 102.136  -4.991  1.00 72.83           C  
ANISOU  525  CB  LEU A  64     9723  10120   7828   -625   -826   1797       C  
ATOM    526  CG  LEU A  64      39.044 103.285  -4.017  1.00 71.35           C  
ANISOU  526  CG  LEU A  64     9432   9852   7825   -441   -790   1785       C  
ATOM    527  CD1 LEU A  64      37.745 103.817  -3.452  1.00 71.18           C  
ANISOU  527  CD1 LEU A  64     9291   9856   7897   -390   -852   1949       C  
ATOM    528  CD2 LEU A  64      39.971 102.841  -2.896  1.00 68.19           C  
ANISOU  528  CD2 LEU A  64     9065   9357   7486   -298   -730   1576       C  
ATOM    529  N   ARG A  65      39.316 100.281  -7.586  1.00 82.13           N  
ANISOU  529  N   ARG A  65    11118  11439   8650  -1067   -814   1721       N  
ATOM    530  CA  ARG A  65      39.048  99.056  -8.333  1.00 85.12           C  
ANISOU  530  CA  ARG A  65    11549  11911   8880  -1241   -826   1697       C  
ATOM    531  C   ARG A  65      40.293  98.186  -8.422  1.00 81.36           C  
ANISOU  531  C   ARG A  65    11135  11374   8403  -1315   -728   1461       C  
ATOM    532  O   ARG A  65      40.216  96.963  -8.268  1.00 81.81           O  
ANISOU  532  O   ARG A  65    11187  11469   8429  -1363   -720   1375       O  
ATOM    533  CB  ARG A  65      38.538  99.386  -9.739  1.00 91.24           C  
ANISOU  533  CB  ARG A  65    12370  12785   9514  -1430   -881   1852       C  
ATOM    534  CG  ARG A  65      37.062  99.720  -9.814  1.00 95.41           C  
ANISOU  534  CG  ARG A  65    12834  13386  10033  -1409  -1011   2076       C  
ATOM    535  CD  ARG A  65      36.615 100.043 -11.243  1.00 96.77           C  
ANISOU  535  CD  ARG A  65    13068  13644  10055  -1603  -1090   2229       C  
ATOM    536  NE  ARG A  65      35.414 100.879 -11.240  1.00 94.46           N  
ANISOU  536  NE  ARG A  65    12702  13361   9828  -1553  -1228   2451       N  
ATOM    537  CZ  ARG A  65      35.390 102.180 -11.517  1.00 92.11           C  
ANISOU  537  CZ  ARG A  65    12385  13023   9588  -1542  -1275   2587       C  
ATOM    538  NH1 ARG A  65      36.505 102.820 -11.847  1.00 86.77           N  
ANISOU  538  NH1 ARG A  65    11771  12300   8900  -1568  -1183   2526       N  
ATOM    539  NH2 ARG A  65      34.243 102.843 -11.472  1.00 97.50           N  
ANISOU  539  NH2 ARG A  65    12980  13699  10365  -1509  -1412   2779       N  
ATOM    540  N   VAL A  66      41.452  98.801  -8.657  1.00 80.27           N  
ANISOU  540  N   VAL A  66    11045  11128   8326  -1327   -648   1342       N  
ATOM    541  CA  VAL A  66      42.692  98.039  -8.740  1.00 76.36           C  
ANISOU  541  CA  VAL A  66    10602  10534   7878  -1407   -555   1093       C  
ATOM    542  C   VAL A  66      43.020  97.411  -7.392  1.00 81.92           C  
ANISOU  542  C   VAL A  66    11263  11150   8712  -1237   -562    958       C  
ATOM    543  O   VAL A  66      43.373  96.229  -7.306  1.00 85.94           O  
ANISOU  543  O   VAL A  66    11776  11646   9232  -1314   -543    818       O  
ATOM    544  CB  VAL A  66      43.839  98.932  -9.245  1.00 71.69           C  
ANISOU  544  CB  VAL A  66    10073   9811   7356  -1440   -458    981       C  
ATOM    545  CG1 VAL A  66      45.166  98.173  -9.218  1.00 70.69           C  
ANISOU  545  CG1 VAL A  66     9989   9534   7337  -1514   -361    690       C  
ATOM    546  CG2 VAL A  66      43.528  99.450 -10.638  1.00 71.25           C  
ANISOU  546  CG2 VAL A  66    10088   9843   7143  -1636   -450   1117       C  
ATOM    547  N   GLU A  67      42.905  98.193  -6.316  1.00 85.51           N  
ANISOU  547  N   GLU A  67    11674  11545   9272  -1012   -591    999       N  
ATOM    548  CA  GLU A  67      43.230  97.670  -4.994  1.00 83.34           C  
ANISOU  548  CA  GLU A  67    11382  11179   9103   -849   -607    878       C  
ATOM    549  C   GLU A  67      42.265  96.564  -4.585  1.00 75.84           C  
ANISOU  549  C   GLU A  67    10411  10331   8075   -858   -662    947       C  
ATOM    550  O   GLU A  67      42.685  95.547  -4.021  1.00 76.92           O  
ANISOU  550  O   GLU A  67    10561  10415   8252   -845   -663    812       O  
ATOM    551  CB  GLU A  67      43.230  98.813  -3.978  1.00 78.23           C  
ANISOU  551  CB  GLU A  67    10689  10463   8571   -621   -620    916       C  
ATOM    552  CG  GLU A  67      44.382  99.781  -4.191  1.00 78.28           C  
ANISOU  552  CG  GLU A  67    10705  10337   8701   -573   -547    792       C  
ATOM    553  CD  GLU A  67      44.323 100.985  -3.281  1.00 79.30           C  
ANISOU  553  CD  GLU A  67    10756  10421   8952   -354   -548    838       C  
ATOM    554  OE1 GLU A  67      43.332 101.117  -2.528  1.00 81.65           O  
ANISOU  554  OE1 GLU A  67    10997  10792   9234   -262   -605    977       O  
ATOM    555  OE2 GLU A  67      45.262 101.809  -3.339  1.00 77.76           O  
ANISOU  555  OE2 GLU A  67    10551  10112   8884   -280   -480    726       O  
ATOM    556  N   ALA A  68      40.977  96.720  -4.901  1.00 72.13           N  
ANISOU  556  N   ALA A  68     9904   9994   7507   -886   -709   1150       N  
ATOM    557  CA  ALA A  68      40.021  95.658  -4.603  1.00 69.68           C  
ANISOU  557  CA  ALA A  68     9570   9770   7134   -896   -743   1204       C  
ATOM    558  C   ALA A  68      40.289  94.419  -5.443  1.00 70.29           C  
ANISOU  558  C   ALA A  68     9656   9911   7140  -1087   -711   1110       C  
ATOM    559  O   ALA A  68      40.108  93.292  -4.965  1.00 70.83           O  
ANISOU  559  O   ALA A  68     9703   9996   7213  -1076   -708   1050       O  
ATOM    560  CB  ALA A  68      38.593  96.148  -4.830  1.00 64.22           C  
ANISOU  560  CB  ALA A  68     8832   9179   6390   -889   -800   1421       C  
ATOM    561  N   PHE A  69      40.740  94.609  -6.682  1.00 70.54           N  
ANISOU  561  N   PHE A  69     9715   9976   7111  -1269   -678   1089       N  
ATOM    562  CA  PHE A  69      41.026  93.473  -7.549  1.00 75.84           C  
ANISOU  562  CA  PHE A  69    10381  10711   7723  -1481   -632    987       C  
ATOM    563  C   PHE A  69      42.254  92.697  -7.082  1.00 78.54           C  
ANISOU  563  C   PHE A  69    10725  10923   8196  -1496   -578    747       C  
ATOM    564  O   PHE A  69      42.266  91.462  -7.134  1.00 77.69           O  
ANISOU  564  O   PHE A  69    10566  10856   8098  -1588   -558    661       O  
ATOM    565  CB  PHE A  69      41.198  93.959  -8.993  1.00 79.12           C  
ANISOU  565  CB  PHE A  69    10846  11185   8031  -1689   -603   1025       C  
ATOM    566  CG  PHE A  69      41.726  92.912  -9.932  1.00 79.65           C  
ANISOU  566  CG  PHE A  69    10911  11296   8056  -1938   -529    881       C  
ATOM    567  CD1 PHE A  69      40.921  91.872 -10.356  1.00 77.81           C  
ANISOU  567  CD1 PHE A  69    10612  11217   7734  -2043   -542    924       C  
ATOM    568  CD2 PHE A  69      43.031  92.976 -10.398  1.00 82.71           C  
ANISOU  568  CD2 PHE A  69    11352  11560   8513  -2073   -436    688       C  
ATOM    569  CE1 PHE A  69      41.411  90.907 -11.214  1.00 81.85           C  
ANISOU  569  CE1 PHE A  69    11097  11778   8223  -2285   -462    782       C  
ATOM    570  CE2 PHE A  69      43.525  92.017 -11.260  1.00 83.87           C  
ANISOU  570  CE2 PHE A  69    11485  11737   8646  -2328   -355    538       C  
ATOM    571  CZ  PHE A  69      42.715  90.981 -11.668  1.00 85.09           C  
ANISOU  571  CZ  PHE A  69    11560  12064   8707  -2438   -368    589       C  
ATOM    572  N   GLU A  70      43.302  93.392  -6.631  1.00 80.87           N  
ANISOU  572  N   GLU A  70    11064  11049   8613  -1407   -557    629       N  
ATOM    573  CA  GLU A  70      44.494  92.674  -6.187  1.00 77.86           C  
ANISOU  573  CA  GLU A  70    10684  10511   8389  -1423   -526    388       C  
ATOM    574  C   GLU A  70      44.271  91.928  -4.875  1.00 76.51           C  
ANISOU  574  C   GLU A  70    10484  10306   8281  -1259   -589    370       C  
ATOM    575  O   GLU A  70      44.948  90.927  -4.616  1.00 77.34           O  
ANISOU  575  O   GLU A  70    10565  10328   8494  -1314   -585    203       O  
ATOM    576  CB  GLU A  70      45.677  93.635  -6.049  1.00 76.80           C  
ANISOU  576  CB  GLU A  70    10605  10183   8392  -1356   -490    248       C  
ATOM    577  CG  GLU A  70      46.140  94.267  -7.353  1.00 82.99           C  
ANISOU  577  CG  GLU A  70    11438  10957   9137  -1539   -401    217       C  
ATOM    578  CD  GLU A  70      47.407  95.096  -7.185  1.00 94.23           C  
ANISOU  578  CD  GLU A  70    12910  12157  10736  -1467   -342     35       C  
ATOM    579  OE1 GLU A  70      48.030  95.029  -6.102  1.00 97.60           O  
ANISOU  579  OE1 GLU A  70    13326  12429  11329  -1294   -378    -96       O  
ATOM    580  OE2 GLU A  70      47.778  95.820  -8.135  1.00 97.33           O  
ANISOU  580  OE2 GLU A  70    13357  12520  11103  -1579   -258     19       O  
ATOM    581  N   TYR A  71      43.321  92.374  -4.050  1.00 74.76           N  
ANISOU  581  N   TYR A  71    10264  10138   8002  -1073   -645    535       N  
ATOM    582  CA  TYR A  71      43.103  91.781  -2.734  1.00 69.83           C  
ANISOU  582  CA  TYR A  71     9643   9467   7421   -912   -696    523       C  
ATOM    583  C   TYR A  71      41.980  90.750  -2.707  1.00 72.82           C  
ANISOU  583  C   TYR A  71     9973   9987   7708   -946   -699    624       C  
ATOM    584  O   TYR A  71      42.140  89.693  -2.085  1.00 73.18           O  
ANISOU  584  O   TYR A  71    10006   9997   7804   -926   -711    543       O  
ATOM    585  CB  TYR A  71      42.822  92.880  -1.699  1.00 63.39           C  
ANISOU  585  CB  TYR A  71     8866   8598   6624   -689   -734    610       C  
ATOM    586  CG  TYR A  71      42.944  92.415  -0.262  1.00 63.38           C  
ANISOU  586  CG  TYR A  71     8906   8500   6677   -524   -784    555       C  
ATOM    587  CD1 TYR A  71      44.128  91.860   0.208  1.00 68.09           C  
ANISOU  587  CD1 TYR A  71     9536   8940   7396   -510   -814    360       C  
ATOM    588  CD2 TYR A  71      41.878  92.533   0.626  1.00 61.42           C  
ANISOU  588  CD2 TYR A  71     8673   8299   6365   -394   -804    691       C  
ATOM    589  CE1 TYR A  71      44.250  91.428   1.523  1.00 69.54           C  
ANISOU  589  CE1 TYR A  71     9777   9030   7615   -364   -879    319       C  
ATOM    590  CE2 TYR A  71      41.988  92.104   1.941  1.00 63.95           C  
ANISOU  590  CE2 TYR A  71     9058   8529   6712   -258   -845    644       C  
ATOM    591  CZ  TYR A  71      43.178  91.551   2.385  1.00 68.28           C  
ANISOU  591  CZ  TYR A  71     9650   8935   7359   -241   -890    466       C  
ATOM    592  OH  TYR A  71      43.305  91.123   3.690  1.00 66.47           O  
ANISOU  592  OH  TYR A  71     9502   8609   7143   -110   -950    427       O  
ATOM    593  N   TYR A  72      40.850  91.024  -3.370  1.00 68.98           N  
ANISOU  593  N   TYR A  72     9454   9650   7105   -993   -693    793       N  
ATOM    594  CA  TYR A  72      39.699  90.128  -3.362  1.00 66.50           C  
ANISOU  594  CA  TYR A  72     9087   9458   6723  -1005   -688    881       C  
ATOM    595  C   TYR A  72      39.553  89.316  -4.642  1.00 71.97           C  
ANISOU  595  C   TYR A  72     9706  10283   7355  -1222   -646    860       C  
ATOM    596  O   TYR A  72      38.731  88.392  -4.680  1.00 73.59           O  
ANISOU  596  O   TYR A  72     9844  10587   7529  -1237   -628    896       O  
ATOM    597  CB  TYR A  72      38.409  90.919  -3.133  1.00 63.52           C  
ANISOU  597  CB  TYR A  72     8712   9134   6288   -898   -718   1073       C  
ATOM    598  CG  TYR A  72      38.387  91.677  -1.830  1.00 66.11           C  
ANISOU  598  CG  TYR A  72     9094   9347   6676   -698   -744   1097       C  
ATOM    599  CD1 TYR A  72      38.642  93.042  -1.794  1.00 66.00           C  
ANISOU  599  CD1 TYR A  72     9099   9282   6696   -639   -764   1144       C  
ATOM    600  CD2 TYR A  72      38.111  91.029  -0.632  1.00 68.77           C  
ANISOU  600  CD2 TYR A  72     9464   9629   7039   -573   -741   1069       C  
ATOM    601  CE1 TYR A  72      38.621  93.741  -0.603  1.00 69.50           C  
ANISOU  601  CE1 TYR A  72     9573   9631   7203   -465   -778   1156       C  
ATOM    602  CE2 TYR A  72      38.092  91.720   0.569  1.00 70.92           C  
ANISOU  602  CE2 TYR A  72     9796   9799   7353   -408   -758   1084       C  
ATOM    603  CZ  TYR A  72      38.345  93.077   0.578  1.00 74.90           C  
ANISOU  603  CZ  TYR A  72    10299  10262   7896   -356   -775   1124       C  
ATOM    604  OH  TYR A  72      38.321  93.769   1.770  1.00 77.70           O  
ANISOU  604  OH  TYR A  72    10694  10526   8301   -200   -783   1130       O  
ATOM    605  N   HIS A  73      40.315  89.648  -5.685  1.00 76.91           N  
ANISOU  605  N   HIS A  73    10343  10912   7969  -1390   -618    796       N  
ATOM    606  CA  HIS A  73      40.218  88.990  -6.990  1.00 75.21           C  
ANISOU  606  CA  HIS A  73    10068  10827   7682  -1626   -571    771       C  
ATOM    607  C   HIS A  73      38.816  89.115  -7.579  1.00 77.85           C  
ANISOU  607  C   HIS A  73    10373  11322   7884  -1639   -603    959       C  
ATOM    608  O   HIS A  73      38.318  88.205  -8.242  1.00 87.05           O  
ANISOU  608  O   HIS A  73    11458  12619   8999  -1761   -574    955       O  
ATOM    609  CB  HIS A  73      40.640  87.523  -6.912  1.00 69.05           C  
ANISOU  609  CB  HIS A  73     9194  10056   6987  -1722   -519    613       C  
ATOM    610  CG  HIS A  73      42.119  87.325  -6.868  1.00 69.91           C  
ANISOU  610  CG  HIS A  73     9314  10009   7240  -1813   -485    399       C  
ATOM    611  ND1 HIS A  73      42.713  86.110  -7.131  1.00 69.30           N  
ANISOU  611  ND1 HIS A  73     9134   9925   7272  -1977   -430    230       N  
ATOM    612  CD2 HIS A  73      43.126  88.189  -6.602  1.00 70.81           C  
ANISOU  612  CD2 HIS A  73     9516   9952   7437  -1766   -495    313       C  
ATOM    613  CE1 HIS A  73      44.024  86.234  -7.029  1.00 71.85           C  
ANISOU  613  CE1 HIS A  73     9489  10064   7748  -2035   -416     45       C  
ATOM    614  NE2 HIS A  73      44.300  87.486  -6.708  1.00 72.17           N  
ANISOU  614  NE2 HIS A  73     9650  10000   7772  -1901   -453     87       N  
ATOM    615  N   THR A  74      38.175  90.255  -7.339  1.00 77.87           N  
ANISOU  615  N   THR A  74    10427  11307   7851  -1514   -667   1117       N  
ATOM    616  CA  THR A  74      36.890  90.537  -7.955  1.00 80.71           C  
ANISOU  616  CA  THR A  74    10765  11784   8116  -1533   -721   1293       C  
ATOM    617  C   THR A  74      36.657  92.042  -7.942  1.00 85.01           C  
ANISOU  617  C   THR A  74    11369  12276   8653  -1458   -788   1436       C  
ATOM    618  O   THR A  74      37.134  92.753  -7.052  1.00 86.50           O  
ANISOU  618  O   THR A  74    11592  12346   8929  -1317   -789   1416       O  
ATOM    619  CB  THR A  74      35.736  89.806  -7.252  1.00 74.86           C  
ANISOU  619  CB  THR A  74     9959  11078   7407  -1405   -728   1343       C  
ATOM    620  OG1 THR A  74      34.504  90.118  -7.912  1.00 80.15           O  
ANISOU  620  OG1 THR A  74    10603  11834   8014  -1427   -791   1498       O  
ATOM    621  CG2 THR A  74      35.630  90.221  -5.800  1.00 72.66           C  
ANISOU  621  CG2 THR A  74     9715  10668   7224  -1184   -739   1357       C  
ATOM    622  N   THR A  75      35.932  92.515  -8.953  1.00 85.27           N  
ANISOU  622  N   THR A  75    11408  12399   8592  -1558   -849   1577       N  
ATOM    623  CA  THR A  75      35.516  93.907  -9.046  1.00 90.47           C  
ANISOU  623  CA  THR A  75    12098  13020   9258  -1503   -929   1739       C  
ATOM    624  C   THR A  75      34.005  94.042  -8.949  1.00 97.88           C  
ANISOU  624  C   THR A  75    12981  13990  10218  -1432  -1020   1898       C  
ATOM    625  O   THR A  75      33.467  95.124  -9.206  1.00110.18           O  
ANISOU  625  O   THR A  75    14543  15526  11795  -1420  -1109   2050       O  
ATOM    626  CB  THR A  75      36.032  94.543 -10.340  1.00 92.71           C  
ANISOU  626  CB  THR A  75    12452  13344   9428  -1688   -942   1779       C  
ATOM    627  OG1 THR A  75      35.525  93.827 -11.475  1.00 91.79           O  
ANISOU  627  OG1 THR A  75    12334  13366   9177  -1872   -965   1809       O  
ATOM    628  CG2 THR A  75      37.556  94.520 -10.364  1.00 90.02           C  
ANISOU  628  CG2 THR A  75    12168  12925   9111  -1749   -837   1597       C  
ATOM    629  N   ASP A  76      33.317  92.966  -8.592  1.00 96.76           N  
ANISOU  629  N   ASP A  76    12782  13885  10097  -1389   -998   1857       N  
ATOM    630  CA  ASP A  76      31.875  92.972  -8.407  1.00105.58           C  
ANISOU  630  CA  ASP A  76    13843  14998  11273  -1310  -1066   1969       C  
ATOM    631  C   ASP A  76      31.490  94.031  -7.379  1.00112.03           C  
ANISOU  631  C   ASP A  76    14654  15681  12231  -1149  -1098   2045       C  
ATOM    632  O   ASP A  76      31.975  93.982  -6.236  1.00112.42           O  
ANISOU  632  O   ASP A  76    14716  15646  12351  -1025  -1027   1959       O  
ATOM    633  CB  ASP A  76      31.409  91.586  -7.961  1.00105.90           C  
ANISOU  633  CB  ASP A  76    13825  15072  11342  -1258   -993   1869       C  
ATOM    634  CG  ASP A  76      29.905  91.409  -8.043  1.00104.17           C  
ANISOU  634  CG  ASP A  76    13544  14851  11183  -1206  -1050   1954       C  
ATOM    635  OD1 ASP A  76      29.173  92.419  -8.030  1.00105.12           O  
ANISOU  635  OD1 ASP A  76    13665  14899  11377  -1168  -1146   2083       O  
ATOM    636  OD2 ASP A  76      29.452  90.246  -8.110  1.00105.15           O  
ANISOU  636  OD2 ASP A  76    13608  15036  11309  -1203   -995   1881       O  
ATOM    637  N   PRO A  77      30.668  95.017  -7.743  1.00111.47           N  
ANISOU  637  N   PRO A  77    14561  15582  12212  -1158  -1206   2201       N  
ATOM    638  CA  PRO A  77      30.283  96.040  -6.761  1.00106.52           C  
ANISOU  638  CA  PRO A  77    13897  14824  11751  -1025  -1225   2264       C  
ATOM    639  C   PRO A  77      29.482  95.483  -5.594  1.00 97.81           C  
ANISOU  639  C   PRO A  77    12758  13633  10771   -889  -1168   2207       C  
ATOM    640  O   PRO A  77      29.626  95.978  -4.469  1.00 93.32           O  
ANISOU  640  O   PRO A  77    12186  12962  10309   -774  -1120   2178       O  
ATOM    641  CB  PRO A  77      29.457  97.031  -7.596  1.00109.69           C  
ANISOU  641  CB  PRO A  77    14262  15218  12197  -1098  -1369   2444       C  
ATOM    642  CG  PRO A  77      28.954  96.221  -8.760  1.00109.97           C  
ANISOU  642  CG  PRO A  77    14313  15365  12107  -1227  -1431   2468       C  
ATOM    643  CD  PRO A  77      30.052  95.243  -9.062  1.00110.57           C  
ANISOU  643  CD  PRO A  77    14446  15546  12019  -1299  -1324   2326       C  
ATOM    644  N   SER A  78      28.659  94.456  -5.821  1.00 92.81           N  
ANISOU  644  N   SER A  78    12101  13034  10128   -901  -1161   2179       N  
ATOM    645  CA  SER A  78      27.855  93.892  -4.743  1.00 91.57           C  
ANISOU  645  CA  SER A  78    11922  12777  10092   -775  -1088   2116       C  
ATOM    646  C   SER A  78      28.644  92.955  -3.838  1.00 89.95           C  
ANISOU  646  C   SER A  78    11769  12575   9835   -700   -959   1969       C  
ATOM    647  O   SER A  78      28.058  92.372  -2.923  1.00 88.60           O  
ANISOU  647  O   SER A  78    11601  12323   9739   -600   -882   1908       O  
ATOM    648  CB  SER A  78      26.659  93.130  -5.313  1.00 92.47           C  
ANISOU  648  CB  SER A  78    11983  12911  10241   -798  -1117   2126       C  
ATOM    649  OG  SER A  78      27.079  91.911  -5.898  1.00 98.20           O  
ANISOU  649  OG  SER A  78    12709  13775  10827   -857  -1064   2040       O  
ATOM    650  N   PHE A  79      29.948  92.798  -4.066  1.00 89.85           N  
ANISOU  650  N   PHE A  79    11799  12632   9706   -750   -935   1906       N  
ATOM    651  CA  PHE A  79      30.732  91.867  -3.264  1.00 85.61           C  
ANISOU  651  CA  PHE A  79    11305  12085   9138   -691   -838   1766       C  
ATOM    652  C   PHE A  79      30.898  92.387  -1.843  1.00 85.76           C  
ANISOU  652  C   PHE A  79    11376  11969   9240   -550   -800   1739       C  
ATOM    653  O   PHE A  79      30.562  91.699  -0.872  1.00 87.07           O  
ANISOU  653  O   PHE A  79    11573  12070   9439   -457   -729   1676       O  
ATOM    654  CB  PHE A  79      32.093  91.628  -3.914  1.00 82.05           C  
ANISOU  654  CB  PHE A  79    10878  11713   8584   -798   -832   1690       C  
ATOM    655  CG  PHE A  79      32.943  90.641  -3.182  1.00 72.56           C  
ANISOU  655  CG  PHE A  79     9707  10487   7377   -756   -756   1543       C  
ATOM    656  CD1 PHE A  79      32.750  89.284  -3.355  1.00 66.13           C  
ANISOU  656  CD1 PHE A  79     8844   9741   6541   -793   -700   1469       C  
ATOM    657  CD2 PHE A  79      33.935  91.071  -2.318  1.00 72.60           C  
ANISOU  657  CD2 PHE A  79     9777  10395   7413   -678   -747   1476       C  
ATOM    658  CE1 PHE A  79      33.533  88.369  -2.685  1.00 67.42           C  
ANISOU  658  CE1 PHE A  79     9024   9873   6720   -763   -644   1341       C  
ATOM    659  CE2 PHE A  79      34.724  90.160  -1.640  1.00 74.97           C  
ANISOU  659  CE2 PHE A  79    10111  10654   7722   -643   -704   1344       C  
ATOM    660  CZ  PHE A  79      34.522  88.805  -1.825  1.00 71.98           C  
ANISOU  660  CZ  PHE A  79     9682  10340   7326   -690   -656   1281       C  
ATOM    661  N   LEU A  80      31.425  93.607  -1.705  1.00 87.30           N  
ANISOU  661  N   LEU A  80    11582  12120   9469   -534   -840   1783       N  
ATOM    662  CA  LEU A  80      31.603  94.193  -0.380  1.00 88.33           C  
ANISOU  662  CA  LEU A  80    11750  12132   9680   -407   -803   1754       C  
ATOM    663  C   LEU A  80      30.269  94.338   0.337  1.00 85.14           C  
ANISOU  663  C   LEU A  80    11324  11634   9393   -344   -776   1800       C  
ATOM    664  O   LEU A  80      30.188  94.149   1.555  1.00 86.33           O  
ANISOU  664  O   LEU A  80    11533  11690   9578   -249   -706   1737       O  
ATOM    665  CB  LEU A  80      32.302  95.548  -0.485  1.00 95.07           C  
ANISOU  665  CB  LEU A  80    12583  12965  10574   -402   -844   1796       C  
ATOM    666  CG  LEU A  80      33.831  95.540  -0.561  1.00100.90           C  
ANISOU  666  CG  LEU A  80    13372  13715  11251   -404   -833   1693       C  
ATOM    667  CD1 LEU A  80      34.306  95.148  -1.958  1.00102.65           C  
ANISOU  667  CD1 LEU A  80    13589  14042  11372   -554   -859   1689       C  
ATOM    668  CD2 LEU A  80      34.413  96.890  -0.134  1.00102.99           C  
ANISOU  668  CD2 LEU A  80    13613  13915  11602   -331   -839   1705       C  
ATOM    669  N   GLY A  81      29.212  94.673  -0.400  1.00 86.54           N  
ANISOU  669  N   GLY A  81    11424  11818   9639   -405   -831   1900       N  
ATOM    670  CA  GLY A  81      27.898  94.751   0.215  1.00 89.49           C  
ANISOU  670  CA  GLY A  81    11769  12072  10163   -361   -800   1920       C  
ATOM    671  C   GLY A  81      27.466  93.433   0.830  1.00 87.49           C  
ANISOU  671  C   GLY A  81    11574  11785   9885   -301   -697   1819       C  
ATOM    672  O   GLY A  81      27.006  93.386   1.973  1.00 88.17           O  
ANISOU  672  O   GLY A  81    11706  11743  10050   -225   -611   1768       O  
ATOM    673  N   ARG A  82      27.632  92.337   0.087  1.00 82.20           N  
ANISOU  673  N   ARG A  82    10898  11227   9106   -343   -693   1783       N  
ATOM    674  CA  ARG A  82      27.258  91.036   0.629  1.00 79.49           C  
ANISOU  674  CA  ARG A  82    10592  10861   8750   -281   -587   1687       C  
ATOM    675  C   ARG A  82      28.232  90.577   1.703  1.00 75.62           C  
ANISOU  675  C   ARG A  82    10207  10344   8182   -210   -518   1596       C  
ATOM    676  O   ARG A  82      27.838  89.859   2.630  1.00 69.92           O  
ANISOU  676  O   ARG A  82     9549   9539   7480   -131   -419   1529       O  
ATOM    677  CB  ARG A  82      27.171  89.998  -0.488  1.00 78.99           C  
ANISOU  677  CB  ARG A  82    10462  10936   8614   -351   -596   1668       C  
ATOM    678  CG  ARG A  82      26.066  90.265  -1.492  1.00 77.95           C  
ANISOU  678  CG  ARG A  82    10239  10819   8560   -408   -669   1746       C  
ATOM    679  CD  ARG A  82      25.987  89.175  -2.552  1.00 79.10           C  
ANISOU  679  CD  ARG A  82    10314  11112   8627   -475   -667   1712       C  
ATOM    680  NE  ARG A  82      27.096  89.195  -3.505  1.00 77.77           N  
ANISOU  680  NE  ARG A  82    10139  11103   8308   -600   -727   1727       N  
ATOM    681  CZ  ARG A  82      28.155  88.397  -3.427  1.00 74.64           C  
ANISOU  681  CZ  ARG A  82     9755  10787   7816   -628   -666   1635       C  
ATOM    682  NH1 ARG A  82      28.242  87.524  -2.436  1.00 75.87           N  
ANISOU  682  NH1 ARG A  82     9936  10891   8001   -531   -559   1540       N  
ATOM    683  NH2 ARG A  82      29.121  88.463  -4.338  1.00 71.90           N  
ANISOU  683  NH2 ARG A  82     9401  10558   7359   -763   -709   1632       N  
ATOM    684  N   TYR A  83      29.498  90.985   1.608  1.00 75.78           N  
ANISOU  684  N   TYR A  83    10253  10416   8123   -234   -570   1587       N  
ATOM    685  CA  TYR A  83      30.465  90.597   2.626  1.00 73.12           C  
ANISOU  685  CA  TYR A  83    10019  10034   7729   -164   -533   1496       C  
ATOM    686  C   TYR A  83      30.213  91.332   3.936  1.00 71.68           C  
ANISOU  686  C   TYR A  83     9916   9711   7609    -70   -496   1496       C  
ATOM    687  O   TYR A  83      30.324  90.736   5.013  1.00 77.66           O  
ANISOU  687  O   TYR A  83    10780  10393   8335      4   -433   1428       O  
ATOM    688  CB  TYR A  83      31.880  90.856   2.122  1.00 76.93           C  
ANISOU  688  CB  TYR A  83    10501  10583   8146   -215   -600   1464       C  
ATOM    689  CG  TYR A  83      32.949  90.870   3.194  1.00 82.31           C  
ANISOU  689  CG  TYR A  83    11285  11184   8806   -134   -600   1378       C  
ATOM    690  CD1 TYR A  83      33.216  89.742   3.960  1.00 83.16           C  
ANISOU  690  CD1 TYR A  83    11469  11252   8877    -84   -560   1293       C  
ATOM    691  CD2 TYR A  83      33.721  92.003   3.410  1.00 83.47           C  
ANISOU  691  CD2 TYR A  83    11447  11291   8979   -104   -646   1378       C  
ATOM    692  CE1 TYR A  83      34.206  89.755   4.929  1.00 83.26           C  
ANISOU  692  CE1 TYR A  83    11585  11178   8870    -12   -586   1216       C  
ATOM    693  CE2 TYR A  83      34.712  92.021   4.368  1.00 84.35           C  
ANISOU  693  CE2 TYR A  83    11650  11320   9080    -21   -659   1288       C  
ATOM    694  CZ  TYR A  83      34.951  90.900   5.126  1.00 85.26           C  
ANISOU  694  CZ  TYR A  83    11854  11389   9150     21   -639   1209       C  
ATOM    695  OH  TYR A  83      35.941  90.936   6.080  1.00 85.36           O  
ANISOU  695  OH  TYR A  83    11969  11307   9156    103   -677   1122       O  
ATOM    696  N   MET A  84      29.859  92.620   3.870  1.00 72.49           N  
ANISOU  696  N   MET A  84     9965   9775   7803    -81   -531   1571       N  
ATOM    697  CA  MET A  84      29.565  93.362   5.094  1.00 78.38           C  
ANISOU  697  CA  MET A  84    10762  10391   8629    -14   -481   1561       C  
ATOM    698  C   MET A  84      28.258  92.899   5.727  1.00 82.88           C  
ANISOU  698  C   MET A  84    11366  10847   9279      8   -380   1542       C  
ATOM    699  O   MET A  84      28.134  92.871   6.958  1.00 84.66           O  
ANISOU  699  O   MET A  84    11697  10960   9511     65   -298   1486       O  
ATOM    700  CB  MET A  84      29.520  94.865   4.813  1.00 80.44           C  
ANISOU  700  CB  MET A  84    10920  10642   9002    -43   -538   1643       C  
ATOM    701  CG  MET A  84      30.848  95.468   4.360  1.00 84.66           C  
ANISOU  701  CG  MET A  84    11433  11257   9479    -46   -611   1643       C  
ATOM    702  SD  MET A  84      31.979  95.966   5.681  1.00 87.99           S  
ANISOU  702  SD  MET A  84    11941  11609   9883     65   -586   1550       S  
ATOM    703  CE  MET A  84      32.828  94.437   6.043  1.00 86.17           C  
ANISOU  703  CE  MET A  84    11857  11387   9495    103   -581   1434       C  
ATOM    704  N   SER A  85      27.267  92.537   4.910  1.00 82.57           N  
ANISOU  704  N   SER A  85    11245  10821   9307    -39   -380   1578       N  
ATOM    705  CA  SER A  85      26.038  91.980   5.467  1.00 80.02           C  
ANISOU  705  CA  SER A  85    10955  10368   9081    -11   -268   1532       C  
ATOM    706  C   SER A  85      26.310  90.656   6.167  1.00 79.36           C  
ANISOU  706  C   SER A  85    10998  10276   8880     56   -172   1440       C  
ATOM    707  O   SER A  85      25.798  90.408   7.264  1.00 80.95           O  
ANISOU  707  O   SER A  85    11307  10338   9113    105    -55   1380       O  
ATOM    708  CB  SER A  85      24.987  91.800   4.375  1.00 76.14           C  
ANISOU  708  CB  SER A  85    10343   9890   8696    -63   -301   1574       C  
ATOM    709  OG  SER A  85      24.637  93.048   3.815  1.00 82.14           O  
ANISOU  709  OG  SER A  85    10994  10630   9586   -128   -400   1667       O  
ATOM    710  N   ALA A  86      27.120  89.796   5.549  1.00 78.26           N  
ANISOU  710  N   ALA A  86    10845  10278   8614     48   -214   1425       N  
ATOM    711  CA  ALA A  86      27.458  88.529   6.184  1.00 76.87           C  
ANISOU  711  CA  ALA A  86    10768  10096   8344    105   -137   1344       C  
ATOM    712  C   ALA A  86      28.287  88.751   7.441  1.00 71.98           C  
ANISOU  712  C   ALA A  86    10304   9401   7644    161   -132   1307       C  
ATOM    713  O   ALA A  86      28.062  88.091   8.462  1.00 65.81           O  
ANISOU  713  O   ALA A  86     9654   8521   6829    220    -37   1252       O  
ATOM    714  CB  ALA A  86      28.205  87.627   5.202  1.00 76.75           C  
ANISOU  714  CB  ALA A  86    10673  10244   8245     59   -190   1329       C  
ATOM    715  N   LEU A  87      29.249  89.678   7.386  1.00 73.39           N  
ANISOU  715  N   LEU A  87    10475   9617   7793    147   -232   1331       N  
ATOM    716  CA  LEU A  87      30.073  89.956   8.558  1.00 77.10           C  
ANISOU  716  CA  LEU A  87    11086  10013   8195    208   -243   1288       C  
ATOM    717  C   LEU A  87      29.241  90.485   9.715  1.00 77.75           C  
ANISOU  717  C   LEU A  87    11265   9946   8332    240   -144   1278       C  
ATOM    718  O   LEU A  87      29.623  90.318  10.877  1.00 74.97           O  
ANISOU  718  O   LEU A  87    11072   9511   7900    292   -115   1228       O  
ATOM    719  CB  LEU A  87      31.180  90.951   8.215  1.00 74.56           C  
ANISOU  719  CB  LEU A  87    10713   9748   7869    197   -356   1303       C  
ATOM    720  CG  LEU A  87      32.213  91.197   9.319  1.00 73.56           C  
ANISOU  720  CG  LEU A  87    10719   9554   7678    270   -392   1241       C  
ATOM    721  CD1 LEU A  87      32.877  89.895   9.736  1.00 75.01           C  
ANISOU  721  CD1 LEU A  87    11016   9724   7760    302   -410   1171       C  
ATOM    722  CD2 LEU A  87      33.258  92.198   8.872  1.00 75.69           C  
ANISOU  722  CD2 LEU A  87    10914   9870   7976    270   -488   1240       C  
ATOM    723  N   ASN A  88      28.102  91.119   9.426  1.00 83.54           N  
ANISOU  723  N   ASN A  88    11905  10628   9209    197    -94   1318       N  
ATOM    724  CA  ASN A  88      27.244  91.598  10.503  1.00 87.09           C  
ANISOU  724  CA  ASN A  88    12433  10913   9743    200     21   1288       C  
ATOM    725  C   ASN A  88      26.656  90.446  11.301  1.00 88.33           C  
ANISOU  725  C   ASN A  88    12747  10964   9850    237    157   1217       C  
ATOM    726  O   ASN A  88      26.298  90.623  12.470  1.00 95.82           O  
ANISOU  726  O   ASN A  88    13835  11770  10802    245    261   1168       O  
ATOM    727  CB  ASN A  88      26.124  92.474   9.953  1.00 91.20           C  
ANISOU  727  CB  ASN A  88    12800  11376  10474    132     37   1333       C  
ATOM    728  CG  ASN A  88      25.507  93.351  11.021  1.00 96.67           C  
ANISOU  728  CG  ASN A  88    13532  11904  11294    104    136   1298       C  
ATOM    729  OD1 ASN A  88      24.585  92.937  11.726  1.00 97.51           O  
ANISOU  729  OD1 ASN A  88    13731  11856  11462     96    278   1230       O  
ATOM    730  ND2 ASN A  88      26.015  94.570  11.150  1.00 99.88           N  
ANISOU  730  ND2 ASN A  88    13861  12336  11752     85     75   1332       N  
ATOM    731  N   HIS A  89      26.537  89.269  10.691  1.00 83.20           N  
ANISOU  731  N   HIS A  89    12074  10379   9160    256    169   1207       N  
ATOM    732  CA  HIS A  89      26.052  88.095  11.404  1.00 85.33           C  
ANISOU  732  CA  HIS A  89    12482  10556   9384    303    304   1141       C  
ATOM    733  C   HIS A  89      27.182  87.232  11.954  1.00 86.67           C  
ANISOU  733  C   HIS A  89    12787  10774   9371    354    259   1118       C  
ATOM    734  O   HIS A  89      27.081  86.731  13.082  1.00 83.83           O  
ANISOU  734  O   HIS A  89    12618  10298   8934    393    350   1072       O  
ATOM    735  CB  HIS A  89      25.168  87.247  10.491  1.00 85.81           C  
ANISOU  735  CB  HIS A  89    12421  10644   9537    304    365   1129       C  
ATOM    736  CG  HIS A  89      23.821  87.840  10.228  1.00 85.12           C  
ANISOU  736  CG  HIS A  89    12246  10436   9657    268    438   1121       C  
ATOM    737  ND1 HIS A  89      23.624  88.884   9.350  1.00 86.79           N  
ANISOU  737  ND1 HIS A  89    12296  10694   9987    204    330   1188       N  
ATOM    738  CD2 HIS A  89      22.598  87.519  10.712  1.00 85.10           C  
ANISOU  738  CD2 HIS A  89    12296  10250   9788    283    605   1045       C  
ATOM    739  CE1 HIS A  89      22.339  89.186   9.310  1.00 87.52           C  
ANISOU  739  CE1 HIS A  89    12335  10631  10286    178    411   1157       C  
ATOM    740  NE2 HIS A  89      21.695  88.372  10.127  1.00 86.38           N  
ANISOU  740  NE2 HIS A  89    12319  10340  10164    225    585   1060       N  
ATOM    741  N   THR A  90      28.243  87.021  11.167  1.00 89.20           N  
ANISOU  741  N   THR A  90    13013  11246   9631    345    121   1143       N  
ATOM    742  CA  THR A  90      29.299  86.110  11.596  1.00 86.43           C  
ANISOU  742  CA  THR A  90    12764  10924   9153    383     64   1110       C  
ATOM    743  C   THR A  90      30.045  86.634  12.817  1.00 81.00           C  
ANISOU  743  C   THR A  90    12265  10146   8367    420     14   1092       C  
ATOM    744  O   THR A  90      30.525  85.837  13.630  1.00 83.05           O  
ANISOU  744  O   THR A  90    12682  10350   8522    462      6   1060       O  
ATOM    745  CB  THR A  90      30.288  85.850  10.454  1.00 86.59           C  
ANISOU  745  CB  THR A  90    12629  11103   9168    341    -67   1119       C  
ATOM    746  OG1 THR A  90      30.947  87.068  10.085  1.00 80.75           O  
ANISOU  746  OG1 THR A  90    11832  10405   8446    312   -177   1147       O  
ATOM    747  CG2 THR A  90      29.562  85.284   9.245  1.00 90.71           C  
ANISOU  747  CG2 THR A  90    12968  11726   9770    296    -18   1133       C  
ATOM    748  N   LYS A  91      30.165  87.955  12.967  1.00 78.08           N  
ANISOU  748  N   LYS A  91    11876   9758   8034    406    -26   1111       N  
ATOM    749  CA  LYS A  91      30.810  88.472  14.169  1.00 82.97           C  
ANISOU  749  CA  LYS A  91    12668  10291   8565    446    -62   1082       C  
ATOM    750  C   LYS A  91      29.931  88.333  15.413  1.00 81.85           C  
ANISOU  750  C   LYS A  91    12722   9994   8382    453     88   1053       C  
ATOM    751  O   LYS A  91      30.445  88.477  16.528  1.00 79.22           O  
ANISOU  751  O   LYS A  91    12577   9584   7938    483     65   1024       O  
ATOM    752  CB  LYS A  91      31.279  89.922  13.960  1.00 83.75           C  
ANISOU  752  CB  LYS A  91    12664  10427   8731    435   -140   1100       C  
ATOM    753  CG  LYS A  91      30.213  90.994  13.845  1.00 86.69           C  
ANISOU  753  CG  LYS A  91    12932  10763   9245    384    -48   1133       C  
ATOM    754  CD  LYS A  91      30.883  92.346  13.562  1.00 88.08           C  
ANISOU  754  CD  LYS A  91    12981  10995   9490    383   -139   1153       C  
ATOM    755  CE  LYS A  91      29.888  93.508  13.566  1.00 88.90           C  
ANISOU  755  CE  LYS A  91    12966  11049   9763    324    -57   1185       C  
ATOM    756  NZ  LYS A  91      29.289  93.765  12.224  1.00 87.57           N  
ANISOU  756  NZ  LYS A  91    12592  10953   9727    264    -81   1257       N  
ATOM    757  N   LYS A  92      28.637  88.035  15.252  1.00 83.52           N  
ANISOU  757  N   LYS A  92    12904  10145   8683    423    242   1050       N  
ATOM    758  CA  LYS A  92      27.735  87.761  16.368  1.00 83.97           C  
ANISOU  758  CA  LYS A  92    13156  10031   8716    417    416   1002       C  
ATOM    759  C   LYS A  92      27.664  86.277  16.717  1.00 85.21           C  
ANISOU  759  C   LYS A  92    13454  10150   8770    463    481    978       C  
ATOM    760  O   LYS A  92      26.969  85.909  17.671  1.00 80.94           O  
ANISOU  760  O   LYS A  92    13105   9457   8190    462    637    934       O  
ATOM    761  CB  LYS A  92      26.319  88.270  16.063  1.00 81.85           C  
ANISOU  761  CB  LYS A  92    12782   9673   8644    358    565    986       C  
ATOM    762  CG  LYS A  92      26.199  89.773  15.892  1.00 83.29           C  
ANISOU  762  CG  LYS A  92    12828   9856   8961    297    528   1008       C  
ATOM    763  CD  LYS A  92      24.779  90.155  15.486  1.00 86.57           C  
ANISOU  763  CD  LYS A  92    13119  10164   9611    231    652    988       C  
ATOM    764  CE  LYS A  92      24.649  91.642  15.177  1.00 88.86           C  
ANISOU  764  CE  LYS A  92    13231  10461  10071    162    598   1022       C  
ATOM    765  NZ  LYS A  92      23.302  91.969  14.629  1.00 86.26           N  
ANISOU  765  NZ  LYS A  92    12754  10020  10002     92    682   1007       N  
ATOM    766  N   TRP A  93      28.347  85.424  15.960  1.00 88.90           N  
ANISOU  766  N   TRP A  93    13823  10746   9209    494    376   1001       N  
ATOM    767  CA  TRP A  93      28.380  83.995  16.220  1.00 88.98           C  
ANISOU  767  CA  TRP A  93    13925  10737   9147    537    424    983       C  
ATOM    768  C   TRP A  93      29.377  83.668  17.329  1.00 89.21           C  
ANISOU  768  C   TRP A  93    14189  10708   8999    571    328    980       C  
ATOM    769  O   TRP A  93      30.223  84.485  17.710  1.00 87.92           O  
ANISOU  769  O   TRP A  93    14084  10549   8775    570    195    985       O  
ATOM    770  CB  TRP A  93      28.756  83.235  14.951  1.00 89.12           C  
ANISOU  770  CB  TRP A  93    13716  10917   9230    537    349    999       C  
ATOM    771  CG  TRP A  93      27.677  83.169  13.925  1.00 86.53           C  
ANISOU  771  CG  TRP A  93    13187  10635   9055    517    455    996       C  
ATOM    772  CD1 TRP A  93      26.366  83.506  14.085  1.00 84.95           C  
ANISOU  772  CD1 TRP A  93    13000  10318   8960    512    618    969       C  
ATOM    773  CD2 TRP A  93      27.822  82.752  12.565  1.00 85.20           C  
ANISOU  773  CD2 TRP A  93    12775  10631   8967    492    398   1010       C  
ATOM    774  NE1 TRP A  93      25.680  83.308  12.911  1.00 84.97           N  
ANISOU  774  NE1 TRP A  93    12783  10397   9105    500    651    969       N  
ATOM    775  CE2 TRP A  93      26.554  82.848  11.961  1.00 83.66           C  
ANISOU  775  CE2 TRP A  93    12460  10416   8911    485    519    998       C  
ATOM    776  CE3 TRP A  93      28.903  82.299  11.800  1.00 78.30           C  
ANISOU  776  CE3 TRP A  93    11772   9907   8070    463    260   1020       C  
ATOM    777  CZ2 TRP A  93      26.337  82.508  10.628  1.00 76.71           C  
ANISOU  777  CZ2 TRP A  93    11347   9677   8122    458    497   1007       C  
ATOM    778  CZ3 TRP A  93      28.685  81.959  10.478  1.00 69.26           C  
ANISOU  778  CZ3 TRP A  93    10394   8904   7017    420    258   1022       C  
ATOM    779  CH2 TRP A  93      27.413  82.066   9.905  1.00 70.20           C  
ANISOU  779  CH2 TRP A  93    10408   9016   7249    421    370   1021       C  
ATOM    780  N   LYS A  94      29.286  82.438  17.831  1.00 93.28           N  
ANISOU  780  N   LYS A  94    14833  11166   9443    606    390    969       N  
ATOM    781  CA  LYS A  94      30.201  81.920  18.838  1.00 99.76           C  
ANISOU  781  CA  LYS A  94    15882  11922  10101    637    282    974       C  
ATOM    782  C   LYS A  94      31.092  80.865  18.197  1.00 99.73           C  
ANISOU  782  C   LYS A  94    15746  12020  10127    653    147    986       C  
ATOM    783  O   LYS A  94      30.600  79.973  17.496  1.00101.05           O  
ANISOU  783  O   LYS A  94    15758  12249  10389    656    241    981       O  
ATOM    784  CB  LYS A  94      29.439  81.321  20.024  1.00105.25           C  
ANISOU  784  CB  LYS A  94    16853  12448  10687    651    456    957       C  
ATOM    785  CG  LYS A  94      28.659  82.337  20.858  1.00110.21           C  
ANISOU  785  CG  LYS A  94    17650  12943  11282    609    595    925       C  
ATOM    786  CD  LYS A  94      29.585  83.301  21.595  1.00113.39           C  
ANISOU  786  CD  LYS A  94    18189  13331  11564    597    435    932       C  
ATOM    787  CE  LYS A  94      28.803  84.417  22.283  1.00113.82           C  
ANISOU  787  CE  LYS A  94    18345  13276  11626    532    582    891       C  
ATOM    788  NZ  LYS A  94      28.127  85.329  21.309  1.00111.29           N  
ANISOU  788  NZ  LYS A  94    17749  13017  11521    492    645    882       N  
ATOM    789  N   TYR A  95      32.400  80.954  18.456  1.00 95.43           N  
ANISOU  789  N   TYR A  95    15256  11481   9523    660    -69    987       N  
ATOM    790  CA  TYR A  95      33.401  80.092  17.833  1.00 91.14           C  
ANISOU  790  CA  TYR A  95    14569  11014   9048    652   -222    979       C  
ATOM    791  C   TYR A  95      34.160  79.345  18.925  1.00 85.40           C  
ANISOU  791  C   TYR A  95    14073  10166   8207    683   -345    985       C  
ATOM    792  O   TYR A  95      35.283  79.726  19.286  1.00 88.78           O  
ANISOU  792  O   TYR A  95    14580  10551   8601    692   -552    967       O  
ATOM    793  CB  TYR A  95      34.355  80.900  16.954  1.00 93.88           C  
ANISOU  793  CB  TYR A  95    14729  11456   9483    619   -386    956       C  
ATOM    794  CG  TYR A  95      33.649  81.689  15.874  1.00 95.35           C  
ANISOU  794  CG  TYR A  95    14704  11757   9769    581   -287    966       C  
ATOM    795  CD1 TYR A  95      33.339  81.108  14.654  1.00 94.68           C  
ANISOU  795  CD1 TYR A  95    14372  11799   9802    535   -232    963       C  
ATOM    796  CD2 TYR A  95      33.282  83.012  16.082  1.00 97.71           C  
ANISOU  796  CD2 TYR A  95    15042  12035  10050    584   -255    977       C  
ATOM    797  CE1 TYR A  95      32.691  81.820  13.669  1.00 96.75           C  
ANISOU  797  CE1 TYR A  95    14457  12157  10145    498   -164    980       C  
ATOM    798  CE2 TYR A  95      32.631  83.733  15.102  1.00 97.63           C  
ANISOU  798  CE2 TYR A  95    14838  12114  10141    545   -185    996       C  
ATOM    799  CZ  TYR A  95      32.338  83.133  13.897  1.00 98.28           C  
ANISOU  799  CZ  TYR A  95    14702  12316  10325    504   -148   1001       C  
ATOM    800  OH  TYR A  95      31.690  83.846  12.915  1.00100.44           O  
ANISOU  800  OH  TYR A  95    14800  12673  10691    461   -100   1027       O  
ATOM    801  N   PRO A  96      33.584  78.273  19.464  1.00 81.17           N  
ANISOU  801  N   PRO A  96    13653   9565   7622    704   -229   1005       N  
ATOM    802  CA  PRO A  96      34.260  77.538  20.535  1.00 90.47           C  
ANISOU  802  CA  PRO A  96    15072  10619   8685    729   -355   1026       C  
ATOM    803  C   PRO A  96      35.431  76.730  20.007  1.00 91.30           C  
ANISOU  803  C   PRO A  96    15010  10763   8916    707   -559   1010       C  
ATOM    804  O   PRO A  96      35.416  76.230  18.880  1.00 86.25           O  
ANISOU  804  O   PRO A  96    14075  10248   8447    668   -523    988       O  
ATOM    805  CB  PRO A  96      33.161  76.620  21.079  1.00 92.64           C  
ANISOU  805  CB  PRO A  96    15478  10821   8901    754   -130   1050       C  
ATOM    806  CG  PRO A  96      32.265  76.394  19.901  1.00 85.84           C  
ANISOU  806  CG  PRO A  96    14321  10085   8208    745     58   1027       C  
ATOM    807  CD  PRO A  96      32.273  77.686  19.129  1.00 81.15           C  
ANISOU  807  CD  PRO A  96    13570   9585   7678    713     25   1007       C  
ATOM    808  N   GLN A  97      36.459  76.606  20.847  1.00 97.09           N  
ANISOU  808  N   GLN A  97    15935  11379   9576    721   -781   1013       N  
ATOM    809  CA  GLN A  97      37.627  75.781  20.538  1.00 94.10           C  
ANISOU  809  CA  GLN A  97    15430  10985   9341    690   -996    986       C  
ATOM    810  C   GLN A  97      37.323  74.343  20.931  1.00 94.07           C  
ANISOU  810  C   GLN A  97    15468  10931   9341    694   -938   1032       C  
ATOM    811  O   GLN A  97      37.483  73.950  22.089  1.00 94.15           O  
ANISOU  811  O   GLN A  97    15767  10797   9208    726  -1016   1078       O  
ATOM    812  CB  GLN A  97      38.860  76.305  21.256  1.00 94.04           C  
ANISOU  812  CB  GLN A  97    15601  10847   9283    710  -1275    958       C  
ATOM    813  CG  GLN A  97      39.320  77.636  20.728  1.00 95.74           C  
ANISOU  813  CG  GLN A  97    15715  11115   9547    711  -1338    896       C  
ATOM    814  CD  GLN A  97      39.883  77.525  19.333  1.00 94.93           C  
ANISOU  814  CD  GLN A  97    15264  11121   9686    642  -1379    828       C  
ATOM    815  OE1 GLN A  97      39.548  78.319  18.453  1.00 98.77           O  
ANISOU  815  OE1 GLN A  97    15578  11729  10223    621  -1274    809       O  
ATOM    816  NE2 GLN A  97      40.752  76.541  19.121  1.00 91.19           N  
ANISOU  816  NE2 GLN A  97    14685  10594   9371    595  -1532    788       N  
ATOM    817  N   VAL A  98      36.876  73.554  19.965  1.00 98.98           N  
ANISOU  817  N   VAL A  98    15802  11677  10131    660   -797   1020       N  
ATOM    818  CA  VAL A  98      36.505  72.164  20.186  1.00107.01           C  
ANISOU  818  CA  VAL A  98    16794  12672  11193    669   -704   1055       C  
ATOM    819  C   VAL A  98      37.674  71.291  19.753  1.00108.53           C  
ANISOU  819  C   VAL A  98    16775  12862  11601    600   -914   1022       C  
ATOM    820  O   VAL A  98      37.934  71.135  18.555  1.00111.41           O  
ANISOU  820  O   VAL A  98    16798  13358  12174    528   -903    959       O  
ATOM    821  CB  VAL A  98      35.224  71.798  19.427  1.00111.41           C  
ANISOU  821  CB  VAL A  98    17146  13360  11824    683   -401   1048       C  
ATOM    822  CG1 VAL A  98      34.851  70.352  19.697  1.00115.31           C  
ANISOU  822  CG1 VAL A  98    17605  13827  12380    708   -289   1077       C  
ATOM    823  CG2 VAL A  98      34.088  72.737  19.816  1.00113.86           C  
ANISOU  823  CG2 VAL A  98    17649  13642  11970    734   -204   1061       C  
ATOM    824  N   ASN A  99      38.391  70.736  20.731  1.00108.57           N  
ANISOU  824  N   ASN A  99    16985  12705  11563    610  -1110   1058       N  
ATOM    825  CA  ASN A  99      39.475  69.783  20.488  1.00111.68           C  
ANISOU  825  CA  ASN A  99    17195  13051  12189    537  -1319   1026       C  
ATOM    826  C   ASN A  99      40.554  70.380  19.583  1.00104.75           C  
ANISOU  826  C   ASN A  99    16090  12204  11504    455  -1499    919       C  
ATOM    827  O   ASN A  99      40.918  69.813  18.551  1.00103.35           O  
ANISOU  827  O   ASN A  99    15566  12115  11585    358  -1494    850       O  
ATOM    828  CB  ASN A  99      38.929  68.476  19.904  1.00120.30           C  
ANISOU  828  CB  ASN A  99    18004  14244  13459    507  -1138   1034       C  
ATOM    829  CG  ASN A  99      39.879  67.309  20.097  1.00128.76           C  
ANISOU  829  CG  ASN A  99    18969  15215  14738    442  -1341   1032       C  
ATOM    830  OD1 ASN A  99      40.867  67.411  20.824  1.00136.59           O  
ANISOU  830  OD1 ASN A  99    20151  16031  15714    432  -1624   1038       O  
ATOM    831  ND2 ASN A  99      39.584  66.191  19.442  1.00128.74           N  
ANISOU  831  ND2 ASN A  99    18647  15317  14953    395  -1200   1017       N  
ATOM    832  N   GLY A 100      41.072  71.541  19.981  1.00100.95           N  
ANISOU  832  N   GLY A 100    15807  11644  10904    490  -1647    895       N  
ATOM    833  CA  GLY A 100      42.121  72.206  19.238  1.00 96.94           C  
ANISOU  833  CA  GLY A 100    15129  11133  10570    429  -1812    783       C  
ATOM    834  C   GLY A 100      41.697  72.835  17.933  1.00 99.42           C  
ANISOU  834  C   GLY A 100    15176  11641  10959    381  -1633    732       C  
ATOM    835  O   GLY A 100      42.498  73.557  17.328  1.00103.89           O  
ANISOU  835  O   GLY A 100    15634  12202  11638    335  -1742    639       O  
ATOM    836  N   LEU A 101      40.475  72.587  17.472  1.00 98.65           N  
ANISOU  836  N   LEU A 101    14972  11701  10809    390  -1364    783       N  
ATOM    837  CA  LEU A 101      39.956  73.166  16.244  1.00 95.58           C  
ANISOU  837  CA  LEU A 101    14347  11496  10472    346  -1198    749       C  
ATOM    838  C   LEU A 101      38.911  74.225  16.571  1.00 92.35           C  
ANISOU  838  C   LEU A 101    14121  11127   9839    435  -1044    810       C  
ATOM    839  O   LEU A 101      38.343  74.254  17.666  1.00 94.86           O  
ANISOU  839  O   LEU A 101    14715  11355   9972    519   -994    878       O  
ATOM    840  CB  LEU A 101      39.348  72.089  15.340  1.00 94.94           C  
ANISOU  840  CB  LEU A 101    13963  11566  10543    281  -1016    742       C  
ATOM    841  CG  LEU A 101      40.278  70.960  14.891  1.00 95.29           C  
ANISOU  841  CG  LEU A 101    13759  11591  10856    165  -1131    670       C  
ATOM    842  CD1 LEU A 101      39.484  69.863  14.201  1.00 91.71           C  
ANISOU  842  CD1 LEU A 101    13028  11292  10524    126   -915    675       C  
ATOM    843  CD2 LEU A 101      41.373  71.492  13.975  1.00 95.71           C  
ANISOU  843  CD2 LEU A 101    13631  11648  11085     44  -1270    552       C  
ATOM    844  N   THR A 102      38.656  75.094  15.598  1.00 86.66           N  
ANISOU  844  N   THR A 102    13246  10534   9149    402   -964    783       N  
ATOM    845  CA  THR A 102      37.701  76.187  15.744  1.00 81.21           C  
ANISOU  845  CA  THR A 102    12673   9880   8301    465   -828    830       C  
ATOM    846  C   THR A 102      36.391  75.786  15.073  1.00 80.09           C  
ANISOU  846  C   THR A 102    12376   9872   8184    461   -580    859       C  
ATOM    847  O   THR A 102      36.341  75.610  13.851  1.00 72.94           O  
ANISOU  847  O   THR A 102    11193   9107   7412    387   -529    825       O  
ATOM    848  CB  THR A 102      38.248  77.477  15.139  1.00 75.78           C  
ANISOU  848  CB  THR A 102    11921   9232   7641    438   -912    787       C  
ATOM    849  OG1 THR A 102      39.485  77.825  15.775  1.00 75.97           O  
ANISOU  849  OG1 THR A 102    12081   9115   7667    457  -1140    739       O  
ATOM    850  CG2 THR A 102      37.253  78.600  15.343  1.00 74.84           C  
ANISOU  850  CG2 THR A 102    11907   9140   7388    494   -778    839       C  
ATOM    851  N   SER A 103      35.343  75.614  15.873  1.00 83.57           N  
ANISOU  851  N   SER A 103    12998  10254   8501    537   -423    912       N  
ATOM    852  CA  SER A 103      34.013  75.282  15.388  1.00 80.26           C  
ANISOU  852  CA  SER A 103    12463   9918   8114    557   -179    925       C  
ATOM    853  C   SER A 103      33.099  76.510  15.476  1.00 79.89           C  
ANISOU  853  C   SER A 103    12515   9858   7980    588    -69    945       C  
ATOM    854  O   SER A 103      33.550  77.630  15.740  1.00 75.89           O  
ANISOU  854  O   SER A 103    12115   9314   7405    584   -179    950       O  
ATOM    855  CB  SER A 103      33.461  74.093  16.174  1.00 71.91           C  
ANISOU  855  CB  SER A 103    11516   8779   7027    615    -56    947       C  
ATOM    856  OG  SER A 103      32.229  73.661  15.630  1.00 68.20           O  
ANISOU  856  OG  SER A 103    10901   8382   6631    643    185    936       O  
ATOM    857  N   ILE A 104      31.805  76.304  15.227  1.00 80.16           N  
ANISOU  857  N   ILE A 104    12493   9915   8048    618    151    946       N  
ATOM    858  CA  ILE A 104      30.809  77.371  15.298  1.00 80.72           C  
ANISOU  858  CA  ILE A 104    12636   9949   8087    636    270    954       C  
ATOM    859  C   ILE A 104      29.586  76.858  16.050  1.00 82.81           C  
ANISOU  859  C   ILE A 104    13052  10089   8324    699    499    944       C  
ATOM    860  O   ILE A 104      29.064  75.784  15.733  1.00 84.55           O  
ANISOU  860  O   ILE A 104    13153  10340   8631    730    632    921       O  
ATOM    861  CB  ILE A 104      30.395  77.891  13.905  1.00 79.49           C  
ANISOU  861  CB  ILE A 104    12206   9941   8057    588    297    944       C  
ATOM    862  CG1 ILE A 104      31.617  78.191  13.036  1.00 79.36           C  
ANISOU  862  CG1 ILE A 104    12024  10047   8083    512    100    939       C  
ATOM    863  CG2 ILE A 104      29.561  79.151  14.035  1.00 75.48           C  
ANISOU  863  CG2 ILE A 104    11771   9372   7535    592    368    957       C  
ATOM    864  CD1 ILE A 104      31.256  78.577  11.619  1.00 75.30           C  
ANISOU  864  CD1 ILE A 104    11253   9685   7673    450    123    936       C  
ATOM    865  N   LYS A 105      29.151  77.613  17.061  1.00 82.74           N  
ANISOU  865  N   LYS A 105    13301   9933   8203    715    558    948       N  
ATOM    866  CA  LYS A 105      27.899  77.325  17.755  1.00 84.03           C  
ANISOU  866  CA  LYS A 105    13623   9947   8357    756    803    917       C  
ATOM    867  C   LYS A 105      26.713  77.463  16.805  1.00 82.04           C  
ANISOU  867  C   LYS A 105    13154   9733   8283    761    971    873       C  
ATOM    868  O   LYS A 105      26.650  78.395  15.999  1.00 84.76           O  
ANISOU  868  O   LYS A 105    13340  10161   8705    718    905    881       O  
ATOM    869  CB  LYS A 105      27.723  78.256  18.956  1.00 89.37           C  
ANISOU  869  CB  LYS A 105    14604  10460   8893    738    829    917       C  
ATOM    870  CG  LYS A 105      26.453  77.994  19.762  1.00 90.62           C  
ANISOU  870  CG  LYS A 105    14959  10429   9044    758   1100    864       C  
ATOM    871  CD  LYS A 105      26.207  79.094  20.779  1.00 97.20           C  
ANISOU  871  CD  LYS A 105    16046  11114   9773    705   1141    847       C  
ATOM    872  CE  LYS A 105      24.881  78.894  21.501  1.00103.06           C  
ANISOU  872  CE  LYS A 105    16972  11644  10542    700   1437    770       C  
ATOM    873  NZ  LYS A 105      24.548  80.044  22.395  1.00107.90           N  
ANISOU  873  NZ  LYS A 105    17793  12111  11093    618   1501    733       N  
ATOM    874  N   TRP A 106      25.781  76.512  16.888  1.00 81.36           N  
ANISOU  874  N   TRP A 106    13060   9579   8275    819   1185    825       N  
ATOM    875  CA  TRP A 106      24.698  76.431  15.916  1.00 89.78           C  
ANISOU  875  CA  TRP A 106    13896  10680   9537    841   1332    769       C  
ATOM    876  C   TRP A 106      23.900  77.735  15.907  1.00 92.38           C  
ANISOU  876  C   TRP A 106    14261  10909   9928    799   1381    745       C  
ATOM    877  O   TRP A 106      23.444  78.208  16.954  1.00 94.29           O  
ANISOU  877  O   TRP A 106    14751  10962  10114    786   1486    716       O  
ATOM    878  CB  TRP A 106      23.794  75.234  16.245  1.00101.46           C  
ANISOU  878  CB  TRP A 106    15404  12053  11092    927   1580    701       C  
ATOM    879  CG  TRP A 106      22.738  75.464  17.307  1.00118.54           C  
ANISOU  879  CG  TRP A 106    17836  13957  13246    949   1806    634       C  
ATOM    880  CD1 TRP A 106      22.936  75.713  18.637  1.00124.35           C  
ANISOU  880  CD1 TRP A 106    18913  14530  13802    924   1828    648       C  
ATOM    881  CD2 TRP A 106      21.315  75.327  17.136  1.00125.21           C  
ANISOU  881  CD2 TRP A 106    18633  14659  14284    998   2061    524       C  
ATOM    882  NE1 TRP A 106      21.724  75.823  19.285  1.00125.73           N  
ANISOU  882  NE1 TRP A 106    19258  14472  14043    934   2088    552       N  
ATOM    883  CE2 TRP A 106      20.716  75.576  18.390  1.00127.18           C  
ANISOU  883  CE2 TRP A 106    19204  14650  14468    984   2236    469       C  
ATOM    884  CE3 TRP A 106      20.491  75.043  16.039  1.00124.82           C  
ANISOU  884  CE3 TRP A 106    18301  14662  14463   1047   2154    456       C  
ATOM    885  CZ2 TRP A 106      19.329  75.551  18.575  1.00126.03           C  
ANISOU  885  CZ2 TRP A 106    19102  14281  14502   1014   2510    337       C  
ATOM    886  CZ3 TRP A 106      19.116  75.019  16.226  1.00123.65           C  
ANISOU  886  CZ3 TRP A 106    18192  14294  14495   1094   2409    330       C  
ATOM    887  CH2 TRP A 106      18.550  75.272  17.483  1.00123.76           C  
ANISOU  887  CH2 TRP A 106    18526  14035  14462   1075   2589    266       C  
ATOM    888  N   ALA A 107      23.759  78.328  14.718  1.00 85.10           N  
ANISOU  888  N   ALA A 107    13091  10114   9130    764   1300    756       N  
ATOM    889  CA  ALA A 107      23.006  79.565  14.540  1.00 82.73           C  
ANISOU  889  CA  ALA A 107    12771   9730   8932    717   1322    741       C  
ATOM    890  C   ALA A 107      22.812  79.876  13.064  1.00 90.15           C  
ANISOU  890  C   ALA A 107    13413  10825  10013    690   1233    759       C  
ATOM    891  O   ALA A 107      23.771  79.834  12.290  1.00 95.75           O  
ANISOU  891  O   ALA A 107    13980  11733  10667    658   1059    819       O  
ATOM    892  CB  ALA A 107      23.713  80.744  15.210  1.00 78.09           C  
ANISOU  892  CB  ALA A 107    12339   9113   8219    652   1189    792       C  
ATOM    893  N   ASP A 108      21.583  80.210  12.670  1.00 88.96           N  
ANISOU  893  N   ASP A 108    13177  10571  10053    695   1347    702       N  
ATOM    894  CA  ASP A 108      21.286  80.615  11.298  1.00 83.74           C  
ANISOU  894  CA  ASP A 108    12257  10034   9525    663   1250    725       C  
ATOM    895  C   ASP A 108      21.671  79.516  10.311  1.00 82.40           C  
ANISOU  895  C   ASP A 108    11883  10072   9352    693   1215    729       C  
ATOM    896  O   ASP A 108      22.156  79.787   9.209  1.00 85.36           O  
ANISOU  896  O   ASP A 108    12077  10634   9722    635   1059    785       O  
ATOM    897  CB  ASP A 108      21.990  81.930  10.941  1.00 84.35           C  
ANISOU  897  CB  ASP A 108    12300  10203   9547    571   1042    818       C  
ATOM    898  CG  ASP A 108      21.682  83.056  11.920  1.00 86.44           C  
ANISOU  898  CG  ASP A 108    12734  10280   9829    529   1077    812       C  
ATOM    899  OD1 ASP A 108      20.531  83.136  12.402  1.00 88.74           O  
ANISOU  899  OD1 ASP A 108    13090  10358  10268    538   1248    728       O  
ATOM    900  OD2 ASP A 108      22.596  83.863  12.206  1.00 82.48           O  
ANISOU  900  OD2 ASP A 108    12292   9836   9210    482    941    877       O  
ATOM    901  N   ASN A 109      21.455  78.263  10.712  1.00 75.88           N  
ANISOU  901  N   ASN A 109    11083   9211   8535    776   1372    665       N  
ATOM    902  CA  ASN A 109      21.747  77.105   9.868  1.00 75.03           C  
ANISOU  902  CA  ASN A 109    10760   9291   8456    805   1375    650       C  
ATOM    903  C   ASN A 109      23.213  77.080   9.420  1.00 70.38           C  
ANISOU  903  C   ASN A 109    10098   8917   7727    723   1167    731       C  
ATOM    904  O   ASN A 109      23.525  76.726   8.281  1.00 68.68           O  
ANISOU  904  O   ASN A 109     9651   8895   7551    679   1096    737       O  
ATOM    905  CB  ASN A 109      20.805  77.049   8.659  1.00 80.28           C  
ANISOU  905  CB  ASN A 109    11184  10012   9309    821   1411    603       C  
ATOM    906  CG  ASN A 109      19.345  76.857   9.055  1.00 80.38           C  
ANISOU  906  CG  ASN A 109    11241   9789   9511    917   1634    488       C  
ATOM    907  OD1 ASN A 109      19.029  76.027   9.910  1.00 80.81           O  
ANISOU  907  OD1 ASN A 109    11409   9716   9579   1003   1824    418       O  
ATOM    908  ND2 ASN A 109      18.447  77.591   8.400  1.00 78.41           N  
ANISOU  908  ND2 ASN A 109    10898   9470   9424    901   1611    462       N  
ATOM    909  N   ASN A 110      24.129  77.440  10.322  1.00 68.50           N  
ANISOU  909  N   ASN A 110    10059   8634   7334    696   1074    780       N  
ATOM    910  CA  ASN A 110      25.547  77.514   9.985  1.00 70.18           C  
ANISOU  910  CA  ASN A 110    10221   9002   7441    619    874    836       C  
ATOM    911  C   ASN A 110      26.271  76.175  10.114  1.00 72.70           C  
ANISOU  911  C   ASN A 110    10484   9396   7744    633    881    815       C  
ATOM    912  O   ASN A 110      27.504  76.147  10.056  1.00 73.24           O  
ANISOU  912  O   ASN A 110    10542   9543   7744    569    721    842       O  
ATOM    913  CB  ASN A 110      26.249  78.555  10.862  1.00 68.34           C  
ANISOU  913  CB  ASN A 110    10212   8680   7074    591    752    886       C  
ATOM    914  CG  ASN A 110      26.164  78.226  12.340  1.00 80.90           C  
ANISOU  914  CG  ASN A 110    12075  10091   8574    654    844    870       C  
ATOM    915  OD1 ASN A 110      25.777  77.121  12.726  1.00 87.28           O  
ANISOU  915  OD1 ASN A 110    12909  10848   9405    717    983    830       O  
ATOM    916  ND2 ASN A 110      26.505  79.194  13.178  1.00 82.98           N  
ANISOU  916  ND2 ASN A 110    12540  10254   8733    636    773    900       N  
ATOM    917  N   CYS A 111      25.537  75.074  10.284  1.00 71.06           N  
ANISOU  917  N   CYS A 111    10227   9152   7622    714   1066    758       N  
ATOM    918  CA  CYS A 111      26.182  73.782  10.486  1.00 71.58           C  
ANISOU  918  CA  CYS A 111    10227   9274   7695    728   1082    741       C  
ATOM    919  C   CYS A 111      27.060  73.397   9.298  1.00 73.02           C  
ANISOU  919  C   CYS A 111    10128   9678   7937    625    958    737       C  
ATOM    920  O   CYS A 111      28.154  72.849   9.483  1.00 77.46           O  
ANISOU  920  O   CYS A 111    10669  10282   8479    574    854    745       O  
ATOM    921  CB  CYS A 111      25.125  72.713  10.761  1.00 78.29           C  
ANISOU  921  CB  CYS A 111    11039  10052   8656    841   1329    673       C  
ATOM    922  SG  CYS A 111      23.987  72.398   9.403  1.00 85.93           S  
ANISOU  922  SG  CYS A 111    11685  11135   9828    874   1468    595       S  
ATOM    923  N   TYR A 112      26.607  73.679   8.071  1.00 69.77           N  
ANISOU  923  N   TYR A 112     9502   9399   7609    581    965    719       N  
ATOM    924  CA  TYR A 112      27.428  73.354   6.907  1.00 68.34           C  
ANISOU  924  CA  TYR A 112     9065   9426   7477    457    862    705       C  
ATOM    925  C   TYR A 112      28.683  74.218   6.849  1.00 70.05           C  
ANISOU  925  C   TYR A 112     9364   9661   7589    346    645    752       C  
ATOM    926  O   TYR A 112      29.739  73.744   6.410  1.00 61.12           O  
ANISOU  926  O   TYR A 112     8102   8630   6493    242    553    726       O  
ATOM    927  CB  TYR A 112      26.609  73.486   5.616  1.00 65.99           C  
ANISOU  927  CB  TYR A 112     8545   9259   7270    431    915    678       C  
ATOM    928  CG  TYR A 112      26.370  74.906   5.157  1.00 70.31           C  
ANISOU  928  CG  TYR A 112     9168   9794   7754    385    805    735       C  
ATOM    929  CD1 TYR A 112      27.181  75.489   4.192  1.00 74.07           C  
ANISOU  929  CD1 TYR A 112     9552  10409   8184    242    647    765       C  
ATOM    930  CD2 TYR A 112      25.335  75.666   5.689  1.00 74.99           C  
ANISOU  930  CD2 TYR A 112     9920  10221   8352    473    865    752       C  
ATOM    931  CE1 TYR A 112      26.972  76.797   3.770  1.00 79.64           C  
ANISOU  931  CE1 TYR A 112    10322  11100   8836    201    545    827       C  
ATOM    932  CE2 TYR A 112      25.114  76.971   5.271  1.00 78.25           C  
ANISOU  932  CE2 TYR A 112    10378  10616   8735    423    758    809       C  
ATOM    933  CZ  TYR A 112      25.938  77.532   4.312  1.00 80.86           C  
ANISOU  933  CZ  TYR A 112    10616  11099   9009    293    595    854       C  
ATOM    934  OH  TYR A 112      25.731  78.828   3.892  1.00 81.55           O  
ANISOU  934  OH  TYR A 112    10745  11170   9072    245    488    919       O  
ATOM    935  N   LEU A 113      28.595  75.478   7.288  1.00 72.92           N  
ANISOU  935  N   LEU A 113     9933   9921   7853    362    571    806       N  
ATOM    936  CA  LEU A 113      29.797  76.298   7.396  1.00 70.50           C  
ANISOU  936  CA  LEU A 113     9721   9606   7459    285    380    838       C  
ATOM    937  C   LEU A 113      30.735  75.752   8.457  1.00 70.93           C  
ANISOU  937  C   LEU A 113     9918   9563   7470    306    314    829       C  
ATOM    938  O   LEU A 113      31.952  75.692   8.245  1.00 70.88           O  
ANISOU  938  O   LEU A 113     9865   9591   7475    220    170    808       O  
ATOM    939  CB  LEU A 113      29.437  77.748   7.716  1.00 72.97           C  
ANISOU  939  CB  LEU A 113    10205   9827   7695    310    334    894       C  
ATOM    940  CG  LEU A 113      29.245  78.712   6.551  1.00 77.02           C  
ANISOU  940  CG  LEU A 113    10594  10442   8226    231    271    926       C  
ATOM    941  CD1 LEU A 113      28.846  80.080   7.077  1.00 82.49           C  
ANISOU  941  CD1 LEU A 113    11452  11018   8872    266    239    981       C  
ATOM    942  CD2 LEU A 113      30.526  78.811   5.730  1.00 71.68           C  
ANISOU  942  CD2 LEU A 113     9808   9888   7539    104    128    912       C  
ATOM    943  N   ALA A 114      30.186  75.356   9.610  1.00 68.39           N  
ANISOU  943  N   ALA A 114     9779   9101   7106    416    414    838       N  
ATOM    944  CA  ALA A 114      31.018  74.812  10.677  1.00 63.74           C  
ANISOU  944  CA  ALA A 114     9350   8405   6463    439    339    841       C  
ATOM    945  C   ALA A 114      31.760  73.568  10.207  1.00 66.03           C  
ANISOU  945  C   ALA A 114     9425   8789   6875    374    306    795       C  
ATOM    946  O   ALA A 114      32.966  73.427  10.448  1.00 71.45           O  
ANISOU  946  O   ALA A 114    10136   9441   7568    315    141    783       O  
ATOM    947  CB  ALA A 114      30.157  74.506  11.902  1.00 56.04           C  
ANISOU  947  CB  ALA A 114     8607   7269   5418    556    484    857       C  
ATOM    948  N   THR A 115      31.059  72.666   9.514  1.00 56.09           N  
ANISOU  948  N   THR A 115     7935   7641   5738    378    463    758       N  
ATOM    949  CA  THR A 115      31.713  71.474   8.985  1.00 59.07           C  
ANISOU  949  CA  THR A 115     8058   8122   6263    298    452    705       C  
ATOM    950  C   THR A 115      32.812  71.851   7.999  1.00 57.66           C  
ANISOU  950  C   THR A 115     7719   8050   6140    136    292    668       C  
ATOM    951  O   THR A 115      33.918  71.301   8.051  1.00 60.18           O  
ANISOU  951  O   THR A 115     7965   8354   6548     48    176    628       O  
ATOM    952  CB  THR A 115      30.683  70.558   8.318  1.00 69.55           C  
ANISOU  952  CB  THR A 115     9139   9567   7719    336    665    661       C  
ATOM    953  OG1 THR A 115      29.714  70.130   9.284  1.00 71.51           O  
ANISOU  953  OG1 THR A 115     9545   9688   7940    489    832    676       O  
ATOM    954  CG2 THR A 115      31.364  69.328   7.723  1.00 73.11           C  
ANISOU  954  CG2 THR A 115     9286  10142   8351    236    666    597       C  
ATOM    955  N   ALA A 116      32.531  72.800   7.103  1.00 56.83           N  
ANISOU  955  N   ALA A 116     7562   8034   5996     87    281    676       N  
ATOM    956  CA  ALA A 116      33.535  73.226   6.134  1.00 51.76           C  
ANISOU  956  CA  ALA A 116     6790   7482   5396    -75    150    635       C  
ATOM    957  C   ALA A 116      34.711  73.915   6.810  1.00 53.77           C  
ANISOU  957  C   ALA A 116     7241   7597   5592    -94    -41    639       C  
ATOM    958  O   ALA A 116      35.866  73.701   6.421  1.00 57.52           O  
ANISOU  958  O   ALA A 116     7613   8076   6167   -220   -153    569       O  
ATOM    959  CB  ALA A 116      32.903  74.142   5.087  1.00 48.52           C  
ANISOU  959  CB  ALA A 116     6315   7184   4936   -114    180    659       C  
ATOM    960  N   LEU A 117      34.440  74.762   7.807  1.00 51.78           N  
ANISOU  960  N   LEU A 117     7264   7211   5198     25    -75    704       N  
ATOM    961  CA  LEU A 117      35.524  75.445   8.511  1.00 52.82           C  
ANISOU  961  CA  LEU A 117     7586   7208   5277     27   -256    700       C  
ATOM    962  C   LEU A 117      36.416  74.445   9.236  1.00 59.71           C  
ANISOU  962  C   LEU A 117     8484   7976   6228     17   -349    659       C  
ATOM    963  O   LEU A 117      37.644  74.599   9.259  1.00 66.60           O  
ANISOU  963  O   LEU A 117     9364   8775   7165    -53   -517    601       O  
ATOM    964  CB  LEU A 117      34.955  76.472   9.491  1.00 57.60           C  
ANISOU  964  CB  LEU A 117     8466   7699   5720    153   -250    773       C  
ATOM    965  CG  LEU A 117      35.969  77.205  10.373  1.00 60.23           C  
ANISOU  965  CG  LEU A 117     9013   7886   5985    183   -426    768       C  
ATOM    966  CD1 LEU A 117      36.866  78.090   9.525  1.00 66.27           C  
ANISOU  966  CD1 LEU A 117     9687   8693   6799     93   -542    723       C  
ATOM    967  CD2 LEU A 117      35.269  78.020  11.454  1.00 54.75           C  
ANISOU  967  CD2 LEU A 117     8579   7086   5138    300   -384    834       C  
ATOM    968  N   LEU A 118      35.818  73.407   9.830  1.00 56.15           N  
ANISOU  968  N   LEU A 118     8044   7502   5789     87   -245    683       N  
ATOM    969  CA  LEU A 118      36.624  72.378  10.475  1.00 56.85           C  
ANISOU  969  CA  LEU A 118     8137   7494   5971     70   -340    655       C  
ATOM    970  C   LEU A 118      37.437  71.603   9.451  1.00 61.10           C  
ANISOU  970  C   LEU A 118     8356   8123   6735    -95   -379    558       C  
ATOM    971  O   LEU A 118      38.591  71.240   9.710  1.00 65.96           O  
ANISOU  971  O   LEU A 118     8958   8632   7470   -167   -544    502       O  
ATOM    972  CB  LEU A 118      35.730  71.428  11.275  1.00 58.80           C  
ANISOU  972  CB  LEU A 118     8454   7701   6186    180   -194    705       C  
ATOM    973  CG  LEU A 118      35.043  72.026  12.503  1.00 63.44           C  
ANISOU  973  CG  LEU A 118     9392   8151   6562    322   -154    783       C  
ATOM    974  CD1 LEU A 118      33.976  71.086  13.021  1.00 62.42           C  
ANISOU  974  CD1 LEU A 118     9294   8001   6423    418     50    813       C  
ATOM    975  CD2 LEU A 118      36.075  72.345  13.595  1.00 61.70           C  
ANISOU  975  CD2 LEU A 118     9434   7753   6255    339   -373    800       C  
ATOM    976  N   THR A 119      36.862  71.362   8.272  1.00 62.79           N  
ANISOU  976  N   THR A 119     8310   8523   7024   -168   -234    528       N  
ATOM    977  CA  THR A 119      37.586  70.640   7.231  1.00 63.51           C  
ANISOU  977  CA  THR A 119     8082   8714   7333   -351   -246    424       C  
ATOM    978  C   THR A 119      38.766  71.458   6.722  1.00 66.10           C  
ANISOU  978  C   THR A 119     8417   8993   7704   -483   -410    350       C  
ATOM    979  O   THR A 119      39.853  70.918   6.482  1.00 61.61           O  
ANISOU  979  O   THR A 119     7706   8370   7334   -624   -508    248       O  
ATOM    980  CB  THR A 119      36.635  70.308   6.083  1.00 59.99           C  
ANISOU  980  CB  THR A 119     7381   8486   6928   -396    -50    408       C  
ATOM    981  OG1 THR A 119      35.538  69.532   6.578  1.00 67.46           O  
ANISOU  981  OG1 THR A 119     8316   9454   7861   -257    116    457       O  
ATOM    982  CG2 THR A 119      37.356  69.525   5.002  1.00 51.47           C  
ANISOU  982  CG2 THR A 119     5961   7519   6076   -607    -42    290       C  
ATOM    983  N   LEU A 120      38.574  72.771   6.577  1.00 69.20           N  
ANISOU  983  N   LEU A 120     8971   9387   7935   -439   -435    393       N  
ATOM    984  CA  LEU A 120      39.635  73.629   6.069  1.00 66.77           C  
ANISOU  984  CA  LEU A 120     8675   9028   7664   -548   -566    319       C  
ATOM    985  C   LEU A 120      40.825  73.680   7.018  1.00 64.74           C  
ANISOU  985  C   LEU A 120     8574   8551   7475   -527   -765    269       C  
ATOM    986  O   LEU A 120      41.954  73.940   6.581  1.00 63.41           O  
ANISOU  986  O   LEU A 120     8347   8304   7441   -650   -875    156       O  
ATOM    987  CB  LEU A 120      39.087  75.029   5.811  1.00 66.32           C  
ANISOU  987  CB  LEU A 120     8758   9016   7423   -483   -545    391       C  
ATOM    988  CG  LEU A 120      38.118  75.167   4.640  1.00 61.82           C  
ANISOU  988  CG  LEU A 120     8027   8650   6811   -539   -395    423       C  
ATOM    989  CD1 LEU A 120      37.399  76.493   4.738  1.00 61.43           C  
ANISOU  989  CD1 LEU A 120     8151   8604   6585   -435   -386    522       C  
ATOM    990  CD2 LEU A 120      38.866  75.061   3.324  1.00 60.91           C  
ANISOU  990  CD2 LEU A 120     7694   8626   6822   -756   -401    316       C  
ATOM    991  N   GLN A 121      40.603  73.445   8.312  1.00 70.97           N  
ANISOU  991  N   GLN A 121     9382   8497   9085   -556    -36    468       N  
ATOM    992  CA  GLN A 121      41.695  73.440   9.282  1.00 66.28           C  
ANISOU  992  CA  GLN A 121     8859   7871   8454   -597    -87    526       C  
ATOM    993  C   GLN A 121      42.461  72.122   9.314  1.00 65.76           C  
ANISOU  993  C   GLN A 121     8646   7795   8544   -626   -122    508       C  
ATOM    994  O   GLN A 121      43.420  72.003  10.085  1.00 68.23           O  
ANISOU  994  O   GLN A 121     9002   8076   8847   -663   -172    552       O  
ATOM    995  CB  GLN A 121      41.163  73.751  10.683  1.00 65.34           C  
ANISOU  995  CB  GLN A 121     8885   7681   8258   -554    -54    628       C  
ATOM    996  CG  GLN A 121      40.477  75.104  10.792  1.00 69.39           C  
ANISOU  996  CG  GLN A 121     9560   8198   8606   -522    -24    652       C  
ATOM    997  CD  GLN A 121      39.833  75.336  12.148  1.00 70.35           C  
ANISOU  997  CD  GLN A 121     9821   8249   8659   -467     23    750       C  
ATOM    998  OE1 GLN A 121      40.519  75.617  13.131  1.00 75.51           O  
ANISOU  998  OE1 GLN A 121    10599   8859   9234   -488    -16    814       O  
ATOM    999  NE2 GLN A 121      38.507  75.229  12.205  1.00 64.14           N  
ANISOU  999  NE2 GLN A 121     9017   7449   7903   -396    106    763       N  
ATOM   1000  N   GLN A 122      42.071  71.132   8.512  1.00 63.28           N  
ANISOU 1000  N   GLN A 122     8166   7502   8377   -607   -102    445       N  
ATOM   1001  CA  GLN A 122      42.720  69.831   8.535  1.00 62.81           C  
ANISOU 1001  CA  GLN A 122     7964   7428   8473   -627   -136    424       C  
ATOM   1002  C   GLN A 122      43.311  69.405   7.199  1.00 63.81           C  
ANISOU 1002  C   GLN A 122     7948   7619   8679   -659   -165    319       C  
ATOM   1003  O   GLN A 122      43.894  68.318   7.121  1.00 62.33           O  
ANISOU 1003  O   GLN A 122     7635   7423   8623   -673   -196    293       O  
ATOM   1004  CB  GLN A 122      41.736  68.767   9.037  1.00 62.46           C  
ANISOU 1004  CB  GLN A 122     7845   7331   8554   -571    -93    459       C  
ATOM   1005  CG  GLN A 122      41.330  68.979  10.492  1.00 64.94           C  
ANISOU 1005  CG  GLN A 122     8292   7576   8806   -544    -65    569       C  
ATOM   1006  CD  GLN A 122      40.308  67.974  10.989  1.00 71.60           C  
ANISOU 1006  CD  GLN A 122     9065   8370   9769   -490    -15    610       C  
ATOM   1007  OE1 GLN A 122      39.232  67.821  10.413  1.00 76.43           O  
ANISOU 1007  OE1 GLN A 122     9612   8995  10432   -445     35    586       O  
ATOM   1008  NE2 GLN A 122      40.656  67.260  12.050  1.00 78.40           N  
ANISOU 1008  NE2 GLN A 122     9935   9171  10681   -498    -35    674       N  
ATOM   1009  N   ILE A 123      43.186  70.215   6.149  1.00 70.18           N  
ANISOU 1009  N   ILE A 123     8773   8486   9407   -670   -155    258       N  
ATOM   1010  CA  ILE A 123      43.777  69.906   4.852  1.00 70.23           C  
ANISOU 1010  CA  ILE A 123     8660   8555   9469   -701   -177    158       C  
ATOM   1011  C   ILE A 123      44.712  71.038   4.442  1.00 68.53           C  
ANISOU 1011  C   ILE A 123     8527   8393   9117   -763   -209    139       C  
ATOM   1012  O   ILE A 123      44.464  72.209   4.752  1.00 65.96           O  
ANISOU 1012  O   ILE A 123     8349   8068   8645   -767   -204    181       O  
ATOM   1013  CB  ILE A 123      42.707  69.661   3.767  1.00 69.82           C  
ANISOU 1013  CB  ILE A 123     8531   8525   9471   -659   -138     90       C  
ATOM   1014  CG1 ILE A 123      41.800  70.877   3.609  1.00 75.81           C  
ANISOU 1014  CG1 ILE A 123     9416   9293  10094   -638   -104    105       C  
ATOM   1015  CG2 ILE A 123      41.882  68.415   4.093  1.00 60.77           C  
ANISOU 1015  CG2 ILE A 123     7281   7327   8481   -605   -117    106       C  
ATOM   1016  CD1 ILE A 123      40.742  70.692   2.544  1.00 75.13           C  
ANISOU 1016  CD1 ILE A 123     9263   9222  10062   -600    -75     41       C  
ATOM   1017  N   GLU A 124      45.803  70.674   3.766  1.00 70.90           N  
ANISOU 1017  N   GLU A 124     8732   8738   9469   -810   -243     78       N  
ATOM   1018  CA  GLU A 124      46.775  71.640   3.271  1.00 76.64           C  
ANISOU 1018  CA  GLU A 124     9514   9522  10084   -875   -273     57       C  
ATOM   1019  C   GLU A 124      46.209  72.365   2.054  1.00 75.02           C  
ANISOU 1019  C   GLU A 124     9329   9374   9800   -874   -245    -11       C  
ATOM   1020  O   GLU A 124      45.900  71.735   1.038  1.00 73.26           O  
ANISOU 1020  O   GLU A 124     8995   9181   9662   -856   -224    -91       O  
ATOM   1021  CB  GLU A 124      48.081  70.934   2.914  1.00 85.76           C  
ANISOU 1021  CB  GLU A 124    10545  10707  11334   -921   -309     12       C  
ATOM   1022  CG  GLU A 124      49.218  71.881   2.558  1.00 94.36           C  
ANISOU 1022  CG  GLU A 124    11684  11851  12320   -995   -343      6       C  
ATOM   1023  CD  GLU A 124      50.478  71.153   2.131  1.00 99.17           C  
ANISOU 1023  CD  GLU A 124    12154  12492  13034  -1035   -370    -43       C  
ATOM   1024  OE1 GLU A 124      50.853  70.160   2.794  1.00 99.35           O  
ANISOU 1024  OE1 GLU A 124    12100  12469  13180  -1024   -394    -22       O  
ATOM   1025  OE2 GLU A 124      51.097  71.580   1.131  1.00 98.95           O  
ANISOU 1025  OE2 GLU A 124    12096  12536  12965  -1079   -366   -101       O  
ATOM   1026  N   LEU A 125      46.088  73.689   2.143  1.00 74.03           N  
ANISOU 1026  N   LEU A 125     9352   9263   9513   -895   -251     21       N  
ATOM   1027  CA  LEU A 125      45.392  74.448   1.112  1.00 69.74           C  
ANISOU 1027  CA  LEU A 125     8850   8762   8888   -890   -228    -34       C  
ATOM   1028  C   LEU A 125      45.900  75.882   1.091  1.00 69.21           C  
ANISOU 1028  C   LEU A 125     8925   8726   8644   -944   -259     -9       C  
ATOM   1029  O   LEU A 125      45.989  76.526   2.140  1.00 65.28           O  
ANISOU 1029  O   LEU A 125     8553   8190   8058   -947   -281     74       O  
ATOM   1030  CB  LEU A 125      43.881  74.425   1.363  1.00 67.93           C  
ANISOU 1030  CB  LEU A 125     8655   8487   8668   -816   -185    -13       C  
ATOM   1031  CG  LEU A 125      42.966  74.703   0.175  1.00 73.76           C  
ANISOU 1031  CG  LEU A 125     9379   9253   9391   -794   -160    -85       C  
ATOM   1032  CD1 LEU A 125      43.097  73.596  -0.865  1.00 74.82           C  
ANISOU 1032  CD1 LEU A 125     9350   9414   9664   -791   -154   -174       C  
ATOM   1033  CD2 LEU A 125      41.527  74.851   0.643  1.00 75.88           C  
ANISOU 1033  CD2 LEU A 125     9701   9470   9660   -724   -121    -44       C  
ATOM   1034  N   LYS A 126      46.205  76.384  -0.104  1.00 74.30           N  
ANISOU 1034  N   LYS A 126     9558   9438   9233   -987   -264    -80       N  
ATOM   1035  CA  LYS A 126      46.666  77.754  -0.288  1.00 77.54           C  
ANISOU 1035  CA  LYS A 126    10100   9885   9478  -1044   -298    -63       C  
ATOM   1036  C   LYS A 126      45.712  78.493  -1.218  1.00 75.22           C  
ANISOU 1036  C   LYS A 126     9865   9615   9100  -1030   -279   -114       C  
ATOM   1037  O   LYS A 126      45.448  78.033  -2.334  1.00 74.12           O  
ANISOU 1037  O   LYS A 126     9633   9509   9020  -1025   -255   -197       O  
ATOM   1038  CB  LYS A 126      48.080  77.782  -0.872  1.00 84.09           C  
ANISOU 1038  CB  LYS A 126    10867  10775  10306  -1123   -327    -96       C  
ATOM   1039  CG  LYS A 126      49.132  77.054  -0.043  1.00 96.70           C  
ANISOU 1039  CG  LYS A 126    12396  12349  11996  -1143   -354    -52       C  
ATOM   1040  CD  LYS A 126      49.305  77.673   1.341  1.00100.62           C  
ANISOU 1040  CD  LYS A 126    13032  12787  12414  -1149   -397     56       C  
ATOM   1041  CE  LYS A 126      50.465  77.033   2.091  1.00 99.23           C  
ANISOU 1041  CE  LYS A 126    12793  12585  12324  -1180   -437     99       C  
ATOM   1042  NZ  LYS A 126      50.256  75.572   2.297  1.00102.67           N  
ANISOU 1042  NZ  LYS A 126    13087  12989  12935  -1132   -409     76       N  
ATOM   1043  N   PHE A 127      45.209  79.637  -0.763  1.00 71.16           N  
ANISOU 1043  N   PHE A 127     9509   9081   8448  -1023   -295    -63       N  
ATOM   1044  CA  PHE A 127      44.261  80.427  -1.537  1.00 68.22           C  
ANISOU 1044  CA  PHE A 127     9208   8723   7990  -1008   -286   -104       C  
ATOM   1045  C   PHE A 127      44.980  81.473  -2.384  1.00 68.14           C  
ANISOU 1045  C   PHE A 127     9265   8777   7849  -1088   -326   -136       C  
ATOM   1046  O   PHE A 127      45.986  82.049  -1.960  1.00 67.80           O  
ANISOU 1046  O   PHE A 127     9284   8750   7729  -1146   -369    -90       O  
ATOM   1047  CB  PHE A 127      43.251  81.120  -0.622  1.00 68.41           C  
ANISOU 1047  CB  PHE A 127     9368   8689   7936   -952   -280    -37       C  
ATOM   1048  CG  PHE A 127      42.239  80.191  -0.007  1.00 68.83           C  
ANISOU 1048  CG  PHE A 127     9358   8682   8110   -868   -229    -14       C  
ATOM   1049  CD1 PHE A 127      41.279  79.573  -0.793  1.00 67.61           C  
ANISOU 1049  CD1 PHE A 127     9108   8524   8055   -823   -192    -75       C  
ATOM   1050  CD2 PHE A 127      42.228  79.964   1.362  1.00 69.39           C  
ANISOU 1050  CD2 PHE A 127     9473   8697   8195   -834   -221     73       C  
ATOM   1051  CE1 PHE A 127      40.341  78.727  -0.228  1.00 69.70           C  
ANISOU 1051  CE1 PHE A 127     9312   8735   8437   -749   -147    -48       C  
ATOM   1052  CE2 PHE A 127      41.290  79.123   1.933  1.00 69.35           C  
ANISOU 1052  CE2 PHE A 127     9411   8639   8300   -760   -170     99       C  
ATOM   1053  CZ  PHE A 127      40.347  78.501   1.138  1.00 70.43           C  
ANISOU 1053  CZ  PHE A 127     9443   8776   8540   -718   -133     40       C  
ATOM   1054  N   ASN A 128      44.451  81.715  -3.590  1.00 68.88           N  
ANISOU 1054  N   ASN A 128     9347   8903   7919  -1093   -315   -214       N  
ATOM   1055  CA  ASN A 128      44.993  82.726  -4.496  1.00 65.73           C  
ANISOU 1055  CA  ASN A 128     9018   8565   7392  -1169   -350   -249       C  
ATOM   1056  C   ASN A 128      44.592  84.141  -4.077  1.00 66.85           C  
ANISOU 1056  C   ASN A 128     9345   8689   7367  -1176   -392   -198       C  
ATOM   1057  O   ASN A 128      45.454  85.031  -4.082  1.00 64.02           O  
ANISOU 1057  O   ASN A 128     9068   8364   6892  -1247   -440   -171       O  
ATOM   1058  CB  ASN A 128      44.571  82.462  -5.945  1.00 65.97           C  
ANISOU 1058  CB  ASN A 128     8980   8631   7453  -1173   -328   -351       C  
ATOM   1059  CG  ASN A 128      45.228  81.228  -6.530  1.00 69.29           C  
ANISOU 1059  CG  ASN A 128     9232   9083   8011  -1182   -296   -410       C  
ATOM   1060  OD1 ASN A 128      46.366  80.895  -6.192  1.00 69.26           O  
ANISOU 1060  OD1 ASN A 128     9172   9105   8040  -1221   -302   -387       O  
ATOM   1061  ND2 ASN A 128      44.517  80.550  -7.426  1.00 67.83           N  
ANISOU 1061  ND2 ASN A 128     8969   8895   7910  -1145   -267   -487       N  
ATOM   1062  N   PRO A 129      43.325  84.424  -3.758  1.00 69.38           N  
ANISOU 1062  N   PRO A 129     9733   8958   7668  -1107   -378   -183       N  
ATOM   1063  CA  PRO A 129      42.980  85.774  -3.283  1.00 66.52           C  
ANISOU 1063  CA  PRO A 129     9553   8576   7147  -1108   -421   -133       C  
ATOM   1064  C   PRO A 129      43.681  86.068  -1.971  1.00 73.15           C  
ANISOU 1064  C   PRO A 129    10472   9387   7934  -1118   -450    -37       C  
ATOM   1065  O   PRO A 129      43.588  85.279  -1.018  1.00 74.63           O  
ANISOU 1065  O   PRO A 129    10613   9530   8214  -1068   -420      9       O  
ATOM   1066  CB  PRO A 129      41.456  85.714  -3.093  1.00 61.94           C  
ANISOU 1066  CB  PRO A 129     8994   7939   6600  -1016   -384   -136       C  
ATOM   1067  CG  PRO A 129      41.014  84.607  -3.945  1.00 70.48           C  
ANISOU 1067  CG  PRO A 129     9921   9029   7830   -991   -340   -210       C  
ATOM   1068  CD  PRO A 129      42.115  83.590  -3.878  1.00 71.98           C  
ANISOU 1068  CD  PRO A 129     9983   9247   8121  -1025   -327   -214       C  
ATOM   1069  N   PRO A 130      44.410  87.182  -1.885  1.00 74.17           N  
ANISOU 1069  N   PRO A 130    10724   9538   7919  -1183   -515     -3       N  
ATOM   1070  CA  PRO A 130      45.067  87.522  -0.612  1.00 68.83           C  
ANISOU 1070  CA  PRO A 130    10140   8825   7186  -1192   -556     92       C  
ATOM   1071  C   PRO A 130      44.094  87.698   0.539  1.00 68.11           C  
ANISOU 1071  C   PRO A 130    10151   8658   7070  -1104   -538    154       C  
ATOM   1072  O   PRO A 130      44.442  87.375   1.679  1.00 63.77           O  
ANISOU 1072  O   PRO A 130     9624   8063   6543  -1085   -541    225       O  
ATOM   1073  CB  PRO A 130      45.811  88.822  -0.940  1.00 64.95           C  
ANISOU 1073  CB  PRO A 130     9774   8371   6533  -1277   -635    108       C  
ATOM   1074  CG  PRO A 130      46.024  88.762  -2.422  1.00 70.94           C  
ANISOU 1074  CG  PRO A 130    10445   9203   7306  -1333   -625     18       C  
ATOM   1075  CD  PRO A 130      44.798  88.093  -2.974  1.00 71.52           C  
ANISOU 1075  CD  PRO A 130    10440   9263   7473  -1260   -559    -49       C  
ATOM   1076  N   ALA A 131      42.882  88.196   0.281  1.00 70.28           N  
ANISOU 1076  N   ALA A 131    10490   8915   7299  -1049   -518    130       N  
ATOM   1077  CA  ALA A 131      41.905  88.334   1.356  1.00 70.51           C  
ANISOU 1077  CA  ALA A 131    10607   8873   7310   -959   -488    187       C  
ATOM   1078  C   ALA A 131      41.569  86.985   1.971  1.00 72.90           C  
ANISOU 1078  C   ALA A 131    10784   9139   7775   -897   -417    204       C  
ATOM   1079  O   ALA A 131      41.410  86.871   3.193  1.00 77.90           O  
ANISOU 1079  O   ALA A 131    11480   9716   8403   -849   -401    278       O  
ATOM   1080  CB  ALA A 131      40.636  89.008   0.837  1.00 73.77           C  
ANISOU 1080  CB  ALA A 131    11084   9276   7669   -909   -474    148       C  
ATOM   1081  N   LEU A 132      41.454  85.949   1.142  1.00 75.85           N  
ANISOU 1081  N   LEU A 132    10986   9543   8292   -898   -375    137       N  
ATOM   1082  CA  LEU A 132      41.146  84.627   1.675  1.00 77.39           C  
ANISOU 1082  CA  LEU A 132    11055   9703   8647   -844   -315    151       C  
ATOM   1083  C   LEU A 132      42.326  84.055   2.448  1.00 77.61           C  
ANISOU 1083  C   LEU A 132    11049   9722   8715   -882   -336    201       C  
ATOM   1084  O   LEU A 132      42.150  83.523   3.548  1.00 77.88           O  
ANISOU 1084  O   LEU A 132    11090   9702   8799   -835   -310    263       O  
ATOM   1085  CB  LEU A 132      40.741  83.687   0.541  1.00 75.56           C  
ANISOU 1085  CB  LEU A 132    10654   9500   8555   -836   -277     64       C  
ATOM   1086  CG  LEU A 132      39.244  83.538   0.300  1.00 72.28           C  
ANISOU 1086  CG  LEU A 132    10217   9053   8194   -757   -227     41       C  
ATOM   1087  CD1 LEU A 132      39.012  82.519  -0.791  1.00 69.55           C  
ANISOU 1087  CD1 LEU A 132     9704   8730   7993   -757   -202    -41       C  
ATOM   1088  CD2 LEU A 132      38.549  83.126   1.585  1.00 74.33           C  
ANISOU 1088  CD2 LEU A 132    10495   9246   8502   -678   -177    118       C  
ATOM   1089  N   GLN A 133      43.535  84.167   1.894  1.00 76.84           N  
ANISOU 1089  N   GLN A 133    10919   9677   8599   -967   -385    177       N  
ATOM   1090  CA  GLN A 133      44.708  83.606   2.556  1.00 75.45           C  
ANISOU 1090  CA  GLN A 133    10699   9493   8475  -1007   -412    220       C  
ATOM   1091  C   GLN A 133      44.991  84.308   3.879  1.00 74.34           C  
ANISOU 1091  C   GLN A 133    10724   9297   8226  -1003   -455    320       C  
ATOM   1092  O   GLN A 133      45.416  83.668   4.847  1.00 79.28           O  
ANISOU 1092  O   GLN A 133    11333   9878   8914   -993   -458    375       O  
ATOM   1093  CB  GLN A 133      45.920  83.681   1.625  1.00 79.28           C  
ANISOU 1093  CB  GLN A 133    11115  10049   8958  -1099   -452    173       C  
ATOM   1094  CG  GLN A 133      47.102  82.826   2.063  1.00 88.83           C  
ANISOU 1094  CG  GLN A 133    12226  11256  10269  -1137   -470    197       C  
ATOM   1095  CD  GLN A 133      46.827  81.328   1.987  1.00100.14           C  
ANISOU 1095  CD  GLN A 133    13485  12677  11886  -1092   -414    160       C  
ATOM   1096  OE1 GLN A 133      45.796  80.892   1.471  1.00103.69           O  
ANISOU 1096  OE1 GLN A 133    13875  13126  12395  -1038   -361    110       O  
ATOM   1097  NE2 GLN A 133      47.755  80.533   2.511  1.00103.34           N  
ANISOU 1097  NE2 GLN A 133    13809  13068  12387  -1115   -432    186       N  
ATOM   1098  N   ASP A 134      44.765  85.623   3.940  1.00 75.68           N  
ANISOU 1098  N   ASP A 134    11060   9464   8233  -1010   -494    343       N  
ATOM   1099  CA  ASP A 134      44.940  86.345   5.196  1.00 77.95           C  
ANISOU 1099  CA  ASP A 134    11522   9690   8404   -997   -538    437       C  
ATOM   1100  C   ASP A 134      43.895  85.909   6.220  1.00 82.78           C  
ANISOU 1100  C   ASP A 134    12170  10232   9052   -899   -474    482       C  
ATOM   1101  O   ASP A 134      44.222  85.638   7.381  1.00 92.46           O  
ANISOU 1101  O   ASP A 134    13449  11399  10281   -884   -485    556       O  
ATOM   1102  CB  ASP A 134      44.865  87.857   4.953  1.00 81.16           C  
ANISOU 1102  CB  ASP A 134    12100  10111   8628  -1023   -597    445       C  
ATOM   1103  CG  ASP A 134      46.005  88.375   4.074  1.00 85.78           C  
ANISOU 1103  CG  ASP A 134    12668  10762   9164  -1128   -666    416       C  
ATOM   1104  OD1 ASP A 134      46.811  87.555   3.582  1.00 84.76           O  
ANISOU 1104  OD1 ASP A 134    12386  10673   9146  -1177   -659    383       O  
ATOM   1105  OD2 ASP A 134      46.086  89.608   3.866  1.00 87.02           O  
ANISOU 1105  OD2 ASP A 134    12962  10930   9170  -1162   -727    427       O  
ATOM   1106  N   ALA A 135      42.633  85.804   5.800  1.00 79.16           N  
ANISOU 1106  N   ALA A 135    11678   9775   8625   -833   -408    441       N  
ATOM   1107  CA  ALA A 135      41.587  85.368   6.718  1.00 78.54           C  
ANISOU 1107  CA  ALA A 135    11620   9633   8588   -739   -338    485       C  
ATOM   1108  C   ALA A 135      41.728  83.895   7.075  1.00 78.46           C  
ANISOU 1108  C   ALA A 135    11456   9604   8752   -724   -293    492       C  
ATOM   1109  O   ALA A 135      41.307  83.481   8.160  1.00 82.66           O  
ANISOU 1109  O   ALA A 135    12022  10075   9310   -667   -253    555       O  
ATOM   1110  CB  ALA A 135      40.212  85.631   6.111  1.00 81.16           C  
ANISOU 1110  CB  ALA A 135    11943   9972   8922   -676   -282    439       C  
ATOM   1111  N   TYR A 136      42.321  83.098   6.184  1.00 81.31           N  
ANISOU 1111  N   TYR A 136    11651  10015   9229   -773   -300    429       N  
ATOM   1112  CA  TYR A 136      42.521  81.679   6.460  1.00 86.23           C  
ANISOU 1112  CA  TYR A 136    12123  10621  10021   -763   -268    430       C  
ATOM   1113  C   TYR A 136      43.447  81.474   7.650  1.00 90.20           C  
ANISOU 1113  C   TYR A 136    12683  11074  10513   -786   -309    509       C  
ATOM   1114  O   TYR A 136      43.176  80.638   8.522  1.00 86.65           O  
ANISOU 1114  O   TYR A 136    12205  10572  10147   -744   -274    554       O  
ATOM   1115  CB  TYR A 136      43.090  80.997   5.215  1.00 90.41           C  
ANISOU 1115  CB  TYR A 136    12479  11215  10657   -814   -277    342       C  
ATOM   1116  CG  TYR A 136      43.119  79.485   5.245  1.00 93.34           C  
ANISOU 1116  CG  TYR A 136    12676  11574  11216   -795   -242    324       C  
ATOM   1117  CD1 TYR A 136      42.373  78.762   6.165  1.00 91.47           C  
ANISOU 1117  CD1 TYR A 136    12423  11275  11055   -729   -194    374       C  
ATOM   1118  CD2 TYR A 136      43.903  78.780   4.341  1.00 97.36           C  
ANISOU 1118  CD2 TYR A 136    13035  12133  11823   -844   -259    255       C  
ATOM   1119  CE1 TYR A 136      42.411  77.379   6.181  1.00 93.81           C  
ANISOU 1119  CE1 TYR A 136    12562  11559  11522   -715   -171    358       C  
ATOM   1120  CE2 TYR A 136      43.946  77.403   4.348  1.00 93.53           C  
ANISOU 1120  CE2 TYR A 136    12394  11635  11507   -826   -235    235       C  
ATOM   1121  CZ  TYR A 136      43.202  76.707   5.267  1.00 93.70           C  
ANISOU 1121  CZ  TYR A 136    12404  11594  11604   -763   -195    287       C  
ATOM   1122  OH  TYR A 136      43.261  75.332   5.262  1.00 94.15           O  
ANISOU 1122  OH  TYR A 136    12307  11637  11830   -748   -180    267       O  
ATOM   1123  N   TYR A 137      44.543  82.232   7.712  1.00 94.67           N  
ANISOU 1123  N   TYR A 137    13335  11654  10980   -856   -388    531       N  
ATOM   1124  CA  TYR A 137      45.458  82.092   8.838  1.00 94.62           C  
ANISOU 1124  CA  TYR A 137    13394  11594  10963   -883   -440    609       C  
ATOM   1125  C   TYR A 137      44.822  82.586  10.130  1.00 95.02           C  
ANISOU 1125  C   TYR A 137    13623  11567  10913   -822   -427    695       C  
ATOM   1126  O   TYR A 137      44.950  81.936  11.174  1.00101.19           O  
ANISOU 1126  O   TYR A 137    14419  12285  11745   -801   -422    754       O  
ATOM   1127  CB  TYR A 137      46.770  82.815   8.545  1.00 94.54           C  
ANISOU 1127  CB  TYR A 137    13428  11616  10876   -975   -532    613       C  
ATOM   1128  CG  TYR A 137      47.602  82.102   7.503  1.00101.33           C  
ANISOU 1128  CG  TYR A 137    14101  12544  11857  -1036   -541    541       C  
ATOM   1129  CD1 TYR A 137      48.596  82.768   6.797  1.00106.78           C  
ANISOU 1129  CD1 TYR A 137    14793  13289  12488  -1119   -602    519       C  
ATOM   1130  CD2 TYR A 137      47.391  80.756   7.225  1.00105.87           C  
ANISOU 1130  CD2 TYR A 137    14496  13125  12604  -1010   -487    496       C  
ATOM   1131  CE1 TYR A 137      49.356  82.113   5.842  1.00109.53           C  
ANISOU 1131  CE1 TYR A 137    14970  13701  12944  -1171   -600    453       C  
ATOM   1132  CE2 TYR A 137      48.143  80.093   6.275  1.00109.22           C  
ANISOU 1132  CE2 TYR A 137    14754  13609  13136  -1059   -492    427       C  
ATOM   1133  CZ  TYR A 137      49.124  80.775   5.586  1.00110.89           C  
ANISOU 1133  CZ  TYR A 137    14971  13878  13285  -1137   -544    405       C  
ATOM   1134  OH  TYR A 137      49.876  80.117   4.639  1.00112.45           O  
ANISOU 1134  OH  TYR A 137    15003  14137  13588  -1182   -541    336       O  
ATOM   1135  N   ARG A 138      44.128  83.729  10.084  1.00 92.82           N  
ANISOU 1135  N   ARG A 138    13487  11288  10491   -790   -422    702       N  
ATOM   1136  CA  ARG A 138      43.445  84.215  11.278  1.00 89.63           C  
ANISOU 1136  CA  ARG A 138    13257  10812   9987   -722   -399    779       C  
ATOM   1137  C   ARG A 138      42.291  83.310  11.671  1.00 88.45           C  
ANISOU 1137  C   ARG A 138    13034  10630   9942   -636   -296    785       C  
ATOM   1138  O   ARG A 138      41.875  83.323  12.833  1.00 84.91           O  
ANISOU 1138  O   ARG A 138    12698  10114   9450   -582   -266    858       O  
ATOM   1139  CB  ARG A 138      42.924  85.635  11.069  1.00 88.84           C  
ANISOU 1139  CB  ARG A 138    13319  10722   9716   -702   -416    777       C  
ATOM   1140  CG  ARG A 138      43.985  86.670  10.752  1.00 93.07           C  
ANISOU 1140  CG  ARG A 138    13951  11282  10128   -785   -524    781       C  
ATOM   1141  CD  ARG A 138      43.403  88.071  10.913  1.00105.00           C  
ANISOU 1141  CD  ARG A 138    15660  12778  11456   -752   -546    801       C  
ATOM   1142  NE  ARG A 138      44.421  89.110  11.048  1.00114.54           N  
ANISOU 1142  NE  ARG A 138    17010  13982  12527   -822   -661    837       N  
ATOM   1143  CZ  ARG A 138      44.152  90.381  11.336  1.00119.05           C  
ANISOU 1143  CZ  ARG A 138    17778  14530  12925   -803   -706    867       C  
ATOM   1144  NH1 ARG A 138      42.897  90.770  11.520  1.00121.98           N  
ANISOU 1144  NH1 ARG A 138    18225  14880  13241   -713   -641    862       N  
ATOM   1145  NH2 ARG A 138      45.136  91.266  11.438  1.00118.53           N  
ANISOU 1145  NH2 ARG A 138    17832  14458  12745   -873   -819    903       N  
ATOM   1146  N   ALA A 139      41.746  82.549  10.722  1.00 91.04           N  
ANISOU 1146  N   ALA A 139    13184  11005  10404   -624   -241    713       N  
ATOM   1147  CA  ALA A 139      40.726  81.572  11.070  1.00 94.97           C  
ANISOU 1147  CA  ALA A 139    13592  11472  11022   -551   -150    724       C  
ATOM   1148  C   ALA A 139      41.339  80.411  11.839  1.00 93.38           C  
ANISOU 1148  C   ALA A 139    13318  11230  10934   -566   -156    765       C  
ATOM   1149  O   ALA A 139      40.727  79.893  12.780  1.00 89.17           O  
ANISOU 1149  O   ALA A 139    12806  10639  10435   -509    -99    822       O  
ATOM   1150  CB  ALA A 139      40.008  81.071   9.819  1.00 99.66           C  
ANISOU 1150  CB  ALA A 139    14016  12120  11730   -536   -103    637       C  
ATOM   1151  N   ARG A 140      42.539  79.969  11.439  1.00 99.78           N  
ANISOU 1151  N   ARG A 140    14038  12067  11806   -642   -222    737       N  
ATOM   1152  CA  ARG A 140      43.202  78.919  12.205  1.00105.49           C  
ANISOU 1152  CA  ARG A 140    14702  12745  12633   -661   -241    777       C  
ATOM   1153  C   ARG A 140      43.611  79.407  13.588  1.00104.84           C  
ANISOU 1153  C   ARG A 140    14809  12585  12439   -660   -280    874       C  
ATOM   1154  O   ARG A 140      43.666  78.610  14.529  1.00105.48           O  
ANISOU 1154  O   ARG A 140    14888  12606  12586   -643   -270    928       O  
ATOM   1155  CB  ARG A 140      44.437  78.391  11.472  1.00108.04           C  
ANISOU 1155  CB  ARG A 140    14889  13113  13048   -741   -305    724       C  
ATOM   1156  CG  ARG A 140      44.130  77.595  10.222  1.00113.51           C  
ANISOU 1156  CG  ARG A 140    15380  13869  13879   -740   -267    630       C  
ATOM   1157  CD  ARG A 140      45.399  77.128   9.548  1.00117.36           C  
ANISOU 1157  CD  ARG A 140    15744  14400  14446   -815   -327    579       C  
ATOM   1158  NE  ARG A 140      45.093  76.299   8.392  1.00123.25           N  
ANISOU 1158  NE  ARG A 140    16305  15201  15324   -808   -289    489       N  
ATOM   1159  CZ  ARG A 140      44.877  74.990   8.461  1.00132.56           C  
ANISOU 1159  CZ  ARG A 140    17344  16360  16664   -781   -262    475       C  
ATOM   1160  NH1 ARG A 140      44.906  74.375   9.638  1.00134.03           N  
ANISOU 1160  NH1 ARG A 140    17553  16476  16898   -762   -264    545       N  
ATOM   1161  NH2 ARG A 140      44.614  74.298   7.361  1.00137.98           N  
ANISOU 1161  NH2 ARG A 140    17872  17092  17461   -774   -236    390       N  
ATOM   1162  N   ALA A 141      43.907  80.702  13.728  1.00101.77           N  
ANISOU 1162  N   ALA A 141    14592  12195  11881   -678   -331    899       N  
ATOM   1163  CA  ALA A 141      44.222  81.257  15.041  1.00 97.78           C  
ANISOU 1163  CA  ALA A 141    14288  11609  11253   -670   -373    993       C  
ATOM   1164  C   ALA A 141      42.980  81.326  15.920  1.00104.77           C  
ANISOU 1164  C   ALA A 141    15279  12441  12090   -576   -284   1045       C  
ATOM   1165  O   ALA A 141      42.988  80.849  17.058  1.00119.24           O  
ANISOU 1165  O   ALA A 141    17176  14199  13932   -552   -273   1115       O  
ATOM   1166  CB  ALA A 141      44.855  82.639  14.893  1.00 96.94           C  
ANISOU 1166  CB  ALA A 141    14338  11516  10981   -715   -458   1004       C  
ATOM   1167  N   GLY A 142      41.891  81.884  15.398  1.00105.94           N  
ANISOU 1167  N   GLY A 142    15439  12622  12190   -520   -218   1012       N  
ATOM   1168  CA  GLY A 142      40.685  82.033  16.188  1.00110.25           C  
ANISOU 1168  CA  GLY A 142    16082  13121  12686   -426   -127   1060       C  
ATOM   1169  C   GLY A 142      39.724  83.077  15.659  1.00118.33           C  
ANISOU 1169  C   GLY A 142    17174  14176  13608   -375    -87   1029       C  
ATOM   1170  O   GLY A 142      38.521  83.002  15.931  1.00122.24           O  
ANISOU 1170  O   GLY A 142    17676  14655  14114   -292     10   1043       O  
ATOM   1171  N   GLU A 143      40.233  84.062  14.914  1.00117.76           N  
ANISOU 1171  N   GLU A 143    17155  14150  13441   -424   -161    989       N  
ATOM   1172  CA  GLU A 143      39.386  85.071  14.273  1.00117.87           C  
ANISOU 1172  CA  GLU A 143    17225  14197  13362   -385   -138    949       C  
ATOM   1173  C   GLU A 143      38.786  84.472  12.997  1.00114.22           C  
ANISOU 1173  C   GLU A 143    16556  13802  13041   -385    -90    862       C  
ATOM   1174  O   GLU A 143      39.190  84.757  11.868  1.00116.05           O  
ANISOU 1174  O   GLU A 143    16722  14096  13277   -442   -139    793       O  
ATOM   1175  CB  GLU A 143      40.172  86.346  13.992  1.00123.41           C  
ANISOU 1175  CB  GLU A 143    18068  14916  13905   -442   -244    944       C  
ATOM   1176  CG  GLU A 143      39.398  87.421  13.214  1.00127.13           C  
ANISOU 1176  CG  GLU A 143    18597  15426  14282   -414   -237    896       C  
ATOM   1177  CD  GLU A 143      40.244  88.646  12.889  1.00126.95           C  
ANISOU 1177  CD  GLU A 143    18707  15423  14106   -481   -352    891       C  
ATOM   1178  OE1 GLU A 143      41.413  88.701  13.335  1.00125.78           O  
ANISOU 1178  OE1 GLU A 143    18615  15254  13922   -545   -435    933       O  
ATOM   1179  OE2 GLU A 143      39.761  89.524  12.140  1.00125.30           O  
ANISOU 1179  OE2 GLU A 143    18537  15249  13821   -474   -363    846       O  
ATOM   1180  N   ALA A 144      37.806  83.594  13.204  1.00109.73           N  
ANISOU 1180  N   ALA A 144    15886  13215  12592   -319      8    868       N  
ATOM   1181  CA  ALA A 144      37.118  82.938  12.104  1.00105.94           C  
ANISOU 1181  CA  ALA A 144    15214  12783  12254   -309     55    795       C  
ATOM   1182  C   ALA A 144      35.875  83.689  11.646  1.00100.46           C  
ANISOU 1182  C   ALA A 144    14556  12100  11513   -244    107    767       C  
ATOM   1183  O   ALA A 144      35.290  83.313  10.627  1.00104.17           O  
ANISOU 1183  O   ALA A 144    14883  12608  12088   -238    132    701       O  
ATOM   1184  CB  ALA A 144      36.732  81.510  12.503  1.00105.36           C  
ANISOU 1184  CB  ALA A 144    14995  12683  12354   -278    124    816       C  
ATOM   1185  N   ALA A 145      35.451  84.728  12.372  1.00 91.36           N  
ANISOU 1185  N   ALA A 145    13591  10911  10208   -192    119    815       N  
ATOM   1186  CA  ALA A 145      34.269  85.481  11.959  1.00 86.15           C  
ANISOU 1186  CA  ALA A 145    12969  10260   9505   -127    164    788       C  
ATOM   1187  C   ALA A 145      34.496  86.172  10.619  1.00 86.04           C  
ANISOU 1187  C   ALA A 145    12932  10306   9455   -182     93    704       C  
ATOM   1188  O   ALA A 145      33.596  86.218   9.771  1.00 86.32           O  
ANISOU 1188  O   ALA A 145    12886  10364   9548   -153    125    649       O  
ATOM   1189  CB  ALA A 145      33.885  86.498  13.033  1.00 85.62           C  
ANISOU 1189  CB  ALA A 145    13121  10140   9270    -61    184    855       C  
ATOM   1190  N   ASN A 146      35.693  86.731  10.421  1.00 85.52           N  
ANISOU 1190  N   ASN A 146    12939  10263   9290   -264     -6    695       N  
ATOM   1191  CA  ASN A 146      36.025  87.382   9.158  1.00 79.70           C  
ANISOU 1191  CA  ASN A 146    12185   9586   8511   -327    -77    618       C  
ATOM   1192  C   ASN A 146      36.125  86.370   8.024  1.00 79.38           C  
ANISOU 1192  C   ASN A 146    11929   9595   8636   -369    -68    544       C  
ATOM   1193  O   ASN A 146      35.735  86.659   6.887  1.00 80.72           O  
ANISOU 1193  O   ASN A 146    12047   9805   8819   -383    -80    472       O  
ATOM   1194  CB  ASN A 146      37.337  88.147   9.315  1.00 79.97           C  
ANISOU 1194  CB  ASN A 146    12345   9630   8410   -408   -183    639       C  
ATOM   1195  CG  ASN A 146      37.376  89.412   8.500  1.00 82.28           C  
ANISOU 1195  CG  ASN A 146    12733   9958   8570   -442   -252    595       C  
ATOM   1196  OD1 ASN A 146      37.848  89.409   7.364  1.00 87.15           O  
ANISOU 1196  OD1 ASN A 146    13264  10635   9216   -513   -296    528       O  
ATOM   1197  ND2 ASN A 146      36.882  90.508   9.073  1.00 84.08           N  
ANISOU 1197  ND2 ASN A 146    13147  10150   8651   -390   -263    631       N  
ATOM   1198  N   PHE A 147      36.624  85.171   8.319  1.00 78.06           N  
ANISOU 1198  N   PHE A 147    11640   9422   8596   -388    -49    559       N  
ATOM   1199  CA  PHE A 147      36.805  84.163   7.280  1.00 69.45           C  
ANISOU 1199  CA  PHE A 147    10350   8377   7663   -427    -45    489       C  
ATOM   1200  C   PHE A 147      35.467  83.581   6.836  1.00 67.99           C  
ANISOU 1200  C   PHE A 147    10048   8183   7603   -358     32    457       C  
ATOM   1201  O   PHE A 147      35.264  83.318   5.645  1.00 65.23           O  
ANISOU 1201  O   PHE A 147     9584   7872   7328   -380     23    380       O  
ATOM   1202  CB  PHE A 147      37.746  83.077   7.791  1.00 68.39           C  
ANISOU 1202  CB  PHE A 147    10128   8232   7624   -464    -54    517       C  
ATOM   1203  CG  PHE A 147      38.099  82.040   6.771  1.00 65.24           C  
ANISOU 1203  CG  PHE A 147     9532   7878   7378   -506    -59    445       C  
ATOM   1204  CD1 PHE A 147      38.727  82.398   5.594  1.00 67.53           C  
ANISOU 1204  CD1 PHE A 147     9787   8230   7641   -575   -114    371       C  
ATOM   1205  CD2 PHE A 147      37.866  80.698   7.020  1.00 64.91           C  
ANISOU 1205  CD2 PHE A 147     9347   7814   7502   -479    -12    452       C  
ATOM   1206  CE1 PHE A 147      39.072  81.445   4.660  1.00 71.19           C  
ANISOU 1206  CE1 PHE A 147    10078   8733   8239   -609   -116    303       C  
ATOM   1207  CE2 PHE A 147      38.216  79.738   6.096  1.00 67.50           C  
ANISOU 1207  CE2 PHE A 147     9501   8179   7966   -514    -22    384       C  
ATOM   1208  CZ  PHE A 147      38.820  80.112   4.912  1.00 71.07           C  
ANISOU 1208  CZ  PHE A 147     9922   8693   8388   -577    -71    308       C  
ATOM   1209  N   CYS A 148      34.545  83.361   7.778  1.00 67.58           N  
ANISOU 1209  N   CYS A 148    10023   8078   7577   -276    107    519       N  
ATOM   1210  CA  CYS A 148      33.237  82.827   7.410  1.00 70.52           C  
ANISOU 1210  CA  CYS A 148    10282   8438   8075   -209    180    499       C  
ATOM   1211  C   CYS A 148      32.443  83.824   6.578  1.00 75.75           C  
ANISOU 1211  C   CYS A 148    10993   9115   8671   -188    170    448       C  
ATOM   1212  O   CYS A 148      31.674  83.423   5.697  1.00 74.06           O  
ANISOU 1212  O   CYS A 148    10659   8911   8570   -170    190    395       O  
ATOM   1213  CB  CYS A 148      32.446  82.440   8.659  1.00 70.24           C  
ANISOU 1213  CB  CYS A 148    10273   8343   8074   -127    269    583       C  
ATOM   1214  SG  CYS A 148      33.212  81.144   9.666  1.00 78.26           S  
ANISOU 1214  SG  CYS A 148    11222   9329   9185   -147    284    646       S  
ATOM   1215  N   ALA A 149      32.613  85.121   6.840  1.00 78.39           N  
ANISOU 1215  N   ALA A 149    11508   9449   8829   -190    132    464       N  
ATOM   1216  CA  ALA A 149      31.937  86.122   6.026  1.00 73.89           C  
ANISOU 1216  CA  ALA A 149    10993   8892   8188   -177    108    412       C  
ATOM   1217  C   ALA A 149      32.473  86.114   4.600  1.00 72.40           C  
ANISOU 1217  C   ALA A 149    10724   8760   8023   -258     39    321       C  
ATOM   1218  O   ALA A 149      31.702  86.226   3.638  1.00 71.47           O  
ANISOU 1218  O   ALA A 149    10550   8652   7954   -245     38    261       O  
ATOM   1219  CB  ALA A 149      32.094  87.505   6.658  1.00 68.74           C  
ANISOU 1219  CB  ALA A 149    10559   8225   7335   -165     72    450       C  
ATOM   1220  N   LEU A 150      33.791  85.967   4.445  1.00 67.48           N  
ANISOU 1220  N   LEU A 150    10096   8174   7370   -342    -20    311       N  
ATOM   1221  CA  LEU A 150      34.370  85.880   3.111  1.00 60.94           C  
ANISOU 1221  CA  LEU A 150     9187   7403   6566   -420    -76    227       C  
ATOM   1222  C   LEU A 150      33.871  84.637   2.382  1.00 63.67           C  
ANISOU 1222  C   LEU A 150     9336   7752   7102   -405    -35    177       C  
ATOM   1223  O   LEU A 150      33.501  84.708   1.203  1.00 59.99           O  
ANISOU 1223  O   LEU A 150     8815   7310   6670   -422    -56    102       O  
ATOM   1224  CB  LEU A 150      35.894  85.884   3.209  1.00 58.47           C  
ANISOU 1224  CB  LEU A 150     8895   7125   6196   -507   -136    236       C  
ATOM   1225  CG  LEU A 150      36.531  87.237   3.539  1.00 59.20           C  
ANISOU 1225  CG  LEU A 150     9177   7224   6092   -546   -206    267       C  
ATOM   1226  CD1 LEU A 150      38.026  87.094   3.683  1.00 63.67           C  
ANISOU 1226  CD1 LEU A 150     9741   7819   6631   -631   -262    283       C  
ATOM   1227  CD2 LEU A 150      36.206  88.251   2.467  1.00 61.04           C  
ANISOU 1227  CD2 LEU A 150     9470   7488   6235   -572   -253    204       C  
ATOM   1228  N   ILE A 151      33.817  83.495   3.079  1.00 62.61           N  
ANISOU 1228  N   ILE A 151     9103   7592   7095   -373     18    218       N  
ATOM   1229  CA  ILE A 151      33.293  82.275   2.466  1.00 60.01           C  
ANISOU 1229  CA  ILE A 151     8591   7259   6953   -354     52    178       C  
ATOM   1230  C   ILE A 151      31.879  82.510   1.954  1.00 62.59           C  
ANISOU 1230  C   ILE A 151     8896   7559   7324   -292     82    152       C  
ATOM   1231  O   ILE A 151      31.560  82.212   0.797  1.00 61.81           O  
ANISOU 1231  O   ILE A 151     8706   7477   7304   -307     62     79       O  
ATOM   1232  CB  ILE A 151      33.346  81.102   3.464  1.00 54.67           C  
ANISOU 1232  CB  ILE A 151     7829   6547   6394   -322    104    240       C  
ATOM   1233  CG1 ILE A 151      34.799  80.747   3.786  1.00 55.50           C  
ANISOU 1233  CG1 ILE A 151     7930   6677   6480   -390     62    252       C  
ATOM   1234  CG2 ILE A 151      32.598  79.886   2.927  1.00 51.50           C  
ANISOU 1234  CG2 ILE A 151     7248   6131   6187   -289    140    209       C  
ATOM   1235  CD1 ILE A 151      34.947  79.620   4.777  1.00 51.71           C  
ANISOU 1235  CD1 ILE A 151     7378   6159   6109   -367    101    312       C  
ATOM   1236  N   LEU A 152      31.020  83.080   2.801  1.00 64.90           N  
ANISOU 1236  N   LEU A 152     9281   7810   7567   -221    129    212       N  
ATOM   1237  CA  LEU A 152      29.655  83.371   2.380  1.00 65.54           C  
ANISOU 1237  CA  LEU A 152     9345   7863   7693   -158    158    194       C  
ATOM   1238  C   LEU A 152      29.632  84.322   1.189  1.00 69.30           C  
ANISOU 1238  C   LEU A 152     9879   8368   8083   -199     88    115       C  
ATOM   1239  O   LEU A 152      28.831  84.146   0.263  1.00 69.75           O  
ANISOU 1239  O   LEU A 152     9857   8415   8229   -184     82     61       O  
ATOM   1240  CB  LEU A 152      28.858  83.954   3.549  1.00 61.16           C  
ANISOU 1240  CB  LEU A 152     8898   7263   7076    -76    221    273       C  
ATOM   1241  CG  LEU A 152      28.517  83.006   4.702  1.00 57.95           C  
ANISOU 1241  CG  LEU A 152     8431   6817   6770    -19    306    354       C  
ATOM   1242  CD1 LEU A 152      28.127  83.789   5.937  1.00 57.29           C  
ANISOU 1242  CD1 LEU A 152     8501   6698   6568     45    358    432       C  
ATOM   1243  CD2 LEU A 152      27.397  82.068   4.308  1.00 61.55           C  
ANISOU 1243  CD2 LEU A 152     8721   7246   7419     30    358    345       C  
ATOM   1244  N   ALA A 153      30.509  85.331   1.188  1.00 67.45           N  
ANISOU 1244  N   ALA A 153     9783   8166   7678   -255     28    109       N  
ATOM   1245  CA  ALA A 153      30.510  86.290   0.086  1.00 64.00           C  
ANISOU 1245  CA  ALA A 153     9412   7756   7148   -299    -42     39       C  
ATOM   1246  C   ALA A 153      31.028  85.664  -1.204  1.00 68.54           C  
ANISOU 1246  C   ALA A 153     9871   8372   7798   -368    -83    -45       C  
ATOM   1247  O   ALA A 153      30.465  85.894  -2.280  1.00 76.68           O  
ANISOU 1247  O   ALA A 153    10881   9403   8850   -376   -113   -111       O  
ATOM   1248  CB  ALA A 153      31.335  87.521   0.457  1.00 61.17           C  
ANISOU 1248  CB  ALA A 153     9235   7421   6588   -342    -98     61       C  
ATOM   1249  N   TYR A 154      32.091  84.862  -1.121  1.00 69.18           N  
ANISOU 1249  N   TYR A 154     9877   8484   7922   -418    -85    -43       N  
ATOM   1250  CA  TYR A 154      32.638  84.253  -2.330  1.00 66.61           C  
ANISOU 1250  CA  TYR A 154     9444   8200   7663   -480   -119   -124       C  
ATOM   1251  C   TYR A 154      31.689  83.218  -2.924  1.00 65.83           C  
ANISOU 1251  C   TYR A 154     9195   8070   7746   -435    -88   -161       C  
ATOM   1252  O   TYR A 154      31.583  83.106  -4.153  1.00 62.33           O  
ANISOU 1252  O   TYR A 154     8704   7643   7337   -465   -123   -240       O  
ATOM   1253  CB  TYR A 154      33.995  83.619  -2.043  1.00 62.91           C  
ANISOU 1253  CB  TYR A 154     8927   7770   7207   -537   -126   -111       C  
ATOM   1254  CG  TYR A 154      35.150  84.596  -2.055  1.00 62.53           C  
ANISOU 1254  CG  TYR A 154     8999   7768   6992   -614   -183   -108       C  
ATOM   1255  CD1 TYR A 154      35.601  85.151  -3.244  1.00 57.71           C  
ANISOU 1255  CD1 TYR A 154     8413   7205   6309   -684   -237   -180       C  
ATOM   1256  CD2 TYR A 154      35.804  84.943  -0.880  1.00 68.06           C  
ANISOU 1256  CD2 TYR A 154     9791   8460   7609   -620   -186    -30       C  
ATOM   1257  CE1 TYR A 154      36.661  86.039  -3.260  1.00 66.01           C  
ANISOU 1257  CE1 TYR A 154     9569   8299   7212   -759   -291   -171       C  
ATOM   1258  CE2 TYR A 154      36.864  85.828  -0.884  1.00 66.70           C  
ANISOU 1258  CE2 TYR A 154     9726   8325   7291   -692   -246    -21       C  
ATOM   1259  CZ  TYR A 154      37.292  86.373  -2.074  1.00 66.52           C  
ANISOU 1259  CZ  TYR A 154     9718   8354   7202   -763   -297    -90       C  
ATOM   1260  OH  TYR A 154      38.355  87.250  -2.068  1.00 57.79           O  
ANISOU 1260  OH  TYR A 154     8716   7287   5956   -839   -358    -75       O  
ATOM   1261  N   CYS A 155      30.992  82.454  -2.077  1.00 65.04           N  
ANISOU 1261  N   CYS A 155     9024   7924   7763   -364    -25   -103       N  
ATOM   1262  CA  CYS A 155      30.080  81.415  -2.549  1.00 66.65           C  
ANISOU 1262  CA  CYS A 155     9080   8092   8151   -319      1   -126       C  
ATOM   1263  C   CYS A 155      28.707  81.945  -2.942  1.00 79.00           C  
ANISOU 1263  C   CYS A 155    10666   9613   9737   -265      4   -139       C  
ATOM   1264  O   CYS A 155      27.869  81.154  -3.390  1.00 87.87           O  
ANISOU 1264  O   CYS A 155    11671  10701  11016   -228     17   -157       O  
ATOM   1265  CB  CYS A 155      29.897  80.339  -1.477  1.00 60.80           C  
ANISOU 1265  CB  CYS A 155     8248   7320   7535   -270     66    -54       C  
ATOM   1266  SG  CYS A 155      31.422  79.561  -0.899  1.00 66.56           S  
ANISOU 1266  SG  CYS A 155     8937   8084   8267   -325     61    -32       S  
ATOM   1267  N   ASN A 156      28.458  83.243  -2.783  1.00 80.73           N  
ANISOU 1267  N   ASN A 156    11031   9831   9812   -258    -13   -129       N  
ATOM   1268  CA  ASN A 156      27.151  83.846  -3.038  1.00 77.39           C  
ANISOU 1268  CA  ASN A 156    10639   9363   9404   -201    -10   -136       C  
ATOM   1269  C   ASN A 156      26.054  83.110  -2.267  1.00 70.26           C  
ANISOU 1269  C   ASN A 156     9641   8403   8650   -111     69    -71       C  
ATOM   1270  O   ASN A 156      25.098  82.578  -2.831  1.00 76.44           O  
ANISOU 1270  O   ASN A 156    10320   9148   9576    -76     73    -93       O  
ATOM   1271  CB  ASN A 156      26.839  83.899  -4.534  1.00 82.17           C  
ANISOU 1271  CB  ASN A 156    11207   9968  10047   -235    -75   -229       C  
ATOM   1272  CG  ASN A 156      25.740  84.892  -4.854  1.00 81.01           C  
ANISOU 1272  CG  ASN A 156    11138   9781   9861   -196    -97   -243       C  
ATOM   1273  OD1 ASN A 156      25.460  85.793  -4.064  1.00 79.62           O  
ANISOU 1273  OD1 ASN A 156    11075   9594   9584   -159    -77   -195       O  
ATOM   1274  ND2 ASN A 156      25.108  84.731  -6.011  1.00 80.99           N  
ANISOU 1274  ND2 ASN A 156    11079   9752   9940   -203   -142   -310       N  
ATOM   1275  N   LYS A 157      26.223  83.086  -0.948  1.00 64.25           N  
ANISOU 1275  N   LYS A 157     8922   7636   7853    -76    130     12       N  
ATOM   1276  CA  LYS A 157      25.286  82.454  -0.029  1.00 67.50           C  
ANISOU 1276  CA  LYS A 157     9263   7999   8385      7    216     87       C  
ATOM   1277  C   LYS A 157      24.974  83.445   1.081  1.00 74.98           C  
ANISOU 1277  C   LYS A 157    10355   8929   9203     61    262    155       C  
ATOM   1278  O   LYS A 157      25.888  83.925   1.761  1.00 77.48           O  
ANISOU 1278  O   LYS A 157    10788   9271   9379     33    254    184       O  
ATOM   1279  CB  LYS A 157      25.861  81.158   0.555  1.00 64.11           C  
ANISOU 1279  CB  LYS A 157     8724   7574   8060     -3    252    126       C  
ATOM   1280  CG  LYS A 157      26.068  80.046  -0.463  1.00 69.40           C  
ANISOU 1280  CG  LYS A 157     9240   8253   8876    -42    213     63       C  
ATOM   1281  CD  LYS A 157      24.829  79.166  -0.556  1.00 72.71           C  
ANISOU 1281  CD  LYS A 157     9518   8618   9491     20    253     84       C  
ATOM   1282  CE  LYS A 157      24.522  78.538   0.800  1.00 73.18           C  
ANISOU 1282  CE  LYS A 157     9540   8649   9616     75    340    184       C  
ATOM   1283  NZ  LYS A 157      23.281  77.721   0.790  1.00 73.11           N  
ANISOU 1283  NZ  LYS A 157     9393   8587   9798    136    383    216       N  
ATOM   1284  N   THR A 158      23.695  83.760   1.254  1.00 74.72           N  
ANISOU 1284  N   THR A 158    10320   8853   9219    139    308    179       N  
ATOM   1285  CA  THR A 158      23.295  84.668   2.315  1.00 75.73           C  
ANISOU 1285  CA  THR A 158    10582   8959   9231    202    361    242       C  
ATOM   1286  C   THR A 158      23.146  83.925   3.637  1.00 83.70           C  
ANISOU 1286  C   THR A 158    11557   9946  10299    256    461    337       C  
ATOM   1287  O   THR A 158      22.820  82.734   3.677  1.00 87.44           O  
ANISOU 1287  O   THR A 158    11878  10403  10943    269    501    358       O  
ATOM   1288  CB  THR A 158      21.982  85.359   1.955  1.00 72.31           C  
ANISOU 1288  CB  THR A 158    10162   8488   8825    267    371    228       C  
ATOM   1289  OG1 THR A 158      21.047  84.381   1.492  1.00 69.52           O  
ANISOU 1289  OG1 THR A 158     9632   8101   8683    299    400    224       O  
ATOM   1290  CG2 THR A 158      22.212  86.380   0.858  1.00 77.93           C  
ANISOU 1290  CG2 THR A 158    10962   9219   9427    215    269    143       C  
ATOM   1291  N   VAL A 159      23.375  84.658   4.729  1.00 79.82           N  
ANISOU 1291  N   VAL A 159    11218   9450   9661    287    496    396       N  
ATOM   1292  CA  VAL A 159      23.284  84.073   6.060  1.00 76.56           C  
ANISOU 1292  CA  VAL A 159    10802   9012   9275    336    590    489       C  
ATOM   1293  C   VAL A 159      21.864  83.585   6.315  1.00 74.77           C  
ANISOU 1293  C   VAL A 159    10466   8741   9203    424    685    532       C  
ATOM   1294  O   VAL A 159      20.886  84.175   5.838  1.00 78.65           O  
ANISOU 1294  O   VAL A 159    10954   9213   9715    470    690    507       O  
ATOM   1295  CB  VAL A 159      23.733  85.099   7.114  1.00 74.72           C  
ANISOU 1295  CB  VAL A 159    10777   8776   8839    357    602    538       C  
ATOM   1296  CG1 VAL A 159      23.773  84.471   8.499  1.00 74.53           C  
ANISOU 1296  CG1 VAL A 159    10764   8723   8829    399    694    634       C  
ATOM   1297  CG2 VAL A 159      25.090  85.659   6.743  1.00 72.41           C  
ANISOU 1297  CG2 VAL A 159    10587   8525   8401    265    497    495       C  
ATOM   1298  N   GLY A 160      21.747  82.468   7.025  1.00 69.62           N  
ANISOU 1298  N   GLY A 160     9713   8070   8668    444    757    595       N  
ATOM   1299  CA  GLY A 160      20.459  81.922   7.391  1.00 72.23           C  
ANISOU 1299  CA  GLY A 160     9934   8360   9149    525    855    650       C  
ATOM   1300  C   GLY A 160      19.943  80.845   6.466  1.00 71.22           C  
ANISOU 1300  C   GLY A 160     9600   8222   9238    509    835    618       C  
ATOM   1301  O   GLY A 160      18.994  80.141   6.831  1.00 74.46           O  
ANISOU 1301  O   GLY A 160     9895   8597   9798    565    914    675       O  
ATOM   1302  N   GLU A 161      20.531  80.698   5.287  1.00 69.44           N  
ANISOU 1302  N   GLU A 161     9328   8024   9032    435    732    531       N  
ATOM   1303  CA  GLU A 161      20.105  79.696   4.328  1.00 70.05           C  
ANISOU 1303  CA  GLU A 161     9223   8088   9306    417    698    493       C  
ATOM   1304  C   GLU A 161      20.840  78.378   4.546  1.00 67.51           C  
ANISOU 1304  C   GLU A 161     8796   7776   9078    373    694    511       C  
ATOM   1305  O   GLU A 161      22.000  78.351   4.966  1.00 66.51           O  
ANISOU 1305  O   GLU A 161     8741   7682   8850    324    672    513       O  
ATOM   1306  CB  GLU A 161      20.326  80.203   2.905  1.00 80.33           C  
ANISOU 1306  CB  GLU A 161    10533   9409  10578    364    590    387       C  
ATOM   1307  CG  GLU A 161      19.374  81.323   2.529  1.00 85.41           C  
ANISOU 1307  CG  GLU A 161    11245  10030  11178    411    585    365       C  
ATOM   1308  CD  GLU A 161      17.929  80.862   2.511  1.00 86.89           C  
ANISOU 1308  CD  GLU A 161    11301  10162  11551    484    642    403       C  
ATOM   1309  OE1 GLU A 161      17.680  79.718   2.074  1.00 87.74           O  
ANISOU 1309  OE1 GLU A 161    11249  10251  11838    472    631    401       O  
ATOM   1310  OE2 GLU A 161      17.046  81.635   2.942  1.00 87.13           O  
ANISOU 1310  OE2 GLU A 161    11388  10166  11552    555    697    437       O  
ATOM   1311  N   LEU A 162      20.134  77.280   4.278  1.00 72.05           N  
ANISOU 1311  N   LEU A 162     9200   8321   9856    392    711    527       N  
ATOM   1312  CA  LEU A 162      20.732  75.952   4.310  1.00 71.35           C  
ANISOU 1312  CA  LEU A 162     8994   8236   9881    351    692    534       C  
ATOM   1313  C   LEU A 162      21.786  75.832   3.216  1.00 73.08           C  
ANISOU 1313  C   LEU A 162     9205   8495  10069    268    584    435       C  
ATOM   1314  O   LEU A 162      21.707  76.489   2.174  1.00 75.39           O  
ANISOU 1314  O   LEU A 162     9528   8799  10320    248    521    358       O  
ATOM   1315  CB  LEU A 162      19.658  74.880   4.117  1.00 72.46           C  
ANISOU 1315  CB  LEU A 162     8954   8330  10248    388    720    567       C  
ATOM   1316  CG  LEU A 162      18.472  74.932   5.085  1.00 74.80           C  
ANISOU 1316  CG  LEU A 162     9232   8586  10604    472    834    666       C  
ATOM   1317  CD1 LEU A 162      17.357  73.979   4.676  1.00 73.19           C  
ANISOU 1317  CD1 LEU A 162     8844   8335  10632    504    844    691       C  
ATOM   1318  CD2 LEU A 162      18.942  74.633   6.496  1.00 80.88           C  
ANISOU 1318  CD2 LEU A 162    10058   9359  11312    483    913    753       C  
ATOM   1319  N   GLY A 163      22.786  74.983   3.457  1.00 73.55           N  
ANISOU 1319  N   GLY A 163     9225   8574  10148    221    563    436       N  
ATOM   1320  CA  GLY A 163      23.933  74.905   2.575  1.00 68.93           C  
ANISOU 1320  CA  GLY A 163     8644   8032   9514    144    473    349       C  
ATOM   1321  C   GLY A 163      24.380  73.479   2.325  1.00 63.33           C  
ANISOU 1321  C   GLY A 163     7788   7320   8954    113    442    335       C  
ATOM   1322  O   GLY A 163      23.835  72.523   2.881  1.00 61.35           O  
ANISOU 1322  O   GLY A 163     7435   7032   8843    147    485    397       O  
ATOM   1323  N   ASP A 164      25.377  73.365   1.447  1.00 63.05           N  
ANISOU 1323  N   ASP A 164     7746   7324   8886     49    364    251       N  
ATOM   1324  CA  ASP A 164      26.008  72.108   1.063  1.00 61.62           C  
ANISOU 1324  CA  ASP A 164     7440   7148   8824     13    321    218       C  
ATOM   1325  C   ASP A 164      27.507  72.224   1.309  1.00 66.44           C  
ANISOU 1325  C   ASP A 164     8117   7808   9319    -49    292    197       C  
ATOM   1326  O   ASP A 164      28.138  73.192   0.868  1.00 68.42           O  
ANISOU 1326  O   ASP A 164     8471   8100   9424    -88    258    148       O  
ATOM   1327  CB  ASP A 164      25.725  71.800  -0.410  1.00 58.44           C  
ANISOU 1327  CB  ASP A 164     6953   6741   8509     -2    253    126       C  
ATOM   1328  CG  ASP A 164      26.274  70.461  -0.849  1.00 67.49           C  
ANISOU 1328  CG  ASP A 164     7969   7887   9787    -29    207     89       C  
ATOM   1329  OD1 ASP A 164      25.496  69.491  -0.932  1.00 73.38           O  
ANISOU 1329  OD1 ASP A 164     8590   8585  10704      4    208    112       O  
ATOM   1330  OD2 ASP A 164      27.489  70.379  -1.121  1.00 74.72           O  
ANISOU 1330  OD2 ASP A 164     8903   8848  10638    -84    169     38       O  
ATOM   1331  N   VAL A 165      28.078  71.243   2.012  1.00 64.50           N  
ANISOU 1331  N   VAL A 165     7810   7555   9143    -59    300    236       N  
ATOM   1332  CA  VAL A 165      29.500  71.307   2.340  1.00 58.87           C  
ANISOU 1332  CA  VAL A 165     7153   6882   8334   -116    271    225       C  
ATOM   1333  C   VAL A 165      30.354  71.072   1.097  1.00 61.37           C  
ANISOU 1333  C   VAL A 165     7417   7240   8659   -172    197    120       C  
ATOM   1334  O   VAL A 165      31.330  71.793   0.853  1.00 59.34           O  
ANISOU 1334  O   VAL A 165     7246   7031   8270   -223    167     82       O  
ATOM   1335  CB  VAL A 165      29.836  70.306   3.456  1.00 57.79           C  
ANISOU 1335  CB  VAL A 165     6966   6718   8276   -111    295    297       C  
ATOM   1336  CG1 VAL A 165      31.337  70.182   3.617  1.00 52.43           C  
ANISOU 1336  CG1 VAL A 165     6314   6074   7534   -174    249    274       C  
ATOM   1337  CG2 VAL A 165      29.196  70.749   4.760  1.00 64.80           C  
ANISOU 1337  CG2 VAL A 165     7941   7570   9108    -63    373    401       C  
ATOM   1338  N   ARG A 166      29.999  70.064   0.292  1.00 62.60           N  
ANISOU 1338  N   ARG A 166     7436   7380   8970   -164    168     74       N  
ATOM   1339  CA  ARG A 166      30.771  69.783  -0.916  1.00 61.79           C  
ANISOU 1339  CA  ARG A 166     7284   7315   8878   -211    105    -28       C  
ATOM   1340  C   ARG A 166      30.680  70.938  -1.904  1.00 67.34           C  
ANISOU 1340  C   ARG A 166     8077   8050   9461   -232     81    -94       C  
ATOM   1341  O   ARG A 166      31.675  71.309  -2.541  1.00 67.11           O  
ANISOU 1341  O   ARG A 166     8085   8072   9341   -286     44   -159       O  
ATOM   1342  CB  ARG A 166      30.289  68.485  -1.565  1.00 56.58           C  
ANISOU 1342  CB  ARG A 166     6470   6620   8408   -189     75    -62       C  
ATOM   1343  CG  ARG A 166      31.110  68.077  -2.772  1.00 59.31           C  
ANISOU 1343  CG  ARG A 166     6763   7002   8771   -231     14   -168       C  
ATOM   1344  CD  ARG A 166      30.524  66.872  -3.458  1.00 72.29           C  
ANISOU 1344  CD  ARG A 166     8269   8603  10595   -203    -22   -202       C  
ATOM   1345  NE  ARG A 166      29.249  67.145  -4.101  1.00 85.47           N  
ANISOU 1345  NE  ARG A 166     9933  10232  12310   -166    -28   -211       N  
ATOM   1346  CZ  ARG A 166      29.140  67.600  -5.342  1.00 95.08           C  
ANISOU 1346  CZ  ARG A 166    11178  11460  13487   -182    -69   -296       C  
ATOM   1347  NH1 ARG A 166      30.229  67.824  -6.068  1.00 93.86           N  
ANISOU 1347  NH1 ARG A 166    11058  11362  13243   -233    -99   -377       N  
ATOM   1348  NH2 ARG A 166      27.944  67.824  -5.861  1.00102.70           N  
ANISOU 1348  NH2 ARG A 166    12137  12380  14505   -148    -80   -299       N  
ATOM   1349  N   GLU A 167      29.493  71.525  -2.033  1.00 69.00           N  
ANISOU 1349  N   GLU A 167     8321   8229   9668   -190    101    -77       N  
ATOM   1350  CA  GLU A 167      29.338  72.680  -2.902  1.00 71.28           C  
ANISOU 1350  CA  GLU A 167     8705   8540   9838   -209     75   -134       C  
ATOM   1351  C   GLU A 167      30.165  73.848  -2.394  1.00 66.77           C  
ANISOU 1351  C   GLU A 167     8283   8015   9074   -246     82   -117       C  
ATOM   1352  O   GLU A 167      30.778  74.577  -3.182  1.00 65.63           O  
ANISOU 1352  O   GLU A 167     8206   7915   8816   -296     42   -181       O  
ATOM   1353  CB  GLU A 167      27.856  73.046  -3.001  1.00 83.21           C  
ANISOU 1353  CB  GLU A 167    10219  10000  11397   -150     96   -109       C  
ATOM   1354  CG  GLU A 167      27.534  74.180  -3.961  1.00 90.06           C  
ANISOU 1354  CG  GLU A 167    11178  10878  12161   -166     60   -171       C  
ATOM   1355  CD  GLU A 167      26.038  74.406  -4.098  1.00 94.83           C  
ANISOU 1355  CD  GLU A 167    11765  11423  12842   -105     74   -148       C  
ATOM   1356  OE1 GLU A 167      25.642  75.440  -4.680  1.00 96.54           O  
ANISOU 1356  OE1 GLU A 167    12070  11640  12970   -109     49   -184       O  
ATOM   1357  OE2 GLU A 167      25.261  73.570  -3.585  1.00 95.60           O  
ANISOU 1357  OE2 GLU A 167    11761  11473  13088    -54    109    -90       O  
ATOM   1358  N   THR A 168      30.224  74.020  -1.074  1.00 66.17           N  
ANISOU 1358  N   THR A 168     8261   7926   8955   -225    130    -28       N  
ATOM   1359  CA  THR A 168      31.031  75.098  -0.514  1.00 61.55           C  
ANISOU 1359  CA  THR A 168     7821   7376   8188   -259    128     -4       C  
ATOM   1360  C   THR A 168      32.519  74.846  -0.725  1.00 65.83           C  
ANISOU 1360  C   THR A 168     8353   7968   8690   -329     87    -43       C  
ATOM   1361  O   THR A 168      33.264  75.766  -1.079  1.00 69.59           O  
ANISOU 1361  O   THR A 168     8926   8490   9026   -381     54    -74       O  
ATOM   1362  CB  THR A 168      30.714  75.256   0.967  1.00 56.32           C  
ANISOU 1362  CB  THR A 168     7223   6680   7496   -215    188    101       C  
ATOM   1363  OG1 THR A 168      29.331  75.603   1.113  1.00 58.31           O  
ANISOU 1363  OG1 THR A 168     7489   6890   7778   -148    232    134       O  
ATOM   1364  CG2 THR A 168      31.592  76.330   1.596  1.00 54.42           C  
ANISOU 1364  CG2 THR A 168     7141   6468   7069   -250    177    129       C  
ATOM   1365  N   MET A 169      32.968  73.603  -0.532  1.00 65.68           N  
ANISOU 1365  N   MET A 169     8216   7943   8799   -334     85    -40       N  
ATOM   1366  CA  MET A 169      34.383  73.301  -0.717  1.00 63.27           C  
ANISOU 1366  CA  MET A 169     7887   7681   8471   -397     48    -76       C  
ATOM   1367  C   MET A 169      34.809  73.533  -2.159  1.00 63.44           C  
ANISOU 1367  C   MET A 169     7891   7752   8462   -442      3   -179       C  
ATOM   1368  O   MET A 169      35.845  74.153  -2.419  1.00 65.93           O  
ANISOU 1368  O   MET A 169     8269   8119   8665   -501    -23   -207       O  
ATOM   1369  CB  MET A 169      34.679  71.860  -0.300  1.00 64.20           C  
ANISOU 1369  CB  MET A 169     7872   7777   8746   -386     50    -59       C  
ATOM   1370  CG  MET A 169      34.419  71.578   1.163  1.00 65.66           C  
ANISOU 1370  CG  MET A 169     8079   7914   8954   -351     91     45       C  
ATOM   1371  SD  MET A 169      35.379  72.610   2.291  1.00 61.92           S  
ANISOU 1371  SD  MET A 169     7770   7455   8301   -387     91    111       S  
ATOM   1372  CE  MET A 169      37.042  72.004   2.001  1.00 51.42           C  
ANISOU 1372  CE  MET A 169     6374   6168   6996   -460     34     64       C  
ATOM   1373  N   SER A 170      34.017  73.047  -3.115  1.00 67.67           N  
ANISOU 1373  N   SER A 170     8345   8269   9097   -417     -6   -235       N  
ATOM   1374  CA  SER A 170      34.426  73.166  -4.511  1.00 70.07           C  
ANISOU 1374  CA  SER A 170     8634   8615   9377   -459    -47   -337       C  
ATOM   1375  C   SER A 170      34.461  74.623  -4.970  1.00 73.83           C  
ANISOU 1375  C   SER A 170     9250   9123   9679   -493    -63   -359       C  
ATOM   1376  O   SER A 170      35.284  74.978  -5.822  1.00 76.57           O  
ANISOU 1376  O   SER A 170     9621   9523   9949   -551    -93   -425       O  
ATOM   1377  CB  SER A 170      33.513  72.326  -5.400  1.00 65.37           C  
ANISOU 1377  CB  SER A 170     7932   7981   8926   -421    -61   -387       C  
ATOM   1378  OG  SER A 170      32.199  72.839  -5.385  1.00 74.21           O  
ANISOU 1378  OG  SER A 170     9092   9055  10050   -375    -48   -361       O  
ATOM   1379  N   TYR A 171      33.586  75.478  -4.425  1.00 71.50           N  
ANISOU 1379  N   TYR A 171     9049   8798   9319   -458    -43   -305       N  
ATOM   1380  CA  TYR A 171      33.672  76.908  -4.717  1.00 72.38           C  
ANISOU 1380  CA  TYR A 171     9306   8939   9257   -491    -63   -319       C  
ATOM   1381  C   TYR A 171      34.984  77.492  -4.212  1.00 72.90           C  
ANISOU 1381  C   TYR A 171     9453   9055   9192   -551    -76   -295       C  
ATOM   1382  O   TYR A 171      35.627  78.288  -4.907  1.00 81.23           O  
ANISOU 1382  O   TYR A 171    10578  10159  10128   -610   -111   -341       O  
ATOM   1383  CB  TYR A 171      32.485  77.656  -4.107  1.00 80.45           C  
ANISOU 1383  CB  TYR A 171    10411   9915  10243   -434    -37   -261       C  
ATOM   1384  CG  TYR A 171      31.319  77.840  -5.052  1.00 92.93           C  
ANISOU 1384  CG  TYR A 171    11977  11463  11869   -404    -53   -309       C  
ATOM   1385  CD1 TYR A 171      30.158  77.090  -4.912  1.00102.33           C  
ANISOU 1385  CD1 TYR A 171    13073  12593  13213   -336    -26   -285       C  
ATOM   1386  CD2 TYR A 171      31.385  78.753  -6.094  1.00 97.95           C  
ANISOU 1386  CD2 TYR A 171    12694  12125  12397   -446   -101   -377       C  
ATOM   1387  CE1 TYR A 171      29.094  77.250  -5.777  1.00104.76           C  
ANISOU 1387  CE1 TYR A 171    13367  12865  13573   -310    -49   -327       C  
ATOM   1388  CE2 TYR A 171      30.325  78.923  -6.963  1.00103.73           C  
ANISOU 1388  CE2 TYR A 171    13418  12820  13173   -421   -124   -421       C  
ATOM   1389  CZ  TYR A 171      29.182  78.167  -6.799  1.00109.15           C  
ANISOU 1389  CZ  TYR A 171    14009  13443  14019   -352   -100   -396       C  
ATOM   1390  OH  TYR A 171      28.120  78.326  -7.661  1.00117.19           O  
ANISOU 1390  OH  TYR A 171    15017  14417  15091   -328   -131   -437       O  
ATOM   1391  N   LEU A 172      35.389  77.129  -2.995  1.00 65.46           N  
ANISOU 1391  N   LEU A 172     8505   8098   8268   -538    -51   -220       N  
ATOM   1392  CA  LEU A 172      36.654  77.629  -2.470  1.00 61.59           C  
ANISOU 1392  CA  LEU A 172     8089   7646   7667   -595    -71   -191       C  
ATOM   1393  C   LEU A 172      37.841  77.030  -3.212  1.00 57.97           C  
ANISOU 1393  C   LEU A 172     7541   7239   7245   -656    -97   -255       C  
ATOM   1394  O   LEU A 172      38.869  77.698  -3.371  1.00 64.62           O  
ANISOU 1394  O   LEU A 172     8447   8130   7977   -721   -127   -264       O  
ATOM   1395  CB  LEU A 172      36.758  77.335  -0.971  1.00 62.58           C  
ANISOU 1395  CB  LEU A 172     8235   7734   7811   -565    -42    -95       C  
ATOM   1396  CG  LEU A 172      35.781  78.099  -0.070  1.00 64.51           C  
ANISOU 1396  CG  LEU A 172     8594   7932   7984   -508    -10    -22       C  
ATOM   1397  CD1 LEU A 172      35.950  77.714   1.393  1.00 64.30           C  
ANISOU 1397  CD1 LEU A 172     8589   7866   7976   -481     20     72       C  
ATOM   1398  CD2 LEU A 172      35.936  79.600  -0.247  1.00 64.83           C  
ANISOU 1398  CD2 LEU A 172     8796   7998   7839   -539    -42    -25       C  
ATOM   1399  N   PHE A 173      37.722  75.785  -3.693  1.00 56.21           N  
ANISOU 1399  N   PHE A 173     7172   7006   7177   -636    -89   -299       N  
ATOM   1400  CA  PHE A 173      38.821  75.169  -4.433  1.00 62.48           C  
ANISOU 1400  CA  PHE A 173     7878   7849   8014   -686   -109   -365       C  
ATOM   1401  C   PHE A 173      39.144  75.922  -5.720  1.00 63.92           C  
ANISOU 1401  C   PHE A 173     8106   8086   8095   -739   -134   -445       C  
ATOM   1402  O   PHE A 173      40.283  75.877  -6.192  1.00 68.60           O  
ANISOU 1402  O   PHE A 173     8673   8732   8659   -796   -148   -484       O  
ATOM   1403  CB  PHE A 173      38.483  73.714  -4.776  1.00 65.63           C  
ANISOU 1403  CB  PHE A 173     8121   8220   8597   -645   -100   -402       C  
ATOM   1404  CG  PHE A 173      38.489  72.795  -3.591  1.00 64.76           C  
ANISOU 1404  CG  PHE A 173     7945   8066   8595   -610    -82   -332       C  
ATOM   1405  CD1 PHE A 173      37.822  71.574  -3.634  1.00 63.88           C  
ANISOU 1405  CD1 PHE A 173     7711   7910   8649   -559    -73   -339       C  
ATOM   1406  CD2 PHE A 173      39.159  73.143  -2.435  1.00 61.88           C  
ANISOU 1406  CD2 PHE A 173     7647   7701   8166   -630    -80   -256       C  
ATOM   1407  CE1 PHE A 173      37.824  70.725  -2.540  1.00 63.23           C  
ANISOU 1407  CE1 PHE A 173     7572   7786   8666   -530    -59   -272       C  
ATOM   1408  CE2 PHE A 173      39.164  72.297  -1.333  1.00 60.26           C  
ANISOU 1408  CE2 PHE A 173     7390   7449   8056   -600    -66   -190       C  
ATOM   1409  CZ  PHE A 173      38.499  71.088  -1.387  1.00 60.00           C  
ANISOU 1409  CZ  PHE A 173     7234   7377   8187   -551    -54   -198       C  
ATOM   1410  N   GLN A 174      38.160  76.612  -6.311  1.00 62.68           N  
ANISOU 1410  N   GLN A 174     8016   7914   7885   -721   -140   -469       N  
ATOM   1411  CA  GLN A 174      38.459  77.424  -7.484  1.00 67.00           C  
ANISOU 1411  CA  GLN A 174     8627   8510   8322   -777   -168   -540       C  
ATOM   1412  C   GLN A 174      39.426  78.555  -7.173  1.00 70.34           C  
ANISOU 1412  C   GLN A 174     9164   8981   8580   -843   -188   -508       C  
ATOM   1413  O   GLN A 174      40.193  78.976  -8.049  1.00 76.52           O  
ANISOU 1413  O   GLN A 174     9969   9821   9285   -908   -208   -562       O  
ATOM   1414  CB  GLN A 174      37.166  77.976  -8.077  1.00 71.75           C  
ANISOU 1414  CB  GLN A 174     9285   9075   8900   -744   -179   -565       C  
ATOM   1415  CG  GLN A 174      36.265  76.894  -8.613  1.00 79.92           C  
ANISOU 1415  CG  GLN A 174    10205  10062  10097   -689   -172   -605       C  
ATOM   1416  CD  GLN A 174      35.074  77.468  -9.319  1.00 91.65           C  
ANISOU 1416  CD  GLN A 174    11747  11512  11563   -665   -193   -636       C  
ATOM   1417  OE1 GLN A 174      34.759  78.648  -9.161  1.00101.72           O  
ANISOU 1417  OE1 GLN A 174    13147  12788  12714   -675   -206   -613       O  
ATOM   1418  NE2 GLN A 174      34.430  76.658 -10.149  1.00 95.80           N  
ANISOU 1418  NE2 GLN A 174    12188  12004  12210   -635   -205   -693       N  
ATOM   1419  N   HIS A 175      39.415  79.051  -5.942  1.00 72.34           N  
ANISOU 1419  N   HIS A 175     9496   9211   8778   -829   -185   -420       N  
ATOM   1420  CA  HIS A 175      40.330  80.106  -5.534  1.00 72.11           C  
ANISOU 1420  CA  HIS A 175     9583   9219   8599   -889   -213   -380       C  
ATOM   1421  C   HIS A 175      41.585  79.552  -4.880  1.00 67.88           C  
ANISOU 1421  C   HIS A 175     8988   8703   8100   -923   -214   -345       C  
ATOM   1422  O   HIS A 175      42.333  80.305  -4.256  1.00 70.55           O  
ANISOU 1422  O   HIS A 175     9417   9056   8333   -965   -241   -291       O  
ATOM   1423  CB  HIS A 175      39.621  81.071  -4.574  1.00 73.50           C  
ANISOU 1423  CB  HIS A 175     9898   9352   8677   -854   -217   -304       C  
ATOM   1424  CG  HIS A 175      38.502  81.845  -5.207  1.00 72.58           C  
ANISOU 1424  CG  HIS A 175     9858   9219   8501   -830   -227   -336       C  
ATOM   1425  ND1 HIS A 175      38.716  82.951  -6.003  1.00 71.39           N  
ANISOU 1425  ND1 HIS A 175     9808   9107   8211   -887   -270   -374       N  
ATOM   1426  CD2 HIS A 175      37.158  81.696  -5.125  1.00 71.56           C  
ANISOU 1426  CD2 HIS A 175     9719   9035   8434   -757   -203   -331       C  
ATOM   1427  CE1 HIS A 175      37.552  83.435  -6.402  1.00 73.31           C  
ANISOU 1427  CE1 HIS A 175    10102   9317   8434   -849   -275   -395       C  
ATOM   1428  NE2 HIS A 175      36.592  82.693  -5.882  1.00 72.36           N  
ANISOU 1428  NE2 HIS A 175     9914   9140   8439   -769   -234   -370       N  
ATOM   1429  N   ALA A 176      41.826  78.250  -5.008  1.00 59.07           N  
ANISOU 1429  N   ALA A 176     7771   7143   7531   -594   -455    492       N  
ATOM   1430  CA  ALA A 176      43.006  77.614  -4.456  1.00 65.00           C  
ANISOU 1430  CA  ALA A 176     8384   7920   8393   -661   -480    490       C  
ATOM   1431  C   ALA A 176      43.989  77.246  -5.560  1.00 66.23           C  
ANISOU 1431  C   ALA A 176     8423   8147   8594   -709   -415    465       C  
ATOM   1432  O   ALA A 176      43.608  77.013  -6.709  1.00 69.29           O  
ANISOU 1432  O   ALA A 176     8809   8566   8953   -656   -357    439       O  
ATOM   1433  CB  ALA A 176      42.624  76.359  -3.662  1.00 68.87           C  
ANISOU 1433  CB  ALA A 176     8780   8416   8973   -582   -520    468       C  
ATOM   1434  N   ASN A 177      45.267  77.186  -5.180  1.00 67.01           N  
ANISOU 1434  N   ASN A 177     8426   8270   8765   -801   -429    471       N  
ATOM   1435  CA  ASN A 177      46.362  76.823  -6.080  1.00 67.84           C  
ANISOU 1435  CA  ASN A 177     8402   8447   8927   -852   -364    456       C  
ATOM   1436  C   ASN A 177      46.494  75.304  -6.093  1.00 71.10           C  
ANISOU 1436  C   ASN A 177     8661   8927   9428   -775   -373    419       C  
ATOM   1437  O   ASN A 177      47.274  74.705  -5.351  1.00 84.61           O  
ANISOU 1437  O   ASN A 177    10262  10669  11219   -794   -419    408       O  
ATOM   1438  CB  ASN A 177      47.654  77.500  -5.649  1.00 70.32           C  
ANISOU 1438  CB  ASN A 177     8673   8761   9283   -990   -377    475       C  
ATOM   1439  CG  ASN A 177      48.741  77.390  -6.693  1.00 74.51           C  
ANISOU 1439  CG  ASN A 177     9089   9359   9862  -1053   -285    469       C  
ATOM   1440  OD1 ASN A 177      48.761  76.450  -7.482  1.00 79.63           O  
ANISOU 1440  OD1 ASN A 177     9649  10068  10538   -980   -235    448       O  
ATOM   1441  ND2 ASN A 177      49.661  78.344  -6.695  1.00 81.19           N  
ANISOU 1441  ND2 ASN A 177     9939  10189  10719  -1188   -259    489       N  
ATOM   1442  N   LEU A 178      45.694  74.666  -6.942  1.00 75.41           N  
ANISOU 1442  N   LEU A 178     9211   9492   9951   -679   -336    395       N  
ATOM   1443  CA  LEU A 178      45.696  73.214  -7.061  1.00 79.12           C  
ANISOU 1443  CA  LEU A 178     9560  10015  10487   -600   -340    360       C  
ATOM   1444  C   LEU A 178      46.168  72.744  -8.432  1.00 92.29           C  
ANISOU 1444  C   LEU A 178    11167  11744  12157   -575   -264    348       C  
ATOM   1445  O   LEU A 178      45.962  71.579  -8.784  1.00 92.98           O  
ANISOU 1445  O   LEU A 178    11189  11868  12273   -494   -263    320       O  
ATOM   1446  CB  LEU A 178      44.298  72.663  -6.777  1.00 73.33           C  
ANISOU 1446  CB  LEU A 178     8877   9245   9741   -500   -373    337       C  
ATOM   1447  CG  LEU A 178      43.707  72.937  -5.393  1.00 73.80           C  
ANISOU 1447  CG  LEU A 178     9003   9237   9800   -496   -437    352       C  
ATOM   1448  CD1 LEU A 178      42.386  72.201  -5.215  1.00 72.99           C  
ANISOU 1448  CD1 LEU A 178     8917   9107   9708   -398   -448    325       C  
ATOM   1449  CD2 LEU A 178      44.694  72.559  -4.301  1.00 72.42           C  
ANISOU 1449  CD2 LEU A 178     8758   9069   9692   -532   -484    355       C  
ATOM   1450  N   ASP A 179      46.798  73.626  -9.217  1.00102.35           N  
ANISOU 1450  N   ASP A 179    12473  13020  13397   -641   -195    372       N  
ATOM   1451  CA  ASP A 179      47.215  73.256 -10.566  1.00110.61           C  
ANISOU 1451  CA  ASP A 179    13486  14106  14435   -603   -109    369       C  
ATOM   1452  C   ASP A 179      48.286  72.172 -10.579  1.00106.59           C  
ANISOU 1452  C   ASP A 179    12810  13682  14009   -597    -98    366       C  
ATOM   1453  O   ASP A 179      48.400  71.447 -11.573  1.00106.46           O  
ANISOU 1453  O   ASP A 179    12764  13700  13986   -522    -48    360       O  
ATOM   1454  CB  ASP A 179      47.734  74.483 -11.323  1.00121.08           C  
ANISOU 1454  CB  ASP A 179    14894  15403  15709   -679    -20    399       C  
ATOM   1455  CG  ASP A 179      48.673  75.338 -10.486  1.00127.73           C  
ANISOU 1455  CG  ASP A 179    15702  16240  16590   -825    -30    427       C  
ATOM   1456  OD1 ASP A 179      48.515  76.577 -10.496  1.00130.10           O  
ANISOU 1456  OD1 ASP A 179    16134  16476  16822   -893     -6    447       O  
ATOM   1457  OD2 ASP A 179      49.554  74.773  -9.800  1.00129.57           O  
ANISOU 1457  OD2 ASP A 179    15786  16530  16915   -868    -68    425       O  
ATOM   1458  N   SER A 180      49.054  72.032  -9.501  1.00103.23           N  
ANISOU 1458  N   SER A 180    12285  13287  13651   -661   -150    367       N  
ATOM   1459  CA  SER A 180      50.075  70.997  -9.432  1.00 97.57           C  
ANISOU 1459  CA  SER A 180    11412  12659  13003   -643   -148    358       C  
ATOM   1460  C   SER A 180      49.514  69.642  -9.020  1.00 91.50           C  
ANISOU 1460  C   SER A 180    10616  11907  12244   -532   -205    323       C  
ATOM   1461  O   SER A 180      50.275  68.671  -8.954  1.00 90.54           O  
ANISOU 1461  O   SER A 180    10383  11859  12159   -495   -207    310       O  
ATOM   1462  CB  SER A 180      51.184  71.415  -8.460  1.00 97.03           C  
ANISOU 1462  CB  SER A 180    11247  12619  13002   -748   -189    361       C  
ATOM   1463  OG  SER A 180      50.653  71.764  -7.193  1.00 97.62           O  
ANISOU 1463  OG  SER A 180    11386  12630  13075   -767   -285    351       O  
ATOM   1464  N   CYS A 181      48.209  69.546  -8.768  1.00 84.54           N  
ANISOU 1464  N   CYS A 181     9834  10960  11327   -478   -244    305       N  
ATOM   1465  CA  CYS A 181      47.604  68.271  -8.414  1.00 77.10           C  
ANISOU 1465  CA  CYS A 181     8876  10021  10399   -383   -284    270       C  
ATOM   1466  C   CYS A 181      47.331  67.463  -9.671  1.00 74.03           C  
ANISOU 1466  C   CYS A 181     8486   9659   9983   -296   -239    259       C  
ATOM   1467  O   CYS A 181      46.873  67.998 -10.685  1.00 73.75           O  
ANISOU 1467  O   CYS A 181     8522   9598   9902   -281   -198    267       O  
ATOM   1468  CB  CYS A 181      46.301  68.476  -7.642  1.00 78.40           C  
ANISOU 1468  CB  CYS A 181     9137  10103  10550   -362   -334    256       C  
ATOM   1469  SG  CYS A 181      46.465  69.239  -6.016  1.00 79.81           S  
ANISOU 1469  SG  CYS A 181     9349  10227  10750   -429   -401    272       S  
ATOM   1470  N   LYS A 182      47.579  66.161  -9.585  1.00 69.59           N  
ANISOU 1470  N   LYS A 182     7862   9142   9438   -228   -251    237       N  
ATOM   1471  CA  LYS A 182      47.514  65.287 -10.743  1.00 72.38           C  
ANISOU 1471  CA  LYS A 182     8214   9524   9762   -142   -215    231       C  
ATOM   1472  C   LYS A 182      46.884  63.965 -10.334  1.00 76.40           C  
ANISOU 1472  C   LYS A 182     8728  10023  10278    -64   -257    190       C  
ATOM   1473  O   LYS A 182      47.219  63.402  -9.288  1.00 82.67           O  
ANISOU 1473  O   LYS A 182     9483  10832  11097    -64   -288    174       O  
ATOM   1474  CB  LYS A 182      48.917  65.072 -11.332  1.00 75.38           C  
ANISOU 1474  CB  LYS A 182     8505   9991  10145   -142   -158    262       C  
ATOM   1475  CG  LYS A 182      48.990  64.216 -12.587  1.00 76.96           C  
ANISOU 1475  CG  LYS A 182     8719  10218  10303    -41   -116    270       C  
ATOM   1476  CD  LYS A 182      50.441  64.074 -13.037  1.00 84.71           C  
ANISOU 1476  CD  LYS A 182     9605  11290  11292    -42    -50    309       C  
ATOM   1477  CE  LYS A 182      50.583  63.172 -14.251  1.00 91.98           C  
ANISOU 1477  CE  LYS A 182    10554  12235  12161     75     -6    327       C  
ATOM   1478  NZ  LYS A 182      52.014  62.982 -14.637  1.00 93.17           N  
ANISOU 1478  NZ  LYS A 182    10602  12480  12318     85     66    371       N  
ATOM   1479  N   ARG A 183      45.973  63.475 -11.163  1.00 73.63           N  
ANISOU 1479  N   ARG A 183     8435   9640   9903      4   -259    169       N  
ATOM   1480  CA  ARG A 183      45.313  62.201 -10.930  1.00 72.45           C  
ANISOU 1480  CA  ARG A 183     8297   9470   9760     70   -291    127       C  
ATOM   1481  C   ARG A 183      45.335  61.400 -12.221  1.00 71.91           C  
ANISOU 1481  C   ARG A 183     8250   9421   9650    156   -276    124       C  
ATOM   1482  O   ARG A 183      45.025  61.933 -13.291  1.00 70.01           O  
ANISOU 1482  O   ARG A 183     8059   9160   9382    180   -261    132       O  
ATOM   1483  CB  ARG A 183      43.878  62.417 -10.443  1.00 72.09           C  
ANISOU 1483  CB  ARG A 183     8306   9343   9743     59   -328     92       C  
ATOM   1484  CG  ARG A 183      43.007  61.173 -10.462  1.00 72.30           C  
ANISOU 1484  CG  ARG A 183     8350   9335   9785    118   -351     44       C  
ATOM   1485  CD  ARG A 183      41.663  61.451  -9.809  1.00 71.64           C  
ANISOU 1485  CD  ARG A 183     8296   9176   9747     96   -375     13       C  
ATOM   1486  NE  ARG A 183      41.805  61.620  -8.366  1.00 70.05           N  
ANISOU 1486  NE  ARG A 183     8091   8950   9576     54   -373     23       N  
ATOM   1487  CZ  ARG A 183      40.829  62.023  -7.561  1.00 71.40           C  
ANISOU 1487  CZ  ARG A 183     8291   9054   9784     32   -381     14       C  
ATOM   1488  NH1 ARG A 183      39.631  62.306  -8.061  1.00 72.38           N  
ANISOU 1488  NH1 ARG A 183     8434   9142   9926     43   -394    -11       N  
ATOM   1489  NH2 ARG A 183      41.050  62.144  -6.257  1.00 67.94           N  
ANISOU 1489  NH2 ARG A 183     7867   8582   9364     11   -378     28       N  
ATOM   1490  N   VAL A 184      45.704  60.127 -12.120  1.00 72.38           N  
ANISOU 1490  N   VAL A 184     8292   9515   9696    214   -281    112       N  
ATOM   1491  CA  VAL A 184      45.763  59.233 -13.269  1.00 71.29           C  
ANISOU 1491  CA  VAL A 184     8190   9391   9508    307   -274    113       C  
ATOM   1492  C   VAL A 184      44.785  58.099 -13.024  1.00 72.06           C  
ANISOU 1492  C   VAL A 184     8332   9436   9613    347   -318     60       C  
ATOM   1493  O   VAL A 184      44.952  57.318 -12.078  1.00 74.03           O  
ANISOU 1493  O   VAL A 184     8567   9693   9868    347   -323     41       O  
ATOM   1494  CB  VAL A 184      47.180  58.687 -13.509  1.00 67.08           C  
ANISOU 1494  CB  VAL A 184     7607   8949   8932    350   -232    154       C  
ATOM   1495  CG1 VAL A 184      47.188  57.776 -14.730  1.00 65.33           C  
ANISOU 1495  CG1 VAL A 184     7447   8730   8646    461   -226    164       C  
ATOM   1496  CG2 VAL A 184      48.166  59.827 -13.681  1.00 65.36           C  
ANISOU 1496  CG2 VAL A 184     7327   8779   8726    292   -179    204       C  
ATOM   1497  N   LEU A 185      43.781  58.000 -13.884  1.00 71.96           N  
ANISOU 1497  N   LEU A 185     8377   9366   9599    386   -349     30       N  
ATOM   1498  CA  LEU A 185      42.768  56.963 -13.802  1.00 71.74           C  
ANISOU 1498  CA  LEU A 185     8386   9281   9590    414   -393    -26       C  
ATOM   1499  C   LEU A 185      42.975  55.938 -14.904  1.00 70.09           C  
ANISOU 1499  C   LEU A 185     8235   9079   9318    512   -408    -25       C  
ATOM   1500  O   LEU A 185      43.570  56.214 -15.949  1.00 65.48           O  
ANISOU 1500  O   LEU A 185     7677   8521   8679    570   -390     15       O  
ATOM   1501  CB  LEU A 185      41.366  57.556 -13.910  1.00 72.99           C  
ANISOU 1501  CB  LEU A 185     8560   9369   9806    386   -434    -73       C  
ATOM   1502  CG  LEU A 185      41.014  58.525 -12.790  1.00 76.67           C  
ANISOU 1502  CG  LEU A 185     8988   9817  10326    300   -422    -71       C  
ATOM   1503  CD1 LEU A 185      39.583  58.991 -12.936  1.00 85.10           C  
ANISOU 1503  CD1 LEU A 185    10068  10822  11443    290   -463   -120       C  
ATOM   1504  CD2 LEU A 185      41.213  57.838 -11.454  1.00 77.58           C  
ANISOU 1504  CD2 LEU A 185     9080   9927  10469    267   -402    -78       C  
ATOM   1505  N   ASN A 186      42.451  54.746 -14.660  1.00 74.30           N  
ANISOU 1505  N   ASN A 186     8801   9577   9855    533   -436    -68       N  
ATOM   1506  CA  ASN A 186      42.572  53.653 -15.612  1.00 80.59           C  
ANISOU 1506  CA  ASN A 186     9672  10367  10583    628   -461    -69       C  
ATOM   1507  C   ASN A 186      41.290  52.840 -15.626  1.00 84.20           C  
ANISOU 1507  C   ASN A 186    10170  10739  11085    622   -519   -143       C  
ATOM   1508  O   ASN A 186      40.861  52.334 -14.585  1.00 92.12           O  
ANISOU 1508  O   ASN A 186    11156  11712  12133    565   -506   -179       O  
ATOM   1509  CB  ASN A 186      43.768  52.776 -15.250  1.00 84.05           C  
ANISOU 1509  CB  ASN A 186    10117  10874  10944    671   -420    -32       C  
ATOM   1510  CG  ASN A 186      44.067  51.749 -16.304  1.00 89.43           C  
ANISOU 1510  CG  ASN A 186    10891  11558  11532    783   -439    -14       C  
ATOM   1511  OD1 ASN A 186      44.732  52.026 -17.304  1.00 90.39           O  
ANISOU 1511  OD1 ASN A 186    11035  11714  11596    856   -423     39       O  
ATOM   1512  ND2 ASN A 186      43.560  50.541 -16.089  1.00 94.95           N  
ANISOU 1512  ND2 ASN A 186    11656  12210  12211    802   -468    -58       N  
ATOM   1513  N   VAL A 187      40.703  52.698 -16.812  1.00 83.26           N  
ANISOU 1513  N   VAL A 187    10108  10574  10953    685   -579   -167       N  
ATOM   1514  CA  VAL A 187      39.498  51.904 -17.030  1.00 82.02           C  
ANISOU 1514  CA  VAL A 187     9986  10336  10844    683   -650   -244       C  
ATOM   1515  C   VAL A 187      39.860  50.718 -17.911  1.00 80.24           C  
ANISOU 1515  C   VAL A 187     9866  10097  10525    783   -684   -234       C  
ATOM   1516  O   VAL A 187      40.503  50.889 -18.954  1.00 76.70           O  
ANISOU 1516  O   VAL A 187     9476   9670   9995    880   -691   -186       O  
ATOM   1517  CB  VAL A 187      38.381  52.749 -17.673  1.00 75.68           C  
ANISOU 1517  CB  VAL A 187     9166   9482  10107    682   -716   -296       C  
ATOM   1518  CG1 VAL A 187      37.079  51.965 -17.731  1.00 69.03           C  
ANISOU 1518  CG1 VAL A 187     8326   8561   9343    660   -791   -387       C  
ATOM   1519  CG2 VAL A 187      38.197  54.051 -16.910  1.00 74.23           C  
ANISOU 1519  CG2 VAL A 187     8900   9321   9984    603   -676   -288       C  
ATOM   1520  N   VAL A 188      39.460  49.520 -17.495  1.00 82.25           N  
ANISOU 1520  N   VAL A 188    10158  10308  10785    764   -698   -276       N  
ATOM   1521  CA  VAL A 188      39.773  48.294 -18.222  1.00 84.10           C  
ANISOU 1521  CA  VAL A 188    10513  10523  10919    856   -733   -267       C  
ATOM   1522  C   VAL A 188      38.471  47.592 -18.592  1.00 81.22           C  
ANISOU 1522  C   VAL A 188    10185  10055  10619    835   -823   -355       C  
ATOM   1523  O   VAL A 188      37.588  47.415 -17.743  1.00 76.30           O  
ANISOU 1523  O   VAL A 188     9503   9386  10101    731   -814   -418       O  
ATOM   1524  CB  VAL A 188      40.712  47.377 -17.411  1.00 85.65           C  
ANISOU 1524  CB  VAL A 188    10748  10767  11028    865   -663   -231       C  
ATOM   1525  CG1 VAL A 188      40.074  46.927 -16.098  1.00 87.82           C  
ANISOU 1525  CG1 VAL A 188    10992  10998  11380    759   -626   -289       C  
ATOM   1526  CG2 VAL A 188      41.108  46.176 -18.246  1.00 89.77           C  
ANISOU 1526  CG2 VAL A 188    11412  11274  11421    976   -698   -210       C  
ATOM   1527  N   CYS A 189      38.338  47.229 -19.867  1.00 90.38           N  
ANISOU 1527  N   CYS A 189    11444  11174  11723    937   -909   -360       N  
ATOM   1528  CA  CYS A 189      37.222  46.431 -20.355  1.00 92.11           C  
ANISOU 1528  CA  CYS A 189    11713  11293  11991    932  -1012   -446       C  
ATOM   1529  C   CYS A 189      37.717  45.067 -20.813  1.00 91.68           C  
ANISOU 1529  C   CYS A 189    11813  11211  11809   1013  -1036   -421       C  
ATOM   1530  O   CYS A 189      38.877  44.906 -21.205  1.00 90.46           O  
ANISOU 1530  O   CYS A 189    11740  11113  11516   1118   -998   -334       O  
ATOM   1531  CB  CYS A 189      36.491  47.130 -21.507  1.00 96.62           C  
ANISOU 1531  CB  CYS A 189    12289  11816  12604    995  -1121   -491       C  
ATOM   1532  SG  CYS A 189      35.072  46.208 -22.180  1.00102.06           S  
ANISOU 1532  SG  CYS A 189    13024  12381  13372    992  -1277   -613       S  
ATOM   1533  N   LYS A 190      36.819  44.084 -20.763  1.00101.60           N  
ANISOU 1533  N   LYS A 190    13111  12379  13112    964  -1097   -498       N  
ATOM   1534  CA  LYS A 190      37.207  42.712 -21.074  1.00113.35           C  
ANISOU 1534  CA  LYS A 190    14764  13831  14473   1029  -1118   -481       C  
ATOM   1535  C   LYS A 190      37.517  42.520 -22.557  1.00116.35           C  
ANISOU 1535  C   LYS A 190    15285  14181  14740   1191  -1217   -445       C  
ATOM   1536  O   LYS A 190      38.355  41.678 -22.902  1.00113.37           O  
ANISOU 1536  O   LYS A 190    15056  13816  14204   1293  -1205   -379       O  
ATOM   1537  CB  LYS A 190      36.108  41.754 -20.618  1.00118.20           C  
ANISOU 1537  CB  LYS A 190    15387  14346  15177    917  -1152   -578       C  
ATOM   1538  CG  LYS A 190      35.871  41.789 -19.113  1.00118.95           C  
ANISOU 1538  CG  LYS A 190    15378  14454  15364    774  -1033   -605       C  
ATOM   1539  CD  LYS A 190      34.638  40.995 -18.706  1.00121.36           C  
ANISOU 1539  CD  LYS A 190    15671  14648  15791    651  -1054   -708       C  
ATOM   1540  CE  LYS A 190      34.378  41.122 -17.210  1.00118.85           C  
ANISOU 1540  CE  LYS A 190    15258  14331  15568    522   -922   -728       C  
ATOM   1541  NZ  LYS A 190      33.147  40.405 -16.774  1.00116.92           N  
ANISOU 1541  NZ  LYS A 190    14989  13974  15461    391   -919   -828       N  
ATOM   1542  N   THR A 191      36.866  43.275 -23.443  1.00121.31           N  
ANISOU 1542  N   THR A 191    15887  14769  15438   1232  -1314   -485       N  
ATOM   1543  CA  THR A 191      37.135  43.181 -24.877  1.00128.17           C  
ANISOU 1543  CA  THR A 191    16907  15593  16199   1406  -1408   -453       C  
ATOM   1544  C   THR A 191      37.588  44.493 -25.499  1.00127.38           C  
ANISOU 1544  C   THR A 191    16778  15538  16083   1494  -1384   -403       C  
ATOM   1545  O   THR A 191      38.427  44.478 -26.406  1.00131.52           O  
ANISOU 1545  O   THR A 191    17432  16067  16474   1650  -1379   -320       O  
ATOM   1546  CB  THR A 191      35.893  42.671 -25.631  1.00135.39           C  
ANISOU 1546  CB  THR A 191    17878  16381  17183   1415  -1576   -562       C  
ATOM   1547  OG1 THR A 191      34.750  43.464 -25.285  1.00136.13           O  
ANISOU 1547  OG1 THR A 191    17802  16459  17461   1304  -1615   -665       O  
ATOM   1548  CG2 THR A 191      35.627  41.201 -25.311  1.00136.76           C  
ANISOU 1548  CG2 THR A 191    18142  16491  17328   1360  -1605   -596       C  
ATOM   1549  N   CYS A 192      37.053  45.630 -25.042  1.00123.09           N  
ANISOU 1549  N   CYS A 192    16078  15021  15667   1404  -1361   -447       N  
ATOM   1550  CA  CYS A 192      37.468  46.912 -25.597  1.00117.49           C  
ANISOU 1550  CA  CYS A 192    15355  14347  14937   1479  -1328   -403       C  
ATOM   1551  C   CYS A 192      38.939  47.175 -25.310  1.00108.93           C  
ANISOU 1551  C   CYS A 192    14273  13366  13750   1510  -1184   -277       C  
ATOM   1552  O   CYS A 192      39.652  47.760 -26.135  1.00110.18           O  
ANISOU 1552  O   CYS A 192    14501  13537  13826   1629  -1151   -208       O  
ATOM   1553  CB  CYS A 192      36.605  48.040 -25.029  1.00117.49           C  
ANISOU 1553  CB  CYS A 192    15196  14362  15083   1368  -1326   -474       C  
ATOM   1554  SG  CYS A 192      34.872  47.998 -25.529  1.00126.35           S  
ANISOU 1554  SG  CYS A 192    16293  15378  16336   1356  -1501   -630       S  
ATOM   1555  N   GLY A 193      39.410  46.750 -24.145  1.00102.68           N  
ANISOU 1555  N   GLY A 193    13406  12644  12963   1408  -1095   -250       N  
ATOM   1556  CA  GLY A 193      40.790  46.950 -23.758  1.00101.05           C  
ANISOU 1556  CA  GLY A 193    13178  12544  12672   1428   -969   -145       C  
ATOM   1557  C   GLY A 193      40.907  47.872 -22.574  1.00101.70           C  
ANISOU 1557  C   GLY A 193    13092  12700  12848   1291   -881   -147       C  
ATOM   1558  O   GLY A 193      40.005  47.922 -21.725  1.00102.96           O  
ANISOU 1558  O   GLY A 193    13164  12835  13122   1168   -899   -222       O  
ATOM   1559  N   GLN A 194      42.010  48.620 -22.487  1.00105.08           N  
ANISOU 1559  N   GLN A 194    13473  13215  13236   1309   -784    -65       N  
ATOM   1560  CA  GLN A 194      42.267  49.487 -21.352  1.00106.82           C  
ANISOU 1560  CA  GLN A 194    13548  13507  13533   1186   -704    -59       C  
ATOM   1561  C   GLN A 194      42.568  50.889 -21.862  1.00104.51           C  
ANISOU 1561  C   GLN A 194    13218  13234  13257   1199   -664    -22       C  
ATOM   1562  O   GLN A 194      43.178  51.069 -22.918  1.00104.40           O  
ANISOU 1562  O   GLN A 194    13286  13220  13163   1315   -645     36       O  
ATOM   1563  CB  GLN A 194      43.403  48.902 -20.504  1.00110.90           C  
ANISOU 1563  CB  GLN A 194    14036  14115  13986   1176   -623     -4       C  
ATOM   1564  CG  GLN A 194      43.734  49.569 -19.185  1.00117.10           C  
ANISOU 1564  CG  GLN A 194    14685  14967  14841   1058   -554     -3       C  
ATOM   1565  CD  GLN A 194      44.902  48.852 -18.535  1.00117.47           C  
ANISOU 1565  CD  GLN A 194    14729  15102  14804   1087   -492     42       C  
ATOM   1566  OE1 GLN A 194      44.925  47.624 -18.558  1.00114.31           O  
ANISOU 1566  OE1 GLN A 194    14423  14685  14324   1144   -512     32       O  
ATOM   1567  NE2 GLN A 194      45.765  49.577 -17.823  1.00120.02           N  
ANISOU 1567  NE2 GLN A 194    14944  15511  15148   1039   -425     77       N  
ATOM   1568  N   GLN A 195      42.144  51.889 -21.090  1.00102.70           N  
ANISOU 1568  N   GLN A 195    12879  13017  13125   1084   -644    -53       N  
ATOM   1569  CA  GLN A 195      42.297  53.286 -21.476  1.00 99.80           C  
ANISOU 1569  CA  GLN A 195    12487  12658  12773   1080   -606    -29       C  
ATOM   1570  C   GLN A 195      42.502  54.128 -20.232  1.00 97.13           C  
ANISOU 1570  C   GLN A 195    12021  12377  12506    945   -544    -22       C  
ATOM   1571  O   GLN A 195      41.731  54.027 -19.274  1.00 97.82           O  
ANISOU 1571  O   GLN A 195    12049  12447  12673    853   -572    -77       O  
ATOM   1572  CB  GLN A 195      41.072  53.782 -22.253  1.00103.43           C  
ANISOU 1572  CB  GLN A 195    13002  13027  13270   1117   -693   -101       C  
ATOM   1573  CG  GLN A 195      41.052  55.290 -22.491  1.00109.25           C  
ANISOU 1573  CG  GLN A 195    13725  13763  14019   1102   -653    -92       C  
ATOM   1574  CD  GLN A 195      42.096  55.746 -23.493  1.00114.78           C  
ANISOU 1574  CD  GLN A 195    14510  14474  14627   1204   -578    -12       C  
ATOM   1575  OE1 GLN A 195      42.403  55.038 -24.454  1.00117.94           O  
ANISOU 1575  OE1 GLN A 195    15019  14842  14949   1333   -596     14       O  
ATOM   1576  NE2 GLN A 195      42.649  56.935 -23.273  1.00114.01           N  
ANISOU 1576  NE2 GLN A 195    14369  14413  14536   1148   -489     30       N  
ATOM   1577  N   GLN A 196      43.541  54.957 -20.249  1.00 95.20           N  
ANISOU 1577  N   GLN A 196    11740  12194  12237    935   -459     47       N  
ATOM   1578  CA  GLN A 196      43.905  55.772 -19.102  1.00 94.45           C  
ANISOU 1578  CA  GLN A 196    11534  12154  12200    813   -406     61       C  
ATOM   1579  C   GLN A 196      43.762  57.251 -19.437  1.00 86.64           C  
ANISOU 1579  C   GLN A 196    10545  11146  11230    781   -377     70       C  
ATOM   1580  O   GLN A 196      44.075  57.681 -20.552  1.00 88.67           O  
ANISOU 1580  O   GLN A 196    10876  11383  11433    861   -347    102       O  
ATOM   1581  CB  GLN A 196      45.339  55.430 -18.658  1.00 97.91           C  
ANISOU 1581  CB  GLN A 196    11913  12688  12599    812   -333    128       C  
ATOM   1582  CG  GLN A 196      46.429  55.969 -19.571  1.00104.28           C  
ANISOU 1582  CG  GLN A 196    12733  13538  13352    870   -255    204       C  
ATOM   1583  CD  GLN A 196      47.820  55.782 -19.003  1.00113.24           C  
ANISOU 1583  CD  GLN A 196    13774  14780  14470    852   -185    260       C  
ATOM   1584  OE1 GLN A 196      47.992  55.219 -17.923  1.00118.89           O  
ANISOU 1584  OE1 GLN A 196    14430  15539  15204    808   -202    238       O  
ATOM   1585  NE2 GLN A 196      48.826  56.244 -19.739  1.00114.11           N  
ANISOU 1585  NE2 GLN A 196    13875  14934  14548    892   -102    330       N  
ATOM   1586  N   THR A 197      43.264  58.022 -18.469  1.00 83.26           N  
ANISOU 1586  N   THR A 197    10052  10714  10870    673   -382     43       N  
ATOM   1587  CA  THR A 197      43.112  59.467 -18.595  1.00 86.23           C  
ANISOU 1587  CA  THR A 197    10436  11072  11255    631   -354     50       C  
ATOM   1588  C   THR A 197      43.778  60.151 -17.409  1.00 82.71           C  
ANISOU 1588  C   THR A 197     9897  10681  10849    512   -304     85       C  
ATOM   1589  O   THR A 197      44.012  59.539 -16.364  1.00 74.90           O  
ANISOU 1589  O   THR A 197     8840   9726   9894    465   -311     81       O  
ATOM   1590  CB  THR A 197      41.637  59.900 -18.683  1.00 87.62           C  
ANISOU 1590  CB  THR A 197    10649  11176  11465    631   -428    -24       C  
ATOM   1591  OG1 THR A 197      40.980  59.647 -17.436  1.00 88.08           O  
ANISOU 1591  OG1 THR A 197    10634  11234  11599    545   -460    -61       O  
ATOM   1592  CG2 THR A 197      40.920  59.143 -19.791  1.00 89.19           C  
ANISOU 1592  CG2 THR A 197    10934  11317  11637    748   -501    -73       C  
ATOM   1593  N   THR A 198      44.062  61.441 -17.578  1.00 87.39           N  
ANISOU 1593  N   THR A 198    10501  11271  11431    470   -255    113       N  
ATOM   1594  CA  THR A 198      44.761  62.237 -16.575  1.00 86.72           C  
ANISOU 1594  CA  THR A 198    10341  11229  11379    357   -213    148       C  
ATOM   1595  C   THR A 198      43.934  63.462 -16.209  1.00 86.65           C  
ANISOU 1595  C   THR A 198    10369  11171  11385    294   -230    127       C  
ATOM   1596  O   THR A 198      43.411  64.154 -17.091  1.00 87.84           O  
ANISOU 1596  O   THR A 198    10611  11274  11492    339   -225    113       O  
ATOM   1597  CB  THR A 198      46.141  62.671 -17.082  1.00 85.76           C  
ANISOU 1597  CB  THR A 198    10195  11159  11230    349   -121    215       C  
ATOM   1598  OG1 THR A 198      46.915  61.514 -17.417  1.00 87.70           O  
ANISOU 1598  OG1 THR A 198    10408  11459  11453    420   -104    240       O  
ATOM   1599  CG2 THR A 198      46.877  63.472 -16.017  1.00 84.23           C  
ANISOU 1599  CG2 THR A 198     9914  11009  11082    223    -92    242       C  
ATOM   1600  N   LEU A 199      43.817  63.723 -14.910  1.00 80.47           N  
ANISOU 1600  N   LEU A 199     9530  10395  10651    205   -250    123       N  
ATOM   1601  CA  LEU A 199      43.065  64.851 -14.383  1.00 70.98           C  
ANISOU 1601  CA  LEU A 199     8365   9149   9455    147   -268    112       C  
ATOM   1602  C   LEU A 199      44.008  65.745 -13.595  1.00 67.85           C  
ANISOU 1602  C   LEU A 199     7930   8780   9069     44   -229    160       C  
ATOM   1603  O   LEU A 199      44.879  65.258 -12.870  1.00 69.69           O  
ANISOU 1603  O   LEU A 199     8080   9062   9338      7   -224    179       O  
ATOM   1604  CB  LEU A 199      41.920  64.394 -13.479  1.00 66.05           C  
ANISOU 1604  CB  LEU A 199     7725   8489   8882    141   -331     65       C  
ATOM   1605  CG  LEU A 199      40.827  63.551 -14.123  1.00 66.12           C  
ANISOU 1605  CG  LEU A 199     7758   8463   8900    224   -381      5       C  
ATOM   1606  CD1 LEU A 199      39.863  63.043 -13.063  1.00 64.63           C  
ANISOU 1606  CD1 LEU A 199     7533   8243   8780    198   -420    -34       C  
ATOM   1607  CD2 LEU A 199      40.098  64.383 -15.159  1.00 66.13           C  
ANISOU 1607  CD2 LEU A 199     7847   8427   8853    279   -397    -22       C  
ATOM   1608  N   LYS A 200      43.836  67.053 -13.751  1.00 63.42           N  
ANISOU 1608  N   LYS A 200     7438   8186   8472      3   -207    175       N  
ATOM   1609  CA  LYS A 200      44.631  68.035 -13.035  1.00 63.37           C  
ANISOU 1609  CA  LYS A 200     7413   8192   8473   -105   -179    217       C  
ATOM   1610  C   LYS A 200      43.715  69.104 -12.456  1.00 59.37           C  
ANISOU 1610  C   LYS A 200     6990   7626   7941   -143   -210    211       C  
ATOM   1611  O   LYS A 200      42.591  69.307 -12.918  1.00 58.50           O  
ANISOU 1611  O   LYS A 200     6961   7474   7793    -81   -234    177       O  
ATOM   1612  CB  LYS A 200      45.698  68.651 -13.950  1.00 73.98           C  
ANISOU 1612  CB  LYS A 200     8768   9557   9785   -130    -91    258       C  
ATOM   1613  CG  LYS A 200      46.812  67.672 -14.302  1.00 84.57           C  
ANISOU 1613  CG  LYS A 200    10008  10970  11157   -103    -52    279       C  
ATOM   1614  CD  LYS A 200      47.776  68.228 -15.342  1.00 95.12           C  
ANISOU 1614  CD  LYS A 200    11359  12319  12465   -112     53    323       C  
ATOM   1615  CE  LYS A 200      48.744  67.142 -15.822  1.00 99.35           C  
ANISOU 1615  CE  LYS A 200    11804  12927  13019    -54     92    346       C  
ATOM   1616  NZ  LYS A 200      49.638  67.584 -16.935  1.00100.86           N  
ANISOU 1616  NZ  LYS A 200    12013  13124  13184    -44    211    393       N  
ATOM   1617  N   GLY A 201      44.204  69.774 -11.416  1.00 57.37           N  
ANISOU 1617  N   GLY A 201     6720   7371   7707   -238   -218    242       N  
ATOM   1618  CA  GLY A 201      43.455  70.846 -10.793  1.00 56.01           C  
ANISOU 1618  CA  GLY A 201     6642   7142   7498   -273   -246    248       C  
ATOM   1619  C   GLY A 201      42.436  70.370  -9.779  1.00 57.49           C  
ANISOU 1619  C   GLY A 201     6824   7299   7721   -242   -311    225       C  
ATOM   1620  O   GLY A 201      42.680  69.404  -9.052  1.00 61.49           O  
ANISOU 1620  O   GLY A 201     7249   7824   8292   -238   -334    217       O  
ATOM   1621  N   VAL A 202      41.288  71.042  -9.718  1.00 60.56           N  
ANISOU 1621  N   VAL A 202     7308   7640   8064   -214   -332    215       N  
ATOM   1622  CA  VAL A 202      40.279  70.687  -8.726  1.00 62.88           C  
ANISOU 1622  CA  VAL A 202     7598   7898   8395   -186   -378    200       C  
ATOM   1623  C   VAL A 202      39.786  69.265  -8.952  1.00 67.04           C  
ANISOU 1623  C   VAL A 202     8043   8441   8988   -120   -391    151       C  
ATOM   1624  O   VAL A 202      39.555  68.513  -7.998  1.00 69.51           O  
ANISOU 1624  O   VAL A 202     8310   8737   9364   -116   -407    143       O  
ATOM   1625  CB  VAL A 202      39.120  71.698  -8.756  1.00 60.84           C  
ANISOU 1625  CB  VAL A 202     7453   7596   8069   -155   -394    197       C  
ATOM   1626  CG1 VAL A 202      38.098  71.346  -7.695  1.00 62.12           C  
ANISOU 1626  CG1 VAL A 202     7605   7721   8278   -125   -427    190       C  
ATOM   1627  CG2 VAL A 202      39.644  73.098  -8.548  1.00 59.07           C  
ANISOU 1627  CG2 VAL A 202     7332   7349   7764   -223   -379    248       C  
ATOM   1628  N   GLU A 203      39.639  68.863 -10.217  1.00 68.38           N  
ANISOU 1628  N   GLU A 203     8207   8634   9141    -62   -381    115       N  
ATOM   1629  CA  GLU A 203      39.124  67.532 -10.521  1.00 67.11           C  
ANISOU 1629  CA  GLU A 203     7982   8480   9036     -1   -401     65       C  
ATOM   1630  C   GLU A 203      40.032  66.423 -10.013  1.00 71.67           C  
ANISOU 1630  C   GLU A 203     8476   9088   9665    -20   -390     75       C  
ATOM   1631  O   GLU A 203      39.595  65.269  -9.929  1.00 73.05           O  
ANISOU 1631  O   GLU A 203     8610   9258   9889     18   -404     38       O  
ATOM   1632  CB  GLU A 203      38.910  67.381 -12.023  1.00 65.61           C  
ANISOU 1632  CB  GLU A 203     7823   8301   8806     73   -402     29       C  
ATOM   1633  CG  GLU A 203      37.680  68.105 -12.511  1.00 74.95           C  
ANISOU 1633  CG  GLU A 203     9080   9451   9948    128   -434    -12       C  
ATOM   1634  CD  GLU A 203      37.483  67.998 -14.005  1.00 77.40           C  
ANISOU 1634  CD  GLU A 203     9442   9760  10209    219   -444    -56       C  
ATOM   1635  OE1 GLU A 203      38.372  68.458 -14.756  1.00 77.10           O  
ANISOU 1635  OE1 GLU A 203     9458   9728  10106    224   -397    -25       O  
ATOM   1636  OE2 GLU A 203      36.434  67.454 -14.423  1.00 75.56           O  
ANISOU 1636  OE2 GLU A 203     9194   9510  10004    290   -500   -123       O  
ATOM   1637  N   ALA A 204      41.286  66.743  -9.688  1.00 66.64           N  
ANISOU 1637  N   ALA A 204     7818   8484   9018    -76   -365    120       N  
ATOM   1638  CA  ALA A 204      42.230  65.752  -9.195  1.00 57.02           C  
ANISOU 1638  CA  ALA A 204     6525   7305   7837    -81   -359    124       C  
ATOM   1639  C   ALA A 204      42.042  65.452  -7.718  1.00 62.26           C  
ANISOU 1639  C   ALA A 204     7180   7931   8544    -99   -382    122       C  
ATOM   1640  O   ALA A 204      42.622  64.480  -7.221  1.00 66.92           O  
ANISOU 1640  O   ALA A 204     7726   8543   9159    -82   -382    111       O  
ATOM   1641  CB  ALA A 204      43.664  66.219  -9.446  1.00 49.58           C  
ANISOU 1641  CB  ALA A 204     5545   6418   6874   -130   -327    165       C  
ATOM   1642  N   VAL A 205      41.261  66.258  -7.002  1.00 64.29           N  
ANISOU 1642  N   VAL A 205     7496   8130   8802   -121   -398    134       N  
ATOM   1643  CA  VAL A 205      41.086  66.091  -5.566  1.00 62.06           C  
ANISOU 1643  CA  VAL A 205     7231   7794   8554   -126   -413    140       C  
ATOM   1644  C   VAL A 205      39.649  65.788  -5.180  1.00 62.18           C  
ANISOU 1644  C   VAL A 205     7278   7745   8603    -86   -411    115       C  
ATOM   1645  O   VAL A 205      39.366  65.608  -3.993  1.00 67.75           O  
ANISOU 1645  O   VAL A 205     8015   8391   9338    -78   -408    123       O  
ATOM   1646  CB  VAL A 205      41.600  67.322  -4.791  1.00 57.41           C  
ANISOU 1646  CB  VAL A 205     6693   7182   7938   -185   -434    188       C  
ATOM   1647  CG1 VAL A 205      43.053  67.622  -5.158  1.00 54.81           C  
ANISOU 1647  CG1 VAL A 205     6312   6919   7595   -238   -432    207       C  
ATOM   1648  CG2 VAL A 205      40.715  68.523  -5.066  1.00 55.12           C  
ANISOU 1648  CG2 VAL A 205     6485   6856   7602   -197   -437    209       C  
ATOM   1649  N   MET A 206      38.732  65.709  -6.140  1.00 62.54           N  
ANISOU 1649  N   MET A 206     7318   7797   8649    -57   -410     83       N  
ATOM   1650  CA  MET A 206      37.338  65.404  -5.849  1.00 64.98           C  
ANISOU 1650  CA  MET A 206     7631   8052   9005    -24   -407     52       C  
ATOM   1651  C   MET A 206      36.886  64.212  -6.677  1.00 67.00           C  
ANISOU 1651  C   MET A 206     7831   8325   9303     13   -407     -9       C  
ATOM   1652  O   MET A 206      37.238  64.087  -7.855  1.00 69.03           O  
ANISOU 1652  O   MET A 206     8071   8629   9527     31   -422    -25       O  
ATOM   1653  CB  MET A 206      36.420  66.596  -6.128  1.00 61.79           C  
ANISOU 1653  CB  MET A 206     7279   7633   8563    -17   -423     61       C  
ATOM   1654  CG  MET A 206      36.747  67.830  -5.327  1.00 67.79           C  
ANISOU 1654  CG  MET A 206     8119   8367   9270    -52   -427    123       C  
ATOM   1655  SD  MET A 206      35.586  69.173  -5.640  1.00 73.89           S  
ANISOU 1655  SD  MET A 206     8976   9123   9977    -25   -443    132       S  
ATOM   1656  CE  MET A 206      34.046  68.432  -5.097  1.00 74.14           C  
ANISOU 1656  CE  MET A 206     8960   9109  10099     28   -430     93       C  
ATOM   1657  N   TYR A 207      36.106  63.338  -6.050  1.00 63.87           N  
ANISOU 1657  N   TYR A 207     7413   7878   8977     27   -387    -40       N  
ATOM   1658  CA  TYR A 207      35.467  62.231  -6.741  1.00 58.65           C  
ANISOU 1658  CA  TYR A 207     6703   7215   8366     53   -392   -103       C  
ATOM   1659  C   TYR A 207      34.048  62.092  -6.213  1.00 66.50           C  
ANISOU 1659  C   TYR A 207     7678   8147   9441     55   -374   -134       C  
ATOM   1660  O   TYR A 207      33.805  62.232  -5.008  1.00 69.81           O  
ANISOU 1660  O   TYR A 207     8125   8510   9889     44   -333   -105       O  
ATOM   1661  CB  TYR A 207      36.232  60.912  -6.555  1.00 57.01           C  
ANISOU 1661  CB  TYR A 207     6484   7011   8165     60   -369   -116       C  
ATOM   1662  CG  TYR A 207      35.619  59.757  -7.322  1.00 64.08           C  
ANISOU 1662  CG  TYR A 207     7345   7899   9102     83   -380   -180       C  
ATOM   1663  CD1 TYR A 207      35.893  59.568  -8.674  1.00 59.42           C  
ANISOU 1663  CD1 TYR A 207     6746   7358   8471    114   -423   -199       C  
ATOM   1664  CD2 TYR A 207      34.739  58.874  -6.703  1.00 68.36           C  
ANISOU 1664  CD2 TYR A 207     7876   8374   9725     74   -345   -220       C  
ATOM   1665  CE1 TYR A 207      35.326  58.521  -9.382  1.00 59.20           C  
ANISOU 1665  CE1 TYR A 207     6701   7315   8478    139   -447   -259       C  
ATOM   1666  CE2 TYR A 207      34.164  57.826  -7.404  1.00 69.84           C  
ANISOU 1666  CE2 TYR A 207     8034   8547   9954     83   -360   -282       C  
ATOM   1667  CZ  TYR A 207      34.460  57.656  -8.745  1.00 65.69           C  
ANISOU 1667  CZ  TYR A 207     7503   8073   9383    117   -420   -302       C  
ATOM   1668  OH  TYR A 207      33.887  56.620  -9.444  1.00 64.97           O  
ANISOU 1668  OH  TYR A 207     7396   7960   9331    130   -449   -365       O  
ATOM   1669  N   MET A 208      33.116  61.827  -7.122  1.00 66.52           N  
ANISOU 1669  N   MET A 208     7634   8157   9482     76   -407   -195       N  
ATOM   1670  CA  MET A 208      31.702  61.677  -6.796  1.00 66.48           C  
ANISOU 1670  CA  MET A 208     7584   8107   9571     76   -395   -236       C  
ATOM   1671  C   MET A 208      31.284  60.265  -7.201  1.00 68.95           C  
ANISOU 1671  C   MET A 208     7839   8398   9961     71   -395   -306       C  
ATOM   1672  O   MET A 208      31.121  59.981  -8.392  1.00 73.10           O  
ANISOU 1672  O   MET A 208     8337   8956  10481     97   -458   -358       O  
ATOM   1673  CB  MET A 208      30.863  62.731  -7.515  1.00 70.61           C  
ANISOU 1673  CB  MET A 208     8097   8660  10073    109   -448   -258       C  
ATOM   1674  CG  MET A 208      29.404  62.636  -7.180  1.00 72.16           C  
ANISOU 1674  CG  MET A 208     8226   8820  10369    113   -437   -303       C  
ATOM   1675  SD  MET A 208      29.184  63.074  -5.454  1.00 80.00           S  
ANISOU 1675  SD  MET A 208     9261   9747  11387     93   -348   -227       S  
ATOM   1676  CE  MET A 208      27.648  62.242  -5.152  1.00 87.24           C  
ANISOU 1676  CE  MET A 208    10069  10613  12464     82   -305   -294       C  
ATOM   1677  N   GLY A 209      31.114  59.380  -6.224  1.00 70.91           N  
ANISOU 1677  N   GLY A 209     8085   8582  10276     44   -325   -309       N  
ATOM   1678  CA  GLY A 209      30.701  58.024  -6.532  1.00 75.75           C  
ANISOU 1678  CA  GLY A 209     8659   9163  10960     29   -316   -375       C  
ATOM   1679  C   GLY A 209      30.844  57.059  -5.375  1.00 78.74           C  
ANISOU 1679  C   GLY A 209     9077   9465  11377      5   -220   -367       C  
ATOM   1680  O   GLY A 209      30.010  56.168  -5.192  1.00 81.29           O  
ANISOU 1680  O   GLY A 209     9365   9727  11796    -25   -177   -419       O  
ATOM   1681  N   THR A 210      31.911  57.219  -4.595  1.00 79.87           N  
ANISOU 1681  N   THR A 210     9298   9605  11445     19   -185   -308       N  
ATOM   1682  CA  THR A 210      32.133  56.373  -3.434  1.00 77.88           C  
ANISOU 1682  CA  THR A 210     9112   9272  11207     19    -94   -301       C  
ATOM   1683  C   THR A 210      32.827  57.179  -2.347  1.00 69.22           C  
ANISOU 1683  C   THR A 210     8090   8157  10053     43    -69   -232       C  
ATOM   1684  O   THR A 210      33.553  58.136  -2.625  1.00 67.81           O  
ANISOU 1684  O   THR A 210     7917   8046   9803     52   -129   -189       O  
ATOM   1685  CB  THR A 210      32.961  55.126  -3.769  1.00 80.88           C  
ANISOU 1685  CB  THR A 210     9533   9663  11533     33    -93   -330       C  
ATOM   1686  OG1 THR A 210      33.221  54.393  -2.565  1.00 81.51           O  
ANISOU 1686  OG1 THR A 210     9703   9658  11607     48      0   -326       O  
ATOM   1687  CG2 THR A 210      34.280  55.514  -4.416  1.00 79.43           C  
ANISOU 1687  CG2 THR A 210     9364   9579  11238     65   -161   -295       C  
ATOM   1688  N   LEU A 211      32.577  56.789  -1.101  1.00 65.07           N  
ANISOU 1688  N   LEU A 211     7632   7529   9562     55     22   -222       N  
ATOM   1689  CA  LEU A 211      33.244  57.415   0.029  1.00 58.49           C  
ANISOU 1689  CA  LEU A 211     6892   6658   8673     93     41   -163       C  
ATOM   1690  C   LEU A 211      34.609  56.804   0.311  1.00 62.80           C  
ANISOU 1690  C   LEU A 211     7509   7221   9130    132     31   -164       C  
ATOM   1691  O   LEU A 211      35.458  57.462   0.923  1.00 66.19           O  
ANISOU 1691  O   LEU A 211     7993   7657   9497    161      3   -121       O  
ATOM   1692  CB  LEU A 211      32.378  57.299   1.282  1.00 47.84           C  
ANISOU 1692  CB  LEU A 211     5606   5178   7392    111    147   -149       C  
ATOM   1693  CG  LEU A 211      31.008  57.965   1.273  1.00 48.38           C  
ANISOU 1693  CG  LEU A 211     5609   5221   7551     88    173   -138       C  
ATOM   1694  CD1 LEU A 211      30.360  57.739   2.622  1.00 45.07           C  
ANISOU 1694  CD1 LEU A 211     5274   4661   7189    120    298   -114       C  
ATOM   1695  CD2 LEU A 211      31.127  59.453   0.969  1.00 51.43           C  
ANISOU 1695  CD2 LEU A 211     5979   5679   7882     92     88    -85       C  
ATOM   1696  N   SER A 212      34.822  55.558  -0.100  1.00 63.82           N  
ANISOU 1696  N   SER A 212     7643   7357   9250    136     51   -215       N  
ATOM   1697  CA  SER A 212      36.025  54.810   0.244  1.00 62.54           C  
ANISOU 1697  CA  SER A 212     7559   7205   8997    189     54   -225       C  
ATOM   1698  C   SER A 212      37.179  55.186  -0.677  1.00 62.27           C  
ANISOU 1698  C   SER A 212     7469   7305   8884    192    -40   -208       C  
ATOM   1699  O   SER A 212      37.106  54.976  -1.892  1.00 63.06           O  
ANISOU 1699  O   SER A 212     7500   7477   8984    168    -82   -226       O  
ATOM   1700  CB  SER A 212      35.736  53.312   0.157  1.00 58.72           C  
ANISOU 1700  CB  SER A 212     7120   6669   8521    196    120   -285       C  
ATOM   1701  OG  SER A 212      36.894  52.537   0.395  1.00 55.20           O  
ANISOU 1701  OG  SER A 212     6757   6245   7970    260    120   -300       O  
ATOM   1702  N   TYR A 213      38.253  55.721  -0.093  1.00 65.66           N  
ANISOU 1702  N   TYR A 213     7933   7764   9251    226    -73   -177       N  
ATOM   1703  CA  TYR A 213      39.474  55.942  -0.863  1.00 65.87           C  
ANISOU 1703  CA  TYR A 213     7906   7915   9208    231   -145   -163       C  
ATOM   1704  C   TYR A 213      40.083  54.613  -1.301  1.00 70.86           C  
ANISOU 1704  C   TYR A 213     8559   8586   9779    277   -133   -203       C  
ATOM   1705  O   TYR A 213      40.610  54.500  -2.414  1.00 64.32           O  
ANISOU 1705  O   TYR A 213     7669   7856   8912    273   -175   -199       O  
ATOM   1706  CB  TYR A 213      40.484  56.734  -0.031  1.00 56.59           C  
ANISOU 1706  CB  TYR A 213     6756   6754   7991    253   -183   -130       C  
ATOM   1707  CG  TYR A 213      41.608  57.347  -0.838  1.00 59.97           C  
ANISOU 1707  CG  TYR A 213     7100   7310   8376    232   -252   -105       C  
ATOM   1708  CD1 TYR A 213      41.482  57.543  -2.211  1.00 64.18           C  
ANISOU 1708  CD1 TYR A 213     7553   7921   8913    192   -272    -95       C  
ATOM   1709  CD2 TYR A 213      42.797  57.728  -0.230  1.00 59.63           C  
ANISOU 1709  CD2 TYR A 213     7061   7303   8293    255   -294    -93       C  
ATOM   1710  CE1 TYR A 213      42.509  58.110  -2.954  1.00 64.69           C  
ANISOU 1710  CE1 TYR A 213     7549   8092   8940    174   -315    -68       C  
ATOM   1711  CE2 TYR A 213      43.831  58.292  -0.963  1.00 62.09           C  
ANISOU 1711  CE2 TYR A 213     7283   7730   8578    225   -344    -70       C  
ATOM   1712  CZ  TYR A 213      43.683  58.481  -2.322  1.00 66.87           C  
ANISOU 1712  CZ  TYR A 213     7815   8406   9187    183   -345    -54       C  
ATOM   1713  OH  TYR A 213      44.712  59.043  -3.047  1.00 64.15           O  
ANISOU 1713  OH  TYR A 213     7390   8165   8819    156   -374    -27       O  
ATOM   1714  N   GLU A 214      40.001  53.593  -0.438  1.00 75.78           N  
ANISOU 1714  N   GLU A 214     9285   9126  10382    328    -70   -240       N  
ATOM   1715  CA  GLU A 214      40.561  52.284  -0.761  1.00 76.45           C  
ANISOU 1715  CA  GLU A 214     9419   9240  10389    383    -53   -280       C  
ATOM   1716  C   GLU A 214      39.860  51.653  -1.957  1.00 71.41           C  
ANISOU 1716  C   GLU A 214     8740   8618   9776    343    -53   -301       C  
ATOM   1717  O   GLU A 214      40.512  51.082  -2.840  1.00 70.81           O  
ANISOU 1717  O   GLU A 214     8652   8623   9628    373    -86   -305       O  
ATOM   1718  CB  GLU A 214      40.473  51.363   0.457  1.00 83.65           C  
ANISOU 1718  CB  GLU A 214    10477  10036  11269    448     27   -320       C  
ATOM   1719  CG  GLU A 214      41.512  51.623   1.529  1.00 91.75           C  
ANISOU 1719  CG  GLU A 214    11571  11060  12229    529      8   -318       C  
ATOM   1720  CD  GLU A 214      42.891  51.116   1.140  1.00103.45           C  
ANISOU 1720  CD  GLU A 214    13044  12663  13599    598    -44   -334       C  
ATOM   1721  OE1 GLU A 214      43.500  51.666   0.197  1.00106.98           O  
ANISOU 1721  OE1 GLU A 214    13369  13237  14041    565   -113   -301       O  
ATOM   1722  OE2 GLU A 214      43.357  50.145   1.770  1.00109.78           O  
ANISOU 1722  OE2 GLU A 214    13969  13430  14314    694     -9   -379       O  
ATOM   1723  N   GLN A 215      38.524  51.706  -1.984  1.00 69.44           N  
ANISOU 1723  N   GLN A 215     8473   8287   9626    284    -18   -316       N  
ATOM   1724  CA  GLN A 215      37.796  51.149  -3.121  1.00 73.10           C  
ANISOU 1724  CA  GLN A 215     8892   8759  10125    246    -35   -346       C  
ATOM   1725  C   GLN A 215      38.150  51.868  -4.415  1.00 72.27           C  
ANISOU 1725  C   GLN A 215     8691   8766  10002    235   -125   -317       C  
ATOM   1726  O   GLN A 215      38.096  51.270  -5.494  1.00 76.21           O  
ANISOU 1726  O   GLN A 215     9180   9299  10478    243   -160   -336       O  
ATOM   1727  CB  GLN A 215      36.288  51.199  -2.869  1.00 77.66           C  
ANISOU 1727  CB  GLN A 215     9443   9235  10829    181     13   -373       C  
ATOM   1728  CG  GLN A 215      35.484  50.415  -3.890  1.00 84.19           C  
ANISOU 1728  CG  GLN A 215    10236  10051  11703    144     -5   -422       C  
ATOM   1729  CD  GLN A 215      35.618  48.912  -3.703  1.00 89.50           C  
ANISOU 1729  CD  GLN A 215    11018  10663  12324    166     53   -466       C  
ATOM   1730  OE1 GLN A 215      35.363  48.385  -2.621  1.00 98.36           O  
ANISOU 1730  OE1 GLN A 215    12228  11684  13460    170    153   -485       O  
ATOM   1731  NE2 GLN A 215      36.037  48.217  -4.757  1.00 85.38           N  
ANISOU 1731  NE2 GLN A 215    10511  10198  11731    191     -4   -481       N  
ATOM   1732  N   PHE A 216      38.525  53.143  -4.328  1.00 72.38           N  
ANISOU 1732  N   PHE A 216     8650   8829  10020    222   -161   -270       N  
ATOM   1733  CA  PHE A 216      38.947  53.876  -5.514  1.00 67.11           C  
ANISOU 1733  CA  PHE A 216     7912   8260   9327    216   -229   -241       C  
ATOM   1734  C   PHE A 216      40.255  53.326  -6.072  1.00 61.22           C  
ANISOU 1734  C   PHE A 216     7180   7603   8478    274   -249   -225       C  
ATOM   1735  O   PHE A 216      40.498  53.420  -7.283  1.00 50.97           O  
ANISOU 1735  O   PHE A 216     5849   6368   7151    288   -289   -212       O  
ATOM   1736  CB  PHE A 216      39.064  55.361  -5.170  1.00 64.18           C  
ANISOU 1736  CB  PHE A 216     7500   7908   8977    183   -249   -195       C  
ATOM   1737  CG  PHE A 216      39.158  56.262  -6.358  1.00 64.55           C  
ANISOU 1737  CG  PHE A 216     7489   8025   9013    168   -301   -171       C  
ATOM   1738  CD1 PHE A 216      39.849  57.460  -6.275  1.00 65.65           C  
ANISOU 1738  CD1 PHE A 216     7605   8212   9128    148   -320   -122       C  
ATOM   1739  CD2 PHE A 216      38.487  55.962  -7.530  1.00 70.48           C  
ANISOU 1739  CD2 PHE A 216     8220   8780   9779    175   -332   -201       C  
ATOM   1740  CE1 PHE A 216      39.920  58.313  -7.357  1.00 65.61           C  
ANISOU 1740  CE1 PHE A 216     7568   8258   9104    137   -353   -101       C  
ATOM   1741  CE2 PHE A 216      38.556  56.811  -8.623  1.00 70.88           C  
ANISOU 1741  CE2 PHE A 216     8241   8881   9808    179   -375   -182       C  
ATOM   1742  CZ  PHE A 216      39.272  57.990  -8.533  1.00 70.26           C  
ANISOU 1742  CZ  PHE A 216     8149   8848   9698    159   -377   -131       C  
ATOM   1743  N   LYS A 217      41.111  52.765  -5.207  1.00 58.96           N  
ANISOU 1743  N   LYS A 217     6948   7323   8133    320   -220   -228       N  
ATOM   1744  CA  LYS A 217      42.367  52.142  -5.622  1.00 61.20           C  
ANISOU 1744  CA  LYS A 217     7245   7697   8313    389   -233   -218       C  
ATOM   1745  C   LYS A 217      42.199  50.681  -6.030  1.00 70.21           C  
ANISOU 1745  C   LYS A 217     8466   8815   9395    438   -214   -255       C  
ATOM   1746  O   LYS A 217      42.825  50.240  -6.999  1.00 69.40           O  
ANISOU 1746  O   LYS A 217     8363   8786   9218    487   -239   -238       O  
ATOM   1747  CB  LYS A 217      43.400  52.248  -4.498  1.00 58.87           C  
ANISOU 1747  CB  LYS A 217     6970   7425   7972    429   -223   -213       C  
ATOM   1748  CG  LYS A 217      43.645  53.665  -4.012  1.00 58.01           C  
ANISOU 1748  CG  LYS A 217     6797   7331   7915    379   -250   -177       C  
ATOM   1749  CD  LYS A 217      44.539  53.674  -2.789  1.00 61.30           C  
ANISOU 1749  CD  LYS A 217     7248   7748   8295    426   -253   -187       C  
ATOM   1750  CE  LYS A 217      44.806  55.089  -2.311  1.00 62.94           C  
ANISOU 1750  CE  LYS A 217     7401   7963   8552    372   -291   -152       C  
ATOM   1751  NZ  LYS A 217      45.633  55.082  -1.077  1.00 69.10           N  
ANISOU 1751  NZ  LYS A 217     8223   8731   9302    427   -310   -171       N  
ATOM   1752  N   LYS A 218      41.364  49.916  -5.306  1.00 73.85           N  
ANISOU 1752  N   LYS A 218     9007   9167   9885    428   -163   -301       N  
ATOM   1753  CA  LYS A 218      41.106  48.524  -5.679  1.00 78.73           C  
ANISOU 1753  CA  LYS A 218     9717   9748  10449    461   -141   -340       C  
ATOM   1754  C   LYS A 218      40.243  48.418  -6.931  1.00 77.81           C  
ANISOU 1754  C   LYS A 218     9562   9621  10383    421   -185   -351       C  
ATOM   1755  O   LYS A 218      40.343  47.425  -7.661  1.00 73.87           O  
ANISOU 1755  O   LYS A 218     9126   9126   9814    462   -201   -365       O  
ATOM   1756  CB  LYS A 218      40.451  47.740  -4.533  1.00 85.77           C  
ANISOU 1756  CB  LYS A 218    10715  10514  11361    455    -59   -390       C  
ATOM   1757  CG  LYS A 218      41.369  47.231  -3.405  1.00 87.44           C  
ANISOU 1757  CG  LYS A 218    11035  10717  11472    540    -12   -404       C  
ATOM   1758  CD  LYS A 218      42.045  48.311  -2.585  1.00 89.70           C  
ANISOU 1758  CD  LYS A 218    11272  11039  11770    555    -31   -374       C  
ATOM   1759  CE  LYS A 218      42.994  47.673  -1.575  1.00 90.77           C  
ANISOU 1759  CE  LYS A 218    11525  11170  11794    662     -2   -402       C  
ATOM   1760  NZ  LYS A 218      43.876  48.646  -0.869  1.00 92.40           N  
ANISOU 1760  NZ  LYS A 218    11682  11428  11999    690    -44   -380       N  
ATOM   1761  N   GLY A 219      39.354  49.387  -7.163  1.00 75.56           N  
ANISOU 1761  N   GLY A 219     9187   9313  10210    351   -210   -348       N  
ATOM   1762  CA  GLY A 219      38.523  49.391  -8.356  1.00 75.16           C  
ANISOU 1762  CA  GLY A 219     9096   9252  10209    326   -268   -368       C  
ATOM   1763  C   GLY A 219      37.045  49.658  -8.148  1.00 74.96           C  
ANISOU 1763  C   GLY A 219     9021   9139  10322    248   -261   -413       C  
ATOM   1764  O   GLY A 219      36.420  49.109  -7.234  1.00 79.45           O  
ANISOU 1764  O   GLY A 219     9624   9618  10943    211   -193   -448       O  
ATOM   1765  N   VAL A 220      36.470  50.500  -9.002  1.00 70.96           N  
ANISOU 1765  N   VAL A 220     8435   8655   9872    228   -326   -414       N  
ATOM   1766  CA  VAL A 220      35.049  50.825  -8.962  1.00 77.63           C  
ANISOU 1766  CA  VAL A 220     9213   9435  10848    165   -335   -462       C  
ATOM   1767  C   VAL A 220      34.425  50.430 -10.294  1.00 80.08           C  
ANISOU 1767  C   VAL A 220     9507   9741  11180    177   -422   -510       C  
ATOM   1768  O   VAL A 220      35.020  50.646 -11.356  1.00 79.09           O  
ANISOU 1768  O   VAL A 220     9398   9675  10977    238   -487   -487       O  
ATOM   1769  CB  VAL A 220      34.825  52.322  -8.661  1.00 77.65           C  
ANISOU 1769  CB  VAL A 220     9143   9465  10895    142   -341   -428       C  
ATOM   1770  CG1 VAL A 220      33.339  52.649  -8.600  1.00 75.63           C  
ANISOU 1770  CG1 VAL A 220     8813   9152  10769     89   -348   -478       C  
ATOM   1771  CG2 VAL A 220      35.510  52.700  -7.354  1.00 78.77           C  
ANISOU 1771  CG2 VAL A 220     9316   9604  11008    139   -270   -380       C  
ATOM   1772  N   GLN A 221      33.225  49.855 -10.236  1.00 80.10           N  
ANISOU 1772  N   GLN A 221     9481   9665  11290    122   -421   -580       N  
ATOM   1773  CA  GLN A 221      32.545  49.399 -11.440  1.00 87.49           C  
ANISOU 1773  CA  GLN A 221    10402  10581  12259    132   -517   -640       C  
ATOM   1774  C   GLN A 221      31.949  50.585 -12.185  1.00 85.37           C  
ANISOU 1774  C   GLN A 221    10048  10349  12039    149   -600   -656       C  
ATOM   1775  O   GLN A 221      31.232  51.403 -11.599  1.00 81.74           O  
ANISOU 1775  O   GLN A 221     9508   9882  11668    105   -575   -664       O  
ATOM   1776  CB  GLN A 221      31.459  48.381 -11.089  1.00100.47           C  
ANISOU 1776  CB  GLN A 221    12033  12127  14015     57   -489   -717       C  
ATOM   1777  CG  GLN A 221      32.001  47.120 -10.436  1.00109.65           C  
ANISOU 1777  CG  GLN A 221    13312  13240  15111     50   -404   -712       C  
ATOM   1778  CD  GLN A 221      33.069  46.447 -11.284  1.00119.60           C  
ANISOU 1778  CD  GLN A 221    14684  14544  16214    137   -457   -682       C  
ATOM   1779  OE1 GLN A 221      32.841  46.124 -12.451  1.00123.88           O  
ANISOU 1779  OE1 GLN A 221    15240  15085  16743    168   -558   -712       O  
ATOM   1780  NE2 GLN A 221      34.248  46.249 -10.704  1.00122.27           N  
ANISOU 1780  NE2 GLN A 221    15105  14922  16428    186   -392   -624       N  
ATOM   1781  N   ILE A 222      32.252  50.678 -13.476  1.00 88.75           N  
ANISOU 1781  N   ILE A 222    10509  10812  12399    225   -696   -658       N  
ATOM   1782  CA  ILE A 222      31.796  51.793 -14.303  1.00 93.70           C  
ANISOU 1782  CA  ILE A 222    11089  11470  13043    266   -777   -676       C  
ATOM   1783  C   ILE A 222      31.353  51.234 -15.651  1.00100.56           C  
ANISOU 1783  C   ILE A 222    11992  12309  13909    327   -898   -741       C  
ATOM   1784  O   ILE A 222      32.064  50.403 -16.234  1.00104.39           O  
ANISOU 1784  O   ILE A 222    12572  12789  14301    382   -919   -721       O  
ATOM   1785  CB  ILE A 222      32.902  52.852 -14.459  1.00 88.95           C  
ANISOU 1785  CB  ILE A 222    10522  10944  12332    319   -755   -591       C  
ATOM   1786  CG1 ILE A 222      32.901  53.801 -13.256  1.00 95.93           C  
ANISOU 1786  CG1 ILE A 222    11353  11846  13251    258   -675   -550       C  
ATOM   1787  CG2 ILE A 222      32.739  53.637 -15.750  1.00 82.82           C  
ANISOU 1787  CG2 ILE A 222     9763  10186  11516    402   -846   -609       C  
ATOM   1788  CD1 ILE A 222      31.573  54.488 -12.998  1.00 99.16           C  
ANISOU 1788  CD1 ILE A 222    11675  12228  13772    220   -696   -603       C  
ATOM   1789  N   PRO A 223      30.195  51.634 -16.172  1.00100.54           N  
ANISOU 1789  N   PRO A 223    11920  12284  13999    331   -985   -823       N  
ATOM   1790  CA  PRO A 223      29.759  51.121 -17.474  1.00 98.15           C  
ANISOU 1790  CA  PRO A 223    11657  11944  13693    403  -1118   -894       C  
ATOM   1791  C   PRO A 223      30.684  51.572 -18.591  1.00 97.95           C  
ANISOU 1791  C   PRO A 223    11743  11952  13521    533  -1166   -844       C  
ATOM   1792  O   PRO A 223      31.262  52.660 -18.551  1.00 92.45           O  
ANISOU 1792  O   PRO A 223    11058  11310  12760    565  -1122   -783       O  
ATOM   1793  CB  PRO A 223      28.359  51.723 -17.645  1.00 99.44           C  
ANISOU 1793  CB  PRO A 223    11705  12092  13986    387  -1195   -992       C  
ATOM   1794  CG  PRO A 223      27.918  52.070 -16.267  1.00100.74           C  
ANISOU 1794  CG  PRO A 223    11764  12265  14249    277  -1083   -977       C  
ATOM   1795  CD  PRO A 223      29.167  52.477 -15.542  1.00101.60           C  
ANISOU 1795  CD  PRO A 223    11935  12419  14248    274   -969   -860       C  
ATOM   1796  N   CYS A 224      30.827  50.712 -19.593  1.00107.20           N  
ANISOU 1796  N   CYS A 224    13011  13082  14639    609  -1252   -868       N  
ATOM   1797  CA  CYS A 224      31.627  51.010 -20.771  1.00113.07           C  
ANISOU 1797  CA  CYS A 224    13879  13838  15246    750  -1298   -823       C  
ATOM   1798  C   CYS A 224      30.718  51.354 -21.950  1.00117.02           C  
ANISOU 1798  C   CYS A 224    14400  14291  15772    846  -1447   -918       C  
ATOM   1799  O   CYS A 224      29.521  51.053 -21.953  1.00117.94           O  
ANISOU 1799  O   CYS A 224    14437  14363  16012    804  -1533  -1025       O  
ATOM   1800  CB  CYS A 224      32.535  49.828 -21.125  1.00109.87           C  
ANISOU 1800  CB  CYS A 224    13597  13416  14734    799  -1290   -771       C  
ATOM   1801  SG  CYS A 224      33.583  50.091 -22.577  1.00109.49           S  
ANISOU 1801  SG  CYS A 224    13715  13373  14514    985  -1327   -701       S  
ATOM   1802  N   THR A 225      31.306  51.996 -22.960  1.00119.05           N  
ANISOU 1802  N   THR A 225    14768  14553  15912    983  -1474   -882       N  
ATOM   1803  CA  THR A 225      30.548  52.350 -24.156  1.00122.64           C  
ANISOU 1803  CA  THR A 225    15279  14954  16365   1108  -1618   -972       C  
ATOM   1804  C   THR A 225      30.119  51.135 -24.968  1.00125.51           C  
ANISOU 1804  C   THR A 225    15716  15233  16740   1166  -1753  -1042       C  
ATOM   1805  O   THR A 225      29.258  51.273 -25.841  1.00123.76           O  
ANISOU 1805  O   THR A 225    15518  14956  16550   1256  -1899  -1146       O  
ATOM   1806  CB  THR A 225      31.362  53.295 -25.041  1.00122.38           C  
ANISOU 1806  CB  THR A 225    15378  14931  16190   1250  -1594   -910       C  
ATOM   1807  OG1 THR A 225      32.540  52.624 -25.505  1.00121.87           O  
ANISOU 1807  OG1 THR A 225    15441  14858  16005   1320  -1550   -816       O  
ATOM   1808  CG2 THR A 225      31.766  54.533 -24.256  1.00121.95           C  
ANISOU 1808  CG2 THR A 225    15258  14952  16125   1184  -1468   -846       C  
ATOM   1809  N   CYS A 226      30.697  49.961 -24.709  1.00131.79           N  
ANISOU 1809  N   CYS A 226    16558  16015  17502   1126  -1716   -991       N  
ATOM   1810  CA  CYS A 226      30.284  48.725 -25.360  1.00138.35           C  
ANISOU 1810  CA  CYS A 226    17466  16759  18341   1162  -1840  -1054       C  
ATOM   1811  C   CYS A 226      29.118  48.040 -24.662  1.00143.54           C  
ANISOU 1811  C   CYS A 226    17985  17383  19171   1013  -1882  -1158       C  
ATOM   1812  O   CYS A 226      28.525  47.122 -25.240  1.00145.59           O  
ANISOU 1812  O   CYS A 226    18288  17561  19468   1030  -2010  -1237       O  
ATOM   1813  CB  CYS A 226      31.462  47.747 -25.441  1.00140.24           C  
ANISOU 1813  CB  CYS A 226    17843  16996  18444   1199  -1778   -948       C  
ATOM   1814  SG  CYS A 226      31.983  47.060 -23.846  1.00143.78           S  
ANISOU 1814  SG  CYS A 226    18209  17503  18918   1024  -1611   -883       S  
ATOM   1815  N   GLY A 227      28.773  48.451 -23.444  1.00146.26           N  
ANISOU 1815  N   GLY A 227    18170  17780  19623    869  -1776  -1158       N  
ATOM   1816  CA  GLY A 227      27.649  47.854 -22.752  1.00147.98           C  
ANISOU 1816  CA  GLY A 227    18250  17962  20015    725  -1792  -1253       C  
ATOM   1817  C   GLY A 227      27.974  47.221 -21.414  1.00145.87           C  
ANISOU 1817  C   GLY A 227    17937  17707  19779    578  -1635  -1197       C  
ATOM   1818  O   GLY A 227      27.374  47.580 -20.396  1.00148.28           O  
ANISOU 1818  O   GLY A 227    18099  18033  20207    461  -1555  -1219       O  
ATOM   1819  N   LYS A 228      28.919  46.284 -21.397  1.00140.28           N  
ANISOU 1819  N   LYS A 228    17364  16986  18952    596  -1586  -1125       N  
ATOM   1820  CA  LYS A 228      29.199  45.513 -20.195  1.00133.90           C  
ANISOU 1820  CA  LYS A 228    16545  16172  18158    475  -1448  -1088       C  
ATOM   1821  C   LYS A 228      29.993  46.342 -19.186  1.00127.21           C  
ANISOU 1821  C   LYS A 228    15656  15411  17268    448  -1296   -992       C  
ATOM   1822  O   LYS A 228      30.412  47.471 -19.455  1.00126.35           O  
ANISOU 1822  O   LYS A 228    15533  15365  17109    517  -1293   -946       O  
ATOM   1823  CB  LYS A 228      29.934  44.221 -20.548  1.00133.18           C  
ANISOU 1823  CB  LYS A 228    16628  16038  17935    519  -1456  -1050       C  
ATOM   1824  CG  LYS A 228      31.196  44.406 -21.368  1.00132.34           C  
ANISOU 1824  CG  LYS A 228    16669  15979  17635    678  -1469   -951       C  
ATOM   1825  CD  LYS A 228      31.800  43.052 -21.703  1.00131.53           C  
ANISOU 1825  CD  LYS A 228    16743  15831  17402    726  -1483   -918       C  
ATOM   1826  CE  LYS A 228      32.962  43.179 -22.664  1.00128.10           C  
ANISOU 1826  CE  LYS A 228    16458  15434  16781    901  -1505   -822       C  
ATOM   1827  NZ  LYS A 228      33.504  41.841 -23.010  1.00125.25           N  
ANISOU 1827  NZ  LYS A 228    16281  15028  16282    960  -1524   -788       N  
ATOM   1828  N   GLN A 229      30.205  45.756 -18.009  1.00123.14           N  
ANISOU 1828  N   GLN A 229    15134  14887  16768    351  -1168   -965       N  
ATOM   1829  CA  GLN A 229      30.744  46.484 -16.867  1.00116.90           C  
ANISOU 1829  CA  GLN A 229    14290  14158  15968    309  -1031   -894       C  
ATOM   1830  C   GLN A 229      32.267  46.490 -16.913  1.00110.73           C  
ANISOU 1830  C   GLN A 229    13621  13444  15009    395   -976   -786       C  
ATOM   1831  O   GLN A 229      32.898  45.431 -17.011  1.00109.91           O  
ANISOU 1831  O   GLN A 229    13636  13322  14802    428   -961   -761       O  
ATOM   1832  CB  GLN A 229      30.258  45.847 -15.561  1.00115.96           C  
ANISOU 1832  CB  GLN A 229    14128  13985  15945    181   -916   -919       C  
ATOM   1833  CG  GLN A 229      30.293  46.760 -14.342  1.00117.79           C  
ANISOU 1833  CG  GLN A 229    14274  14254  16228    126   -798   -878       C  
ATOM   1834  CD  GLN A 229      29.096  47.691 -14.275  1.00122.18           C  
ANISOU 1834  CD  GLN A 229    14677  14808  16939     78   -831   -935       C  
ATOM   1835  OE1 GLN A 229      28.042  47.402 -14.839  1.00122.94           O  
ANISOU 1835  OE1 GLN A 229    14710  14858  17144     50   -919  -1026       O  
ATOM   1836  NE2 GLN A 229      29.255  48.818 -13.585  1.00123.74           N  
ANISOU 1836  NE2 GLN A 229    14817  15056  17143     73   -768   -884       N  
ATOM   1837  N   ALA A 230      32.850  47.685 -16.835  1.00104.79           N  
ANISOU 1837  N   ALA A 230    12829  12768  14220    431   -944   -724       N  
ATOM   1838  CA  ALA A 230      34.290  47.867 -16.758  1.00 97.47           C  
ANISOU 1838  CA  ALA A 230    11969  11915  13150    497   -881   -624       C  
ATOM   1839  C   ALA A 230      34.699  48.176 -15.316  1.00 90.56           C  
ANISOU 1839  C   ALA A 230    11044  11073  12293    424   -757   -583       C  
ATOM   1840  O   ALA A 230      33.863  48.326 -14.422  1.00 91.65           O  
ANISOU 1840  O   ALA A 230    11104  11171  12546    332   -715   -624       O  
ATOM   1841  CB  ALA A 230      34.734  48.972 -17.720  1.00 96.15           C  
ANISOU 1841  CB  ALA A 230    11806  11801  12925    588   -927   -583       C  
ATOM   1842  N   THR A 231      36.009  48.274 -15.089  1.00 82.89           N  
ANISOU 1842  N   THR A 231    10118  10172  11205    473   -699   -503       N  
ATOM   1843  CA  THR A 231      36.551  48.560 -13.766  1.00 77.87           C  
ANISOU 1843  CA  THR A 231     9450   9567  10569    425   -597   -465       C  
ATOM   1844  C   THR A 231      37.508  49.740 -13.867  1.00 79.33           C  
ANISOU 1844  C   THR A 231     9597   9842  10702    460   -581   -393       C  
ATOM   1845  O   THR A 231      38.439  49.728 -14.679  1.00 78.07           O  
ANISOU 1845  O   THR A 231     9483   9738  10441    542   -597   -343       O  
ATOM   1846  CB  THR A 231      37.251  47.336 -13.157  1.00 72.60           C  
ANISOU 1846  CB  THR A 231     8880   8893   9812    445   -536   -453       C  
ATOM   1847  OG1 THR A 231      36.306  46.269 -13.013  1.00 72.13           O  
ANISOU 1847  OG1 THR A 231     8863   8737   9806    398   -539   -523       O  
ATOM   1848  CG2 THR A 231      37.786  47.667 -11.780  1.00 72.63           C  
ANISOU 1848  CG2 THR A 231     8862   8921   9816    413   -443   -425       C  
ATOM   1849  N   LYS A 232      37.264  50.759 -13.051  1.00 76.77           N  
ANISOU 1849  N   LYS A 232     9195   9525  10450    397   -544   -385       N  
ATOM   1850  CA  LYS A 232      38.087  51.957 -12.979  1.00 71.12           C  
ANISOU 1850  CA  LYS A 232     8441   8883   9700    406   -523   -322       C  
ATOM   1851  C   LYS A 232      38.891  51.945 -11.684  1.00 68.87           C  
ANISOU 1851  C   LYS A 232     8151   8625   9393    379   -448   -287       C  
ATOM   1852  O   LYS A 232      38.331  51.701 -10.610  1.00 69.81           O  
ANISOU 1852  O   LYS A 232     8266   8687   9573    327   -408   -316       O  
ATOM   1853  CB  LYS A 232      37.204  53.206 -13.045  1.00 69.02           C  
ANISOU 1853  CB  LYS A 232     8108   8600   9515    363   -549   -339       C  
ATOM   1854  CG  LYS A 232      37.922  54.524 -12.802  1.00 69.89           C  
ANISOU 1854  CG  LYS A 232     8188   8768   9599    351   -520   -278       C  
ATOM   1855  CD  LYS A 232      36.958  55.568 -12.230  1.00 69.14           C  
ANISOU 1855  CD  LYS A 232     8041   8642   9587    291   -521   -297       C  
ATOM   1856  CE  LYS A 232      36.012  56.134 -13.266  1.00 65.90           C  
ANISOU 1856  CE  LYS A 232     7624   8213   9202    319   -589   -340       C  
ATOM   1857  NZ  LYS A 232      36.656  57.222 -14.053  1.00 68.75           N  
ANISOU 1857  NZ  LYS A 232     8012   8620   9489    360   -597   -296       N  
ATOM   1858  N   TYR A 233      40.201  52.195 -11.784  1.00 67.78           N  
ANISOU 1858  N   TYR A 233     8016   8569   9170    421   -429   -228       N  
ATOM   1859  CA  TYR A 233      41.066  52.257 -10.612  1.00 66.82           C  
ANISOU 1859  CA  TYR A 233     7884   8480   9023    409   -376   -201       C  
ATOM   1860  C   TYR A 233      41.904  53.524 -10.657  1.00 64.18           C  
ANISOU 1860  C   TYR A 233     7488   8218   8679    395   -372   -146       C  
ATOM   1861  O   TYR A 233      42.210  54.062 -11.722  1.00 65.76           O  
ANISOU 1861  O   TYR A 233     7673   8460   8853    420   -391   -115       O  
ATOM   1862  CB  TYR A 233      42.082  51.098 -10.504  1.00 74.96           C  
ANISOU 1862  CB  TYR A 233     8978   9555   9950    482   -354   -192       C  
ATOM   1863  CG  TYR A 233      41.711  49.731 -11.033  1.00 82.79           C  
ANISOU 1863  CG  TYR A 233    10059  10505  10894    529   -367   -226       C  
ATOM   1864  CD1 TYR A 233      41.663  49.469 -12.399  1.00 84.82           C  
ANISOU 1864  CD1 TYR A 233    10347  10773  11110    582   -416   -215       C  
ATOM   1865  CD2 TYR A 233      41.498  48.676 -10.161  1.00 85.19           C  
ANISOU 1865  CD2 TYR A 233    10438  10752  11180    530   -328   -267       C  
ATOM   1866  CE1 TYR A 233      41.355  48.200 -12.871  1.00 85.87           C  
ANISOU 1866  CE1 TYR A 233    10576  10861  11190    627   -437   -245       C  
ATOM   1867  CE2 TYR A 233      41.191  47.412 -10.622  1.00 86.65           C  
ANISOU 1867  CE2 TYR A 233    10719  10892  11311    566   -337   -299       C  
ATOM   1868  CZ  TYR A 233      41.123  47.176 -11.972  1.00 86.06           C  
ANISOU 1868  CZ  TYR A 233    10668  10831  11199    612   -398   -287       C  
ATOM   1869  OH  TYR A 233      40.816  45.908 -12.405  1.00 88.60           O  
ANISOU 1869  OH  TYR A 233    11100  11100  11463    648   -416   -318       O  
ATOM   1870  N   LEU A 234      42.323  53.964  -9.475  1.00 68.99           N  
ANISOU 1870  N   LEU A 234     8072   8834   9306    360   -344   -134       N  
ATOM   1871  CA  LEU A 234      43.230  55.095  -9.361  1.00 74.88           C  
ANISOU 1871  CA  LEU A 234     8760   9646  10045    336   -340    -85       C  
ATOM   1872  C   LEU A 234      44.655  54.555  -9.451  1.00 80.21           C  
ANISOU 1872  C   LEU A 234     9424  10412  10639    395   -325    -58       C  
ATOM   1873  O   LEU A 234      45.091  53.788  -8.583  1.00 80.52           O  
ANISOU 1873  O   LEU A 234     9491  10456  10646    428   -311    -78       O  
ATOM   1874  CB  LEU A 234      42.996  55.843  -8.050  1.00 71.09           C  
ANISOU 1874  CB  LEU A 234     8267   9124   9621    276   -331    -87       C  
ATOM   1875  CG  LEU A 234      43.950  56.997  -7.748  1.00 71.29           C  
ANISOU 1875  CG  LEU A 234     8239   9206   9643    239   -334    -42       C  
ATOM   1876  CD1 LEU A 234      43.784  58.093  -8.791  1.00 67.02           C  
ANISOU 1876  CD1 LEU A 234     7670   8684   9110    206   -344    -11       C  
ATOM   1877  CD2 LEU A 234      43.740  57.540  -6.332  1.00 67.71           C  
ANISOU 1877  CD2 LEU A 234     7800   8694   9231    200   -335    -46       C  
ATOM   1878  N   VAL A 235      45.381  54.972 -10.482  1.00 79.26           N  
ANISOU 1878  N   VAL A 235     9268  10363  10485    416   -322    -14       N  
ATOM   1879  CA  VAL A 235      46.753  54.520 -10.697  1.00 76.40           C  
ANISOU 1879  CA  VAL A 235     8879  10100  10052    477   -301     18       C  
ATOM   1880  C   VAL A 235      47.749  55.416  -9.979  1.00 75.34           C  
ANISOU 1880  C   VAL A 235     8656  10027   9942    429   -291     42       C  
ATOM   1881  O   VAL A 235      48.592  54.940  -9.217  1.00 75.05           O  
ANISOU 1881  O   VAL A 235     8599  10042   9876    463   -291     31       O  
ATOM   1882  CB  VAL A 235      47.053  54.423 -12.207  1.00 73.18           C  
ANISOU 1882  CB  VAL A 235     8483   9729   9592    537   -291     58       C  
ATOM   1883  CG1 VAL A 235      48.543  54.212 -12.440  1.00 78.83           C  
ANISOU 1883  CG1 VAL A 235     9147  10558  10247    593   -256    104       C  
ATOM   1884  CG2 VAL A 235      46.272  53.270 -12.802  1.00 65.00           C  
ANISOU 1884  CG2 VAL A 235     7544   8637   8514    602   -316     28       C  
ATOM   1885  N   GLN A 236      47.674  56.720 -10.215  1.00 72.75           N  
ANISOU 1885  N   GLN A 236     8283   9693   9666    355   -288     70       N  
ATOM   1886  CA  GLN A 236      48.598  57.672  -9.627  1.00 65.54           C  
ANISOU 1886  CA  GLN A 236     7287   8830   8784    294   -283     93       C  
ATOM   1887  C   GLN A 236      47.822  58.870  -9.102  1.00 63.45           C  
ANISOU 1887  C   GLN A 236     7035   8492   8582    202   -301     91       C  
ATOM   1888  O   GLN A 236      46.887  59.350  -9.750  1.00 73.59           O  
ANISOU 1888  O   GLN A 236     8362   9721   9878    183   -299     95       O  
ATOM   1889  CB  GLN A 236      49.633  58.108 -10.668  1.00 73.10           C  
ANISOU 1889  CB  GLN A 236     8178   9872   9723    299   -240    146       C  
ATOM   1890  CG  GLN A 236      50.716  59.035 -10.153  1.00 91.16           C  
ANISOU 1890  CG  GLN A 236    10362  12222  12053    227   -231    167       C  
ATOM   1891  CD  GLN A 236      51.834  59.244 -11.161  1.00101.17           C  
ANISOU 1891  CD  GLN A 236    11553  13580  13305    241   -170    219       C  
ATOM   1892  OE1 GLN A 236      51.788  58.724 -12.278  1.00102.11           O  
ANISOU 1892  OE1 GLN A 236    11714  13709  13373    316   -133    245       O  
ATOM   1893  NE2 GLN A 236      52.846  60.010 -10.769  1.00105.68           N  
ANISOU 1893  NE2 GLN A 236    12017  14212  13926    170   -159    234       N  
ATOM   1894  N   GLN A 237      48.216  59.349  -7.927  1.00 60.91           N  
ANISOU 1894  N   GLN A 237     6683   8166   8292    156   -324     84       N  
ATOM   1895  CA  GLN A 237      47.578  60.486  -7.275  1.00 64.06           C  
ANISOU 1895  CA  GLN A 237     7108   8495   8739     77   -345     89       C  
ATOM   1896  C   GLN A 237      48.654  61.341  -6.622  1.00 64.56           C  
ANISOU 1896  C   GLN A 237     7104   8599   8827     16   -364    107       C  
ATOM   1897  O   GLN A 237      49.462  60.832  -5.839  1.00 59.66           O  
ANISOU 1897  O   GLN A 237     6447   8016   8203     48   -389     84       O  
ATOM   1898  CB  GLN A 237      46.553  60.029  -6.227  1.00 68.52           C  
ANISOU 1898  CB  GLN A 237     7747   8964   9321     96   -366     51       C  
ATOM   1899  CG  GLN A 237      45.869  61.165  -5.475  1.00 67.86           C  
ANISOU 1899  CG  GLN A 237     7703   8804   9277     31   -387     63       C  
ATOM   1900  CD  GLN A 237      44.840  61.897  -6.316  1.00 71.72           C  
ANISOU 1900  CD  GLN A 237     8222   9256   9773     -1   -376     78       C  
ATOM   1901  OE1 GLN A 237      44.266  61.337  -7.252  1.00 70.21           O  
ANISOU 1901  OE1 GLN A 237     8041   9066   9570     36   -361     62       O  
ATOM   1902  NE2 GLN A 237      44.609  63.163  -5.991  1.00 76.06           N  
ANISOU 1902  NE2 GLN A 237     8796   9771  10333    -63   -389    105       N  
ATOM   1903  N   GLU A 238      48.669  62.632  -6.954  1.00 70.25           N  
ANISOU 1903  N   GLU A 238     7815   9309   9567    -67   -355    142       N  
ATOM   1904  CA  GLU A 238      49.621  63.588  -6.391  1.00 75.28           C  
ANISOU 1904  CA  GLU A 238     8393   9974  10237   -146   -376    159       C  
ATOM   1905  C   GLU A 238      48.846  64.832  -5.977  1.00 73.62           C  
ANISOU 1905  C   GLU A 238     8258   9676  10039   -221   -396    177       C  
ATOM   1906  O   GLU A 238      48.452  65.639  -6.823  1.00 82.58           O  
ANISOU 1906  O   GLU A 238     9427  10793  11158   -263   -360    205       O  
ATOM   1907  CB  GLU A 238      50.725  63.923  -7.389  1.00 87.70           C  
ANISOU 1907  CB  GLU A 238     9870  11637  11813   -180   -324    192       C  
ATOM   1908  CG  GLU A 238      51.675  62.767  -7.651  1.00 98.80           C  
ANISOU 1908  CG  GLU A 238    11193  13143  13202   -101   -309    180       C  
ATOM   1909  CD  GLU A 238      52.844  63.156  -8.528  1.00109.14           C  
ANISOU 1909  CD  GLU A 238    12396  14545  14528   -136   -248    218       C  
ATOM   1910  OE1 GLU A 238      52.744  64.183  -9.234  1.00116.41           O  
ANISOU 1910  OE1 GLU A 238    13333  15439  15460   -209   -199    255       O  
ATOM   1911  OE2 GLU A 238      53.861  62.430  -8.512  1.00110.54           O  
ANISOU 1911  OE2 GLU A 238    12479  14819  14703    -85   -243    210       O  
ATOM   1912  N   SER A 239      48.628  64.977  -4.678  1.00 71.92           N  
ANISOU 1912  N   SER A 239     8086   9400   9841   -225   -452    161       N  
ATOM   1913  CA  SER A 239      47.866  66.085  -4.121  1.00 67.94           C  
ANISOU 1913  CA  SER A 239     7671   8806   9337   -279   -477    183       C  
ATOM   1914  C   SER A 239      48.025  66.047  -2.607  1.00 67.90           C  
ANISOU 1914  C   SER A 239     7704   8745   9351   -262   -543    166       C  
ATOM   1915  O   SER A 239      48.330  64.991  -2.044  1.00 63.47           O  
ANISOU 1915  O   SER A 239     7126   8196   8793   -187   -559    127       O  
ATOM   1916  CB  SER A 239      46.380  65.995  -4.508  1.00 67.82           C  
ANISOU 1916  CB  SER A 239     7742   8725   9300   -243   -452    183       C  
ATOM   1917  OG  SER A 239      45.769  64.847  -3.945  1.00 68.73           O  
ANISOU 1917  OG  SER A 239     7884   8805   9426   -164   -456    147       O  
ATOM   1918  N   PRO A 240      47.836  67.183  -1.932  1.00 64.59           N  
ANISOU 1918  N   PRO A 240     7352   8257   8931   -319   -583    192       N  
ATOM   1919  CA  PRO A 240      47.929  67.170  -0.466  1.00 61.78           C  
ANISOU 1919  CA  PRO A 240     7059   7828   8586   -285   -652    178       C  
ATOM   1920  C   PRO A 240      46.790  66.428   0.200  1.00 59.69           C  
ANISOU 1920  C   PRO A 240     6893   7475   8311   -192   -637    163       C  
ATOM   1921  O   PRO A 240      46.926  66.054   1.373  1.00 58.13           O  
ANISOU 1921  O   PRO A 240     6752   7216   8117   -130   -678    140       O  
ATOM   1922  CB  PRO A 240      47.910  68.659  -0.098  1.00 60.36           C  
ANISOU 1922  CB  PRO A 240     6946   7591   8396   -372   -693    221       C  
ATOM   1923  CG  PRO A 240      47.219  69.312  -1.230  1.00 60.36           C  
ANISOU 1923  CG  PRO A 240     6969   7601   8365   -422   -632    256       C  
ATOM   1924  CD  PRO A 240      47.607  68.538  -2.456  1.00 63.79           C  
ANISOU 1924  CD  PRO A 240     7292   8136   8809   -409   -570    237       C  
ATOM   1925  N   PHE A 241      45.682  66.203  -0.508  1.00 54.97           N  
ANISOU 1925  N   PHE A 241     6320   6863   7704   -178   -579    171       N  
ATOM   1926  CA  PHE A 241      44.510  65.523   0.032  1.00 50.08           C  
ANISOU 1926  CA  PHE A 241     5780   6159   7090   -105   -550    157       C  
ATOM   1927  C   PHE A 241      43.652  65.049  -1.131  1.00 52.86           C  
ANISOU 1927  C   PHE A 241     6098   6542   7444    -98   -493    146       C  
ATOM   1928  O   PHE A 241      43.896  65.387  -2.292  1.00 61.42           O  
ANISOU 1928  O   PHE A 241     7124   7698   8514   -140   -480    156       O  
ATOM   1929  CB  PHE A 241      43.701  66.436   0.968  1.00 43.21           C  
ANISOU 1929  CB  PHE A 241     5029   5176   6211   -105   -569    195       C  
ATOM   1930  CG  PHE A 241      43.116  67.631   0.281  1.00 42.39           C  
ANISOU 1930  CG  PHE A 241     4950   5075   6080   -169   -563    238       C  
ATOM   1931  CD1 PHE A 241      41.881  67.557  -0.339  1.00 42.27           C  
ANISOU 1931  CD1 PHE A 241     4949   5048   6064   -151   -517    238       C  
ATOM   1932  CD2 PHE A 241      43.812  68.826   0.238  1.00 51.62           C  
ANISOU 1932  CD2 PHE A 241     6132   6260   7223   -246   -606    273       C  
ATOM   1933  CE1 PHE A 241      41.350  68.651  -0.991  1.00 55.39           C  
ANISOU 1933  CE1 PHE A 241     6646   6715   7685   -192   -514    269       C  
ATOM   1934  CE2 PHE A 241      43.286  69.929  -0.408  1.00 60.62           C  
ANISOU 1934  CE2 PHE A 241     7318   7397   8318   -297   -593    309       C  
ATOM   1935  CZ  PHE A 241      42.052  69.841  -1.024  1.00 64.40           C  
ANISOU 1935  CZ  PHE A 241     7820   7866   8783   -262   -549    306       C  
ATOM   1936  N   VAL A 242      42.642  64.247  -0.801  1.00 48.50           N  
ANISOU 1936  N   VAL A 242     5588   5927   6912    -41   -457    123       N  
ATOM   1937  CA  VAL A 242      41.587  63.878  -1.734  1.00 40.20           C  
ANISOU 1937  CA  VAL A 242     4517   4882   5875    -34   -417    107       C  
ATOM   1938  C   VAL A 242      40.275  63.957  -0.976  1.00 53.52           C  
ANISOU 1938  C   VAL A 242     6277   6466   7592     -8   -392    112       C  
ATOM   1939  O   VAL A 242      40.231  63.799   0.249  1.00 62.54           O  
ANISOU 1939  O   VAL A 242     7489   7528   8744     28   -386    118       O  
ATOM   1940  CB  VAL A 242      41.770  62.476  -2.355  1.00 39.63           C  
ANISOU 1940  CB  VAL A 242     4392   4856   5810      7   -390     61       C  
ATOM   1941  CG1 VAL A 242      42.987  62.450  -3.270  1.00 40.60           C  
ANISOU 1941  CG1 VAL A 242     4439   5087   5900    -10   -405     65       C  
ATOM   1942  CG2 VAL A 242      41.872  61.407  -1.272  1.00 42.46           C  
ANISOU 1942  CG2 VAL A 242     4797   5158   6178     68   -370     30       C  
ATOM   1943  N   MET A 243      39.207  64.229  -1.716  1.00 61.59           N  
ANISOU 1943  N   MET A 243     7286   7488   8627    -18   -376    108       N  
ATOM   1944  CA  MET A 243      37.864  64.358  -1.172  1.00 54.13           C  
ANISOU 1944  CA  MET A 243     6387   6461   7718      5   -346    112       C  
ATOM   1945  C   MET A 243      36.970  63.370  -1.908  1.00 59.02           C  
ANISOU 1945  C   MET A 243     6946   7088   8389     21   -314     58       C  
ATOM   1946  O   MET A 243      36.846  63.438  -3.135  1.00 67.86           O  
ANISOU 1946  O   MET A 243     8012   8273   9498      9   -335     36       O  
ATOM   1947  CB  MET A 243      37.361  65.794  -1.319  1.00 51.78           C  
ANISOU 1947  CB  MET A 243     6133   6159   7382    -19   -371    156       C  
ATOM   1948  CG  MET A 243      35.954  66.018  -0.813  1.00 64.78           C  
ANISOU 1948  CG  MET A 243     7819   7733   9060     13   -339    165       C  
ATOM   1949  SD  MET A 243      35.351  67.696  -1.116  1.00 69.35           S  
ANISOU 1949  SD  MET A 243     8463   8320   9567      3   -371    212       S  
ATOM   1950  CE  MET A 243      33.698  67.571  -0.446  1.00 65.87           C  
ANISOU 1950  CE  MET A 243     8040   7803   9185     58   -320    213       C  
ATOM   1951  N   MET A 244      36.415  62.413  -1.170  1.00 60.42           N  
ANISOU 1951  N   MET A 244     7141   7194   8622     51   -261     33       N  
ATOM   1952  CA  MET A 244      35.507  61.409  -1.708  1.00 62.93           C  
ANISOU 1952  CA  MET A 244     7406   7502   9004     57   -227    -23       C  
ATOM   1953  C   MET A 244      34.090  61.721  -1.245  1.00 61.20           C  
ANISOU 1953  C   MET A 244     7191   7211   8849     62   -187    -21       C  
ATOM   1954  O   MET A 244      33.849  61.889  -0.044  1.00 58.91           O  
ANISOU 1954  O   MET A 244     6973   6836   8574     85   -141     13       O  
ATOM   1955  CB  MET A 244      35.919  60.006  -1.258  1.00 66.01           C  
ANISOU 1955  CB  MET A 244     7815   7858   9409     82   -182    -59       C  
ATOM   1956  CG  MET A 244      37.388  59.672  -1.497  1.00 66.28           C  
ANISOU 1956  CG  MET A 244     7849   7962   9372     94   -217    -58       C  
ATOM   1957  SD  MET A 244      37.850  59.570  -3.233  1.00 65.13           S  
ANISOU 1957  SD  MET A 244     7620   7936   9191     77   -269    -76       S  
ATOM   1958  CE  MET A 244      36.848  58.181  -3.744  1.00 58.25           C  
ANISOU 1958  CE  MET A 244     6727   7028   8377     88   -236   -143       C  
ATOM   1959  N   SER A 245      33.159  61.805  -2.197  1.00 59.04           N  
ANISOU 1959  N   SER A 245     6847   6973   8614     51   -206    -57       N  
ATOM   1960  CA  SER A 245      31.788  62.201  -1.916  1.00 54.62           C  
ANISOU 1960  CA  SER A 245     6267   6368   8117     59   -177    -60       C  
ATOM   1961  C   SER A 245      30.801  61.206  -2.506  1.00 61.82           C  
ANISOU 1961  C   SER A 245     7087   7273   9127     47   -158   -136       C  
ATOM   1962  O   SER A 245      31.074  60.539  -3.509  1.00 66.64           O  
ANISOU 1962  O   SER A 245     7651   7933   9737     37   -198   -187       O  
ATOM   1963  CB  SER A 245      31.486  63.589  -2.471  1.00 59.01           C  
ANISOU 1963  CB  SER A 245     6829   6976   8615     65   -234    -35       C  
ATOM   1964  OG  SER A 245      32.313  64.564  -1.872  1.00 68.39           O  
ANISOU 1964  OG  SER A 245     8110   8159   9717     66   -251     37       O  
ATOM   1965  N   ALA A 246      29.633  61.138  -1.877  1.00 62.70           N  
ANISOU 1965  N   ALA A 246     7176   7320   9328     50    -96   -143       N  
ATOM   1966  CA  ALA A 246      28.551  60.263  -2.300  1.00 65.42           C  
ANISOU 1966  CA  ALA A 246     7420   7647   9790     28    -72   -218       C  
ATOM   1967  C   ALA A 246      27.277  60.725  -1.606  1.00 68.26           C  
ANISOU 1967  C   ALA A 246     7749   7955  10232     38    -11   -205       C  
ATOM   1968  O   ALA A 246      27.345  61.396  -0.566  1.00 66.79           O  
ANISOU 1968  O   ALA A 246     7649   7718  10012     68     37   -131       O  
ATOM   1969  CB  ALA A 246      28.857  58.796  -1.963  1.00 62.43           C  
ANISOU 1969  CB  ALA A 246     7057   7207   9456      4     -7   -253       C  
ATOM   1970  N   PRO A 247      26.109  60.410  -2.163  1.00 69.45           N  
ANISOU 1970  N   PRO A 247     7781   8118  10490     21    -16   -274       N  
ATOM   1971  CA  PRO A 247      24.866  60.778  -1.493  1.00 72.41           C  
ANISOU 1971  CA  PRO A 247     8108   8449  10956     33     53   -263       C  
ATOM   1972  C   PRO A 247      24.805  60.152  -0.111  1.00 74.06           C  
ANISOU 1972  C   PRO A 247     8384   8533  11223     27    196   -220       C  
ATOM   1973  O   PRO A 247      25.335  59.049   0.111  1.00 75.59           O  
ANISOU 1973  O   PRO A 247     8614   8673  11435     -2    245   -243       O  
ATOM   1974  CB  PRO A 247      23.783  60.210  -2.420  1.00 74.30           C  
ANISOU 1974  CB  PRO A 247     8188   8724  11320      2     17   -368       C  
ATOM   1975  CG  PRO A 247      24.445  60.137  -3.759  1.00 75.07           C  
ANISOU 1975  CG  PRO A 247     8276   8906  11342      4   -111   -418       C  
ATOM   1976  CD  PRO A 247      25.867  59.773  -3.468  1.00 71.86           C  
ANISOU 1976  CD  PRO A 247     7987   8480  10836     -2    -96   -367       C  
ATOM   1977  N   PRO A 248      24.166  60.825   0.846  1.00 76.30           N  
ANISOU 1977  N   PRO A 248     8703   8762  11527     66    271   -158       N  
ATOM   1978  CA  PRO A 248      24.192  60.352   2.240  1.00 71.21           C  
ANISOU 1978  CA  PRO A 248     8160   7980  10916     84    414   -105       C  
ATOM   1979  C   PRO A 248      23.687  58.925   2.368  1.00 73.12           C  
ANISOU 1979  C   PRO A 248     8342   8146  11296     27    519   -173       C  
ATOM   1980  O   PRO A 248      22.544  58.614   2.030  1.00 80.16           O  
ANISOU 1980  O   PRO A 248     9091   9043  12323    -13    551   -230       O  
ATOM   1981  CB  PRO A 248      23.278  61.346   2.964  1.00 70.14           C  
ANISOU 1981  CB  PRO A 248     8040   7813  10798    140    469    -36       C  
ATOM   1982  CG  PRO A 248      23.351  62.580   2.140  1.00 69.37           C  
ANISOU 1982  CG  PRO A 248     7921   7837  10599    166    333    -25       C  
ATOM   1983  CD  PRO A 248      23.452  62.104   0.715  1.00 74.01           C  
ANISOU 1983  CD  PRO A 248     8386   8528  11208    113    228   -126       C  
ATOM   1984  N   ALA A 249      24.569  58.049   2.837  1.00 72.41           N  
ANISOU 1984  N   ALA A 249     8362   7985  11167     24    568   -172       N  
ATOM   1985  CA  ALA A 249      24.241  56.657   3.086  1.00 66.58           C  
ANISOU 1985  CA  ALA A 249     7614   7154  10531    -25    683   -230       C  
ATOM   1986  C   ALA A 249      24.953  56.212   4.352  1.00 64.21           C  
ANISOU 1986  C   ALA A 249     7506   6721  10169     30    794   -181       C  
ATOM   1987  O   ALA A 249      25.987  56.773   4.725  1.00 61.27           O  
ANISOU 1987  O   ALA A 249     7256   6360   9665     92    738   -126       O  
ATOM   1988  CB  ALA A 249      24.640  55.766   1.905  1.00 68.74           C  
ANISOU 1988  CB  ALA A 249     7817   7499  10801    -86    594   -318       C  
ATOM   1989  N   GLN A 250      24.385  55.205   5.013  1.00 67.21           N  
ANISOU 1989  N   GLN A 250     7918   6972  10648      9    953   -208       N  
ATOM   1990  CA  GLN A 250      24.991  54.661   6.225  1.00 68.81           C  
ANISOU 1990  CA  GLN A 250     8325   7030  10791     75   1073   -174       C  
ATOM   1991  C   GLN A 250      26.372  54.088   5.918  1.00 63.90           C  
ANISOU 1991  C   GLN A 250     7797   6448  10034     93    990   -204       C  
ATOM   1992  O   GLN A 250      26.524  53.247   5.027  1.00 62.71           O  
ANISOU 1992  O   GLN A 250     7579   6353   9894     29    947   -276       O  
ATOM   1993  CB  GLN A 250      24.085  53.586   6.825  1.00 80.28           C  
ANISOU 1993  CB  GLN A 250     9792   8333  12377     39   1270   -211       C  
ATOM   1994  CG  GLN A 250      24.156  53.479   8.342  1.00 87.99           C  
ANISOU 1994  CG  GLN A 250    10979   9127  13328    136   1437   -149       C  
ATOM   1995  CD  GLN A 250      23.402  54.601   9.040  1.00 94.72           C  
ANISOU 1995  CD  GLN A 250    11829   9939  14221    195   1488    -60       C  
ATOM   1996  OE1 GLN A 250      22.697  55.384   8.401  1.00 92.63           O  
ANISOU 1996  OE1 GLN A 250    11393   9784  14020    156   1415    -52       O  
ATOM   1997  NE2 GLN A 250      23.551  54.683  10.358  1.00105.26           N  
ANISOU 1997  NE2 GLN A 250    13369  11113  15511    304   1613      7       N  
ATOM   1998  N   TYR A 251      27.378  54.537   6.665  1.00 67.01           N  
ANISOU 1998  N   TYR A 251     8348   6813  10299    185    964   -148       N  
ATOM   1999  CA  TYR A 251      28.765  54.205   6.360  1.00 72.48           C  
ANISOU 1999  CA  TYR A 251     9111   7571  10858    213    865   -170       C  
ATOM   2000  C   TYR A 251      29.567  54.128   7.652  1.00 73.43           C  
ANISOU 2000  C   TYR A 251     9447   7573  10881    326    921   -135       C  
ATOM   2001  O   TYR A 251      29.342  54.912   8.579  1.00 73.77           O  
ANISOU 2001  O   TYR A 251     9576   7535  10920    393    959    -67       O  
ATOM   2002  CB  TYR A 251      29.374  55.248   5.414  1.00 73.74           C  
ANISOU 2002  CB  TYR A 251     9170   7898  10949    195    686   -147       C  
ATOM   2003  CG  TYR A 251      30.765  54.932   4.910  1.00 67.71           C  
ANISOU 2003  CG  TYR A 251     8438   7224  10065    211    582   -170       C  
ATOM   2004  CD1 TYR A 251      30.969  53.936   3.965  1.00 62.57           C  
ANISOU 2004  CD1 TYR A 251     7729   6634   9413    163    556   -238       C  
ATOM   2005  CD2 TYR A 251      31.872  55.641   5.366  1.00 63.67           C  
ANISOU 2005  CD2 TYR A 251     8011   6737   9442    275    507   -124       C  
ATOM   2006  CE1 TYR A 251      32.230  53.648   3.489  1.00 59.39           C  
ANISOU 2006  CE1 TYR A 251     7351   6317   8896    187    469   -253       C  
ATOM   2007  CE2 TYR A 251      33.144  55.358   4.893  1.00 62.30           C  
ANISOU 2007  CE2 TYR A 251     7847   6655   9169    289    417   -147       C  
ATOM   2008  CZ  TYR A 251      33.315  54.356   3.952  1.00 60.41           C  
ANISOU 2008  CZ  TYR A 251     7548   6479   8926    249    403   -208       C  
ATOM   2009  OH  TYR A 251      34.568  54.049   3.462  1.00 60.43           O  
ANISOU 2009  OH  TYR A 251     7557   6576   8826    272    322   -226       O  
ATOM   2010  N   GLU A 252      30.490  53.172   7.709  1.00 77.11           N  
ANISOU 2010  N   GLU A 252    10011   8026  11260    360    922   -183       N  
ATOM   2011  CA  GLU A 252      31.326  52.948   8.883  1.00 79.01           C  
ANISOU 2011  CA  GLU A 252    10467   8157  11396    483    964   -171       C  
ATOM   2012  C   GLU A 252      32.693  53.588   8.686  1.00 79.56           C  
ANISOU 2012  C   GLU A 252    10545   8343  11340    528    798   -155       C  
ATOM   2013  O   GLU A 252      33.370  53.324   7.687  1.00 82.59           O  
ANISOU 2013  O   GLU A 252    10835   8865  11679    484    698   -191       O  
ATOM   2014  CB  GLU A 252      31.487  51.454   9.158  1.00 85.39           C  
ANISOU 2014  CB  GLU A 252    11399   8869  12174    509   1078   -242       C  
ATOM   2015  CG  GLU A 252      32.381  51.151  10.342  1.00 96.06           C  
ANISOU 2015  CG  GLU A 252    12990  10105  13403    657   1117   -245       C  
ATOM   2016  CD  GLU A 252      32.526  49.665  10.592  1.00 99.48           C  
ANISOU 2016  CD  GLU A 252    13569  10442  13788    692   1236   -320       C  
ATOM   2017  OE1 GLU A 252      32.055  48.879   9.742  1.00 98.18           O  
ANISOU 2017  OE1 GLU A 252    13307  10318  13678    589   1269   -368       O  
ATOM   2018  OE2 GLU A 252      33.123  49.285  11.625  1.00100.02           O  
ANISOU 2018  OE2 GLU A 252    13858  10390  13754    828   1292   -336       O  
ATOM   2019  N   LEU A 253      33.105  54.408   9.651  1.00 80.03           N  
ANISOU 2019  N   LEU A 253    10722   8339  11346    619    771   -101       N  
ATOM   2020  CA  LEU A 253      34.391  55.097   9.615  1.00 73.60           C  
ANISOU 2020  CA  LEU A 253     9918   7619  10426    660    616    -86       C  
ATOM   2021  C   LEU A 253      35.333  54.412  10.595  1.00 75.50           C  
ANISOU 2021  C   LEU A 253    10357   7766  10564    791    637   -124       C  
ATOM   2022  O   LEU A 253      35.115  54.461  11.809  1.00 85.62           O  
ANISOU 2022  O   LEU A 253    11817   8881  11832    895    717   -101       O  
ATOM   2023  CB  LEU A 253      34.227  56.580   9.949  1.00 65.72           C  
ANISOU 2023  CB  LEU A 253     8914   6623   9434    666    547     -4       C  
ATOM   2024  CG  LEU A 253      33.509  57.449   8.911  1.00 54.33           C  
ANISOU 2024  CG  LEU A 253     7285   5298   8059    555    493     30       C  
ATOM   2025  CD1 LEU A 253      33.175  58.808   9.485  1.00 47.40           C  
ANISOU 2025  CD1 LEU A 253     6454   4380   7174    584    460    116       C  
ATOM   2026  CD2 LEU A 253      34.367  57.603   7.672  1.00 51.05           C  
ANISOU 2026  CD2 LEU A 253     6729   5066   7601    483    359      2       C  
ATOM   2027  N   LYS A 254      36.362  53.757  10.069  1.00 79.60           N  
ANISOU 2027  N   LYS A 254    10144   9326  10777     53   -283    -65       N  
ATOM   2028  CA  LYS A 254      37.364  53.094  10.894  1.00 75.53           C  
ANISOU 2028  CA  LYS A 254     9736   8738  10225     24   -364   -148       C  
ATOM   2029  C   LYS A 254      38.473  54.070  11.278  1.00 66.56           C  
ANISOU 2029  C   LYS A 254     8681   7576   9033     25   -331   -175       C  
ATOM   2030  O   LYS A 254      38.973  54.822  10.437  1.00 67.34           O  
ANISOU 2030  O   LYS A 254     8710   7759   9118     51   -318   -177       O  
ATOM   2031  CB  LYS A 254      37.933  51.879  10.154  1.00 77.70           C  
ANISOU 2031  CB  LYS A 254     9951   9079  10492     29   -532   -243       C  
ATOM   2032  CG  LYS A 254      36.846  50.888   9.712  1.00 86.00           C  
ANISOU 2032  CG  LYS A 254    10919  10144  11611     29   -595   -218       C  
ATOM   2033  CD  LYS A 254      37.331  49.439   9.639  1.00 93.09           C  
ANISOU 2033  CD  LYS A 254    11833  11046  12491     17   -764   -310       C  
ATOM   2034  CE  LYS A 254      38.062  49.136   8.337  1.00 96.24           C  
ANISOU 2034  CE  LYS A 254    12163  11564  12842     75   -893   -372       C  
ATOM   2035  NZ  LYS A 254      38.661  47.765   8.333  1.00 95.32           N  
ANISOU 2035  NZ  LYS A 254    12087  11453  12677     70  -1060   -461       N  
ATOM   2036  N   HIS A 255      38.855  54.054  12.555  1.00 58.48           N  
ANISOU 2036  N   HIS A 255     7809   6426   7986      7   -320   -193       N  
ATOM   2037  CA  HIS A 255      39.849  55.000  13.053  1.00 56.36           C  
ANISOU 2037  CA  HIS A 255     7631   6102   7681      8   -304   -213       C  
ATOM   2038  C   HIS A 255      41.185  54.851  12.333  1.00 63.87           C  
ANISOU 2038  C   HIS A 255     8518   7128   8620      3   -413   -301       C  
ATOM   2039  O   HIS A 255      41.659  53.738  12.089  1.00 75.63           O  
ANISOU 2039  O   HIS A 255     9984   8652  10100     -5   -526   -379       O  
ATOM   2040  CB  HIS A 255      40.069  54.809  14.552  1.00 57.04           C  
ANISOU 2040  CB  HIS A 255     7907   6021   7744      7   -305   -236       C  
ATOM   2041  CG  HIS A 255      41.313  55.474  15.061  1.00 64.55           C  
ANISOU 2041  CG  HIS A 255     8956   6899   8670      5   -350   -290       C  
ATOM   2042  ND1 HIS A 255      42.451  54.769  15.393  1.00 64.23           N  
ANISOU 2042  ND1 HIS A 255     8969   6820   8617    -12   -472   -406       N  
ATOM   2043  CD2 HIS A 255      41.603  56.780  15.278  1.00 65.55           C  
ANISOU 2043  CD2 HIS A 255     9136   6981   8788     19   -299   -242       C  
ATOM   2044  CE1 HIS A 255      43.386  55.611  15.796  1.00 62.08           C  
ANISOU 2044  CE1 HIS A 255     8768   6475   8343    -11   -498   -426       C  
ATOM   2045  NE2 HIS A 255      42.897  56.837  15.737  1.00 62.67           N  
ANISOU 2045  NE2 HIS A 255     8846   6542   8423      7   -400   -328       N  
ATOM   2046  N   GLY A 256      41.805  55.989  12.017  1.00 60.93           N  
ANISOU 2046  N   GLY A 256     8124   6778   8250     12   -376   -278       N  
ATOM   2047  CA  GLY A 256      43.102  56.016  11.377  1.00 58.45           C  
ANISOU 2047  CA  GLY A 256     7743   6523   7941     17   -458   -333       C  
ATOM   2048  C   GLY A 256      43.092  55.858   9.872  1.00 63.46           C  
ANISOU 2048  C   GLY A 256     8212   7314   8584     64   -470   -323       C  
ATOM   2049  O   GLY A 256      44.167  55.901   9.259  1.00 66.05           O  
ANISOU 2049  O   GLY A 256     8478   7699   8920     87   -524   -348       O  
ATOM   2050  N   THR A 257      41.924  55.677   9.254  1.00 63.70           N  
ANISOU 2050  N   THR A 257     8173   7409   8619     91   -424   -280       N  
ATOM   2051  CA  THR A 257      41.817  55.438   7.821  1.00 61.02           C  
ANISOU 2051  CA  THR A 257     7699   7203   8284    159   -450   -277       C  
ATOM   2052  C   THR A 257      41.360  56.664   7.042  1.00 68.76           C  
ANISOU 2052  C   THR A 257     8601   8248   9278    208   -324   -206       C  
ATOM   2053  O   THR A 257      41.104  56.559   5.837  1.00 69.92           O  
ANISOU 2053  O   THR A 257     8646   8495   9427    285   -330   -200       O  
ATOM   2054  CB  THR A 257      40.849  54.280   7.550  1.00 53.66           C  
ANISOU 2054  CB  THR A 257     6740   6293   7356    168   -517   -290       C  
ATOM   2055  OG1 THR A 257      39.525  54.645   7.960  1.00 49.63           O  
ANISOU 2055  OG1 THR A 257     6242   5741   6876    144   -416   -222       O  
ATOM   2056  CG2 THR A 257      41.266  53.057   8.329  1.00 49.78           C  
ANISOU 2056  CG2 THR A 257     6331   5739   6842    121   -633   -363       C  
ATOM   2057  N   PHE A 258      41.239  57.816   7.697  1.00 70.78           N  
ANISOU 2057  N   PHE A 258     8915   8445   9534    175   -216   -155       N  
ATOM   2058  CA  PHE A 258      40.789  59.036   7.041  1.00 64.04           C  
ANISOU 2058  CA  PHE A 258     8002   7651   8679    216    -86    -90       C  
ATOM   2059  C   PHE A 258      41.176  60.218   7.912  1.00 67.39           C  
ANISOU 2059  C   PHE A 258     8518   7991   9095    174    -14    -51       C  
ATOM   2060  O   PHE A 258      41.511  60.061   9.089  1.00 71.66           O  
ANISOU 2060  O   PHE A 258     9181   8414   9632    120    -59    -68       O  
ATOM   2061  CB  PHE A 258      39.277  59.011   6.798  1.00 60.81           C  
ANISOU 2061  CB  PHE A 258     7566   7273   8265    232    -14    -43       C  
ATOM   2062  CG  PHE A 258      38.454  59.122   8.060  1.00 65.61           C  
ANISOU 2062  CG  PHE A 258     8289   7777   8862    173     43      8       C  
ATOM   2063  CD1 PHE A 258      37.824  60.313   8.396  1.00 66.42           C  
ANISOU 2063  CD1 PHE A 258     8441   7863   8933    173    181     89       C  
ATOM   2064  CD2 PHE A 258      38.308  58.034   8.910  1.00 61.87           C  
ANISOU 2064  CD2 PHE A 258     7884   7221   8403    131    -36    -19       C  
ATOM   2065  CE1 PHE A 258      37.066  60.417   9.552  1.00 56.55           C  
ANISOU 2065  CE1 PHE A 258     7309   6513   7662    143    240    154       C  
ATOM   2066  CE2 PHE A 258      37.550  58.131  10.067  1.00 56.99           C  
ANISOU 2066  CE2 PHE A 258     7377   6500   7778    101     30     42       C  
ATOM   2067  CZ  PHE A 258      36.931  59.324  10.387  1.00 55.28           C  
ANISOU 2067  CZ  PHE A 258     7213   6265   7527    113    168    134       C  
ATOM   2068  N   THR A 259      41.102  61.413   7.323  1.00 65.21           N  
ANISOU 2068  N   THR A 259     8194   7770   8814    209     94      0       N  
ATOM   2069  CA  THR A 259      41.339  62.650   8.068  1.00 63.50           C  
ANISOU 2069  CA  THR A 259     8068   7475   8583    176    162     49       C  
ATOM   2070  C   THR A 259      40.058  63.126   8.747  1.00 61.64           C  
ANISOU 2070  C   THR A 259     7931   7199   8291    163    263    117       C  
ATOM   2071  O   THR A 259      39.992  63.199   9.976  1.00 67.62           O  
ANISOU 2071  O   THR A 259     8836   7832   9024    127    249    136       O  
ATOM   2072  CB  THR A 259      41.909  63.737   7.150  1.00 67.33           C  
ANISOU 2072  CB  THR A 259     8461   8033   9088    219    234     77       C  
ATOM   2073  OG1 THR A 259      43.164  63.304   6.609  1.00 70.81           O  
ANISOU 2073  OG1 THR A 259     8815   8499   9590    240    146     35       O  
ATOM   2074  CG2 THR A 259      42.129  65.019   7.932  1.00 66.91           C  
ANISOU 2074  CG2 THR A 259     8511   7892   9021    182    287    130       C  
ATOM   2075  N   CYS A 260      39.031  63.440   7.962  1.00 56.81           N  
ANISOU 2075  N   CYS A 260     7247   6686   7653    206    366    157       N  
ATOM   2076  CA  CYS A 260      37.762  63.874   8.531  1.00 56.34           C  
ANISOU 2076  CA  CYS A 260     7267   6601   7537    202    471    237       C  
ATOM   2077  C   CYS A 260      36.651  63.569   7.538  1.00 55.74           C  
ANISOU 2077  C   CYS A 260     7075   6637   7467    246    526    250       C  
ATOM   2078  O   CYS A 260      36.897  63.227   6.379  1.00 54.22           O  
ANISOU 2078  O   CYS A 260     6755   6538   7307    294    491    197       O  
ATOM   2079  CB  CYS A 260      37.786  65.359   8.898  1.00 57.74           C  
ANISOU 2079  CB  CYS A 260     7535   6752   7651    204    574    305       C  
ATOM   2080  SG  CYS A 260      38.118  66.459   7.511  1.00 67.84           S  
ANISOU 2080  SG  CYS A 260     8687   8166   8922    257    666    302       S  
ATOM   2081  N   ALA A 261      35.416  63.669   8.020  1.00 54.06           N  
ANISOU 2081  N   ALA A 261     6912   6405   7224    241    608    327       N  
ATOM   2082  CA  ALA A 261      34.262  63.295   7.224  1.00 53.55           C  
ANISOU 2082  CA  ALA A 261     6741   6423   7183    276    645    344       C  
ATOM   2083  C   ALA A 261      33.087  64.210   7.552  1.00 61.53           C  
ANISOU 2083  C   ALA A 261     7807   7443   8127    287    799    453       C  
ATOM   2084  O   ALA A 261      33.078  64.918   8.566  1.00 61.01           O  
ANISOU 2084  O   ALA A 261     7883   7302   7994    270    863    524       O  
ATOM   2085  CB  ALA A 261      33.892  61.827   7.459  1.00 48.55           C  
ANISOU 2085  CB  ALA A 261     6075   5745   6627    250    533    322       C  
ATOM   2086  N   SER A 262      32.068  64.153   6.698  1.00 62.59           N  
ANISOU 2086  N   SER A 262     7839   7665   8280    326    849    470       N  
ATOM   2087  CA  SER A 262      30.864  64.959   6.841  1.00 64.81           C  
ANISOU 2087  CA  SER A 262     8150   7975   8499    344    999    574       C  
ATOM   2088  C   SER A 262      29.674  64.035   7.046  1.00 70.20           C  
ANISOU 2088  C   SER A 262     8782   8628   9262    332    983    635       C  
ATOM   2089  O   SER A 262      29.360  63.223   6.169  1.00 73.58           O  
ANISOU 2089  O   SER A 262     9078   9099   9779    350    899    579       O  
ATOM   2090  CB  SER A 262      30.639  65.837   5.607  1.00 65.95           C  
ANISOU 2090  CB  SER A 262     8213   8248   8595    409   1087    545       C  
ATOM   2091  OG  SER A 262      31.726  66.716   5.389  1.00 69.72           O  
ANISOU 2091  OG  SER A 262     8725   8750   9014    423   1111    502       O  
ATOM   2092  N   GLU A 263      29.021  64.150   8.201  1.00 72.79           N  
ANISOU 2092  N   GLU A 263     9218   8875   9566    312   1057    755       N  
ATOM   2093  CA  GLU A 263      27.775  63.437   8.445  1.00 76.57           C  
ANISOU 2093  CA  GLU A 263     9642   9322  10129    306   1075    847       C  
ATOM   2094  C   GLU A 263      26.594  64.313   8.055  1.00 71.86           C  
ANISOU 2094  C   GLU A 263     9017   8805   9481    345   1224    943       C  
ATOM   2095  O   GLU A 263      26.568  65.510   8.354  1.00 72.33           O  
ANISOU 2095  O   GLU A 263     9186   8890   9405    370   1351   1002       O  
ATOM   2096  CB  GLU A 263      27.637  63.026   9.913  1.00 83.04           C  
ANISOU 2096  CB  GLU A 263    10592  10002  10958    285   1090    945       C  
ATOM   2097  CG  GLU A 263      26.292  62.346  10.218  1.00 88.76           C  
ANISOU 2097  CG  GLU A 263    11253  10687  11786    285   1130   1070       C  
ATOM   2098  CD  GLU A 263      26.035  62.151  11.703  1.00 93.20           C  
ANISOU 2098  CD  GLU A 263    11965  11110  12339    298   1192   1198       C  
ATOM   2099  OE1 GLU A 263      26.738  62.776  12.523  1.00 95.64           O  
ANISOU 2099  OE1 GLU A 263    12451  11355  12534    320   1224   1204       O  
ATOM   2100  OE2 GLU A 263      25.135  61.361  12.055  1.00 96.16           O  
ANISOU 2100  OE2 GLU A 263    12282  11426  12828    295   1205   1295       O  
ATOM   2101  N   TYR A 264      25.615  63.708   7.387  1.00 72.98           N  
ANISOU 2101  N   TYR A 264     9016   8983   9731    352   1201    959       N  
ATOM   2102  CA  TYR A 264      24.390  64.393   6.995  1.00 76.76           C  
ANISOU 2102  CA  TYR A 264     9449   9534  10182    388   1332   1050       C  
ATOM   2103  C   TYR A 264      23.204  63.535   7.400  1.00 81.95           C  
ANISOU 2103  C   TYR A 264    10032  10126  10981    368   1327   1172       C  
ATOM   2104  O   TYR A 264      23.064  62.402   6.927  1.00 83.65           O  
ANISOU 2104  O   TYR A 264    10118  10314  11351    347   1183   1116       O  
ATOM   2105  CB  TYR A 264      24.353  64.668   5.492  1.00 78.98           C  
ANISOU 2105  CB  TYR A 264     9609   9934  10464    437   1307    934       C  
ATOM   2106  CG  TYR A 264      23.156  65.487   5.060  1.00 79.87           C  
ANISOU 2106  CG  TYR A 264     9689  10129  10528    480   1450   1012       C  
ATOM   2107  CD1 TYR A 264      22.070  64.893   4.431  1.00 77.35           C  
ANISOU 2107  CD1 TYR A 264     9226   9821  10340    494   1409   1031       C  
ATOM   2108  CD2 TYR A 264      23.115  66.856   5.284  1.00 78.12           C  
ANISOU 2108  CD2 TYR A 264     9584   9970  10128    508   1619   1065       C  
ATOM   2109  CE1 TYR A 264      20.981  65.643   4.030  1.00 75.03           C  
ANISOU 2109  CE1 TYR A 264     8903   9604  10003    536   1538   1098       C  
ATOM   2110  CE2 TYR A 264      22.034  67.610   4.891  1.00 74.07           C  
ANISOU 2110  CE2 TYR A 264     9051   9541   9553    550   1754   1133       C  
ATOM   2111  CZ  TYR A 264      20.971  67.004   4.266  1.00 72.74           C  
ANISOU 2111  CZ  TYR A 264     8734   9386   9517    564   1717   1148       C  
ATOM   2112  OH  TYR A 264      19.900  67.773   3.879  1.00 70.85           O  
ANISOU 2112  OH  TYR A 264     8476   9231   9214    608   1853   1213       O  
ATOM   2113  N   THR A 265      22.341  64.086   8.249  1.00 84.15           N  
ANISOU 2113  N   THR A 265    10391  10376  11207    383   1481   1346       N  
ATOM   2114  CA  THR A 265      21.157  63.401   8.742  1.00 83.81           C  
ANISOU 2114  CA  THR A 265    10279  10265  11301    374   1509   1500       C  
ATOM   2115  C   THR A 265      19.922  64.172   8.306  1.00 89.78           C  
ANISOU 2115  C   THR A 265    10979  11105  12027    413   1649   1610       C  
ATOM   2116  O   THR A 265      19.890  65.404   8.377  1.00 91.45           O  
ANISOU 2116  O   THR A 265    11303  11388  12056    454   1790   1648       O  
ATOM   2117  CB  THR A 265      21.179  63.282  10.269  1.00 81.75           C  
ANISOU 2117  CB  THR A 265    10174   9877  11012    380   1582   1643       C  
ATOM   2118  OG1 THR A 265      21.391  64.577  10.846  1.00 86.42           O  
ANISOU 2118  OG1 THR A 265    10954  10488  11394    430   1725   1709       O  
ATOM   2119  CG2 THR A 265      22.303  62.359  10.716  1.00 81.17           C  
ANISOU 2119  CG2 THR A 265    10142   9709  10988    342   1435   1531       C  
ATOM   2120  N   GLY A 266      18.916  63.445   7.834  1.00 92.23           N  
ANISOU 2120  N   GLY A 266    11119  11407  12519    400   1600   1656       N  
ATOM   2121  CA  GLY A 266      17.677  64.058   7.405  1.00 91.95           C  
ANISOU 2121  CA  GLY A 266    11012  11442  12481    434   1719   1762       C  
ATOM   2122  C   GLY A 266      17.392  63.779   5.947  1.00100.02           C  
ANISOU 2122  C   GLY A 266    11862  12537  13606    444   1601   1622       C  
ATOM   2123  O   GLY A 266      18.004  62.889   5.349  1.00106.08           O  
ANISOU 2123  O   GLY A 266    12550  13277  14480    424   1412   1473       O  
ATOM   2124  N   ASN A 267      16.474  64.537   5.356  1.00101.04           N  
ANISOU 2124  N   ASN A 267    11943  12755  13692    487   1706   1666       N  
ATOM   2125  CA  ASN A 267      16.139  64.373   3.953  1.00101.06           C  
ANISOU 2125  CA  ASN A 267    11801  12819  13780    520   1601   1530       C  
ATOM   2126  C   ASN A 267      16.828  65.440   3.107  1.00 98.55           C  
ANISOU 2126  C   ASN A 267    11559  12626  13258    584   1658   1373       C  
ATOM   2127  O   ASN A 267      17.540  66.317   3.600  1.00 95.14           O  
ANISOU 2127  O   ASN A 267    11282  12235  12631    590   1773   1374       O  
ATOM   2128  CB  ASN A 267      14.625  64.403   3.729  1.00101.95           C  
ANISOU 2128  CB  ASN A 267    11789  12938  14010    533   1659   1664       C  
ATOM   2129  CG  ASN A 267      13.982  65.648   4.282  1.00102.45           C  
ANISOU 2129  CG  ASN A 267    11959  13077  13890    565   1907   1823       C  
ATOM   2130  OD1 ASN A 267      14.633  66.451   4.944  1.00103.25           O  
ANISOU 2130  OD1 ASN A 267    12238  13210  13781    576   2028   1846       O  
ATOM   2131  ND2 ASN A 267      12.715  65.856   3.946  1.00107.60           N  
ANISOU 2131  ND2 ASN A 267    12509  13761  14611    588   1974   1925       N  
ATOM   2132  N   TYR A 268      16.589  65.348   1.799  1.00100.48           N  
ANISOU 2132  N   TYR A 268    11696  12922  13561    643   1570   1237       N  
ATOM   2133  CA  TYR A 268      17.134  66.284   0.825  1.00103.77           C  
ANISOU 2133  CA  TYR A 268    12163  13453  13811    727   1623   1082       C  
ATOM   2134  C   TYR A 268      16.586  67.700   0.979  1.00104.57           C  
ANISOU 2134  C   TYR A 268    12358  13662  13711    760   1859   1162       C  
ATOM   2135  O   TYR A 268      17.230  68.650   0.517  1.00104.66           O  
ANISOU 2135  O   TYR A 268    12457  13767  13544    815   1945   1061       O  
ATOM   2136  CB  TYR A 268      16.835  65.735  -0.569  1.00111.27           C  
ANISOU 2136  CB  TYR A 268    12980  14408  14891    805   1465    935       C  
ATOM   2137  CG  TYR A 268      15.346  65.614  -0.837  1.00119.86           C  
ANISOU 2137  CG  TYR A 268    13951  15486  16106    816   1474   1024       C  
ATOM   2138  CD1 TYR A 268      14.669  66.563  -1.589  1.00119.22           C  
ANISOU 2138  CD1 TYR A 268    13868  15504  15924    899   1594    989       C  
ATOM   2139  CD2 TYR A 268      14.616  64.539  -0.330  1.00123.56           C  
ANISOU 2139  CD2 TYR A 268    14306  15839  16802    743   1362   1145       C  
ATOM   2140  CE1 TYR A 268      13.308  66.445  -1.828  1.00118.94           C  
ANISOU 2140  CE1 TYR A 268    13721  15457  16016    907   1596   1073       C  
ATOM   2141  CE2 TYR A 268      13.257  64.420  -0.557  1.00124.04           C  
ANISOU 2141  CE2 TYR A 268    14245  15881  17005    748   1365   1241       C  
ATOM   2142  CZ  TYR A 268      12.608  65.374  -1.309  1.00121.60           C  
ANISOU 2142  CZ  TYR A 268    13935  15673  16595    830   1478   1204       C  
ATOM   2143  OH  TYR A 268      11.256  65.256  -1.544  1.00122.29           O  
ANISOU 2143  OH  TYR A 268    13895  15739  16831    835   1475   1299       O  
ATOM   2144  N   GLN A 269      15.424  67.868   1.614  1.00102.37           N  
ANISOU 2144  N   GLN A 269    12066  13375  13455    735   1970   1348       N  
ATOM   2145  CA  GLN A 269      14.854  69.200   1.785  1.00 98.36           C  
ANISOU 2145  CA  GLN A 269    11659  12975  12737    773   2195   1437       C  
ATOM   2146  C   GLN A 269      15.400  69.924   3.010  1.00 93.80           C  
ANISOU 2146  C   GLN A 269    11276  12395  11970    744   2331   1555       C  
ATOM   2147  O   GLN A 269      15.580  71.147   2.968  1.00 91.68           O  
ANISOU 2147  O   GLN A 269    11138  12226  11472    785   2480   1546       O  
ATOM   2148  CB  GLN A 269      13.326  69.134   1.865  1.00101.49           C  
ANISOU 2148  CB  GLN A 269    11960  13373  13229    776   2263   1598       C  
ATOM   2149  CG  GLN A 269      12.679  70.483   1.567  1.00101.83           C  
ANISOU 2149  CG  GLN A 269    12080  13555  13055    841   2469   1631       C  
ATOM   2150  CD  GLN A 269      11.253  70.373   1.066  1.00 98.59           C  
ANISOU 2150  CD  GLN A 269    11530  13166  12763    867   2490   1703       C  
ATOM   2151  OE1 GLN A 269      10.672  69.287   1.027  1.00 98.65           O  
ANISOU 2151  OE1 GLN A 269    11377  13072  13035    831   2351   1753       O  
ATOM   2152  NE2 GLN A 269      10.682  71.505   0.671  1.00 93.68           N  
ANISOU 2152  NE2 GLN A 269    10969  12675  11952    931   2661   1707       N  
ATOM   2153  N   CYS A 270      15.667  69.204   4.098  1.00 89.11           N  
ANISOU 2153  N   CYS A 270    10715  11682  11462    684   2278   1661       N  
ATOM   2154  CA  CYS A 270      16.248  69.812   5.288  1.00 84.09           C  
ANISOU 2154  CA  CYS A 270    10280  11016  10656    673   2378   1762       C  
ATOM   2155  C   CYS A 270      17.052  68.769   6.051  1.00 81.04           C  
ANISOU 2155  C   CYS A 270     9906  10492  10396    616   2239   1756       C  
ATOM   2156  O   CYS A 270      16.543  67.683   6.346  1.00 82.24           O  
ANISOU 2156  O   CYS A 270     9948  10550  10749    582   2158   1829       O  
ATOM   2157  CB  CYS A 270      15.164  70.410   6.185  1.00 85.82           C  
ANISOU 2157  CB  CYS A 270    10589  11241  10778    701   2563   2007       C  
ATOM   2158  SG  CYS A 270      15.835  71.262   7.622  1.00 89.47           S  
ANISOU 2158  SG  CYS A 270    11335  11655  11003    723   2677   2134       S  
ATOM   2159  N   GLY A 271      18.304  69.105   6.376  1.00 76.22           N  
ANISOU 2159  N   GLY A 271     9426   9864   9671    607   2211   1670       N  
ATOM   2160  CA  GLY A 271      19.201  68.174   7.027  1.00 76.04           C  
ANISOU 2160  CA  GLY A 271     9426   9720   9748    558   2075   1634       C  
ATOM   2161  C   GLY A 271      20.028  68.836   8.112  1.00 76.39           C  
ANISOU 2161  C   GLY A 271     9689   9710   9627    564   2131   1682       C  
ATOM   2162  O   GLY A 271      19.865  70.019   8.415  1.00 73.23           O  
ANISOU 2162  O   GLY A 271     9431   9362   9031    607   2273   1759       O  
ATOM   2163  N   HIS A 272      20.915  68.034   8.705  1.00 80.96           N  
ANISOU 2163  N   HIS A 272    10300  10177  10285    525   2006   1634       N  
ATOM   2164  CA  HIS A 272      21.770  68.471   9.802  1.00 83.45           C  
ANISOU 2164  CA  HIS A 272    10822  10407  10478    533   2020   1668       C  
ATOM   2165  C   HIS A 272      23.176  67.942   9.571  1.00 80.62           C  
ANISOU 2165  C   HIS A 272    10445  10011  10177    487   1855   1486       C  
ATOM   2166  O   HIS A 272      23.359  66.737   9.371  1.00 84.85           O  
ANISOU 2166  O   HIS A 272    10860  10500  10878    447   1723   1416       O  
ATOM   2167  CB  HIS A 272      21.235  67.982  11.155  1.00 86.49           C  
ANISOU 2167  CB  HIS A 272    11307  10655  10899    555   2064   1851       C  
ATOM   2168  CG  HIS A 272      21.971  68.537  12.334  1.00 92.97           C  
ANISOU 2168  CG  HIS A 272    12374  11375  11575    594   2085   1901       C  
ATOM   2169  ND1 HIS A 272      22.080  69.889  12.577  1.00 96.35           N  
ANISOU 2169  ND1 HIS A 272    12978  11843  11788    646   2188   1953       N  
ATOM   2170  CD2 HIS A 272      22.642  67.922  13.336  1.00 95.97           C  
ANISOU 2170  CD2 HIS A 272    12863  11606  11994    596   2006   1902       C  
ATOM   2171  CE1 HIS A 272      22.781  70.084  13.680  1.00 95.88           C  
ANISOU 2171  CE1 HIS A 272    13127  11655  11647    682   2159   1987       C  
ATOM   2172  NE2 HIS A 272      23.136  68.906  14.160  1.00 96.52           N  
ANISOU 2172  NE2 HIS A 272    13173  11620  11880    655   2053   1953       N  
ATOM   2173  N   TYR A 273      24.162  68.838   9.602  1.00 72.99           N  
ANISOU 2173  N   TYR A 273     9595   9063   9077    494   1860   1417       N  
ATOM   2174  CA  TYR A 273      25.554  68.488   9.354  1.00 68.74           C  
ANISOU 2174  CA  TYR A 273     9038   8495   8585    457   1716   1257       C  
ATOM   2175  C   TYR A 273      26.320  68.312  10.657  1.00 72.77           C  
ANISOU 2175  C   TYR A 273     9720   8857   9074    446   1659   1288       C  
ATOM   2176  O   TYR A 273      26.221  69.140  11.569  1.00 72.00           O  
ANISOU 2176  O   TYR A 273     9811   8703   8842    487   1742   1398       O  
ATOM   2177  CB  TYR A 273      26.251  69.555   8.502  1.00 63.25           C  
ANISOU 2177  CB  TYR A 273     8343   7904   7787    472   1747   1157       C  
ATOM   2178  CG  TYR A 273      26.256  69.292   7.010  1.00 56.60           C  
ANISOU 2178  CG  TYR A 273     7308   7178   7020    485   1710   1028       C  
ATOM   2179  CD1 TYR A 273      25.530  70.093   6.143  1.00 61.57           C  
ANISOU 2179  CD1 TYR A 273     7890   7932   7573    534   1830   1030       C  
ATOM   2180  CD2 TYR A 273      26.999  68.249   6.469  1.00 54.38           C  
ANISOU 2180  CD2 TYR A 273     6910   6878   6875    463   1555    902       C  
ATOM   2181  CE1 TYR A 273      25.539  69.863   4.779  1.00 66.82           C  
ANISOU 2181  CE1 TYR A 273     8399   8688   8302    572   1794    907       C  
ATOM   2182  CE2 TYR A 273      27.014  68.008   5.110  1.00 58.64           C  
ANISOU 2182  CE2 TYR A 273     7298   7510   7473    503   1514    791       C  
ATOM   2183  CZ  TYR A 273      26.280  68.821   4.264  1.00 65.88           C  
ANISOU 2183  CZ  TYR A 273     8173   8538   8318    563   1634    792       C  
ATOM   2184  OH  TYR A 273      26.280  68.606   2.900  1.00 61.39           O  
ANISOU 2184  OH  TYR A 273     7472   8050   7802    629   1594    677       O  
ATOM   2185  N   LYS A 274      27.104  67.235  10.722  1.00 74.67           N  
ANISOU 2185  N   LYS A 274     9904   9030   9437    403   1510   1186       N  
ATOM   2186  CA  LYS A 274      28.043  66.995  11.807  1.00 76.73           C  
ANISOU 2186  CA  LYS A 274    10315   9151   9689    393   1429   1171       C  
ATOM   2187  C   LYS A 274      29.397  66.632  11.216  1.00 79.44           C  
ANISOU 2187  C   LYS A 274    10583   9508  10092    347   1284    998       C  
ATOM   2188  O   LYS A 274      29.481  66.041  10.135  1.00 81.44           O  
ANISOU 2188  O   LYS A 274    10661   9848  10434    327   1221    902       O  
ATOM   2189  CB  LYS A 274      27.573  65.869  12.745  1.00 74.95           C  
ANISOU 2189  CB  LYS A 274    10118   8803   9556    395   1400   1243       C  
ATOM   2190  CG  LYS A 274      26.333  66.192  13.558  1.00 74.90           C  
ANISOU 2190  CG  LYS A 274    10212   8751   9495    458   1549   1444       C  
ATOM   2191  CD  LYS A 274      25.984  65.043  14.498  1.00 77.46           C  
ANISOU 2191  CD  LYS A 274    10563   8941   9927    470   1524   1514       C  
ATOM   2192  CE  LYS A 274      24.680  65.302  15.243  1.00 80.40           C  
ANISOU 2192  CE  LYS A 274    11013   9270  10266    548   1687   1738       C  
ATOM   2193  NZ  LYS A 274      24.238  64.126  16.043  1.00 81.63           N  
ANISOU 2193  NZ  LYS A 274    11162   9299  10553    566   1679   1818       N  
ATOM   2194  N   HIS A 275      30.457  66.993  11.935  1.00 76.55           N  
ANISOU 2194  N   HIS A 275    10359   9049   9678    342   1226    966       N  
ATOM   2195  CA  HIS A 275      31.830  66.811  11.478  1.00 74.09           C  
ANISOU 2195  CA  HIS A 275     9992   8742   9416    304   1098    822       C  
ATOM   2196  C   HIS A 275      32.490  65.720  12.308  1.00 73.63           C  
ANISOU 2196  C   HIS A 275     9988   8554   9433    277    969    770       C  
ATOM   2197  O   HIS A 275      32.543  65.819  13.539  1.00 76.60           O  
ANISOU 2197  O   HIS A 275    10546   8793   9764    301    969    830       O  
ATOM   2198  CB  HIS A 275      32.619  68.115  11.583  1.00 72.93           C  
ANISOU 2198  CB  HIS A 275     9950   8586   9176    313   1118    819       C  
ATOM   2199  CG  HIS A 275      34.026  68.016  11.083  1.00 68.77           C  
ANISOU 2199  CG  HIS A 275     9351   8064   8716    278   1001    693       C  
ATOM   2200  ND1 HIS A 275      34.340  68.030   9.742  1.00 69.04           N  
ANISOU 2200  ND1 HIS A 275     9206   8229   8796    278   1000    615       N  
ATOM   2201  CD2 HIS A 275      35.203  67.913  11.744  1.00 69.34           C  
ANISOU 2201  CD2 HIS A 275     9507   8021   8819    252    882    640       C  
ATOM   2202  CE1 HIS A 275      35.650  67.938   9.597  1.00 68.68           C  
ANISOU 2202  CE1 HIS A 275     9131   8155   8809    254    896    533       C  
ATOM   2203  NE2 HIS A 275      36.198  67.865  10.797  1.00 68.52           N  
ANISOU 2203  NE2 HIS A 275     9262   7986   8785    230    818    543       N  
ATOM   2204  N   ILE A 276      32.976  64.678  11.640  1.00 71.48           N  
ANISOU 2204  N   ILE A 276     9572   8322   9263    241    857    660       N  
ATOM   2205  CA  ILE A 276      33.714  63.597  12.282  1.00 71.22           C  
ANISOU 2205  CA  ILE A 276     9579   8187   9295    212    726    588       C  
ATOM   2206  C   ILE A 276      35.186  63.768  11.937  1.00 71.90           C  
ANISOU 2206  C   ILE A 276     9645   8279   9394    187    621    475       C  
ATOM   2207  O   ILE A 276      35.532  63.999  10.773  1.00 74.36           O  
ANISOU 2207  O   ILE A 276     9818   8709   9725    188    615    423       O  
ATOM   2208  CB  ILE A 276      33.202  62.212  11.844  1.00 71.51           C  
ANISOU 2208  CB  ILE A 276     9481   8257   9432    192    664    554       C  
ATOM   2209  CG1 ILE A 276      31.886  61.867  12.546  1.00 73.32           C  
ANISOU 2209  CG1 ILE A 276     9752   8429   9679    212    751    679       C  
ATOM   2210  CG2 ILE A 276      34.223  61.137  12.173  1.00 70.34           C  
ANISOU 2210  CG2 ILE A 276     9347   8042   9336    159    513    444       C  
ATOM   2211  CD1 ILE A 276      30.656  62.397  11.861  1.00 73.30           C  
ANISOU 2211  CD1 ILE A 276     9656   8527   9670    235    871    772       C  
ATOM   2212  N   THR A 277      36.046  63.698  12.947  1.00 74.25           N  
ANISOU 2212  N   THR A 277    10084   8444   9684    177    543    444       N  
ATOM   2213  CA  THR A 277      37.481  63.811  12.739  1.00 73.01           C  
ANISOU 2213  CA  THR A 277     9909   8274   9559    149    433    346       C  
ATOM   2214  C   THR A 277      38.184  62.649  13.430  1.00 75.92           C  
ANISOU 2214  C   THR A 277    10330   8543   9974    125    302    262       C  
ATOM   2215  O   THR A 277      37.715  62.136  14.451  1.00 80.21           O  
ANISOU 2215  O   THR A 277    10997   8976  10503    142    305    290       O  
ATOM   2216  CB  THR A 277      38.016  65.159  13.254  1.00 68.42           C  
ANISOU 2216  CB  THR A 277     9458   7619   8920    161    455    385       C  
ATOM   2217  OG1 THR A 277      39.442  65.188  13.144  1.00 68.02           O  
ANISOU 2217  OG1 THR A 277     9381   7535   8927    129    335    299       O  
ATOM   2218  CG2 THR A 277      37.621  65.371  14.698  1.00 68.44           C  
ANISOU 2218  CG2 THR A 277     9690   7458   8857    199    472    456       C  
ATOM   2219  N   SER A 278      39.312  62.235  12.856  1.00 73.88           N  
ANISOU 2219  N   SER A 278     9977   8324   9768     96    193    162       N  
ATOM   2220  CA  SER A 278      40.096  61.106  13.347  1.00 68.28           C  
ANISOU 2220  CA  SER A 278     9302   7545   9095     71     61     67       C  
ATOM   2221  C   SER A 278      41.413  61.615  13.911  1.00 66.56           C  
ANISOU 2221  C   SER A 278     9174   7225   8891     57    -26     18       C  
ATOM   2222  O   SER A 278      42.224  62.189  13.176  1.00 71.48           O  
ANISOU 2222  O   SER A 278     9700   7910   9548     45    -48      3       O  
ATOM   2223  CB  SER A 278      40.356  60.085  12.240  1.00 62.82           C  
ANISOU 2223  CB  SER A 278     8438   6981   8449     59     -9     -4       C  
ATOM   2224  OG  SER A 278      41.294  59.110  12.667  1.00 60.94           O  
ANISOU 2224  OG  SER A 278     8238   6686   8230     35   -140   -101       O  
ATOM   2225  N   LYS A 279      41.622  61.402  15.212  1.00 60.97           N  
ANISOU 2225  N   LYS A 279     8651   6351   8163     67    -78     -2       N  
ATOM   2226  CA  LYS A 279      42.865  61.787  15.872  1.00 65.57           C  
ANISOU 2226  CA  LYS A 279     9337   6807   8769     57   -187    -58       C  
ATOM   2227  C   LYS A 279      43.439  60.600  16.639  1.00 75.23           C  
ANISOU 2227  C   LYS A 279    10647   7934  10004     52   -301   -163       C  
ATOM   2228  O   LYS A 279      43.781  59.584  16.026  1.00 80.42           O  
ANISOU 2228  O   LYS A 279    11183   8684  10688     21   -357   -235       O  
ATOM   2229  CB  LYS A 279      42.623  62.987  16.788  1.00 62.34           C  
ANISOU 2229  CB  LYS A 279     9116   6261   8310    101   -147     20       C  
ATOM   2230  CG  LYS A 279      41.994  64.162  16.056  1.00 62.65           C  
ANISOU 2230  CG  LYS A 279     9085   6404   8318    108    -26    123       C  
ATOM   2231  CD  LYS A 279      41.926  65.403  16.914  1.00 73.29           C  
ANISOU 2231  CD  LYS A 279    10626   7615   9605    152    -10    198       C  
ATOM   2232  CE  LYS A 279      41.732  66.643  16.053  1.00 74.07           C  
ANISOU 2232  CE  LYS A 279    10635   7824   9685    143     79    272       C  
ATOM   2233  NZ  LYS A 279      42.161  67.889  16.756  1.00 77.96           N  
ANISOU 2233  NZ  LYS A 279    11298   8179  10146    168     36    318       N  
ATOM   2234  N   GLU A 280      43.570  60.702  17.966  1.00 77.67           N  
ANISOU 2234  N   GLU A 280    11174   8053  10284     94   -339   -176       N  
ATOM   2235  CA  GLU A 280      43.944  59.512  18.727  1.00 73.66           C  
ANISOU 2235  CA  GLU A 280    10761   7453   9773    103   -425   -279       C  
ATOM   2236  C   GLU A 280      42.797  58.510  18.752  1.00 73.27           C  
ANISOU 2236  C   GLU A 280    10691   7451   9695    120   -343   -253       C  
ATOM   2237  O   GLU A 280      43.027  57.301  18.869  1.00 73.62           O  
ANISOU 2237  O   GLU A 280    10726   7499   9745    105   -404   -342       O  
ATOM   2238  CB  GLU A 280      44.363  59.872  20.155  1.00 67.01           C  
ANISOU 2238  CB  GLU A 280    10176   6378   8905    168   -489   -305       C  
ATOM   2239  CG  GLU A 280      43.226  60.266  21.076  1.00 70.84           C  
ANISOU 2239  CG  GLU A 280    10849   6748   9319    264   -379   -200       C  
ATOM   2240  CD  GLU A 280      42.848  61.723  20.956  1.00 89.91           C  
ANISOU 2240  CD  GLU A 280    13298   9159  11703    288   -312    -79       C  
ATOM   2241  OE1 GLU A 280      43.217  62.355  19.944  1.00 95.90           O  
ANISOU 2241  OE1 GLU A 280    13890  10045  12502    221   -316    -66       O  
ATOM   2242  OE2 GLU A 280      42.173  62.235  21.874  1.00 99.89           O  
ANISOU 2242  OE2 GLU A 280    14765  10292  12895    386   -251      9       O  
ATOM   2243  N   THR A 281      41.564  59.001  18.645  1.00 68.81           N  
ANISOU 2243  N   THR A 281    10119   6921   9104    151   -207   -128       N  
ATOM   2244  CA  THR A 281      40.369  58.187  18.482  1.00 67.56           C  
ANISOU 2244  CA  THR A 281     9898   6823   8948    159   -121    -74       C  
ATOM   2245  C   THR A 281      39.398  58.975  17.599  1.00 70.02           C  
ANISOU 2245  C   THR A 281    10083   7264   9258    154     -1     45       C  
ATOM   2246  O   THR A 281      39.761  59.999  17.012  1.00 68.94           O  
ANISOU 2246  O   THR A 281     9892   7188   9113    138      9     64       O  
ATOM   2247  CB  THR A 281      39.786  57.813  19.855  1.00 66.58           C  
ANISOU 2247  CB  THR A 281     9982   6524   8790    241    -72    -37       C  
ATOM   2248  OG1 THR A 281      38.700  56.895  19.697  1.00 73.31           O  
ANISOU 2248  OG1 THR A 281    10753   7428   9672    240      0     15       O  
ATOM   2249  CG2 THR A 281      39.283  59.044  20.588  1.00 65.12           C  
ANISOU 2249  CG2 THR A 281     9967   6230   8547    324     20     86       C  
ATOM   2250  N   LEU A 282      38.163  58.493  17.489  1.00 69.66           N  
ANISOU 2250  N   LEU A 282     9984   7260   9225    168     91    125       N  
ATOM   2251  CA  LEU A 282      37.152  59.158  16.676  1.00 68.38           C  
ANISOU 2251  CA  LEU A 282     9703   7216   9061    168    206    234       C  
ATOM   2252  C   LEU A 282      36.413  60.210  17.495  1.00 71.78           C  
ANISOU 2252  C   LEU A 282    10293   7556   9424    239    332    372       C  
ATOM   2253  O   LEU A 282      35.907  59.919  18.586  1.00 67.84           O  
ANISOU 2253  O   LEU A 282     9946   6923   8905    303    380    433       O  
ATOM   2254  CB  LEU A 282      36.166  58.144  16.097  1.00 61.03           C  
ANISOU 2254  CB  LEU A 282     8625   6370   8194    147    230    261       C  
ATOM   2255  CG  LEU A 282      36.747  57.253  14.996  1.00 55.00           C  
ANISOU 2255  CG  LEU A 282     7689   5728   7480     91    107    145       C  
ATOM   2256  CD1 LEU A 282      35.670  56.384  14.380  1.00 52.92           C  
ANISOU 2256  CD1 LEU A 282     7286   5538   7285     79    118    183       C  
ATOM   2257  CD2 LEU A 282      37.442  58.089  13.927  1.00 54.78           C  
ANISOU 2257  CD2 LEU A 282     7559   5817   7438     77     88    110       C  
ATOM   2258  N   TYR A 283      36.387  61.438  16.977  1.00 75.14           N  
ANISOU 2258  N   TYR A 283    10695   8050   9805    240    388    422       N  
ATOM   2259  CA  TYR A 283      35.678  62.553  17.584  1.00 76.80           C  
ANISOU 2259  CA  TYR A 283    11052   8201   9928    310    507    560       C  
ATOM   2260  C   TYR A 283      34.553  63.011  16.665  1.00 82.27           C  
ANISOU 2260  C   TYR A 283    11603   9045  10611    303    635    657       C  
ATOM   2261  O   TYR A 283      34.667  62.960  15.435  1.00 83.94           O  
ANISOU 2261  O   TYR A 283    11621   9406  10865    249    618    601       O  
ATOM   2262  CB  TYR A 283      36.623  63.717  17.882  1.00 75.65           C  
ANISOU 2262  CB  TYR A 283    11032   7988   9723    323    456    539       C  
ATOM   2263  CG  TYR A 283      37.501  63.471  19.078  1.00 83.68           C  
ANISOU 2263  CG  TYR A 283    12250   8811  10734    362    345    475       C  
ATOM   2264  CD1 TYR A 283      38.682  62.750  18.959  1.00 93.26           C  
ANISOU 2264  CD1 TYR A 283    13410  10007  12019    306    199    326       C  
ATOM   2265  CD2 TYR A 283      37.151  63.954  20.331  1.00 88.75           C  
ANISOU 2265  CD2 TYR A 283    13148   9281  11294    471    382    565       C  
ATOM   2266  CE1 TYR A 283      39.497  62.519  20.061  1.00 97.30           C  
ANISOU 2266  CE1 TYR A 283    14111  10334  12525    347     91    256       C  
ATOM   2267  CE2 TYR A 283      37.960  63.731  21.438  1.00 93.65           C  
ANISOU 2267  CE2 TYR A 283    13970   9706  11907    527    271    497       C  
ATOM   2268  CZ  TYR A 283      39.128  63.011  21.298  1.00 94.85           C  
ANISOU 2268  CZ  TYR A 283    14058   9844  12138    459    124    336       C  
ATOM   2269  OH  TYR A 283      39.929  62.786  22.395  1.00 92.28           O  
ANISOU 2269  OH  TYR A 283    13936   9320  11806    519      9    258       O  
ATOM   2270  N   CYS A 284      33.461  63.459  17.281  1.00 80.43           N  
ANISOU 2270  N   CYS A 284    11477   8766  10316    373    766    808       N  
ATOM   2271  CA  CYS A 284      32.288  63.948  16.565  1.00 78.97           C  
ANISOU 2271  CA  CYS A 284    11184   8710  10111    379    901    918       C  
ATOM   2272  C   CYS A 284      31.955  65.341  17.072  1.00 81.92           C  
ANISOU 2272  C   CYS A 284    11732   9049  10347    450   1005   1039       C  
ATOM   2273  O   CYS A 284      31.508  65.500  18.212  1.00 87.16           O  
ANISOU 2273  O   CYS A 284    12592   9579  10945    540   1063   1153       O  
ATOM   2274  CB  CYS A 284      31.102  63.007  16.753  1.00 80.00           C  
ANISOU 2274  CB  CYS A 284    11250   8832  10314    396    970   1009       C  
ATOM   2275  SG  CYS A 284      29.617  63.563  15.926  1.00 82.03           S  
ANISOU 2275  SG  CYS A 284    11372   9234  10562    406   1127   1148       S  
ATOM   2276  N   ILE A 285      32.150  66.342  16.224  1.00 78.95           N  
ANISOU 2276  N   ILE A 285    11291   8788   9918    424   1031   1021       N  
ATOM   2277  CA  ILE A 285      31.912  67.734  16.576  1.00 74.71           C  
ANISOU 2277  CA  ILE A 285    10914   8235   9236    484   1117   1125       C  
ATOM   2278  C   ILE A 285      30.572  68.142  15.980  1.00 85.58           C  
ANISOU 2278  C   ILE A 285    12205   9745  10565    504   1279   1243       C  
ATOM   2279  O   ILE A 285      30.404  68.138  14.754  1.00 89.26           O  
ANISOU 2279  O   ILE A 285    12470  10369  11077    451   1300   1185       O  
ATOM   2280  CB  ILE A 285      33.043  68.632  16.059  1.00 64.54           C  
ANISOU 2280  CB  ILE A 285     9617   6981   7924    443   1044   1031       C  
ATOM   2281  CG1 ILE A 285      34.391  68.078  16.508  1.00 63.48           C  
ANISOU 2281  CG1 ILE A 285     9523   6727   7869    410    872    904       C  
ATOM   2282  CG2 ILE A 285      32.843  70.047  16.549  1.00 67.30           C  
ANISOU 2282  CG2 ILE A 285    10162   7292   8118    508   1112   1138       C  
ATOM   2283  CD1 ILE A 285      35.569  68.872  16.003  1.00 67.98           C  
ANISOU 2283  CD1 ILE A 285    10060   7318   8452    364    790    821       C  
ATOM   2284  N   ASP A 286      29.615  68.487  16.842  1.00 88.47           N  
ANISOU 2284  N   ASP A 286    12731  10046  10839    594   1394   1412       N  
ATOM   2285  CA  ASP A 286      28.281  68.931  16.429  1.00 91.67           C  
ANISOU 2285  CA  ASP A 286    13079  10564  11186    626   1558   1548       C  
ATOM   2286  C   ASP A 286      28.080  70.362  16.922  1.00 91.92           C  
ANISOU 2286  C   ASP A 286    13327  10578  11019    708   1646   1666       C  
ATOM   2287  O   ASP A 286      27.445  70.598  17.952  1.00 92.45           O  
ANISOU 2287  O   ASP A 286    13591  10544  10992    814   1726   1828       O  
ATOM   2288  CB  ASP A 286      27.184  67.973  16.973  1.00 91.13           C  
ANISOU 2288  CB  ASP A 286    12987  10442  11197    668   1631   1675       C  
ATOM   2289  CG  ASP A 286      25.786  68.358  16.509  1.00 95.49           C  
ANISOU 2289  CG  ASP A 286    13456  11112  11715    694   1794   1822       C  
ATOM   2290  OD1 ASP A 286      25.663  69.060  15.482  1.00 97.45           O  
ANISOU 2290  OD1 ASP A 286    13600  11511  11915    657   1833   1778       O  
ATOM   2291  OD2 ASP A 286      24.806  67.957  17.172  1.00 95.91           O  
ANISOU 2291  OD2 ASP A 286    13546  11102  11792    760   1889   1985       O  
ATOM   2292  N   GLY A 287      28.628  71.321  16.180  1.00 90.02           N  
ANISOU 2292  N   GLY A 287    13058  10433  10712    668   1634   1590       N  
ATOM   2293  CA  GLY A 287      28.576  72.704  16.605  1.00 88.38           C  
ANISOU 2293  CA  GLY A 287    13062  10208  10312    738   1693   1684       C  
ATOM   2294  C   GLY A 287      29.436  72.947  17.828  1.00 87.78           C  
ANISOU 2294  C   GLY A 287    13243   9927  10182    798   1578   1691       C  
ATOM   2295  O   GLY A 287      30.667  72.974  17.736  1.00 80.85           O  
ANISOU 2295  O   GLY A 287    12354   8996   9367    742   1433   1555       O  
ATOM   2296  N   ALA A 288      28.797  73.133  18.984  1.00 92.09           N  
ANISOU 2296  N   ALA A 288    14027  10349  10615    926   1639   1856       N  
ATOM   2297  CA  ALA A 288      29.515  73.314  20.237  1.00 92.30           C  
ANISOU 2297  CA  ALA A 288    14330  10156  10584   1017   1526   1872       C  
ATOM   2298  C   ALA A 288      29.682  72.023  21.027  1.00 87.06           C  
ANISOU 2298  C   ALA A 288    13690   9342  10045   1048   1462   1846       C  
ATOM   2299  O   ALA A 288      30.372  72.032  22.052  1.00 86.96           O  
ANISOU 2299  O   ALA A 288    13900   9133  10006   1127   1350   1830       O  
ATOM   2300  CB  ALA A 288      28.802  74.354  21.111  1.00 98.14           C  
ANISOU 2300  CB  ALA A 288    15363  10824  11100   1175   1618   2071       C  
ATOM   2301  N   LEU A 289      29.082  70.924  20.576  1.00 85.55           N  
ANISOU 2301  N   LEU A 289    13283   9231   9989    993   1521   1837       N  
ATOM   2302  CA  LEU A 289      29.102  69.657  21.292  1.00 94.96           C  
ANISOU 2302  CA  LEU A 289    14487  10294  11298   1024   1482   1824       C  
ATOM   2303  C   LEU A 289      30.157  68.724  20.706  1.00 95.10           C  
ANISOU 2303  C   LEU A 289    14315  10336  11485    890   1329   1607       C  
ATOM   2304  O   LEU A 289      30.501  68.809  19.524  1.00 98.91           O  
ANISOU 2304  O   LEU A 289    14583  10975  12026    771   1296   1497       O  
ATOM   2305  CB  LEU A 289      27.728  68.979  21.256  1.00102.66           C  
ANISOU 2305  CB  LEU A 289    15353  11324  12328   1056   1640   1971       C  
ATOM   2306  CG  LEU A 289      26.492  69.835  21.547  1.00106.20           C  
ANISOU 2306  CG  LEU A 289    15921  11806  12626   1172   1823   2203       C  
ATOM   2307  CD1 LEU A 289      25.243  68.968  21.631  1.00104.59           C  
ANISOU 2307  CD1 LEU A 289    15595  11621  12523   1203   1959   2350       C  
ATOM   2308  CD2 LEU A 289      26.678  70.624  22.834  1.00107.07           C  
ANISOU 2308  CD2 LEU A 289    16324  11778  12581   1319   1783   2253       C  
ATOM   2309  N   LEU A 290      30.671  67.831  21.555  1.00 90.58           N  
ANISOU 2309  N   LEU A 290    13835   9602  10980    926   1240   1552       N  
ATOM   2310  CA  LEU A 290      31.752  66.920  21.202  1.00 82.67           C  
ANISOU 2310  CA  LEU A 290    12700   8597  10114    819   1085   1352       C  
ATOM   2311  C   LEU A 290      31.415  65.530  21.723  1.00 86.10           C  
ANISOU 2311  C   LEU A 290    13108   8954  10652    842   1091   1352       C  
ATOM   2312  O   LEU A 290      30.825  65.390  22.798  1.00 85.08           O  
ANISOU 2312  O   LEU A 290    13166   8684  10477    975   1168   1480       O  
ATOM   2313  CB  LEU A 290      33.097  67.396  21.770  1.00 78.79           C  
ANISOU 2313  CB  LEU A 290    12384   7966   9589    835    924   1244       C  
ATOM   2314  CG  LEU A 290      34.366  66.652  21.350  1.00 77.88           C  
ANISOU 2314  CG  LEU A 290    12136   7856   9599    723    757   1039       C  
ATOM   2315  CD1 LEU A 290      34.529  66.675  19.854  1.00 81.25           C  
ANISOU 2315  CD1 LEU A 290    12275   8499  10097    589    758    962       C  
ATOM   2316  CD2 LEU A 290      35.580  67.276  22.004  1.00 77.83           C  
ANISOU 2316  CD2 LEU A 290    12318   7692   9560    753    606    963       C  
ATOM   2317  N   THR A 291      31.792  64.507  20.958  1.00 86.28           N  
ANISOU 2317  N   THR A 291    12907   9066  10810    724   1013   1214       N  
ATOM   2318  CA  THR A 291      31.465  63.127  21.295  1.00 83.96           C  
ANISOU 2318  CA  THR A 291    12557   8719  10625    726   1012   1203       C  
ATOM   2319  C   THR A 291      32.590  62.213  20.840  1.00 82.05           C  
ANISOU 2319  C   THR A 291    12194   8502  10478    620    847    996       C  
ATOM   2320  O   THR A 291      33.042  62.314  19.697  1.00 85.44           O  
ANISOU 2320  O   THR A 291    12438   9080  10945    515    785    899       O  
ATOM   2321  CB  THR A 291      30.152  62.697  20.633  1.00 90.47           C  
ANISOU 2321  CB  THR A 291    13181   9669  11525    695   1133   1315       C  
ATOM   2322  OG1 THR A 291      29.079  63.508  21.125  1.00 95.41           O  
ANISOU 2322  OG1 THR A 291    13926  10269  12057    804   1297   1523       O  
ATOM   2323  CG2 THR A 291      29.857  61.229  20.918  1.00 95.69           C  
ANISOU 2323  CG2 THR A 291    13765  10275  12317    684   1116   1298       C  
ATOM   2324  N   LYS A 292      33.017  61.316  21.725  1.00 80.87           N  
ANISOU 2324  N   LYS A 292    12157   8208  10361    661    784    935       N  
ATOM   2325  CA  LYS A 292      34.045  60.329  21.428  1.00 80.78           C  
ANISOU 2325  CA  LYS A 292    12055   8211  10427    574    632    746       C  
ATOM   2326  C   LYS A 292      33.424  58.948  21.263  1.00 78.44           C  
ANISOU 2326  C   LYS A 292    11621   7945  10236    540    649    743       C  
ATOM   2327  O   LYS A 292      32.326  58.667  21.754  1.00 86.89           O  
ANISOU 2327  O   LYS A 292    12718   8965  11330    608    772    887       O  
ATOM   2328  CB  LYS A 292      35.106  60.271  22.532  1.00 85.70           C  
ANISOU 2328  CB  LYS A 292    12911   8644  11007    640    528    650       C  
ATOM   2329  CG  LYS A 292      35.689  61.600  22.930  1.00 96.82           C  
ANISOU 2329  CG  LYS A 292    14496   9971  12319    694    493    666       C  
ATOM   2330  CD  LYS A 292      36.749  61.408  24.004  1.00107.12           C  
ANISOU 2330  CD  LYS A 292    16024  11074  13603    762    365    556       C  
ATOM   2331  CE  LYS A 292      36.180  60.681  25.218  1.00112.46           C  
ANISOU 2331  CE  LYS A 292    16890  11579  14262    901    434    614       C  
ATOM   2332  NZ  LYS A 292      37.203  60.464  26.281  1.00114.85           N  
ANISOU 2332  NZ  LYS A 292    17427  11673  14539    986    307    492       N  
ATOM   2333  N   SER A 293      34.146  58.090  20.549  1.00 74.23           N  
ANISOU 2333  N   SER A 293    10939   7496   9771    439    521    588       N  
ATOM   2334  CA  SER A 293      33.800  56.682  20.396  1.00 78.50           C  
ANISOU 2334  CA  SER A 293    11363   8057  10408    399    491    552       C  
ATOM   2335  C   SER A 293      34.969  55.988  19.713  1.00 82.14           C  
ANISOU 2335  C   SER A 293    11724   8595  10892    306    322    361       C  
ATOM   2336  O   SER A 293      35.772  56.623  19.024  1.00 83.65           O  
ANISOU 2336  O   SER A 293    11862   8869  11053    260    255    289       O  
ATOM   2337  CB  SER A 293      32.496  56.489  19.607  1.00 82.30           C  
ANISOU 2337  CB  SER A 293    11648   8654  10969    366    579    673       C  
ATOM   2338  OG  SER A 293      32.548  57.119  18.339  1.00 88.88           O  
ANISOU 2338  OG  SER A 293    12317   9654  11799    299    557    650       O  
ATOM   2339  N   SER A 294      35.060  54.673  19.917  1.00 86.22           N  
ANISOU 2339  N   SER A 294    12218   9081  11460    286    259    287       N  
ATOM   2340  CA  SER A 294      36.143  53.917  19.297  1.00 91.93           C  
ANISOU 2340  CA  SER A 294    12859   9880  12190    209     98    114       C  
ATOM   2341  C   SER A 294      35.896  53.743  17.805  1.00 92.13           C  
ANISOU 2341  C   SER A 294    12645  10093  12267    132     52    105       C  
ATOM   2342  O   SER A 294      36.832  53.800  17.000  1.00 90.90           O  
ANISOU 2342  O   SER A 294    12412  10034  12091     86    -53      2       O  
ATOM   2343  CB  SER A 294      36.288  52.557  19.978  1.00 95.75           C  
ANISOU 2343  CB  SER A 294    13407  10276  12697    217     45     38       C  
ATOM   2344  OG  SER A 294      36.508  52.706  21.369  1.00 98.34           O  
ANISOU 2344  OG  SER A 294    13972  10417  12974    313     92     40       O  
ATOM   2345  N   GLU A 295      34.641  53.536  17.422  1.00 96.93           N  
ANISOU 2345  N   GLU A 295    13138  10747  12946    129    126    219       N  
ATOM   2346  CA  GLU A 295      34.251  53.397  16.030  1.00101.31           C  
ANISOU 2346  CA  GLU A 295    13479  11459  13554     78     82    219       C  
ATOM   2347  C   GLU A 295      32.998  54.227  15.785  1.00 98.95           C  
ANISOU 2347  C   GLU A 295    13118  11193  13286    103    223    379       C  
ATOM   2348  O   GLU A 295      32.333  54.686  16.718  1.00 98.59           O  
ANISOU 2348  O   GLU A 295    13183  11047  13228    158    354    502       O  
ATOM   2349  CB  GLU A 295      34.047  51.923  15.661  1.00106.66           C  
ANISOU 2349  CB  GLU A 295    14056  12163  14309     38    -29    163       C  
ATOM   2350  CG  GLU A 295      33.387  51.101  16.751  1.00112.48           C  
ANISOU 2350  CG  GLU A 295    14872  12765  15101     61     23    223       C  
ATOM   2351  CD  GLU A 295      33.212  49.647  16.357  1.00119.38           C  
ANISOU 2351  CD  GLU A 295    15644  13662  16052     15    -99    166       C  
ATOM   2352  OE1 GLU A 295      33.646  49.271  15.246  1.00122.25           O  
ANISOU 2352  OE1 GLU A 295    15893  14146  16412    -27   -236     75       O  
ATOM   2353  OE2 GLU A 295      32.662  48.874  17.171  1.00121.64           O  
ANISOU 2353  OE2 GLU A 295    15976  13842  16401     31    -60    214       O  
ATOM   2354  N   TYR A 296      32.684  54.426  14.508  1.00 93.32           N  
ANISOU 2354  N   TYR A 296    12234  10619  12605     76    197    378       N  
ATOM   2355  CA  TYR A 296      31.574  55.279  14.115  1.00 88.89           C  
ANISOU 2355  CA  TYR A 296    11603  10109  12062     98    324    511       C  
ATOM   2356  C   TYR A 296      30.804  54.644  12.970  1.00 85.38           C  
ANISOU 2356  C   TYR A 296    10959   9760  11721     71    262    515       C  
ATOM   2357  O   TYR A 296      31.399  54.057  12.061  1.00 90.40           O  
ANISOU 2357  O   TYR A 296    11505  10472  12369     48    120    398       O  
ATOM   2358  CB  TYR A 296      32.060  56.672  13.698  1.00 88.83           C  
ANISOU 2358  CB  TYR A 296    11624  10172  11957    116    379    503       C  
ATOM   2359  CG  TYR A 296      30.932  57.594  13.311  1.00 88.51           C  
ANISOU 2359  CG  TYR A 296    11526  10190  11912    143    517    633       C  
ATOM   2360  CD1 TYR A 296      30.222  58.297  14.274  1.00 90.47           C  
ANISOU 2360  CD1 TYR A 296    11899  10358  12116    191    667    779       C  
ATOM   2361  CD2 TYR A 296      30.569  57.750  11.981  1.00 90.30           C  
ANISOU 2361  CD2 TYR A 296    11587  10553  12172    134    498    612       C  
ATOM   2362  CE1 TYR A 296      29.186  59.133  13.923  1.00 93.42           C  
ANISOU 2362  CE1 TYR A 296    12227  10795  12474    218    797    902       C  
ATOM   2363  CE2 TYR A 296      29.536  58.581  11.619  1.00 94.81           C  
ANISOU 2363  CE2 TYR A 296    12108  11181  12734    161    625    721       C  
ATOM   2364  CZ  TYR A 296      28.849  59.269  12.593  1.00 97.19           C  
ANISOU 2364  CZ  TYR A 296    12529  11412  12987    197    775    867       C  
ATOM   2365  OH  TYR A 296      27.820  60.096  12.227  1.00 98.44           O  
ANISOU 2365  OH  TYR A 296    12642  11636  13123    225    904    979       O  
ATOM   2366  N   LYS A 297      29.479  54.782  13.014  1.00 77.59           N  
ANISOU 2366  N   LYS A 297     9910   8763  10808     85    364    658       N  
ATOM   2367  CA  LYS A 297      28.615  54.289  11.943  1.00 77.67           C  
ANISOU 2367  CA  LYS A 297     9730   8847  10932     67    303    676       C  
ATOM   2368  C   LYS A 297      27.445  55.248  11.787  1.00 75.80           C  
ANISOU 2368  C   LYS A 297     9448   8643  10710     97    458    824       C  
ATOM   2369  O   LYS A 297      26.591  55.332  12.673  1.00 81.63           O  
ANISOU 2369  O   LYS A 297    10230   9297  11487    116    582    974       O  
ATOM   2370  CB  LYS A 297      28.120  52.877  12.235  1.00 88.00           C  
ANISOU 2370  CB  LYS A 297    10980  10078  12377     35    215    693       C  
ATOM   2371  CG  LYS A 297      27.232  52.311  11.137  1.00 99.45           C  
ANISOU 2371  CG  LYS A 297    12239  11584  13963     18    120    710       C  
ATOM   2372  CD  LYS A 297      26.776  50.893  11.449  1.00106.54           C  
ANISOU 2372  CD  LYS A 297    13078  12394  15007    -19     17    731       C  
ATOM   2373  CE  LYS A 297      25.858  50.358  10.354  1.00110.86           C  
ANISOU 2373  CE  LYS A 297    13437  12979  15706    -33   -101    752       C  
ATOM   2374  NZ  LYS A 297      26.518  50.336   9.013  1.00112.54           N  
ANISOU 2374  NZ  LYS A 297    13596  13303  15860    -12   -260    604       N  
ATOM   2375  N   GLY A 298      27.405  55.967  10.670  1.00 73.68           N  
ANISOU 2375  N   GLY A 298     9095   8495  10405    112    458    786       N  
ATOM   2376  CA  GLY A 298      26.344  56.912  10.419  1.00 73.39           C  
ANISOU 2376  CA  GLY A 298     9015   8505  10364    142    602    909       C  
ATOM   2377  C   GLY A 298      26.262  57.297   8.955  1.00 75.03           C  
ANISOU 2377  C   GLY A 298     9097   8843  10569    162    554    832       C  
ATOM   2378  O   GLY A 298      27.015  56.796   8.113  1.00 72.15           O  
ANISOU 2378  O   GLY A 298     8678   8527  10209    164    406    693       O  
ATOM   2379  N   PRO A 299      25.332  58.193   8.624  1.00 72.91           N  
ANISOU 2379  N   PRO A 299     8789   8631  10284    193    682    925       N  
ATOM   2380  CA  PRO A 299      25.184  58.625   7.226  1.00 69.61           C  
ANISOU 2380  CA  PRO A 299     8262   8332   9856    232    652    849       C  
ATOM   2381  C   PRO A 299      26.231  59.655   6.823  1.00 75.73           C  
ANISOU 2381  C   PRO A 299     9112   9188  10475    266    696    756       C  
ATOM   2382  O   PRO A 299      26.165  60.816   7.240  1.00 81.63           O  
ANISOU 2382  O   PRO A 299     9951   9957  11106    282    851    823       O  
ATOM   2383  CB  PRO A 299      23.768  59.205   7.188  1.00 70.06           C  
ANISOU 2383  CB  PRO A 299     8263   8409   9949    251    788    993       C  
ATOM   2384  CG  PRO A 299      23.527  59.680   8.581  1.00 73.99           C  
ANISOU 2384  CG  PRO A 299     8897   8831  10383    243    946   1142       C  
ATOM   2385  CD  PRO A 299      24.290  58.760   9.499  1.00 75.48           C  
ANISOU 2385  CD  PRO A 299     9165   8910  10604    206    859   1111       C  
ATOM   2386  N   ILE A 300      27.224  59.235   6.040  1.00 73.31           N  
ANISOU 2386  N   ILE A 300     8770   8921  10163    283    559    613       N  
ATOM   2387  CA  ILE A 300      28.311  60.106   5.603  1.00 70.39           C  
ANISOU 2387  CA  ILE A 300     8451   8621   9673    319    590    529       C  
ATOM   2388  C   ILE A 300      28.099  60.474   4.141  1.00 69.88           C  
ANISOU 2388  C   ILE A 300     8283   8664   9605    401    582    463       C  
ATOM   2389  O   ILE A 300      27.621  59.655   3.343  1.00 72.52           O  
ANISOU 2389  O   ILE A 300     8512   9006  10035    434    462    423       O  
ATOM   2390  CB  ILE A 300      29.676  59.427   5.826  1.00 65.47           C  
ANISOU 2390  CB  ILE A 300     7873   7961   9042    295    459    429       C  
ATOM   2391  CG1 ILE A 300      29.814  58.998   7.286  1.00 58.94           C  
ANISOU 2391  CG1 ILE A 300     7159   7015   8222    229    465    484       C  
ATOM   2392  CG2 ILE A 300      30.819  60.356   5.447  1.00 63.12           C  
ANISOU 2392  CG2 ILE A 300     7617   7722   8643    329    498    364       C  
ATOM   2393  CD1 ILE A 300      29.749  60.154   8.272  1.00 56.69           C  
ANISOU 2393  CD1 ILE A 300     7010   6691   7840    223    626    577       C  
ATOM   2394  N   THR A 301      28.440  61.713   3.786  1.00 63.74           N  
ANISOU 2394  N   THR A 301     7541   7960   8715    444    704    451       N  
ATOM   2395  CA  THR A 301      28.326  62.180   2.411  1.00 61.84           C  
ANISOU 2395  CA  THR A 301     7221   7819   8454    543    720    383       C  
ATOM   2396  C   THR A 301      29.644  62.655   1.821  1.00 63.20           C  
ANISOU 2396  C   THR A 301     7412   8044   8556    598    715    293       C  
ATOM   2397  O   THR A 301      29.808  62.609   0.598  1.00 65.41           O  
ANISOU 2397  O   THR A 301     7623   8387   8844    703    673    215       O  
ATOM   2398  CB  THR A 301      27.297  63.318   2.311  1.00 68.68           C  
ANISOU 2398  CB  THR A 301     8095   8744   9255    567    899    458       C  
ATOM   2399  OG1 THR A 301      27.229  63.784   0.958  1.00 72.23           O  
ANISOU 2399  OG1 THR A 301     8479   9288   9678    677    919    378       O  
ATOM   2400  CG2 THR A 301      27.681  64.476   3.233  1.00 66.48           C  
ANISOU 2400  CG2 THR A 301     7947   8463   8848    526   1051    527       C  
ATOM   2401  N   ASP A 302      30.579  63.109   2.649  1.00 65.90           N  
ANISOU 2401  N   ASP A 302     7847   8353   8839    543    754    308       N  
ATOM   2402  CA  ASP A 302      31.911  63.504   2.218  1.00 65.69           C  
ANISOU 2402  CA  ASP A 302     7829   8359   8773    582    742    241       C  
ATOM   2403  C   ASP A 302      32.935  62.914   3.177  1.00 60.48           C  
ANISOU 2403  C   ASP A 302     7235   7613   8133    503    644    229       C  
ATOM   2404  O   ASP A 302      32.723  62.905   4.395  1.00 49.32           O  
ANISOU 2404  O   ASP A 302     5912   6117   6709    421    666    291       O  
ATOM   2405  CB  ASP A 302      32.076  65.034   2.170  1.00 71.12           C  
ANISOU 2405  CB  ASP A 302     8565   9098   9360    603    912    273       C  
ATOM   2406  CG  ASP A 302      31.039  65.709   1.303  1.00 80.68           C  
ANISOU 2406  CG  ASP A 302     9727  10396  10531    681   1028    282       C  
ATOM   2407  OD1 ASP A 302      30.969  65.379   0.099  1.00 84.09           O  
ANISOU 2407  OD1 ASP A 302    10070  10884  10997    785    983    210       O  
ATOM   2408  OD2 ASP A 302      30.303  66.579   1.821  1.00 81.61           O  
ANISOU 2408  OD2 ASP A 302     9908  10525  10575    651   1163    360       O  
ATOM   2409  N   VAL A 303      34.037  62.411   2.621  1.00 58.49           N  
ANISOU 2409  N   VAL A 303     6944   7376   7904    542    539    153       N  
ATOM   2410  CA  VAL A 303      35.159  61.900   3.401  1.00 57.97           C  
ANISOU 2410  CA  VAL A 303     6936   7239   7852    478    443    128       C  
ATOM   2411  C   VAL A 303      36.443  62.482   2.826  1.00 62.64           C  
ANISOU 2411  C   VAL A 303     7502   7871   8426    530    454     93       C  
ATOM   2412  O   VAL A 303      36.649  62.454   1.608  1.00 69.99           O  
ANISOU 2412  O   VAL A 303     8349   8881   9364    639    447     56       O  
ATOM   2413  CB  VAL A 303      35.227  60.361   3.395  1.00 53.75           C  
ANISOU 2413  CB  VAL A 303     6374   6671   7377    467    271     78       C  
ATOM   2414  CG1 VAL A 303      36.265  59.877   4.399  1.00 48.08           C  
ANISOU 2414  CG1 VAL A 303     5736   5872   6661    391    190     53       C  
ATOM   2415  CG2 VAL A 303      33.862  59.752   3.680  1.00 56.30           C  
ANISOU 2415  CG2 VAL A 303     6683   6961   7746    435    258    119       C  
ATOM   2416  N   PHE A 304      37.313  62.976   3.703  1.00 60.87           N  
ANISOU 2416  N   PHE A 304     7354   7584   8190    462    466    110       N  
ATOM   2417  CA  PHE A 304      38.570  63.607   3.321  1.00 58.90           C  
ANISOU 2417  CA  PHE A 304     7077   7355   7948    494    480     97       C  
ATOM   2418  C   PHE A 304      39.733  62.727   3.762  1.00 57.57           C  
ANISOU 2418  C   PHE A 304     6925   7128   7822    455    336     53       C  
ATOM   2419  O   PHE A 304      39.772  62.266   4.908  1.00 57.22           O  
ANISOU 2419  O   PHE A 304     6973   6990   7780    366    273     49       O  
ATOM   2420  CB  PHE A 304      38.701  65.000   3.946  1.00 55.81           C  
ANISOU 2420  CB  PHE A 304     6760   6928   7518    450    596    155       C  
ATOM   2421  CG  PHE A 304      37.743  66.010   3.383  1.00 60.19           C  
ANISOU 2421  CG  PHE A 304     7298   7559   8014    501    751    195       C  
ATOM   2422  CD1 PHE A 304      38.157  66.915   2.419  1.00 58.60           C  
ANISOU 2422  CD1 PHE A 304     7029   7434   7804    581    845    195       C  
ATOM   2423  CD2 PHE A 304      36.433  66.063   3.826  1.00 64.22           C  
ANISOU 2423  CD2 PHE A 304     7861   8063   8476    474    811    238       C  
ATOM   2424  CE1 PHE A 304      37.283  67.846   1.903  1.00 61.05           C  
ANISOU 2424  CE1 PHE A 304     7333   7817   8048    633    992    221       C  
ATOM   2425  CE2 PHE A 304      35.549  66.992   3.309  1.00 66.22           C  
ANISOU 2425  CE2 PHE A 304     8104   8393   8665    523    955    273       C  
ATOM   2426  CZ  PHE A 304      35.974  67.884   2.345  1.00 64.88           C  
ANISOU 2426  CZ  PHE A 304     7875   8302   8474    601   1044    257       C  
ATOM   2427  N   TYR A 305      40.669  62.492   2.848  1.00 51.45           N  
ANISOU 2427  N   TYR A 305     6066   6408   7076    534    290     24       N  
ATOM   2428  CA  TYR A 305      41.835  61.668   3.104  1.00 52.55           C  
ANISOU 2428  CA  TYR A 305     6208   6511   7249    513    158    -13       C  
ATOM   2429  C   TYR A 305      43.101  62.483   2.876  1.00 65.23           C  
ANISOU 2429  C   TYR A 305     7771   8117   8896    534    194     15       C  
ATOM   2430  O   TYR A 305      43.148  63.358   2.003  1.00 65.51           O  
ANISOU 2430  O   TYR A 305     7735   8217   8939    618    303     51       O  
ATOM   2431  CB  TYR A 305      41.850  60.426   2.197  1.00 53.12           C  
ANISOU 2431  CB  TYR A 305     6221   6645   7318    603     48    -59       C  
ATOM   2432  CG  TYR A 305      40.642  59.519   2.334  1.00 55.63           C  
ANISOU 2432  CG  TYR A 305     6563   6955   7619    583    -11    -84       C  
ATOM   2433  CD1 TYR A 305      40.688  58.394   3.148  1.00 53.22           C  
ANISOU 2433  CD1 TYR A 305     6318   6586   7315    506   -136   -122       C  
ATOM   2434  CD2 TYR A 305      39.465  59.772   1.634  1.00 58.15           C  
ANISOU 2434  CD2 TYR A 305     6840   7326   7930    646     55    -68       C  
ATOM   2435  CE1 TYR A 305      39.596  57.560   3.280  1.00 50.88           C  
ANISOU 2435  CE1 TYR A 305     6033   6275   7025    485   -190   -133       C  
ATOM   2436  CE2 TYR A 305      38.364  58.939   1.761  1.00 58.03           C  
ANISOU 2436  CE2 TYR A 305     6832   7292   7926    623     -9    -80       C  
ATOM   2437  CZ  TYR A 305      38.440  57.831   2.585  1.00 54.10           C  
ANISOU 2437  CZ  TYR A 305     6386   6727   7441    541   -132   -107       C  
ATOM   2438  OH  TYR A 305      37.359  56.988   2.727  1.00 54.74           O  
ANISOU 2438  OH  TYR A 305     6465   6781   7553    516   -196   -108       O  
ATOM   2439  N   LYS A 306      44.131  62.177   3.664  1.00 69.73           N  
ANISOU 2439  N   LYS A 306     8382   8609   9502    463    100     -2       N  
ATOM   2440  CA  LYS A 306      45.449  62.763   3.466  1.00 72.85           C  
ANISOU 2440  CA  LYS A 306     8722   8994   9966    478    103     30       C  
ATOM   2441  C   LYS A 306      46.223  61.978   2.416  1.00 62.89           C  
ANISOU 2441  C   LYS A 306     7362   7811   8721    590     44     23       C  
ATOM   2442  O   LYS A 306      46.188  60.743   2.388  1.00 59.77           O  
ANISOU 2442  O   LYS A 306     6989   7432   8291    602    -69    -27       O  
ATOM   2443  CB  LYS A 306      46.231  62.784   4.781  1.00 83.91           C  
ANISOU 2443  CB  LYS A 306    10213  10265  11405    360     16     14       C  
ATOM   2444  CG  LYS A 306      46.196  64.112   5.516  1.00 89.20           C  
ANISOU 2444  CG  LYS A 306    10947  10849  12095    294     86     60       C  
ATOM   2445  CD  LYS A 306      47.240  64.145   6.624  1.00 94.60           C  
ANISOU 2445  CD  LYS A 306    11708  11395  12841    207    -26     43       C  
ATOM   2446  CE  LYS A 306      48.642  63.935   6.074  1.00 98.18           C  
ANISOU 2446  CE  LYS A 306    12046  11867  13390    237    -89     53       C  
ATOM   2447  NZ  LYS A 306      49.010  64.961   5.060  1.00101.77           N  
ANISOU 2447  NZ  LYS A 306    12370  12389  13911    308     24    133       N  
ATOM   2448  N   GLU A 307      46.927  62.706   1.554  1.00 57.81           N  
ANISOU 2448  N   GLU A 307     6618   7215   8132    681    124     82       N  
ATOM   2449  CA  GLU A 307      47.699  62.104   0.479  1.00 59.24           C  
ANISOU 2449  CA  GLU A 307     6709   7470   8328    821     91    102       C  
ATOM   2450  C   GLU A 307      48.928  62.966   0.231  1.00 65.13           C  
ANISOU 2450  C   GLU A 307     7365   8201   9180    850    151    182       C  
ATOM   2451  O   GLU A 307      48.978  64.137   0.616  1.00 65.48           O  
ANISOU 2451  O   GLU A 307     7404   8197   9279    785    236    221       O  
ATOM   2452  CB  GLU A 307      46.853  61.957  -0.799  1.00 62.57           C  
ANISOU 2452  CB  GLU A 307     7090   7993   8691    985    154    101       C  
ATOM   2453  CG  GLU A 307      47.494  61.156  -1.936  1.00 69.21           C  
ANISOU 2453  CG  GLU A 307     7873   8905   9519   1164    101    120       C  
ATOM   2454  CD  GLU A 307      47.871  59.743  -1.527  1.00 77.97           C  
ANISOU 2454  CD  GLU A 307     9038  10001  10587   1128    -78     71       C  
ATOM   2455  OE1 GLU A 307      48.999  59.555  -1.021  1.00 81.49           O  
ANISOU 2455  OE1 GLU A 307     9477  10411  11077   1071   -137     89       O  
ATOM   2456  OE2 GLU A 307      47.040  58.821  -1.698  1.00 78.72           O  
ANISOU 2456  OE2 GLU A 307     9185  10117  10609   1154   -165     13       O  
ATOM   2457  N   ASN A 308      49.945  62.351  -0.374  1.00 68.92           N  
ANISOU 2457  N   ASN A 308     7778   8717   9691    947     98    216       N  
ATOM   2458  CA  ASN A 308      51.132  63.065  -0.823  1.00 67.90           C  
ANISOU 2458  CA  ASN A 308     7535   8584   9679   1007    163    315       C  
ATOM   2459  C   ASN A 308      51.500  62.608  -2.229  1.00 72.31           C  
ANISOU 2459  C   ASN A 308     8013   9243  10219   1231    200    373       C  
ATOM   2460  O   ASN A 308      51.467  63.402  -3.173  1.00 82.49           O  
ANISOU 2460  O   ASN A 308     9224  10577  11542   1368    345    441       O  
ATOM   2461  CB  ASN A 308      52.297  62.853   0.135  1.00 68.38           C  
ANISOU 2461  CB  ASN A 308     7601   8555   9826    884     49    322       C  
ATOM   2462  CG  ASN A 308      53.551  63.556  -0.325  1.00 71.12           C  
ANISOU 2462  CG  ASN A 308     7812   8889  10320    943    109    440       C  
ATOM   2463  OD1 ASN A 308      54.408  62.961  -0.978  1.00 70.13           O  
ANISOU 2463  OD1 ASN A 308     7614   8812  10218   1058     84    498       O  
ATOM   2464  ND2 ASN A 308      53.663  64.835   0.007  1.00 74.69           N  
ANISOU 2464  ND2 ASN A 308     8230   9274  10874    871    189    487       N  
ATOM   2465  N   SER A 309      51.852  61.332  -2.377  1.00 71.64           N  
ANISOU 2465  N   SER A 309     7958   9189  10072   1284     71    348       N  
ATOM   2466  CA  SER A 309      52.121  60.751  -3.690  1.00 69.88           C  
ANISOU 2466  CA  SER A 309     7695   9055   9802   1520     82    402       C  
ATOM   2467  C   SER A 309      51.846  59.254  -3.628  1.00 70.88           C  
ANISOU 2467  C   SER A 309     7919   9211   9803   1537    -88    324       C  
ATOM   2468  O   SER A 309      52.443  58.542  -2.815  1.00 63.15           O  
ANISOU 2468  O   SER A 309     6980   8197   8817   1423   -213    291       O  
ATOM   2469  CB  SER A 309      53.563  61.026  -4.125  1.00 68.41           C  
ANISOU 2469  CB  SER A 309     7396   8873   9725   1615    127    531       C  
ATOM   2470  OG  SER A 309      53.782  60.609  -5.459  1.00 73.16           O  
ANISOU 2470  OG  SER A 309     7967   9555  10277   1879    165    603       O  
ATOM   2471  N   TYR A 310      50.946  58.778  -4.487  1.00 72.16           N  
ANISOU 2471  N   TYR A 310     8122   9430   9867   1683    -99    291       N  
ATOM   2472  CA  TYR A 310      50.568  57.371  -4.545  1.00 64.61           C  
ANISOU 2472  CA  TYR A 310     7260   8497   8791   1714   -270    221       C  
ATOM   2473  C   TYR A 310      50.699  56.868  -5.972  1.00 61.72           C  
ANISOU 2473  C   TYR A 310     6895   8203   8355   1998   -283    275       C  
ATOM   2474  O   TYR A 310      50.166  57.485  -6.894  1.00 67.62           O  
ANISOU 2474  O   TYR A 310     7613   8975   9106   2154   -173    301       O  
ATOM   2475  CB  TYR A 310      49.130  57.191  -4.051  1.00 62.54           C  
ANISOU 2475  CB  TYR A 310     7070   8209   8484   1598   -308    116       C  
ATOM   2476  CG  TYR A 310      48.431  55.941  -4.540  1.00 68.16           C  
ANISOU 2476  CG  TYR A 310     7859   8950   9088   1691   -457     57       C  
ATOM   2477  CD1 TYR A 310      48.609  54.720  -3.910  1.00 64.37           C  
ANISOU 2477  CD1 TYR A 310     7457   8455   8545   1604   -629     -1       C  
ATOM   2478  CD2 TYR A 310      47.563  55.999  -5.628  1.00 75.72           C  
ANISOU 2478  CD2 TYR A 310     8820   9942  10009   1868   -434     53       C  
ATOM   2479  CE1 TYR A 310      47.959  53.591  -4.359  1.00 71.17           C  
ANISOU 2479  CE1 TYR A 310     8392   9336   9316   1686   -777    -51       C  
ATOM   2480  CE2 TYR A 310      46.910  54.878  -6.085  1.00 74.15           C  
ANISOU 2480  CE2 TYR A 310     8695   9753   9726   1956   -591      1       C  
ATOM   2481  CZ  TYR A 310      47.109  53.678  -5.448  1.00 79.36           C  
ANISOU 2481  CZ  TYR A 310     9426  10398  10330   1861   -765    -48       C  
ATOM   2482  OH  TYR A 310      46.450  52.565  -5.913  1.00 89.85           O  
ANISOU 2482  OH  TYR A 310    10830  11729  11580   1948   -935    -97       O  
ATOM   2483  N   THR A 311      51.417  55.760  -6.150  1.00 65.26           N  
ANISOU 2483  N   THR A 311     7389   8679   8729   2077   -418    292       N  
ATOM   2484  CA  THR A 311      51.537  55.082  -7.437  1.00 72.68           C  
ANISOU 2484  CA  THR A 311     8368   9677   9572   2362   -469    342       C  
ATOM   2485  C   THR A 311      51.417  53.580  -7.241  1.00 75.18           C  
ANISOU 2485  C   THR A 311     8802  10005   9756   2353   -689    273       C  
ATOM   2486  O   THR A 311      52.081  53.019  -6.365  1.00 75.28           O  
ANISOU 2486  O   THR A 311     8839  10009   9756   2205   -776    252       O  
ATOM   2487  CB  THR A 311      52.876  55.380  -8.131  1.00 80.91           C  
ANISOU 2487  CB  THR A 311     9335  10754  10654   2547   -380    493       C  
ATOM   2488  OG1 THR A 311      53.953  55.125  -7.219  1.00 85.68           O  
ANISOU 2488  OG1 THR A 311     9913  11342  11299   2388   -431    516       O  
ATOM   2489  CG2 THR A 311      52.951  56.823  -8.625  1.00 83.41           C  
ANISOU 2489  CG2 THR A 311     9535  11062  11094   2620   -157    575       C  
ATOM   2490  N   THR A 312      50.568  52.935  -8.031  1.00 78.55           N  
ANISOU 2490  N   THR A 312     9310  10448  10088   2510   -786    234       N  
ATOM   2491  CA  THR A 312      50.536  51.485  -7.985  1.00 80.01           C  
ANISOU 2491  CA  THR A 312     9613  10645  10142   2533  -1006    183       C  
ATOM   2492  C   THR A 312      51.778  50.944  -8.685  1.00 80.43           C  
ANISOU 2492  C   THR A 312     9695  10753  10112   2750  -1046    293       C  
ATOM   2493  O   THR A 312      52.380  51.612  -9.530  1.00 81.23           O  
ANISOU 2493  O   THR A 312     9736  10880  10248   2953   -912    411       O  
ATOM   2494  CB  THR A 312      49.271  50.941  -8.653  1.00 82.63           C  
ANISOU 2494  CB  THR A 312    10025  10962  10410   2646  -1121    115       C  
ATOM   2495  OG1 THR A 312      49.175  49.529  -8.427  1.00 83.69           O  
ANISOU 2495  OG1 THR A 312    10274  11095  10429   2624  -1349     56       O  
ATOM   2496  CG2 THR A 312      49.302  51.206 -10.146  1.00 80.00           C  
ANISOU 2496  CG2 THR A 312     9706  10653  10039   2985  -1074    194       C  
ATOM   2497  N   THR A 313      52.167  49.725  -8.333  1.00 85.17           N  
ANISOU 2497  N   THR A 313    10391  11373  10597   2717  -1225    261       N  
ATOM   2498  CA  THR A 313      53.262  49.063  -9.027  1.00 89.70           C  
ANISOU 2498  CA  THR A 313    11018  12005  11059   2940  -1286    368       C  
ATOM   2499  C   THR A 313      52.764  48.030 -10.025  1.00 98.87           C  
ANISOU 2499  C   THR A 313    12326  13184  12058   3188  -1464    360       C  
ATOM   2500  O   THR A 313      53.577  47.348 -10.654  1.00101.72           O  
ANISOU 2500  O   THR A 313    12767  13576  12305   3322  -1503    440       O  
ATOM   2501  CB  THR A 313      54.224  48.408  -8.025  1.00 82.94           C  
ANISOU 2501  CB  THR A 313    10182  11168  10163   2765  -1364    352       C  
ATOM   2502  OG1 THR A 313      53.532  47.401  -7.274  1.00 88.21           O  
ANISOU 2502  OG1 THR A 313    10953  11814  10748   2595  -1542    211       O  
ATOM   2503  CG2 THR A 313      54.793  49.448  -7.079  1.00 76.48           C  
ANISOU 2503  CG2 THR A 313     9229  10316   9514   2545  -1207    366       C  
ATOM   2504  N   ILE A 314      51.447  47.922 -10.199  1.00105.47           N  
ANISOU 2504  N   ILE A 314    13202  13974  12898   3175  -1536    263       N  
ATOM   2505  CA  ILE A 314      50.897  46.916 -11.096  1.00112.78           C  
ANISOU 2505  CA  ILE A 314    14277  14875  13699   3290  -1681    233       C  
ATOM   2506  C   ILE A 314      51.251  47.235 -12.542  1.00122.03           C  
ANISOU 2506  C   ILE A 314    15482  16027  14856   3423  -1512    324       C  
ATOM   2507  O   ILE A 314      51.587  46.330 -13.316  1.00128.10           O  
ANISOU 2507  O   ILE A 314    16376  16784  15512   3446  -1551    340       O  
ATOM   2508  CB  ILE A 314      49.378  46.788 -10.882  1.00110.13           C  
ANISOU 2508  CB  ILE A 314    13955  14485  13403   3236  -1807    111       C  
ATOM   2509  CG1 ILE A 314      49.099  46.216  -9.490  1.00102.71           C  
ANISOU 2509  CG1 ILE A 314    13016  13531  12480   2939  -1915      7       C  
ATOM   2510  CG2 ILE A 314      48.747  45.913 -11.957  1.00108.05           C  
ANISOU 2510  CG2 ILE A 314    13832  14163  13058   3264  -1877     79       C  
ATOM   2511  CD1 ILE A 314      49.943  44.997  -9.167  1.00 92.91           C  
ANISOU 2511  CD1 ILE A 314    11881  12331  11090   2932  -2080      9       C  
ATOM   2512  N   LYS A 315      51.097  48.512 -12.951  1.00126.70           N  
ANISOU 2512  N   LYS A 315    15970  16610  15562   3503  -1324    370       N  
ATOM   2513  CA  LYS A 315      51.509  49.043 -14.251  1.00130.71           C  
ANISOU 2513  CA  LYS A 315    16491  17098  16075   3613  -1144    456       C  
ATOM   2514  C   LYS A 315      50.322  48.796 -15.181  1.00130.75           C  
ANISOU 2514  C   LYS A 315    16596  17043  16041   3651  -1194    374       C  
ATOM   2515  O   LYS A 315      49.475  47.954 -14.856  1.00132.31           O  
ANISOU 2515  O   LYS A 315    16864  17215  16192   3590  -1379    276       O  
ATOM   2516  CB  LYS A 315      52.819  48.392 -14.728  1.00133.10           C  
ANISOU 2516  CB  LYS A 315    16859  17427  16287   3643  -1126    551       C  
ATOM   2517  CG  LYS A 315      53.660  49.150 -15.738  1.00135.61           C  
ANISOU 2517  CG  LYS A 315    17142  17740  16643   3740   -920    668       C  
ATOM   2518  CD  LYS A 315      55.082  48.609 -15.759  1.00136.23           C  
ANISOU 2518  CD  LYS A 315    17238  17857  16665   3745   -907    769       C  
ATOM   2519  CE  LYS A 315      55.623  48.507 -17.174  1.00138.57           C  
ANISOU 2519  CE  LYS A 315    17617  18137  16897   3846   -808    834       C  
ATOM   2520  NZ  LYS A 315      55.524  49.796 -17.915  1.00140.57           N  
ANISOU 2520  NZ  LYS A 315    17795  18363  17252   3916   -616    881       N  
ATOM   2521  N   PRO A 316      50.182  49.506 -16.315  1.00129.90           N  
ANISOU 2521  N   PRO A 316    16495  16906  15956   3741  -1044    405       N  
ATOM   2522  CA  PRO A 316      48.958  49.206 -17.069  1.00128.93           C  
ANISOU 2522  CA  PRO A 316    16465  16724  15797   3766  -1122    312       C  
ATOM   2523  C   PRO A 316      48.981  47.827 -17.733  1.00130.12           C  
ANISOU 2523  C   PRO A 316    16779  16851  15809   3776  -1272    282       C  
ATOM   2524  O   PRO A 316      49.041  47.727 -18.958  1.00131.36           O  
ANISOU 2524  O   PRO A 316    17023  16982  15906   3859  -1222    296       O  
ATOM   2525  CB  PRO A 316      48.918  50.321 -18.116  1.00126.31           C  
ANISOU 2525  CB  PRO A 316    16106  16373  15511   3851   -922    351       C  
ATOM   2526  CG  PRO A 316      50.344  50.687 -18.315  1.00126.44           C  
ANISOU 2526  CG  PRO A 316    16080  16428  15534   3887   -778    476       C  
ATOM   2527  CD  PRO A 316      50.944  50.601 -16.940  1.00127.91           C  
ANISOU 2527  CD  PRO A 316    16169  16663  15769   3809   -817    506       C  
TER    2528      PRO A 316                                                      
ATOM   2529  N   MET B  -1      47.210 -12.196 -13.881  1.00128.40           N  
ATOM   2530  CA  MET B  -1      48.444 -12.850 -14.296  1.00127.63           C  
ATOM   2531  C   MET B  -1      48.981 -12.234 -15.584  1.00130.89           C  
ATOM   2532  O   MET B  -1      49.235 -12.949 -16.552  1.00135.12           O  
ATOM   2533  CB  MET B  -1      48.220 -14.351 -14.499  1.00125.96           C  
ATOM   2534  CG  MET B  -1      47.546 -15.056 -13.338  1.00127.31           C  
ATOM   2535  SD  MET B  -1      48.518 -14.980 -11.826  1.00131.19           S  
ATOM   2536  CE  MET B  -1      50.125 -15.495 -12.419  1.00131.43           C  
ATOM   2537  N   ARG B   0      49.149 -10.913 -15.597  1.00129.07           N  
ATOM   2538  CA  ARG B   0      49.631 -10.185 -16.764  1.00126.12           C  
ATOM   2539  C   ARG B   0      51.085  -9.750 -16.548  1.00120.49           C  
ATOM   2540  O   ARG B   0      51.649  -9.898 -15.457  1.00117.87           O  
ATOM   2541  CB  ARG B   0      48.721  -8.989 -17.063  1.00125.46           C  
ATOM   2542  CG  ARG B   0      48.590  -8.644 -18.550  1.00126.19           C  
ATOM   2543  CD  ARG B   0      47.327  -9.234 -19.183  1.00127.23           C  
ATOM   2544  NE  ARG B   0      47.037  -8.643 -20.493  1.00127.93           N  
ATOM   2545  CZ  ARG B   0      46.130  -7.692 -20.710  1.00124.48           C  
ATOM   2546  NH1 ARG B   0      45.405  -7.214 -19.706  1.00122.00           N  
ATOM   2547  NH2 ARG B   0      45.942  -7.219 -21.937  1.00121.86           N  
ATOM   2548  N   GLU B   1      51.689  -9.211 -17.608  1.00116.40           N  
ATOM   2549  CA  GLU B   1      53.117  -8.916 -17.637  1.00112.84           C  
ATOM   2550  C   GLU B   1      53.511  -7.917 -16.545  1.00104.51           C  
ATOM   2551  O   GLU B   1      52.699  -7.130 -16.055  1.00102.88           O  
ATOM   2552  CB  GLU B   1      53.523  -8.375 -19.010  1.00118.81           C  
ATOM   2553  CG  GLU B   1      55.032  -8.300 -19.227  1.00124.53           C  
ATOM   2554  CD  GLU B   1      55.420  -7.900 -20.635  1.00126.73           C  
ATOM   2555  OE1 GLU B   1      54.509  -7.659 -21.457  1.00129.69           O  
ATOM   2556  OE2 GLU B   1      56.637  -7.798 -20.908  1.00123.90           O  
ATOM   2557  N   VAL B   2      54.799  -7.944 -16.190  1.00101.47           N  
ATOM   2558  CA  VAL B   2      55.390  -7.062 -15.185  1.00 98.08           C  
ATOM   2559  C   VAL B   2      56.242  -6.019 -15.905  1.00 93.40           C  
ATOM   2560  O   VAL B   2      57.185  -6.365 -16.625  1.00 82.35           O  
ATOM   2561  CB  VAL B   2      56.228  -7.852 -14.177  1.00 94.01           C  
ATOM   2562  CG1 VAL B   2      56.808  -6.943 -13.110  1.00 87.73           C  
ATOM   2563  CG2 VAL B   2      55.400  -8.957 -13.546  1.00 92.32           C  
ATOM   2564  N   ARG B   3      55.930  -4.740 -15.681  1.00134.40           N  
ANISOU 2564  N   ARG B   3    17549  17906  15609  -1667    619    907       N  
ATOM   2565  CA  ARG B   3      56.696  -3.627 -16.205  1.00117.59           C  
ANISOU 2565  CA  ARG B   3    15430  15724  13524  -1644    547    975       C  
ATOM   2566  C   ARG B   3      57.221  -2.786 -15.053  1.00100.12           C  
ANISOU 2566  C   ARG B   3    13138  13464  11438  -1505    544    943       C  
ATOM   2567  O   ARG B   3      56.454  -2.415 -14.162  1.00 98.55           O  
ANISOU 2567  O   ARG B   3    12835  13281  11330  -1430    506    899       O  
ATOM   2568  CB  ARG B   3      55.835  -2.755 -17.130  1.00118.19           C  
ANISOU 2568  CB  ARG B   3    15462  15815  13632  -1689    384   1048       C  
ATOM   2569  CG  ARG B   3      55.421  -3.440 -18.409  1.00119.75           C  
ANISOU 2569  CG  ARG B   3    15753  16051  13697  -1832    364   1091       C  
ATOM   2570  CD  ARG B   3      56.656  -3.904 -19.165  1.00121.78           C  
ANISOU 2570  CD  ARG B   3    16160  16274  13837  -1896    460   1121       C  
ATOM   2571  NE  ARG B   3      57.464  -2.784 -19.630  1.00131.48           N  
ANISOU 2571  NE  ARG B   3    17403  17442  15110  -1868    405   1193       N  
ATOM   2572  CZ  ARG B   3      57.123  -2.002 -20.642  1.00144.53           C  
ANISOU 2572  CZ  ARG B   3    19069  19091  16755  -1919    277   1278       C  
ATOM   2573  NH1 ARG B   3      55.990  -2.229 -21.277  1.00165.18           N  
ANISOU 2573  NH1 ARG B   3    21682  21759  19320  -1999    182   1299       N  
ATOM   2574  NH2 ARG B   3      57.911  -1.004 -21.007  1.00134.98           N  
ANISOU 2574  NH2 ARG B   3    17875  17820  15591  -1890    240   1343       N  
ATOM   2575  N   THR B   4      58.523  -2.482 -15.064  1.00 93.16           N  
ANISOU 2575  N   THR B   4    12309  12523  10567  -1473    586    961       N  
ATOM   2576  CA  THR B   4      59.132  -1.735 -13.972  1.00 86.97           C  
ANISOU 2576  CA  THR B   4    11460  11687   9897  -1346    583    926       C  
ATOM   2577  C   THR B   4      60.065  -0.663 -14.519  1.00 79.03           C  
ANISOU 2577  C   THR B   4    10462  10612   8952  -1329    525    993       C  
ATOM   2578  O   THR B   4      60.714  -0.844 -15.552  1.00 73.82           O  
ANISOU 2578  O   THR B   4     9892   9932   8222  -1408    553   1051       O  
ATOM   2579  CB  THR B   4      59.920  -2.638 -13.006  1.00 87.19           C  
ANISOU 2579  CB  THR B   4    11532  11702   9895  -1301    717    856       C  
ATOM   2580  OG1 THR B   4      60.914  -3.378 -13.726  1.00 93.44           O  
ANISOU 2580  OG1 THR B   4    12437  12471  10597  -1374    810    883       O  
ATOM   2581  CG2 THR B   4      58.987  -3.600 -12.295  1.00 87.01           C  
ANISOU 2581  CG2 THR B   4    11493  11740   9828  -1302    777    788       C  
ATOM   2582  N   ILE B   5      60.132   0.457 -13.802  1.00 77.51           N  
ANISOU 2582  N   ILE B   5    10177  10380   8892  -1224    450    982       N  
ATOM   2583  CA  ILE B   5      61.142   1.482 -14.023  1.00 77.09           C  
ANISOU 2583  CA  ILE B   5    10120  10249   8921  -1184    408   1029       C  
ATOM   2584  C   ILE B   5      61.706   1.886 -12.667  1.00 76.46           C  
ANISOU 2584  C   ILE B   5     9983  10125   8944  -1059    422    959       C  
ATOM   2585  O   ILE B   5      61.093   1.657 -11.622  1.00 84.35           O  
ANISOU 2585  O   ILE B   5    10933  11155   9962   -997    435    885       O  
ATOM   2586  CB  ILE B   5      60.590   2.715 -14.773  1.00 79.11           C  
ANISOU 2586  CB  ILE B   5    10318  10490   9249  -1194    266   1106       C  
ATOM   2587  CG1 ILE B   5      59.515   3.410 -13.943  1.00 79.99           C  
ANISOU 2587  CG1 ILE B   5    10304  10619   9469  -1111    176   1065       C  
ATOM   2588  CG2 ILE B   5      60.034   2.323 -16.131  1.00 76.32           C  
ANISOU 2588  CG2 ILE B   5    10034  10180   8785  -1321    238   1178       C  
ATOM   2589  CD1 ILE B   5      59.113   4.748 -14.496  1.00 75.46           C  
ANISOU 2589  CD1 ILE B   5     9660  10012   8998  -1097     34   1137       C  
ATOM   2590  N   LYS B   6      62.902   2.470 -12.685  1.00 72.33           N  
ANISOU 2590  N   LYS B   6     9471   9526   8486  -1023    423    982       N  
ATOM   2591  CA  LYS B   6      63.525   2.992 -11.474  1.00 67.70           C  
ANISOU 2591  CA  LYS B   6     8832   8885   8005   -906    415    922       C  
ATOM   2592  C   LYS B   6      63.273   4.489 -11.384  1.00 61.99           C  
ANISOU 2592  C   LYS B   6     8014   8118   7420   -841    287    945       C  
ATOM   2593  O   LYS B   6      63.418   5.208 -12.377  1.00 60.15           O  
ANISOU 2593  O   LYS B   6     7782   7855   7219   -884    227   1028       O  
ATOM   2594  CB  LYS B   6      65.031   2.725 -11.421  1.00 67.10           C  
ANISOU 2594  CB  LYS B   6     8813   8744   7940   -898    490    924       C  
ATOM   2595  CG  LYS B   6      65.418   1.295 -11.098  1.00 76.65           C  
ANISOU 2595  CG  LYS B   6    10099   9979   9045   -925    619    879       C  
ATOM   2596  CD  LYS B   6      66.910   1.195 -10.783  1.00 80.93           C  
ANISOU 2596  CD  LYS B   6    10668  10442   9638   -889    675    871       C  
ATOM   2597  CE  LYS B   6      67.310  -0.227 -10.412  1.00 81.96           C  
ANISOU 2597  CE  LYS B   6    10872  10593   9677   -910    801    828       C  
ATOM   2598  NZ  LYS B   6      67.160  -1.188 -11.546  1.00 81.43           N  
ANISOU 2598  NZ  LYS B   6    10890  10564   9486  -1032    888    871       N  
ATOM   2599  N   VAL B   7      62.843   4.942 -10.210  1.00 57.24           N  
ANISOU 2599  N   VAL B   7     7339   7515   6896   -742    249    872       N  
ATOM   2600  CA  VAL B   7      62.626   6.350  -9.928  1.00 60.62           C  
ANISOU 2600  CA  VAL B   7     7673   7894   7467   -666    136    876       C  
ATOM   2601  C   VAL B   7      63.267   6.660  -8.584  1.00 64.06           C  
ANISOU 2601  C   VAL B   7     8083   8279   7977   -554    143    791       C  
ATOM   2602  O   VAL B   7      63.750   5.769  -7.888  1.00 71.62           O  
ANISOU 2602  O   VAL B   7     9093   9248   8871   -537    227    733       O  
ATOM   2603  CB  VAL B   7      61.131   6.729  -9.923  1.00 63.80           C  
ANISOU 2603  CB  VAL B   7     7997   8346   7899   -660     65    873       C  
ATOM   2604  CG1 VAL B   7      60.496   6.418 -11.269  1.00 65.33           C  
ANISOU 2604  CG1 VAL B   7     8219   8587   8015   -774     41    960       C  
ATOM   2605  CG2 VAL B   7      60.407   6.011  -8.794  1.00 67.12           C  
ANISOU 2605  CG2 VAL B   7     8403   8821   8280   -615    126    776       C  
ATOM   2606  N   PHE B   8      63.245   7.932  -8.208  1.00 59.80           N  
ANISOU 2606  N   PHE B   8     7464   7682   7573   -478     48    782       N  
ATOM   2607  CA  PHE B   8      63.820   8.377  -6.947  1.00 61.06           C  
ANISOU 2607  CA  PHE B   8     7600   7789   7812   -370     36    699       C  
ATOM   2608  C   PHE B   8      62.737   9.064  -6.129  1.00 63.44           C  
ANISOU 2608  C   PHE B   8     7820   8101   8183   -293    -20    638       C  
ATOM   2609  O   PHE B   8      62.004   9.908  -6.653  1.00 69.19           O  
ANISOU 2609  O   PHE B   8     8477   8823   8987   -298    -99    682       O  
ATOM   2610  CB  PHE B   8      65.004   9.324  -7.188  1.00 62.47           C  
ANISOU 2610  CB  PHE B   8     7763   7869   8105   -345    -20    737       C  
ATOM   2611  CG  PHE B   8      66.167   8.685  -7.907  1.00 58.28           C  
ANISOU 2611  CG  PHE B   8     7307   7314   7525   -413     48    791       C  
ATOM   2612  CD1 PHE B   8      67.067   7.879  -7.224  1.00 57.66           C  
ANISOU 2612  CD1 PHE B   8     7282   7221   7406   -391    121    738       C  
ATOM   2613  CD2 PHE B   8      66.353   8.880  -9.270  1.00 47.85           C  
ANISOU 2613  CD2 PHE B   8     6006   5980   6196   -499     42    895       C  
ATOM   2614  CE1 PHE B   8      68.139   7.292  -7.884  1.00 48.52           C  
ANISOU 2614  CE1 PHE B   8     6184   6033   6218   -451    191    786       C  
ATOM   2615  CE2 PHE B   8      67.412   8.291  -9.934  1.00 39.04           C  
ANISOU 2615  CE2 PHE B   8     4961   4837   5038   -562    119    941       C  
ATOM   2616  CZ  PHE B   8      68.311   7.496  -9.238  1.00 39.95           C  
ANISOU 2616  CZ  PHE B   8     5118   4935   5128   -537    196    886       C  
ATOM   2617  N   THR B   9      62.638   8.705  -4.853  1.00 60.12           N  
ANISOU 2617  N   THR B   9     7411   7692   7738   -222     23    538       N  
ATOM   2618  CA  THR B   9      61.725   9.350  -3.921  1.00 57.26           C  
ANISOU 2618  CA  THR B   9     6981   7330   7444   -139    -12    465       C  
ATOM   2619  C   THR B   9      62.515  10.205  -2.942  1.00 52.18           C  
ANISOU 2619  C   THR B   9     6325   6604   6896    -39    -61    400       C  
ATOM   2620  O   THR B   9      63.671   9.906  -2.629  1.00 54.43           O  
ANISOU 2620  O   THR B   9     6668   6852   7161    -26    -42    384       O  
ATOM   2621  CB  THR B   9      60.900   8.327  -3.137  1.00 54.99           C  
ANISOU 2621  CB  THR B   9     6724   7117   7052   -131     80    393       C  
ATOM   2622  OG1 THR B   9      61.778   7.458  -2.409  1.00 54.02           O  
ANISOU 2622  OG1 THR B   9     6691   6992   6841   -113    154    343       O  
ATOM   2623  CG2 THR B   9      60.052   7.504  -4.085  1.00 50.24           C  
ANISOU 2623  CG2 THR B   9     6127   6594   6367   -232    121    452       C  
ATOM   2624  N   THR B  10      61.881  11.262  -2.444  1.00 46.61           N  
ANISOU 2624  N   THR B  10     5542   5867   6302     32   -126    359       N  
ATOM   2625  CA  THR B  10      62.577  12.162  -1.537  1.00 46.95           C  
ANISOU 2625  CA  THR B  10     5572   5826   6442    126   -182    293       C  
ATOM   2626  C   THR B  10      61.562  12.930  -0.706  1.00 56.06           C  
ANISOU 2626  C   THR B  10     6660   6970   7672    206   -208    217       C  
ATOM   2627  O   THR B  10      60.377  12.993  -1.039  1.00 62.04           O  
ANISOU 2627  O   THR B  10     7357   7770   8444    187   -203    236       O  
ATOM   2628  CB  THR B  10      63.493  13.133  -2.296  1.00 45.48           C  
ANISOU 2628  CB  THR B  10     5351   5556   6374    116   -269    365       C  
ATOM   2629  OG1 THR B  10      64.330  13.827  -1.368  1.00 54.06           O  
ANISOU 2629  OG1 THR B  10     6437   6560   7543    200   -318    294       O  
ATOM   2630  CG2 THR B  10      62.674  14.153  -3.078  1.00 45.58           C  
ANISOU 2630  CG2 THR B  10     5269   5552   6497    104   -347    429       C  
ATOM   2631  N   VAL B  11      62.042  13.491   0.401  1.00 64.41           N  
ANISOU 2631  N   VAL B  11     7728   7966   8778    297   -235    127       N  
ATOM   2632  CA  VAL B  11      61.260  14.431   1.196  1.00 70.77           C  
ANISOU 2632  CA  VAL B  11     8471   8738   9679    381   -266     50       C  
ATOM   2633  C   VAL B  11      61.914  15.799   1.280  1.00 77.20           C  
ANISOU 2633  C   VAL B  11     9236   9447  10650    437   -374     42       C  
ATOM   2634  O   VAL B  11      61.281  16.741   1.780  1.00 81.92           O  
ANISOU 2634  O   VAL B  11     9770  10004  11352    503   -410    -12       O  
ATOM   2635  CB  VAL B  11      60.987  13.892   2.618  1.00 67.04           C  
ANISOU 2635  CB  VAL B  11     8066   8290   9115    446   -190    -73       C  
ATOM   2636  CG1 VAL B  11      60.249  12.568   2.552  1.00 71.30           C  
ANISOU 2636  CG1 VAL B  11     8648   8930   9512    391    -78    -65       C  
ATOM   2637  CG2 VAL B  11      62.279  13.750   3.389  1.00 58.00           C  
ANISOU 2637  CG2 VAL B  11     7009   7098   7932    486   -207   -126       C  
ATOM   2638  N   ASP B  12      63.153  15.937   0.812  1.00 77.35           N  
ANISOU 2638  N   ASP B  12     9278   9415  10697    412   -420     93       N  
ATOM   2639  CA  ASP B  12      63.907  17.173   0.914  1.00 77.55           C  
ANISOU 2639  CA  ASP B  12     9259   9333  10873    461   -519     85       C  
ATOM   2640  C   ASP B  12      64.593  17.568  -0.387  1.00 76.51           C  
ANISOU 2640  C   ASP B  12     9093   9160  10816    395   -571    207       C  
ATOM   2641  O   ASP B  12      65.251  18.614  -0.425  1.00 72.31           O  
ANISOU 2641  O   ASP B  12     8519   8533  10422    428   -653    214       O  
ATOM   2642  CB  ASP B  12      64.958  17.057   2.029  1.00 76.46           C  
ANISOU 2642  CB  ASP B  12     9192   9146  10711    521   -529     -8       C  
ATOM   2643  CG  ASP B  12      65.814  15.808   1.900  1.00 81.32           C  
ANISOU 2643  CG  ASP B  12     9897   9803  11199    468   -469     18       C  
ATOM   2644  OD1 ASP B  12      67.013  15.866   2.236  1.00 83.91           O  
ANISOU 2644  OD1 ASP B  12    10257  10068  11554    488   -508     -1       O  
ATOM   2645  OD2 ASP B  12      65.298  14.775   1.424  1.00 88.08           O  
ANISOU 2645  OD2 ASP B  12    10784  10747  11937    405   -387     62       O  
ATOM   2646  N   ASN B  13      64.469  16.761  -1.443  1.00 76.71           N  
ANISOU 2646  N   ASN B  13     9142   9251  10755    302   -523    303       N  
ATOM   2647  CA  ASN B  13      65.155  16.973  -2.718  1.00 79.04           C  
ANISOU 2647  CA  ASN B  13     9426   9512  11091    229   -552    423       C  
ATOM   2648  C   ASN B  13      66.674  17.000  -2.551  1.00 73.58           C  
ANISOU 2648  C   ASN B  13     8772   8747  10436    237   -563    417       C  
ATOM   2649  O   ASN B  13      67.391  17.509  -3.416  1.00 76.87           O  
ANISOU 2649  O   ASN B  13     9167   9104  10934    199   -599    501       O  
ATOM   2650  CB  ASN B  13      64.673  18.252  -3.416  1.00 88.09           C  
ANISOU 2650  CB  ASN B  13    10480  10605  12384    233   -641    489       C  
ATOM   2651  CG  ASN B  13      64.943  18.241  -4.917  1.00 92.49           C  
ANISOU 2651  CG  ASN B  13    11040  11162  12938    137   -651    630       C  
ATOM   2652  OD1 ASN B  13      65.171  17.187  -5.515  1.00 92.28           O  
ANISOU 2652  OD1 ASN B  13    11082  11195  12783     59   -580    678       O  
ATOM   2653  ND2 ASN B  13      64.927  19.422  -5.527  1.00 91.41           N  
ANISOU 2653  ND2 ASN B  13    10836  10953  12941    142   -736    696       N  
ATOM   2654  N   ILE B  14      67.187  16.465  -1.446  1.00 64.43           N  
ANISOU 2654  N   ILE B  14     7670   7589   9223    286   -535    322       N  
ATOM   2655  CA  ILE B  14      68.621  16.337  -1.221  1.00 64.67           C  
ANISOU 2655  CA  ILE B  14     7735   7553   9283    293   -546    313       C  
ATOM   2656  C   ILE B  14      69.039  14.875  -1.148  1.00 61.45           C  
ANISOU 2656  C   ILE B  14     7416   7208   8724    249   -452    311       C  
ATOM   2657  O   ILE B  14      70.022  14.465  -1.776  1.00 60.80           O  
ANISOU 2657  O   ILE B  14     7357   7100   8643    197   -424    373       O  
ATOM   2658  CB  ILE B  14      69.057  17.090   0.054  1.00 64.90           C  
ANISOU 2658  CB  ILE B  14     7753   7505   9401    394   -621    201       C  
ATOM   2659  CG1 ILE B  14      68.715  18.572  -0.068  1.00 69.65           C  
ANISOU 2659  CG1 ILE B  14     8263   8033  10168    435   -712    204       C  
ATOM   2660  CG2 ILE B  14      70.539  16.926   0.287  1.00 54.34           C  
ANISOU 2660  CG2 ILE B  14     6445   6098   8105    399   -642    193       C  
ATOM   2661  CD1 ILE B  14      68.798  19.308   1.243  1.00 72.48           C  
ANISOU 2661  CD1 ILE B  14     8615   8330  10596    536   -778     79       C  
ATOM   2662  N   ASN B  15      68.296  14.069  -0.390  1.00 59.06           N  
ANISOU 2662  N   ASN B  15     7162   6984   8294    270   -394    243       N  
ATOM   2663  CA  ASN B  15      68.545  12.638  -0.256  1.00 60.26           C  
ANISOU 2663  CA  ASN B  15     7400   7201   8297    231   -299    239       C  
ATOM   2664  C   ASN B  15      67.564  11.891  -1.153  1.00 66.96           C  
ANISOU 2664  C   ASN B  15     8258   8145   9040    149   -222    303       C  
ATOM   2665  O   ASN B  15      66.357  11.879  -0.887  1.00 68.04           O  
ANISOU 2665  O   ASN B  15     8377   8339   9136    163   -206    272       O  
ATOM   2666  CB  ASN B  15      68.398  12.188   1.195  1.00 62.04           C  
ANISOU 2666  CB  ASN B  15     7683   7445   8443    306   -282    123       C  
ATOM   2667  CG  ASN B  15      69.498  12.730   2.098  1.00 68.40           C  
ANISOU 2667  CG  ASN B  15     8498   8158   9331    379   -362     58       C  
ATOM   2668  OD1 ASN B  15      70.094  13.771   1.822  1.00 65.46           O  
ANISOU 2668  OD1 ASN B  15     8066   7700   9106    395   -446     78       O  
ATOM   2669  ND2 ASN B  15      69.782  12.008   3.177  1.00 74.61           N  
ANISOU 2669  ND2 ASN B  15     9366   8959  10025    421   -339    -19       N  
ATOM   2670  N   LEU B  16      68.083  11.264  -2.205  1.00 63.43           N  
ANISOU 2670  N   LEU B  16     7839   7710   8552     63   -172    391       N  
ATOM   2671  CA  LEU B  16      67.270  10.490  -3.130  1.00 56.75           C  
ANISOU 2671  CA  LEU B  16     7014   6951   7599    -25   -103    454       C  
ATOM   2672  C   LEU B  16      67.356   9.011  -2.776  1.00 54.29           C  
ANISOU 2672  C   LEU B  16     6788   6703   7137    -53      3    424       C  
ATOM   2673  O   LEU B  16      68.422   8.512  -2.408  1.00 57.70           O  
ANISOU 2673  O   LEU B  16     7266   7099   7557    -41     29    406       O  
ATOM   2674  CB  LEU B  16      67.734  10.711  -4.569  1.00 57.50           C  
ANISOU 2674  CB  LEU B  16     7100   7020   7729   -110   -107    569       C  
ATOM   2675  CG  LEU B  16      67.798  12.168  -5.031  1.00 57.89           C  
ANISOU 2675  CG  LEU B  16     7069   6994   7932    -89   -209    615       C  
ATOM   2676  CD1 LEU B  16      67.995  12.223  -6.534  1.00 60.38           C  
ANISOU 2676  CD1 LEU B  16     7394   7304   8244   -186   -197    737       C  
ATOM   2677  CD2 LEU B  16      66.559  12.953  -4.610  1.00 54.07           C  
ANISOU 2677  CD2 LEU B  16     6518   6530   7498    -36   -273    577       C  
ATOM   2678  N   HIS B  17      66.241   8.304  -2.929  1.00 57.91           N  
ANISOU 2678  N   HIS B  17     7263   7251   7490    -93     62    424       N  
ATOM   2679  CA  HIS B  17      66.147   6.891  -2.576  1.00 55.38           C  
ANISOU 2679  CA  HIS B  17     7021   6995   7026   -120    166    394       C  
ATOM   2680  C   HIS B  17      65.649   6.130  -3.793  1.00 60.96           C  
ANISOU 2680  C   HIS B  17     7749   7766   7645   -231    229    471       C  
ATOM   2681  O   HIS B  17      64.511   6.334  -4.232  1.00 65.79           O  
ANISOU 2681  O   HIS B  17     8321   8428   8250   -260    212    492       O  
ATOM   2682  CB  HIS B  17      65.211   6.683  -1.386  1.00 58.20           C  
ANISOU 2682  CB  HIS B  17     7383   7397   7333    -55    189    301       C  
ATOM   2683  CG  HIS B  17      65.552   7.534  -0.202  1.00 63.08           C  
ANISOU 2683  CG  HIS B  17     7985   7952   8031     53    121    220       C  
ATOM   2684  ND1 HIS B  17      66.655   7.299   0.589  1.00 62.27           N  
ANISOU 2684  ND1 HIS B  17     7937   7801   7923    100    115    176       N  
ATOM   2685  CD2 HIS B  17      64.930   8.614   0.329  1.00 64.14           C  
ANISOU 2685  CD2 HIS B  17     8057   8062   8252    121     54    172       C  
ATOM   2686  CE1 HIS B  17      66.706   8.204   1.550  1.00 62.19           C  
ANISOU 2686  CE1 HIS B  17     7904   7739   7985    191     42    103       C  
ATOM   2687  NE2 HIS B  17      65.668   9.011   1.417  1.00 64.24           N  
ANISOU 2687  NE2 HIS B  17     8094   8012   8301    206     10     97       N  
ATOM   2688  N   THR B  18      66.498   5.259  -4.334  1.00 59.57           N  
ANISOU 2688  N   THR B  18     7639   7587   7409   -292    298    511       N  
ATOM   2689  CA  THR B  18      66.130   4.497  -5.519  1.00 56.20           C  
ANISOU 2689  CA  THR B  18     7248   7215   6890   -403    361    581       C  
ATOM   2690  C   THR B  18      64.972   3.567  -5.204  1.00 55.26           C  
ANISOU 2690  C   THR B  18     7152   7187   6658   -425    425    542       C  
ATOM   2691  O   THR B  18      65.008   2.816  -4.225  1.00 62.23           O  
ANISOU 2691  O   THR B  18     8075   8089   7480   -385    484    476       O  
ATOM   2692  CB  THR B  18      67.319   3.687  -6.024  1.00 56.31           C  
ANISOU 2692  CB  THR B  18     7331   7199   6864   -456    438    618       C  
ATOM   2693  OG1 THR B  18      68.404   4.567  -6.335  1.00 58.87           O  
ANISOU 2693  OG1 THR B  18     7628   7433   7308   -438    385    656       O  
ATOM   2694  CG2 THR B  18      66.926   2.927  -7.278  1.00 58.51           C  
ANISOU 2694  CG2 THR B  18     7657   7532   7041   -574    505    685       C  
ATOM   2695  N   GLN B  19      63.943   3.617  -6.037  1.00 56.01           N  
ANISOU 2695  N   GLN B  19     7220   7335   6727   -490    410    587       N  
ATOM   2696  CA  GLN B  19      62.783   2.748  -5.913  1.00 65.31           C  
ANISOU 2696  CA  GLN B  19     8409   8597   7809   -525    467    560       C  
ATOM   2697  C   GLN B  19      62.470   2.115  -7.259  1.00 63.51           C  
ANISOU 2697  C   GLN B  19     8218   8415   7500   -648    498    634       C  
ATOM   2698  O   GLN B  19      62.630   2.746  -8.308  1.00 67.97           O  
ANISOU 2698  O   GLN B  19     8770   8956   8101   -695    439    710       O  
ATOM   2699  CB  GLN B  19      61.554   3.519  -5.405  1.00 74.32           C  
ANISOU 2699  CB  GLN B  19     9462   9760   9017   -471    404    523       C  
ATOM   2700  CG  GLN B  19      61.757   4.278  -4.098  1.00 71.85           C  
ANISOU 2700  CG  GLN B  19     9114   9399   8787   -350    367    445       C  
ATOM   2701  CD  GLN B  19      61.851   3.363  -2.904  1.00 72.61           C  
ANISOU 2701  CD  GLN B  19     9272   9517   8802   -304    456    363       C  
ATOM   2702  OE1 GLN B  19      61.483   2.194  -2.975  1.00 73.72           O  
ANISOU 2702  OE1 GLN B  19     9461   9715   8833   -358    547    358       O  
ATOM   2703  NE2 GLN B  19      62.342   3.892  -1.791  1.00 78.94           N  
ANISOU 2703  NE2 GLN B  19    10073  10267   9652   -206    427    297       N  
ATOM   2704  N   VAL B  20      62.028   0.864  -7.229  1.00 63.74           N  
ANISOU 2704  N   VAL B  20     8300   8505   7414   -700    592    612       N  
ATOM   2705  CA  VAL B  20      61.546   0.179  -8.423  1.00 71.20           C  
ANISOU 2705  CA  VAL B  20     9283   9500   8270   -819    621    669       C  
ATOM   2706  C   VAL B  20      60.026   0.114  -8.331  1.00 73.59           C  
ANISOU 2706  C   VAL B  20     9526   9869   8565   -833    596    649       C  
ATOM   2707  O   VAL B  20      59.482  -0.428  -7.360  1.00 82.19           O  
ANISOU 2707  O   VAL B  20    10607  10991   9631   -793    653    579       O  
ATOM   2708  CB  VAL B  20      62.154  -1.222  -8.558  1.00 69.59           C  
ANISOU 2708  CB  VAL B  20     9180   9312   7950   -878    747    661       C  
ATOM   2709  CG1 VAL B  20      61.703  -1.847  -9.857  1.00 75.05           C  
ANISOU 2709  CG1 VAL B  20     9919  10049   8550  -1005    770    718       C  
ATOM   2710  CG2 VAL B  20      63.671  -1.149  -8.489  1.00 67.82           C  
ANISOU 2710  CG2 VAL B  20     8999   9013   7756   -851    775    673       C  
ATOM   2711  N   VAL B  21      59.337   0.678  -9.323  1.00 66.51           N  
ANISOU 2711  N   VAL B  21     8587   8989   7693   -889    510    712       N  
ATOM   2712  CA  VAL B  21      57.885   0.830  -9.278  1.00 71.94           C  
ANISOU 2712  CA  VAL B  21     9196   9728   8411   -896    462    700       C  
ATOM   2713  C   VAL B  21      57.245  -0.058 -10.337  1.00 77.76           C  
ANISOU 2713  C   VAL B  21     9974  10524   9046  -1021    481    742       C  
ATOM   2714  O   VAL B  21      57.845  -0.369 -11.371  1.00 79.18           O  
ANISOU 2714  O   VAL B  21    10233  10698   9152  -1105    491    801       O  
ATOM   2715  CB  VAL B  21      57.444   2.298  -9.470  1.00 66.43           C  
ANISOU 2715  CB  VAL B  21     8396   8997   7848   -850    327    736       C  
ATOM   2716  CG1 VAL B  21      58.109   3.183  -8.451  1.00 69.70           C  
ANISOU 2716  CG1 VAL B  21     8775   9346   8362   -731    306    690       C  
ATOM   2717  CG2 VAL B  21      57.757   2.776 -10.867  1.00 60.93           C  
ANISOU 2717  CG2 VAL B  21     7725   8280   7144   -927    249    838       C  
ATOM   2718  N   ASP B  22      56.003  -0.469 -10.065  1.00 79.29           N  
ANISOU 2718  N   ASP B  22    10115  10774   9238  -1035    488    708       N  
ATOM   2719  CA  ASP B  22      55.229  -1.285 -10.992  1.00 86.19           C  
ANISOU 2719  CA  ASP B  22    11015  11705  10029  -1152    492    739       C  
ATOM   2720  C   ASP B  22      54.375  -0.382 -11.874  1.00 87.71           C  
ANISOU 2720  C   ASP B  22    11130  11903  10291  -1186    346    806       C  
ATOM   2721  O   ASP B  22      53.596   0.434 -11.371  1.00 90.38           O  
ANISOU 2721  O   ASP B  22    11355  12236  10750  -1119    276    789       O  
ATOM   2722  CB  ASP B  22      54.355  -2.278 -10.225  1.00 90.64           C  
ANISOU 2722  CB  ASP B  22    11558  12319  10560  -1153    582    667       C  
ATOM   2723  CG  ASP B  22      53.590  -3.229 -11.140  1.00 94.15           C  
ANISOU 2723  CG  ASP B  22    12033  12822  10919  -1278    591    690       C  
ATOM   2724  OD1 ASP B  22      53.999  -3.415 -12.309  1.00 96.11           O  
ANISOU 2724  OD1 ASP B  22    12357  13070  11089  -1370    564    753       O  
ATOM   2725  OD2 ASP B  22      52.584  -3.806 -10.677  1.00 93.65           O  
ANISOU 2725  OD2 ASP B  22    11921  12799  10864  -1286    631    644       O  
ATOM   2726  N   MET B  23      54.512  -0.539 -13.186  1.00 87.16           N  
ANISOU 2726  N   MET B  23    11128  11845  10146  -1292    302    882       N  
ATOM   2727  CA  MET B  23      53.802   0.330 -14.115  1.00 92.09           C  
ANISOU 2727  CA  MET B  23    11695  12470  10826  -1330    151    958       C  
ATOM   2728  C   MET B  23      52.314   0.019 -14.200  1.00 95.50           C  
ANISOU 2728  C   MET B  23    12045  12956  11284  -1370    101    945       C  
ATOM   2729  O   MET B  23      51.591   0.748 -14.887  1.00 98.15           O  
ANISOU 2729  O   MET B  23    12317  13293  11684  -1395    -36   1007       O  
ATOM   2730  CB  MET B  23      54.435   0.219 -15.502  1.00 93.30           C  
ANISOU 2730  CB  MET B  23    11963  12615  10873  -1435    124   1043       C  
ATOM   2731  CG  MET B  23      55.925   0.499 -15.509  1.00 95.12           C  
ANISOU 2731  CG  MET B  23    12270  12784  11086  -1404    181   1061       C  
ATOM   2732  SD  MET B  23      56.414   1.643 -16.801  1.00103.98           S  
ANISOU 2732  SD  MET B  23    13427  13856  12225  -1444     61   1181       S  
ATOM   2733  CE  MET B  23      56.416   0.568 -18.233  1.00103.08           C  
ANISOU 2733  CE  MET B  23    13462  13784  11919  -1609     95   1232       C  
ATOM   2734  N   SER B  24      51.835  -1.026 -13.525  1.00 96.91           N  
ANISOU 2734  N   SER B  24    12219  13176  11425  -1377    205    871       N  
ATOM   2735  CA  SER B  24      50.420  -1.372 -13.555  1.00102.67           C  
ANISOU 2735  CA  SER B  24    12863  13954  12194  -1415    168    854       C  
ATOM   2736  C   SER B  24      49.637  -0.809 -12.378  1.00108.16           C  
ANISOU 2736  C   SER B  24    13418  14640  13038  -1306    169    794       C  
ATOM   2737  O   SER B  24      48.416  -0.663 -12.483  1.00110.74           O  
ANISOU 2737  O   SER B  24    13638  14989  13450  -1322    100    797       O  
ATOM   2738  CB  SER B  24      50.241  -2.895 -13.588  1.00104.28           C  
ANISOU 2738  CB  SER B  24    13142  14208  12273  -1499    286    811       C  
ATOM   2739  OG  SER B  24      50.756  -3.493 -12.413  1.00106.32           O  
ANISOU 2739  OG  SER B  24    13429  14460  12509  -1431    435    732       O  
ATOM   2740  N   MET B  25      50.301  -0.497 -11.270  1.00109.71           N  
ANISOU 2740  N   MET B  25    13614  14801  13272  -1198    244    739       N  
ATOM   2741  CA  MET B  25      49.669   0.111 -10.109  1.00109.93           C  
ANISOU 2741  CA  MET B  25    13524  14811  13434  -1088    254    676       C  
ATOM   2742  C   MET B  25      49.892   1.617 -10.125  1.00110.73           C  
ANISOU 2742  C   MET B  25    13556  14854  13661  -1009    138    712       C  
ATOM   2743  O   MET B  25      50.794   2.125 -10.790  1.00112.81           O  
ANISOU 2743  O   MET B  25    13879  15086  13899  -1023     80    774       O  
ATOM   2744  CB  MET B  25      50.233  -0.479  -8.816  1.00110.46           C  
ANISOU 2744  CB  MET B  25    13643  14872  13455  -1015    406    588       C  
ATOM   2745  CG  MET B  25      50.172  -1.990  -8.739  1.00112.26           C  
ANISOU 2745  CG  MET B  25    13952  15147  13554  -1086    533    553       C  
ATOM   2746  SD  MET B  25      51.184  -2.627  -7.390  1.00111.79           S  
ANISOU 2746  SD  MET B  25    13986  15069  13420  -1005    692    472       S  
ATOM   2747  CE  MET B  25      50.406  -1.841  -5.982  1.00115.07           C  
ANISOU 2747  CE  MET B  25    14288  15463  13972   -875    709    396       C  
ATOM   2748  N   THR B  26      49.049   2.331  -9.387  1.00111.87           N  
ANISOU 2748  N   THR B  26    13574  14981  13951   -928    111    673       N  
ATOM   2749  CA  THR B  26      49.224   3.769  -9.273  1.00112.89           C  
ANISOU 2749  CA  THR B  26    13631  15049  14213   -844     10    697       C  
ATOM   2750  C   THR B  26      50.322   4.091  -8.257  1.00108.10           C  
ANISOU 2750  C   THR B  26    13077  14396  13600   -745     83    638       C  
ATOM   2751  O   THR B  26      50.761   3.239  -7.477  1.00106.12           O  
ANISOU 2751  O   THR B  26    12900  14161  13259   -727    210    572       O  
ATOM   2752  CB  THR B  26      47.912   4.445  -8.873  1.00117.97           C  
ANISOU 2752  CB  THR B  26    14115  15683  15027   -791    -43    675       C  
ATOM   2753  OG1 THR B  26      47.626   4.174  -7.495  1.00119.91           O  
ANISOU 2753  OG1 THR B  26    14332  15928  15301   -709     83    569       O  
ATOM   2754  CG2 THR B  26      46.771   3.922  -9.725  1.00121.68           C  
ANISOU 2754  CG2 THR B  26    14529  16202  15503   -891   -102    718       C  
ATOM   2755  N   TYR B  27      50.777   5.348  -8.282  1.00102.30           N  
ANISOU 2755  N   TYR B  27    12304  13598  12965   -680     -7    666       N  
ATOM   2756  CA  TYR B  27      51.778   5.786  -7.316  1.00 93.44           C  
ANISOU 2756  CA  TYR B  27    11221  12425  11858   -583     40    609       C  
ATOM   2757  C   TYR B  27      51.234   5.755  -5.895  1.00 98.93           C  
ANISOU 2757  C   TYR B  27    11867  13117  12604   -489    126    501       C  
ATOM   2758  O   TYR B  27      51.981   5.467  -4.952  1.00100.49           O  
ANISOU 2758  O   TYR B  27    12136  13301  12746   -433    213    434       O  
ATOM   2759  CB  TYR B  27      52.274   7.191  -7.664  1.00 86.85           C  
ANISOU 2759  CB  TYR B  27    10344  11519  11136   -536    -80    661       C  
ATOM   2760  CG  TYR B  27      53.256   7.223  -8.813  1.00 84.93           C  
ANISOU 2760  CG  TYR B  27    10186  11261  10821   -609   -131    754       C  
ATOM   2761  CD1 TYR B  27      52.858   7.624 -10.082  1.00 86.86           C  
ANISOU 2761  CD1 TYR B  27    10406  11510  11088   -683   -244    857       C  
ATOM   2762  CD2 TYR B  27      54.580   6.845  -8.632  1.00 81.30           C  
ANISOU 2762  CD2 TYR B  27     9834  10781  10276   -606    -62    741       C  
ATOM   2763  CE1 TYR B  27      53.753   7.649 -11.136  1.00 87.82           C  
ANISOU 2763  CE1 TYR B  27    10617  11615  11137   -752   -278    942       C  
ATOM   2764  CE2 TYR B  27      55.481   6.867  -9.681  1.00 79.98           C  
ANISOU 2764  CE2 TYR B  27     9744  10595  10051   -674    -93    825       C  
ATOM   2765  CZ  TYR B  27      55.061   7.270 -10.930  1.00 86.09           C  
ANISOU 2765  CZ  TYR B  27    10499  11373  10837   -748   -195    924       C  
ATOM   2766  OH  TYR B  27      55.949   7.296 -11.981  1.00 90.64           O  
ANISOU 2766  OH  TYR B  27    11162  11928  11349   -817   -214   1008       O  
ATOM   2767  N   GLY B  28      49.941   6.040  -5.722  1.00100.31           N  
ANISOU 2767  N   GLY B  28    11923  13303  12886   -472    105    483       N  
ATOM   2768  CA  GLY B  28      49.353   5.993  -4.395  1.00102.89           C  
ANISOU 2768  CA  GLY B  28    12206  13625  13261   -388    202    380       C  
ATOM   2769  C   GLY B  28      49.345   4.601  -3.801  1.00106.07           C  
ANISOU 2769  C   GLY B  28    12694  14081  13526   -416    351    322       C  
ATOM   2770  O   GLY B  28      49.505   4.437  -2.588  1.00107.28           O  
ANISOU 2770  O   GLY B  28    12882  14222  13657   -341    451    235       O  
ATOM   2771  N   GLN B  29      49.159   3.581  -4.640  1.00107.39           N  
ANISOU 2771  N   GLN B  29    12901  14305  13596   -526    366    369       N  
ATOM   2772  CA  GLN B  29      49.176   2.207  -4.162  1.00108.22           C  
ANISOU 2772  CA  GLN B  29    13090  14458  13572   -561    508    321       C  
ATOM   2773  C   GLN B  29      50.571   1.741  -3.773  1.00103.38           C  
ANISOU 2773  C   GLN B  29    12616  13831  12831   -543    572    302       C  
ATOM   2774  O   GLN B  29      50.700   0.677  -3.157  1.00103.98           O  
ANISOU 2774  O   GLN B  29    12769  13936  12805   -550    696    254       O  
ATOM   2775  CB  GLN B  29      48.592   1.276  -5.226  1.00111.57           C  
ANISOU 2775  CB  GLN B  29    13517  14941  13935   -688    499    375       C  
ATOM   2776  CG  GLN B  29      47.147   1.582  -5.597  1.00116.28           C  
ANISOU 2776  CG  GLN B  29    13971  15554  14658   -714    435    393       C  
ATOM   2777  CD  GLN B  29      46.624   0.678  -6.700  1.00118.52           C  
ANISOU 2777  CD  GLN B  29    14265  15892  14877   -845    408    447       C  
ATOM   2778  OE1 GLN B  29      47.167  -0.400  -6.944  1.00119.35           O  
ANISOU 2778  OE1 GLN B  29    14483  16030  14835   -913    481    449       O  
ATOM   2779  NE2 GLN B  29      45.563   1.114  -7.370  1.00118.25           N  
ANISOU 2779  NE2 GLN B  29    14111  15865  14956   -882    299    491       N  
ATOM   2780  N   GLN B  30      51.608   2.504  -4.106  1.00 99.84           N  
ANISOU 2780  N   GLN B  30    12200  13337  12398   -519    492    340       N  
ATOM   2781  CA  GLN B  30      52.985   2.120  -3.823  1.00 96.17           C  
ANISOU 2781  CA  GLN B  30    11857  12851  11833   -504    539    330       C  
ATOM   2782  C   GLN B  30      53.701   3.068  -2.873  1.00 87.43           C  
ANISOU 2782  C   GLN B  30    10751  11678  10789   -389    516    281       C  
ATOM   2783  O   GLN B  30      54.477   2.616  -2.027  1.00 81.43           O  
ANISOU 2783  O   GLN B  30    10077  10906   9957   -345    589    229       O  
ATOM   2784  CB  GLN B  30      53.771   2.025  -5.138  1.00 93.74           C  
ANISOU 2784  CB  GLN B  30    11603  12541  11472   -591    478    422       C  
ATOM   2785  CG  GLN B  30      53.122   1.123  -6.168  1.00 89.78           C  
ANISOU 2785  CG  GLN B  30    11112  12100  10899   -713    489    472       C  
ATOM   2786  CD  GLN B  30      53.934   1.010  -7.439  1.00 89.06           C  
ANISOU 2786  CD  GLN B  30    11093  12004  10741   -799    442    557       C  
ATOM   2787  OE1 GLN B  30      55.018   0.434  -7.445  1.00 92.08           O  
ANISOU 2787  OE1 GLN B  30    11576  12374  11035   -814    506    558       O  
ATOM   2788  NE2 GLN B  30      53.410   1.558  -8.526  1.00 90.99           N  
ANISOU 2788  NE2 GLN B  30    11287  12254  11031   -858    331    632       N  
ATOM   2789  N   PHE B  31      53.467   4.375  -2.987  1.00 87.19           N  
ANISOU 2789  N   PHE B  31    10629  11603  10896   -339    411    296       N  
ATOM   2790  CA  PHE B  31      54.137   5.352  -2.141  1.00 88.62           C  
ANISOU 2790  CA  PHE B  31    10808  11716  11146   -233    378    248       C  
ATOM   2791  C   PHE B  31      53.210   6.107  -1.205  1.00 93.72           C  
ANISOU 2791  C   PHE B  31    11366  12340  11905   -143    381    175       C  
ATOM   2792  O   PHE B  31      53.684   6.645  -0.199  1.00 91.91           O  
ANISOU 2792  O   PHE B  31    11158  12062  11701    -50    390    106       O  
ATOM   2793  CB  PHE B  31      54.879   6.383  -3.003  1.00 83.44           C  
ANISOU 2793  CB  PHE B  31    10130  11006  10568   -239    253    322       C  
ATOM   2794  CG  PHE B  31      55.976   5.800  -3.840  1.00 76.94           C  
ANISOU 2794  CG  PHE B  31     9400  10187   9648   -313    256    388       C  
ATOM   2795  CD1 PHE B  31      56.651   4.662  -3.426  1.00 75.96           C  
ANISOU 2795  CD1 PHE B  31     9381  10085   9396   -330    359    356       C  
ATOM   2796  CD2 PHE B  31      56.348   6.399  -5.030  1.00 69.59           C  
ANISOU 2796  CD2 PHE B  31     8452   9230   8758   -365    161    482       C  
ATOM   2797  CE1 PHE B  31      57.664   4.126  -4.190  1.00 70.10           C  
ANISOU 2797  CE1 PHE B  31     8720   9340   8577   -397    371    413       C  
ATOM   2798  CE2 PHE B  31      57.363   5.869  -5.796  1.00 67.86           C  
ANISOU 2798  CE2 PHE B  31     8321   9009   8453   -434    178    539       C  
ATOM   2799  CZ  PHE B  31      58.022   4.732  -5.374  1.00 68.96           C  
ANISOU 2799  CZ  PHE B  31     8558   9169   8473   -449    285    503       C  
ATOM   2800  N   GLY B  32      51.915   6.153  -1.498  1.00100.96           N  
ANISOU 2800  N   GLY B  32    12184  13287  12890   -169    376    186       N  
ATOM   2801  CA  GLY B  32      51.029   7.078  -0.837  1.00109.46           C  
ANISOU 2801  CA  GLY B  32    13153  14329  14107    -88    361    133       C  
ATOM   2802  C   GLY B  32      50.951   8.370  -1.624  1.00116.34           C  
ANISOU 2802  C   GLY B  32    13928  15151  15126    -78    215    199       C  
ATOM   2803  O   GLY B  32      51.130   8.383  -2.847  1.00115.86           O  
ANISOU 2803  O   GLY B  32    13862  15102  15057   -157    131    296       O  
ATOM   2804  N   PRO B  33      50.671   9.481  -0.943  1.00122.61           N  
ANISOU 2804  N   PRO B  33    14648  15884  16054     17    185    147       N  
ATOM   2805  CA  PRO B  33      50.643  10.783  -1.629  1.00123.37           C  
ANISOU 2805  CA  PRO B  33    14652  15922  16301     35     44    209       C  
ATOM   2806  C   PRO B  33      51.992  11.091  -2.262  1.00121.56           C  
ANISOU 2806  C   PRO B  33    14497  15661  16031     12    -32    273       C  
ATOM   2807  O   PRO B  33      53.018  11.163  -1.579  1.00124.72           O  
ANISOU 2807  O   PRO B  33    14977  16026  16385     62     -5    223       O  
ATOM   2808  CB  PRO B  33      50.302  11.768  -0.505  1.00124.69           C  
ANISOU 2808  CB  PRO B  33    14757  16025  16595    153     59    116       C  
ATOM   2809  CG  PRO B  33      49.640  10.934   0.545  1.00126.06           C  
ANISOU 2809  CG  PRO B  33    14954  16238  16706    178    206     20       C  
ATOM   2810  CD  PRO B  33      50.315   9.597   0.481  1.00124.44           C  
ANISOU 2810  CD  PRO B  33    14881  16095  16307    112    282     29       C  
ATOM   2811  N   THR B  34      51.984  11.260  -3.584  1.00114.31           N  
ANISOU 2811  N   THR B  34    13552  14750  15130    -66   -129    385       N  
ATOM   2812  CA  THR B  34      53.196  11.452  -4.366  1.00109.27           C  
ANISOU 2812  CA  THR B  34    12985  14085  14448   -106   -190    460       C  
ATOM   2813  C   THR B  34      53.069  12.706  -5.220  1.00109.30           C  
ANISOU 2813  C   THR B  34    12904  14032  14593   -104   -331    545       C  
ATOM   2814  O   THR B  34      52.021  12.953  -5.825  1.00109.28           O  
ANISOU 2814  O   THR B  34    12811  14045  14665   -134   -393    596       O  
ATOM   2815  CB  THR B  34      53.472  10.239  -5.269  1.00107.12           C  
ANISOU 2815  CB  THR B  34    12802  13881  14018   -222   -153    523       C  
ATOM   2816  OG1 THR B  34      53.487   9.045  -4.479  1.00107.03           O  
ANISOU 2816  OG1 THR B  34    12862  13920  13882   -224    -21    447       O  
ATOM   2817  CG2 THR B  34      54.811  10.386  -5.973  1.00107.31           C  
ANISOU 2817  CG2 THR B  34    12908  13871  13995   -258   -191    590       C  
ATOM   2818  N   TYR B  35      54.144  13.488  -5.274  1.00109.54           N  
ANISOU 2818  N   TYR B  35    12961  13992  14666    -71   -383    564       N  
ATOM   2819  CA  TYR B  35      54.182  14.721  -6.044  1.00106.95           C  
ANISOU 2819  CA  TYR B  35    12564  13599  14472    -65   -513    648       C  
ATOM   2820  C   TYR B  35      55.367  14.697  -6.999  1.00 98.94           C  
ANISOU 2820  C   TYR B  35    11634  12565  13393   -130   -547    738       C  
ATOM   2821  O   TYR B  35      56.475  14.310  -6.618  1.00104.10           O  
ANISOU 2821  O   TYR B  35    12376  13206  13972   -121   -487    704       O  
ATOM   2822  CB  TYR B  35      54.290  15.946  -5.131  1.00111.31           C  
ANISOU 2822  CB  TYR B  35    13048  14063  15180     52   -548    580       C  
ATOM   2823  CG  TYR B  35      53.165  16.092  -4.130  1.00117.92           C  
ANISOU 2823  CG  TYR B  35    13803  14906  16096    125   -503    483       C  
ATOM   2824  CD1 TYR B  35      51.947  16.651  -4.498  1.00119.76           C  
ANISOU 2824  CD1 TYR B  35    13911  15134  16460    129   -567    518       C  
ATOM   2825  CD2 TYR B  35      53.330  15.689  -2.811  1.00121.33           C  
ANISOU 2825  CD2 TYR B  35    14282  15343  16474    190   -397    359       C  
ATOM   2826  CE1 TYR B  35      50.920  16.797  -3.580  1.00121.61           C  
ANISOU 2826  CE1 TYR B  35    14063  15365  16779    197   -514    428       C  
ATOM   2827  CE2 TYR B  35      52.310  15.831  -1.885  1.00124.01           C  
ANISOU 2827  CE2 TYR B  35    14553  15682  16882    257   -342    269       C  
ATOM   2828  CZ  TYR B  35      51.109  16.385  -2.274  1.00124.08           C  
ANISOU 2828  CZ  TYR B  35    14431  15683  17031    260   -395    302       C  
ATOM   2829  OH  TYR B  35      50.096  16.526  -1.351  1.00125.07           O  
ANISOU 2829  OH  TYR B  35    14484  15802  17236    327   -328    211       O  
ATOM   2830  N   LEU B  36      55.128  15.112  -8.239  1.00 87.91           N  
ANISOU 2830  N   LEU B  36    10213  11162  12028   -194   -642    855       N  
ATOM   2831  CA  LEU B  36      56.171  15.242  -9.252  1.00 81.42           C  
ANISOU 2831  CA  LEU B  36     9466  10311  11160   -257   -678    952       C  
ATOM   2832  C   LEU B  36      56.148  16.686  -9.737  1.00 91.20           C  
ANISOU 2832  C   LEU B  36    10626  11465  12559   -225   -803   1024       C  
ATOM   2833  O   LEU B  36      55.280  17.069 -10.528  1.00 95.00           O  
ANISOU 2833  O   LEU B  36    11049  11954  13092   -260   -894   1104       O  
ATOM   2834  CB  LEU B  36      55.951  14.263 -10.396  1.00 78.91           C  
ANISOU 2834  CB  LEU B  36     9219  10068  10696   -381   -666   1035       C  
ATOM   2835  CG  LEU B  36      56.875  14.422 -11.600  1.00 76.40           C  
ANISOU 2835  CG  LEU B  36     8982   9720  10327   -458   -701   1147       C  
ATOM   2836  CD1 LEU B  36      58.324  14.297 -11.183  1.00 73.79           C  
ANISOU 2836  CD1 LEU B  36     8726   9344   9965   -433   -626   1112       C  
ATOM   2837  CD2 LEU B  36      56.530  13.385 -12.650  1.00 76.41           C  
ANISOU 2837  CD2 LEU B  36     9060   9800  10172   -580   -683   1213       C  
ATOM   2838  N   ASP B  37      57.109  17.480  -9.264  1.00102.34           N  
ANISOU 2838  N   ASP B  37    12037  12792  14055   -158   -814    997       N  
ATOM   2839  CA  ASP B  37      57.214  18.898  -9.607  1.00107.75           C  
ANISOU 2839  CA  ASP B  37    12650  13383  14906   -118   -925   1057       C  
ATOM   2840  C   ASP B  37      55.942  19.659  -9.230  1.00108.60           C  
ANISOU 2840  C   ASP B  37    12627  13474  15160    -54   -992   1032       C  
ATOM   2841  O   ASP B  37      55.429  20.481  -9.992  1.00107.79           O  
ANISOU 2841  O   ASP B  37    12459  13336  15161    -65  -1100   1123       O  
ATOM   2842  CB  ASP B  37      57.561  19.082 -11.087  1.00110.94           C  
ANISOU 2842  CB  ASP B  37    13101  13775  15275   -212   -989   1205       C  
ATOM   2843  CG  ASP B  37      58.913  18.489 -11.443  1.00116.11           C  
ANISOU 2843  CG  ASP B  37    13876  14426  15815   -267   -916   1229       C  
ATOM   2844  OD1 ASP B  37      59.858  18.646 -10.639  1.00118.71           O  
ANISOU 2844  OD1 ASP B  37    14220  14705  16179   -208   -871   1157       O  
ATOM   2845  OD2 ASP B  37      59.036  17.867 -12.520  1.00118.49           O  
ANISOU 2845  OD2 ASP B  37    14257  14770  15994   -369   -904   1317       O  
ATOM   2846  N   GLY B  38      55.446  19.389  -8.023  1.00112.59           N  
ANISOU 2846  N   GLY B  38    13098  14002  15680     16   -924    907       N  
ATOM   2847  CA  GLY B  38      54.280  20.056  -7.487  1.00117.34           C  
ANISOU 2847  CA  GLY B  38    13576  14582  16428     87   -961    861       C  
ATOM   2848  C   GLY B  38      52.945  19.447  -7.861  1.00121.84           C  
ANISOU 2848  C   GLY B  38    14091  15228  16973     39   -964    886       C  
ATOM   2849  O   GLY B  38      51.966  19.652  -7.130  1.00125.40           O  
ANISOU 2849  O   GLY B  38    14449  15678  17520    101   -946    815       O  
ATOM   2850  N   ALA B  39      52.868  18.694  -8.956  1.00123.24           N  
ANISOU 2850  N   ALA B  39    14326  15471  17030    -70   -982    981       N  
ATOM   2851  CA  ALA B  39      51.605  18.126  -9.406  1.00121.51           C  
ANISOU 2851  CA  ALA B  39    14054  15321  16793   -124  -1002   1012       C  
ATOM   2852  C   ALA B  39      51.326  16.810  -8.694  1.00123.81           C  
ANISOU 2852  C   ALA B  39    14392  15698  16954   -140   -868    917       C  
ATOM   2853  O   ALA B  39      52.201  15.950  -8.585  1.00129.23           O  
ANISOU 2853  O   ALA B  39    15196  16420  17487   -176   -781    893       O  
ATOM   2854  CB  ALA B  39      51.624  17.898 -10.918  1.00118.24           C  
ANISOU 2854  CB  ALA B  39    13690  14937  16298   -239  -1088   1154       C  
ATOM   2855  N   ASP B  40      50.089  16.652  -8.226  1.00125.04           N  
ANISOU 2855  N   ASP B  40    14450  15881  17179   -114   -849    866       N  
ATOM   2856  CA  ASP B  40      49.689  15.424  -7.550  1.00122.31           C  
ANISOU 2856  CA  ASP B  40    14138  15612  16723   -130   -719    780       C  
ATOM   2857  C   ASP B  40      49.550  14.302  -8.574  1.00122.20           C  
ANISOU 2857  C   ASP B  40    14194  15681  16555   -256   -719    853       C  
ATOM   2858  O   ASP B  40      48.698  14.368  -9.466  1.00124.39           O  
ANISOU 2858  O   ASP B  40    14409  15979  16875   -315   -814    933       O  
ATOM   2859  CB  ASP B  40      48.379  15.642  -6.795  1.00124.48           C  
ANISOU 2859  CB  ASP B  40    14279  15883  17134    -67   -693    709       C  
ATOM   2860  CG  ASP B  40      48.093  14.546  -5.778  1.00120.79           C  
ANISOU 2860  CG  ASP B  40    13850  15474  16570    -55   -536    597       C  
ATOM   2861  OD1 ASP B  40      48.633  13.431  -5.925  1.00121.16           O  
ANISOU 2861  OD1 ASP B  40    14012  15582  16439   -121   -464    596       O  
ATOM   2862  OD2 ASP B  40      47.328  14.803  -4.823  1.00121.35           O  
ANISOU 2862  OD2 ASP B  40    13837  15525  16746     21   -477    509       O  
ATOM   2863  N   VAL B  41      50.385  13.273  -8.444  1.00118.72           N  
ANISOU 2863  N   VAL B  41    13883  15285  15940   -298   -618    824       N  
ATOM   2864  CA  VAL B  41      50.362  12.126  -9.340  1.00112.62           C  
ANISOU 2864  CA  VAL B  41    13193  14589  15009   -418   -600    880       C  
ATOM   2865  C   VAL B  41      49.968  10.849  -8.599  1.00111.78           C  
ANISOU 2865  C   VAL B  41    13119  14552  14801   -432   -462    790       C  
ATOM   2866  O   VAL B  41      50.268   9.748  -9.049  1.00110.07           O  
ANISOU 2866  O   VAL B  41    13000  14392  14428   -518   -406    807       O  
ATOM   2867  CB  VAL B  41      51.712  11.961 -10.064  1.00102.58           C  
ANISOU 2867  CB  VAL B  41    12053  13305  13616   -474   -601    943       C  
ATOM   2868  CG1 VAL B  41      51.993  13.178 -10.929  1.00 95.31           C  
ANISOU 2868  CG1 VAL B  41    11103  12318  12793   -474   -739   1046       C  
ATOM   2869  CG2 VAL B  41      52.838  11.746  -9.056  1.00105.16           C  
ANISOU 2869  CG2 VAL B  41    12455  13607  13892   -411   -493    857       C  
ATOM   2870  N   THR B  42      49.278  10.997  -7.465  1.00112.20           N  
ANISOU 2870  N   THR B  42    13090  14595  14944   -348   -401    694       N  
ATOM   2871  CA  THR B  42      48.872   9.839  -6.676  1.00113.95           C  
ANISOU 2871  CA  THR B  42    13341  14876  15080   -354   -261    608       C  
ATOM   2872  C   THR B  42      47.923   8.947  -7.463  1.00123.21           C  
ANISOU 2872  C   THR B  42    14490  16118  16204   -458   -272    652       C  
ATOM   2873  O   THR B  42      48.050   7.717  -7.444  1.00124.94           O  
ANISOU 2873  O   THR B  42    14794  16397  16279   -519   -176    630       O  
ATOM   2874  CB  THR B  42      48.214  10.301  -5.376  1.00111.21           C  
ANISOU 2874  CB  THR B  42    12905  14498  14853   -244   -198    503       C  
ATOM   2875  OG1 THR B  42      49.151  11.067  -4.610  1.00110.82           O  
ANISOU 2875  OG1 THR B  42    12892  14383  14832   -151   -189    453       O  
ATOM   2876  CG2 THR B  42      47.746   9.115  -4.557  1.00109.49           C  
ANISOU 2876  CG2 THR B  42    12719  14337  14547   -251    -47    418       C  
ATOM   2877  N   LYS B  43      46.975   9.556  -8.175  1.00130.79           N  
ANISOU 2877  N   LYS B  43    15337  17070  17289   -480   -394    718       N  
ATOM   2878  CA  LYS B  43      45.885   8.858  -8.839  1.00133.82           C  
ANISOU 2878  CA  LYS B  43    15669  17511  17666   -569   -424    753       C  
ATOM   2879  C   LYS B  43      46.226   8.442 -10.268  1.00133.78           C  
ANISOU 2879  C   LYS B  43    15751  17541  17540   -691   -513    861       C  
ATOM   2880  O   LYS B  43      45.315   8.131 -11.044  1.00135.94           O  
ANISOU 2880  O   LYS B  43    15974  17850  17828   -769   -588    913       O  
ATOM   2881  CB  LYS B  43      44.647   9.757  -8.848  1.00136.28           C  
ANISOU 2881  CB  LYS B  43    15804  17788  18190   -526   -520    768       C  
ATOM   2882  CG  LYS B  43      44.997  11.205  -9.204  1.00137.04           C  
ANISOU 2882  CG  LYS B  43    15852  17807  18410   -471   -653    831       C  
ATOM   2883  CD  LYS B  43      43.783  12.082  -9.465  1.00138.48           C  
ANISOU 2883  CD  LYS B  43    15860  17951  18804   -444   -773    870       C  
ATOM   2884  CE  LYS B  43      44.224  13.478  -9.890  1.00137.10           C  
ANISOU 2884  CE  LYS B  43    15653  17698  18741   -395   -906    942       C  
ATOM   2885  NZ  LYS B  43      43.082  14.359 -10.252  1.00142.12           N  
ANISOU 2885  NZ  LYS B  43    16121  18292  19588   -372  -1039    995       N  
ATOM   2886  N   ILE B  44      47.510   8.416 -10.631  1.00130.19           N  
ANISOU 2886  N   ILE B  44    15426  17074  16967   -712   -503    895       N  
ATOM   2887  CA  ILE B  44      47.931   8.008 -11.964  1.00124.30           C  
ANISOU 2887  CA  ILE B  44    14781  16356  16092   -828   -567    992       C  
ATOM   2888  C   ILE B  44      48.975   6.906 -11.848  1.00119.31           C  
ANISOU 2888  C   ILE B  44    14303  15756  15272   -872   -435    958       C  
ATOM   2889  O   ILE B  44      49.560   6.675 -10.788  1.00120.68           O  
ANISOU 2889  O   ILE B  44    14509  15919  15426   -802   -318    874       O  
ATOM   2890  CB  ILE B  44      48.485   9.181 -12.799  1.00120.18           C  
ANISOU 2890  CB  ILE B  44    14267  15775  15623   -824   -703   1092       C  
ATOM   2891  CG1 ILE B  44      49.914   9.508 -12.385  1.00118.41           C  
ANISOU 2891  CG1 ILE B  44    14129  15502  15358   -770   -639   1072       C  
ATOM   2892  CG2 ILE B  44      47.607  10.412 -12.646  1.00124.55           C  
ANISOU 2892  CG2 ILE B  44    14660  16277  16386   -751   -819   1112       C  
ATOM   2893  CD1 ILE B  44      50.576  10.502 -13.303  1.00119.27           C  
ANISOU 2893  CD1 ILE B  44    14266  15553  15496   -784   -752   1177       C  
ATOM   2894  N   LYS B  45      49.186   6.209 -12.960  1.00117.09           N  
ANISOU 2894  N   LYS B  45    14119  15514  14855   -989   -456   1024       N  
ATOM   2895  CA  LYS B  45      50.130   5.111 -13.074  1.00114.66           C  
ANISOU 2895  CA  LYS B  45    13960  15236  14370  -1047   -338   1005       C  
ATOM   2896  C   LYS B  45      51.430   5.590 -13.715  1.00106.85           C  
ANISOU 2896  C   LYS B  45    13071  14201  13326  -1060   -362   1071       C  
ATOM   2897  O   LYS B  45      51.436   6.570 -14.467  1.00101.49           O  
ANISOU 2897  O   LYS B  45    12367  13485  12711  -1067   -487   1156       O  
ATOM   2898  CB  LYS B  45      49.529   3.966 -13.898  1.00120.49           C  
ANISOU 2898  CB  LYS B  45    14750  16043  14988  -1174   -332   1029       C  
ATOM   2899  CG  LYS B  45      48.249   3.403 -13.291  1.00123.47           C  
ANISOU 2899  CG  LYS B  45    15027  16464  15423  -1170   -299    964       C  
ATOM   2900  CD  LYS B  45      47.729   2.181 -14.037  1.00122.46           C  
ANISOU 2900  CD  LYS B  45    14956  16400  15174  -1297   -284    977       C  
ATOM   2901  CE  LYS B  45      46.424   1.688 -13.420  1.00120.79           C  
ANISOU 2901  CE  LYS B  45    14629  16224  15043  -1291   -252    914       C  
ATOM   2902  NZ  LYS B  45      45.964   0.407 -14.022  1.00120.46           N  
ANISOU 2902  NZ  LYS B  45    14644  16241  14884  -1413   -221    912       N  
ATOM   2903  N   PRO B  46      52.547   4.918 -13.429  1.00102.75           N  
ANISOU 2903  N   PRO B  46    12662  13678  12698  -1064   -241   1036       N  
ATOM   2904  CA  PRO B  46      53.838   5.366 -13.965  1.00100.02           C  
ANISOU 2904  CA  PRO B  46    12404  13281  12318  -1071   -247   1093       C  
ATOM   2905  C   PRO B  46      53.914   5.246 -15.477  1.00 95.94           C  
ANISOU 2905  C   PRO B  46    11970  12778  11706  -1191   -314   1198       C  
ATOM   2906  O   PRO B  46      53.488   4.248 -16.064  1.00 93.30           O  
ANISOU 2906  O   PRO B  46    11695  12500  11253  -1289   -288   1205       O  
ATOM   2907  CB  PRO B  46      54.848   4.431 -13.289  1.00 99.57           C  
ANISOU 2907  CB  PRO B  46    12439  13227  12165  -1057    -93   1024       C  
ATOM   2908  CG  PRO B  46      54.148   3.921 -12.078  1.00 99.55           C  
ANISOU 2908  CG  PRO B  46    12376  13259  12191   -998    -21    923       C  
ATOM   2909  CD  PRO B  46      52.710   3.813 -12.471  1.00 99.49           C  
ANISOU 2909  CD  PRO B  46    12289  13299  12213  -1045    -90    940       C  
ATOM   2910  N   HIS B  47      54.480   6.273 -16.103  1.00 96.62           N  
ANISOU 2910  N   HIS B  47    12066  12805  11839  -1184   -397   1278       N  
ATOM   2911  CA  HIS B  47      54.730   6.279 -17.534  1.00103.57           C  
ANISOU 2911  CA  HIS B  47    13045  13685  12623  -1292   -454   1383       C  
ATOM   2912  C   HIS B  47      56.215   6.038 -17.788  1.00 99.28           C  
ANISOU 2912  C   HIS B  47    12626  13102  11996  -1312   -351   1398       C  
ATOM   2913  O   HIS B  47      57.054   6.188 -16.897  1.00 93.90           O  
ANISOU 2913  O   HIS B  47    11930  12379  11368  -1230   -275   1341       O  
ATOM   2914  CB  HIS B  47      54.286   7.605 -18.162  1.00115.37           C  
ANISOU 2914  CB  HIS B  47    14471  15137  14228  -1278   -620   1477       C  
ATOM   2915  CG  HIS B  47      54.326   7.606 -19.659  1.00124.98           C  
ANISOU 2915  CG  HIS B  47    15791  16360  15336  -1395   -695   1591       C  
ATOM   2916  ND1 HIS B  47      55.284   8.284 -20.381  1.00126.89           N  
ANISOU 2916  ND1 HIS B  47    16109  16540  15563  -1412   -713   1674       N  
ATOM   2917  CD2 HIS B  47      53.525   7.003 -20.570  1.00127.27           C  
ANISOU 2917  CD2 HIS B  47    16128  16707  15522  -1503   -755   1634       C  
ATOM   2918  CE1 HIS B  47      55.071   8.100 -21.672  1.00128.16           C  
ANISOU 2918  CE1 HIS B  47    16367  16721  15606  -1525   -777   1766       C  
ATOM   2919  NE2 HIS B  47      54.009   7.327 -21.814  1.00128.59           N  
ANISOU 2919  NE2 HIS B  47    16407  16848  15603  -1582   -809   1742       N  
ATOM   2920  N   ASN B  48      56.532   5.663 -19.030  1.00104.73           N  
ANISOU 2920  N   ASN B  48    13437  13800  12554  -1425   -351   1474       N  
ATOM   2921  CA  ASN B  48      57.910   5.370 -19.415  1.00105.04           C  
ANISOU 2921  CA  ASN B  48    13599  13800  12512  -1458   -243   1494       C  
ATOM   2922  C   ASN B  48      58.845   6.564 -19.261  1.00105.51           C  
ANISOU 2922  C   ASN B  48    13627  13770  12691  -1382   -269   1530       C  
ATOM   2923  O   ASN B  48      60.058   6.368 -19.104  1.00 99.82           O  
ANISOU 2923  O   ASN B  48    12966  13005  11955  -1370   -162   1515       O  
ATOM   2924  CB  ASN B  48      57.934   4.886 -20.865  1.00102.95           C  
ANISOU 2924  CB  ASN B  48    13471  13558  12088  -1596   -251   1576       C  
ATOM   2925  CG  ASN B  48      57.481   3.455 -21.001  1.00101.26           C  
ANISOU 2925  CG  ASN B  48    13325  13418  11730  -1680   -173   1525       C  
ATOM   2926  OD1 ASN B  48      57.968   2.571 -20.297  1.00 99.27           O  
ANISOU 2926  OD1 ASN B  48    13096  13177  11444  -1661    -37   1445       O  
ATOM   2927  ND2 ASN B  48      56.506   3.223 -21.876  1.00100.80           N  
ANISOU 2927  ND2 ASN B  48    13294  13409  11595  -1772   -266   1571       N  
ATOM   2928  N   SER B  49      58.309   7.789 -19.290  1.00106.14           N  
ANISOU 2928  N   SER B  49    13609  13817  12900  -1331   -406   1577       N  
ATOM   2929  CA  SER B  49      59.101   9.011 -19.196  1.00100.51           C  
ANISOU 2929  CA  SER B  49    12860  13015  12314  -1262   -445   1617       C  
ATOM   2930  C   SER B  49      59.553   9.342 -17.780  1.00 99.09           C  
ANISOU 2930  C   SER B  49    12590  12796  12263  -1136   -399   1521       C  
ATOM   2931  O   SER B  49      60.323  10.294 -17.604  1.00100.29           O  
ANISOU 2931  O   SER B  49    12712  12868  12525  -1076   -420   1541       O  
ATOM   2932  CB  SER B  49      58.309  10.198 -19.747  1.00 94.85           C  
ANISOU 2932  CB  SER B  49    12071  12273  11693  -1253   -613   1704       C  
ATOM   2933  OG  SER B  49      57.148  10.450 -18.980  1.00 94.45           O  
ANISOU 2933  OG  SER B  49    11887  12253  11746  -1187   -688   1651       O  
ATOM   2934  N   HIS B  50      59.108   8.592 -16.775  1.00 90.15           N  
ANISOU 2934  N   HIS B  50    11419  11715  11119  -1096   -339   1418       N  
ATOM   2935  CA  HIS B  50      59.480   8.867 -15.395  1.00 80.86           C  
ANISOU 2935  CA  HIS B  50    10170  10505  10048   -977   -299   1322       C  
ATOM   2936  C   HIS B  50      60.794   8.217 -14.991  1.00 72.01           C  
ANISOU 2936  C   HIS B  50     9126   9357   8876   -969   -170   1277       C  
ATOM   2937  O   HIS B  50      61.291   8.493 -13.894  1.00 74.54           O  
ANISOU 2937  O   HIS B  50     9401   9640   9282   -873   -144   1205       O  
ATOM   2938  CB  HIS B  50      58.364   8.400 -14.455  1.00 79.81           C  
ANISOU 2938  CB  HIS B  50     9961  10434   9928   -934   -291   1233       C  
ATOM   2939  CG  HIS B  50      57.053   9.077 -14.698  1.00 82.02           C  
ANISOU 2939  CG  HIS B  50    10142  10732  10291   -928   -417   1266       C  
ATOM   2940  ND1 HIS B  50      55.860   8.594 -14.205  1.00 83.25           N  
ANISOU 2940  ND1 HIS B  50    10232  10949  10450   -920   -417   1210       N  
ATOM   2941  CD2 HIS B  50      56.747  10.198 -15.394  1.00 83.34           C  
ANISOU 2941  CD2 HIS B  50    10259  10858  10548   -929   -548   1354       C  
ATOM   2942  CE1 HIS B  50      54.876   9.393 -14.581  1.00 86.33           C  
ANISOU 2942  CE1 HIS B  50    10530  11335  10938   -915   -545   1260       C  
ATOM   2943  NE2 HIS B  50      55.388  10.373 -15.304  1.00 84.77           N  
ANISOU 2943  NE2 HIS B  50    10342  11076  10792   -919   -629   1348       N  
ATOM   2944  N   GLU B  51      61.385   7.404 -15.863  1.00 65.92           N  
ANISOU 2944  N   GLU B  51     8472   8599   7975  -1066    -92   1320       N  
ATOM   2945  CA  GLU B  51      62.633   6.712 -15.574  1.00 68.10           C  
ANISOU 2945  CA  GLU B  51     8821   8847   8207  -1065     36   1284       C  
ATOM   2946  C   GLU B  51      63.714   7.677 -15.092  1.00 72.03           C  
ANISOU 2946  C   GLU B  51     9276   9248   8842   -982     22   1282       C  
ATOM   2947  O   GLU B  51      64.180   8.531 -15.851  1.00 79.26           O  
ANISOU 2947  O   GLU B  51    10199  10105   9813  -1001    -26   1363       O  
ATOM   2948  CB  GLU B  51      63.101   5.948 -16.814  1.00 74.43           C  
ANISOU 2948  CB  GLU B  51     9751   9660   8867  -1188    110   1350       C  
ATOM   2949  CG  GLU B  51      64.441   5.247 -16.659  1.00 85.72           C  
ANISOU 2949  CG  GLU B  51    11255  11050  10264  -1195    248   1324       C  
ATOM   2950  CD  GLU B  51      64.320   3.867 -16.037  1.00 97.05           C  
ANISOU 2950  CD  GLU B  51    12728  12543  11603  -1205    355   1241       C  
ATOM   2951  OE1 GLU B  51      63.722   3.748 -14.947  1.00101.45           O  
ANISOU 2951  OE1 GLU B  51    13216  13133  12196  -1133    339   1164       O  
ATOM   2952  OE2 GLU B  51      64.823   2.896 -16.642  1.00102.05           O  
ANISOU 2952  OE2 GLU B  51    13465  13186  12124  -1286    463   1253       O  
ATOM   2953  N   GLY B  52      64.092   7.568 -13.818  1.00 68.45           N  
ANISOU 2953  N   GLY B  52     8781   8779   8450   -889     58   1188       N  
ATOM   2954  CA  GLY B  52      65.160   8.367 -13.258  1.00 68.90           C  
ANISOU 2954  CA  GLY B  52     8800   8744   8636   -810     45   1172       C  
ATOM   2955  C   GLY B  52      64.745   9.705 -12.687  1.00 67.24           C  
ANISOU 2955  C   GLY B  52     8479   8490   8578   -718    -74   1158       C  
ATOM   2956  O   GLY B  52      65.612  10.447 -12.207  1.00 63.80           O  
ANISOU 2956  O   GLY B  52     8007   7973   8260   -651    -96   1142       O  
ATOM   2957  N   LYS B  53      63.460  10.049 -12.739  1.00 68.50           N  
ANISOU 2957  N   LYS B  53     8580   8696   8749   -713   -153   1164       N  
ATOM   2958  CA  LYS B  53      63.003  11.318 -12.200  1.00 71.33           C  
ANISOU 2958  CA  LYS B  53     8830   9010   9261   -624   -262   1149       C  
ATOM   2959  C   LYS B  53      62.830  11.230 -10.681  1.00 69.12           C  
ANISOU 2959  C   LYS B  53     8500   8736   9025   -521   -241   1025       C  
ATOM   2960  O   LYS B  53      62.852  10.154 -10.081  1.00 72.81           O  
ANISOU 2960  O   LYS B  53     9013   9253   9397   -522   -152    957       O  
ATOM   2961  CB  LYS B  53      61.701  11.748 -12.876  1.00 73.77           C  
ANISOU 2961  CB  LYS B  53     9091   9359   9581   -658   -357   1208       C  
ATOM   2962  CG  LYS B  53      61.865  12.136 -14.345  1.00 79.97           C  
ANISOU 2962  CG  LYS B  53     9923  10122  10340   -748   -406   1338       C  
ATOM   2963  CD  LYS B  53      60.644  12.896 -14.858  1.00 85.99           C  
ANISOU 2963  CD  LYS B  53    10612  10898  11161   -755   -535   1399       C  
ATOM   2964  CE  LYS B  53      60.762  13.227 -16.339  1.00 83.31           C  
ANISOU 2964  CE  LYS B  53    10336  10541  10776   -849   -589   1534       C  
ATOM   2965  NZ  LYS B  53      62.002  13.992 -16.627  1.00 84.62           N  
ANISOU 2965  NZ  LYS B  53    10527  10610  11014   -836   -581   1584       N  
ATOM   2966  N   THR B  54      62.676  12.390 -10.057  1.00 63.47           N  
ANISOU 2966  N   THR B  54     7696   7964   8457   -430   -324    995       N  
ATOM   2967  CA  THR B  54      62.601  12.507  -8.608  1.00 58.19           C  
ANISOU 2967  CA  THR B  54     6986   7284   7841   -326   -313    877       C  
ATOM   2968  C   THR B  54      61.185  12.868  -8.181  1.00 59.75           C  
ANISOU 2968  C   THR B  54     7100   7519   8085   -284   -360    840       C  
ATOM   2969  O   THR B  54      60.609  13.835  -8.687  1.00 62.47           O  
ANISOU 2969  O   THR B  54     7372   7836   8530   -280   -454    895       O  
ATOM   2970  CB  THR B  54      63.584  13.561  -8.098  1.00 51.61           C  
ANISOU 2970  CB  THR B  54     6118   6347   7146   -248   -363    855       C  
ATOM   2971  OG1 THR B  54      64.919  13.159  -8.419  1.00 44.31           O  
ANISOU 2971  OG1 THR B  54     5262   5383   6189   -284   -310    883       O  
ATOM   2972  CG2 THR B  54      63.443  13.738  -6.602  1.00 54.36           C  
ANISOU 2972  CG2 THR B  54     6432   6681   7540   -141   -361    730       C  
ATOM   2973  N   PHE B  55      60.638  12.099  -7.244  1.00 61.20           N  
ANISOU 2973  N   PHE B  55     7291   7759   8204   -254   -292    749       N  
ATOM   2974  CA  PHE B  55      59.291  12.296  -6.730  1.00 60.83           C  
ANISOU 2974  CA  PHE B  55     7166   7748   8199   -213   -311    701       C  
ATOM   2975  C   PHE B  55      59.344  12.659  -5.253  1.00 69.41           C  
ANISOU 2975  C   PHE B  55     8227   8800   9347    -99   -292    582       C  
ATOM   2976  O   PHE B  55      60.148  12.103  -4.496  1.00 68.81           O  
ANISOU 2976  O   PHE B  55     8220   8718   9206    -71   -228    519       O  
ATOM   2977  CB  PHE B  55      58.446  11.036  -6.910  1.00 58.24           C  
ANISOU 2977  CB  PHE B  55     6870   7518   7740   -281   -236    695       C  
ATOM   2978  CG  PHE B  55      58.222  10.661  -8.340  1.00 59.78           C  
ANISOU 2978  CG  PHE B  55     7094   7752   7867   -396   -261    804       C  
ATOM   2979  CD1 PHE B  55      57.038  10.984  -8.969  1.00 59.67           C  
ANISOU 2979  CD1 PHE B  55     7008   7766   7897   -429   -334    854       C  
ATOM   2980  CD2 PHE B  55      59.197   9.990  -9.057  1.00 64.43           C  
ANISOU 2980  CD2 PHE B  55     7784   8345   8351   -471   -213    855       C  
ATOM   2981  CE1 PHE B  55      56.827  10.643 -10.283  1.00 63.99           C  
ANISOU 2981  CE1 PHE B  55     7592   8349   8372   -537   -368    954       C  
ATOM   2982  CE2 PHE B  55      58.991   9.642 -10.377  1.00 60.77           C  
ANISOU 2982  CE2 PHE B  55     7361   7915   7812   -580   -232    951       C  
ATOM   2983  CZ  PHE B  55      57.804   9.971 -10.989  1.00 63.22           C  
ANISOU 2983  CZ  PHE B  55     7608   8257   8155   -614   -314   1000       C  
ATOM   2984  N   TYR B  56      58.497  13.604  -4.849  1.00 72.51           N  
ANISOU 2984  N   TYR B  56     8522   9165   9863    -34   -351    551       N  
ATOM   2985  CA  TYR B  56      58.297  13.889  -3.434  1.00 66.41           C  
ANISOU 2985  CA  TYR B  56     7729   8369   9136     70   -322    430       C  
ATOM   2986  C   TYR B  56      57.286  12.915  -2.851  1.00 67.87           C  
ANISOU 2986  C   TYR B  56     7923   8635   9232     65   -227    368       C  
ATOM   2987  O   TYR B  56      56.312  12.541  -3.510  1.00 79.19           O  
ANISOU 2987  O   TYR B  56     9316  10124  10647      5   -225    415       O  
ATOM   2988  CB  TYR B  56      57.801  15.320  -3.223  1.00 62.45           C  
ANISOU 2988  CB  TYR B  56     7119   7797   8814    144   -413    418       C  
ATOM   2989  CG  TYR B  56      58.885  16.339  -2.985  1.00 61.55           C  
ANISOU 2989  CG  TYR B  56     7004   7583   8800    200   -479    408       C  
ATOM   2990  CD1 TYR B  56      59.231  16.721  -1.694  1.00 64.88           C  
ANISOU 2990  CD1 TYR B  56     7437   7956   9259    296   -465    293       C  
ATOM   2991  CD2 TYR B  56      59.564  16.921  -4.046  1.00 71.64           C  
ANISOU 2991  CD2 TYR B  56     8272   8812  10135    155   -555    513       C  
ATOM   2992  CE1 TYR B  56      60.230  17.662  -1.464  1.00 70.35           C  
ANISOU 2992  CE1 TYR B  56     8126   8553  10052    345   -534    280       C  
ATOM   2993  CE2 TYR B  56      60.563  17.865  -3.831  1.00 78.21           C  
ANISOU 2993  CE2 TYR B  56     9097   9547  11073    205   -614    504       C  
ATOM   2994  CZ  TYR B  56      60.894  18.230  -2.540  1.00 72.71           C  
ANISOU 2994  CZ  TYR B  56     8404   8802  10419    299   -607    386       C  
ATOM   2995  OH  TYR B  56      61.885  19.168  -2.331  1.00 60.34           O  
ANISOU 2995  OH  TYR B  56     6827   7136   8965    345   -673    375       O  
ATOM   2996  N   VAL B  57      57.513  12.503  -1.605  1.00 65.08           N  
ANISOU 2996  N   VAL B  57     7622   8283   8822    128   -151    262       N  
ATOM   2997  CA  VAL B  57      56.601  11.600  -0.915  1.00 70.81           C  
ANISOU 2997  CA  VAL B  57     8362   9077   9465    132    -48    195       C  
ATOM   2998  C   VAL B  57      56.411  12.091   0.513  1.00 76.15           C  
ANISOU 2998  C   VAL B  57     9034   9714  10187    242    -18     75       C  
ATOM   2999  O   VAL B  57      57.215  12.860   1.047  1.00 68.10           O  
ANISOU 2999  O   VAL B  57     8029   8622   9223    308    -67     35       O  
ATOM   3000  CB  VAL B  57      57.103  10.137  -0.902  1.00 65.87           C  
ANISOU 3000  CB  VAL B  57     7850   8514   8665     72     50    195       C  
ATOM   3001  CG1 VAL B  57      57.186   9.573  -2.312  1.00 61.89           C  
ANISOU 3001  CG1 VAL B  57     7360   8052   8105    -42     34    306       C  
ATOM   3002  CG2 VAL B  57      58.437  10.049  -0.194  1.00 69.37           C  
ANISOU 3002  CG2 VAL B  57     8382   8911   9063    118     61    150       C  
ATOM   3003  N   LEU B  58      55.327  11.625   1.132  1.00 88.79           N  
ANISOU 3003  N   LEU B  58    10615  11360  11760    258     67     15       N  
ATOM   3004  CA  LEU B  58      55.089  11.915   2.538  1.00 94.39           C  
ANISOU 3004  CA  LEU B  58    11341  12040  12484    357    123   -106       C  
ATOM   3005  C   LEU B  58      55.865  10.928   3.407  1.00 93.66           C  
ANISOU 3005  C   LEU B  58    11386  11969  12231    369    208   -166       C  
ATOM   3006  O   LEU B  58      56.050   9.769   3.033  1.00 95.54           O  
ANISOU 3006  O   LEU B  58    11687  12269  12347    299    266   -127       O  
ATOM   3007  CB  LEU B  58      53.600  11.826   2.864  1.00 95.26           C  
ANISOU 3007  CB  LEU B  58    11372  12183  12638    370    192   -145       C  
ATOM   3008  CG  LEU B  58      52.750  13.097   2.776  1.00 94.76           C  
ANISOU 3008  CG  LEU B  58    11173  12067  12765    420    126   -150       C  
ATOM   3009  CD1 LEU B  58      52.775  13.701   1.382  1.00 94.79           C  
ANISOU 3009  CD1 LEU B  58    11093  12056  12867    362     -1    -29       C  
ATOM   3010  CD2 LEU B  58      51.321  12.801   3.202  1.00100.24           C  
ANISOU 3010  CD2 LEU B  58    11798  12795  13493    431    220   -197       C  
ATOM   3011  N   PRO B  59      56.345  11.369   4.546  1.00 89.27           N  
ANISOU 3011  N   PRO B  59    10882  11361  11675    457    210   -258       N  
ATOM   3012  CA  PRO B  59      57.152  10.474   5.393  1.00 90.85           C  
ANISOU 3012  CA  PRO B  59    11219  11575  11725    472    274   -310       C  
ATOM   3013  C   PRO B  59      56.347   9.322   5.975  1.00 95.66           C  
ANISOU 3013  C   PRO B  59    11881  12255  12211    458    414   -353       C  
ATOM   3014  O   PRO B  59      55.833   9.423   7.104  1.00 98.32           O  
ANISOU 3014  O   PRO B  59    12246  12581  12528    526    481   -448       O  
ATOM   3015  CB  PRO B  59      57.714  11.413   6.459  1.00 89.27           C  
ANISOU 3015  CB  PRO B  59    11051  11294  11573    573    224   -402       C  
ATOM   3016  CG  PRO B  59      56.768  12.577   6.483  1.00 88.83           C  
ANISOU 3016  CG  PRO B  59    10880  11198  11672    620    192   -429       C  
ATOM   3017  CD  PRO B  59      56.288  12.740   5.081  1.00 86.69           C  
ANISOU 3017  CD  PRO B  59    10499  10953  11487    544    142   -316       C  
ATOM   3018  N   ASN B  60      56.245   8.224   5.238  1.00 94.24           N  
ANISOU 3018  N   ASN B  60    11719  12142  11944    369    464   -285       N  
ATOM   3019  CA  ASN B  60      55.641   6.983   5.714  1.00 95.85           C  
ANISOU 3019  CA  ASN B  60    11985  12414  12022    344    599   -314       C  
ATOM   3020  C   ASN B  60      56.680   6.001   6.232  1.00 95.97           C  
ANISOU 3020  C   ASN B  60    12140  12438  11887    341    644   -329       C  
ATOM   3021  O   ASN B  60      56.329   4.885   6.622  1.00 95.18           O  
ANISOU 3021  O   ASN B  60    12106  12389  11671    317    757   -347       O  
ATOM   3022  CB  ASN B  60      54.809   6.325   4.604  1.00102.47           C  
ANISOU 3022  CB  ASN B  60    12756  13319  12860    244    629   -235       C  
ATOM   3023  CG  ASN B  60      53.748   5.369   5.157  1.00117.09           C  
ANISOU 3023  CG  ASN B  60    14622  15227  14639    230    769   -279       C  
ATOM   3024  OD1 ASN B  60      53.763   5.017   6.338  1.00125.33           O  
ANISOU 3024  OD1 ASN B  60    15749  16268  15604    287    857   -360       O  
ATOM   3025  ND2 ASN B  60      52.821   4.950   4.298  1.00118.53           N  
ANISOU 3025  ND2 ASN B  60    14726  15462  14849    153    789   -225       N  
ATOM   3026  N   ASP B  61      57.950   6.374   6.209  1.00 95.55           N  
ANISOU 3026  N   ASP B  61    12130  12333  11843    362    557   -317       N  
ATOM   3027  CA  ASP B  61      59.044   5.531   6.660  1.00 94.79           C  
ANISOU 3027  CA  ASP B  61    12156  12233  11626    363    579   -324       C  
ATOM   3028  C   ASP B  61      59.723   6.204   7.849  1.00 91.74           C  
ANISOU 3028  C   ASP B  61    11833  11779  11246    463    529   -410       C  
ATOM   3029  O   ASP B  61      59.578   7.410   8.069  1.00 93.78           O  
ANISOU 3029  O   ASP B  61    12031  11985  11616    519    457   -447       O  
ATOM   3030  CB  ASP B  61      60.042   5.300   5.516  1.00107.78           C  
ANISOU 3030  CB  ASP B  61    13797  13871  13284    292    519   -229       C  
ATOM   3031  CG  ASP B  61      61.253   4.498   5.939  1.00122.07           C  
ANISOU 3031  CG  ASP B  61    15720  15665  14997    297    533   -233       C  
ATOM   3032  OD1 ASP B  61      61.167   3.252   5.984  1.00127.15           O  
ANISOU 3032  OD1 ASP B  61    16430  16359  15522    253    629   -221       O  
ATOM   3033  OD2 ASP B  61      62.283   5.119   6.265  1.00127.38           O  
ANISOU 3033  OD2 ASP B  61    16411  16270  15718    346    445   -250       O  
ATOM   3034  N   ASP B  62      60.467   5.419   8.629  1.00 95.06           N  
ANISOU 3034  N   ASP B  62    12375  12197  11545    484    562   -441       N  
ATOM   3035  CA  ASP B  62      61.205   6.009   9.745  1.00 97.98           C  
ANISOU 3035  CA  ASP B  62    12817  12501  11911    574    498   -520       C  
ATOM   3036  C   ASP B  62      62.367   6.863   9.254  1.00 94.76           C  
ANISOU 3036  C   ASP B  62    12368  12021  11615    582    357   -487       C  
ATOM   3037  O   ASP B  62      62.642   7.923   9.823  1.00 88.31           O  
ANISOU 3037  O   ASP B  62    11542  11138  10874    652    274   -546       O  
ATOM   3038  CB  ASP B  62      61.693   4.922  10.701  1.00103.98           C  
ANISOU 3038  CB  ASP B  62    13723  13274  12510    593    560   -556       C  
ATOM   3039  CG  ASP B  62      60.561   4.268  11.471  1.00108.62           C  
ANISOU 3039  CG  ASP B  62    14365  13915  12991    605    700   -610       C  
ATOM   3040  OD1 ASP B  62      59.639   4.992  11.913  1.00110.21           O  
ANISOU 3040  OD1 ASP B  62    14526  14109  13240    649    725   -671       O  
ATOM   3041  OD2 ASP B  62      60.595   3.031  11.640  1.00109.97           O  
ANISOU 3041  OD2 ASP B  62    14618  14131  13036    571    789   -591       O  
ATOM   3042  N   THR B  63      63.061   6.425   8.201  1.00109.27           N  
ANISOU 3042  N   THR B  63    18712  12114  10690   1097    518    302       N  
ATOM   3043  CA  THR B  63      64.152   7.237   7.664  1.00108.28           C  
ANISOU 3043  CA  THR B  63    18360  12182  10599   1168    329    322       C  
ATOM   3044  C   THR B  63      63.615   8.491   6.981  1.00 98.45           C  
ANISOU 3044  C   THR B  63    16980  11015   9412   1037    231    364       C  
ATOM   3045  O   THR B  63      64.249   9.552   7.035  1.00 90.67           O  
ANISOU 3045  O   THR B  63    15841  10153   8457   1096    109    370       O  
ATOM   3046  CB  THR B  63      65.009   6.416   6.703  1.00119.16           C  
ANISOU 3046  CB  THR B  63    19664  13627  11984   1200    268    339       C  
ATOM   3047  OG1 THR B  63      64.188   5.915   5.642  1.00135.51           O  
ANISOU 3047  OG1 THR B  63    21771  15645  14073   1043    301    371       O  
ATOM   3048  CG2 THR B  63      65.645   5.247   7.430  1.00117.54           C  
ANISOU 3048  CG2 THR B  63    19584  13353  11724   1346    349    303       C  
ATOM   3049  N   LEU B  64      62.461   8.386   6.314  1.00 95.03           N  
ANISOU 3049  N   LEU B  64    16606  10507   8995    862    283    390       N  
ATOM   3050  CA  LEU B  64      61.866   9.568   5.698  1.00 85.90           C  
ANISOU 3050  CA  LEU B  64    15336   9407   7895    742    190    437       C  
ATOM   3051  C   LEU B  64      61.417  10.565   6.759  1.00 89.07           C  
ANISOU 3051  C   LEU B  64    15758   9788   8298    741    216    424       C  
ATOM   3052  O   LEU B  64      61.544  11.779   6.569  1.00 92.46           O  
ANISOU 3052  O   LEU B  64    15973  10315   8842    722     94    440       O  
ATOM   3053  CB  LEU B  64      60.692   9.172   4.801  1.00 83.67           C  
ANISOU 3053  CB  LEU B  64    15129   9042   7618    560    244    457       C  
ATOM   3054  CG  LEU B  64      61.020   8.386   3.529  1.00 83.46           C  
ANISOU 3054  CG  LEU B  64    15056   9051   7603    547    187    480       C  
ATOM   3055  CD1 LEU B  64      59.764   8.083   2.738  1.00 83.39           C  
ANISOU 3055  CD1 LEU B  64    15125   8958   7600    368    239    480       C  
ATOM   3056  CD2 LEU B  64      62.005   9.155   2.675  1.00 80.62           C  
ANISOU 3056  CD2 LEU B  64    14467   8852   7312    620      0    531       C  
ATOM   3057  N   ARG B  65      60.888  10.070   7.882  1.00 93.15           N  
ANISOU 3057  N   ARG B  65    16455  10171   8765    753    381    375       N  
ATOM   3058  CA  ARG B  65      60.525  10.955   8.987  1.00 89.89           C  
ANISOU 3058  CA  ARG B  65    16020   9736   8400    767    410    347       C  
ATOM   3059  C   ARG B  65      61.751  11.656   9.564  1.00 82.07           C  
ANISOU 3059  C   ARG B  65    14947   8873   7361    961    286    340       C  
ATOM   3060  O   ARG B  65      61.690  12.837   9.920  1.00 84.09           O  
ANISOU 3060  O   ARG B  65    15019   9192   7741    948    210    330       O  
ATOM   3061  CB  ARG B  65      59.776  10.173  10.068  1.00 95.05           C  
ANISOU 3061  CB  ARG B  65    16933  10202   8979    765    634    301       C  
ATOM   3062  CG  ARG B  65      58.290   9.986   9.756  1.00 99.27           C  
ANISOU 3062  CG  ARG B  65    17415  10612   9692    524    756    263       C  
ATOM   3063  CD  ARG B  65      57.544   9.224  10.844  1.00103.95           C  
ANISOU 3063  CD  ARG B  65    18271  10999  10227    516   1006    211       C  
ATOM   3064  NE  ARG B  65      56.332   8.593  10.327  1.00107.80           N  
ANISOU 3064  NE  ARG B  65    18768  11361  10831    298   1148    159       N  
ATOM   3065  CZ  ARG B  65      56.205   7.292  10.085  1.00110.33           C  
ANISOU 3065  CZ  ARG B  65    19332  11563  11027    279   1307    141       C  
ATOM   3066  NH1 ARG B  65      57.216   6.467  10.324  1.00110.16           N  
ANISOU 3066  NH1 ARG B  65    19500  11534  10823    471   1320    172       N  
ATOM   3067  NH2 ARG B  65      55.062   6.814   9.611  1.00115.16           N  
ANISOU 3067  NH2 ARG B  65    19913  12067  11776     67   1432     70       N  
ATOM   3068  N   VAL B  66      62.864  10.941   9.694  1.00 80.11           N  
ANISOU 3068  N   VAL B  66    14689   8667   7081   1120    261    308       N  
ATOM   3069  CA  VAL B  66      64.087  11.571  10.181  1.00 79.01           C  
ANISOU 3069  CA  VAL B  66    14423   8660   6937   1296    142    275       C  
ATOM   3070  C   VAL B  66      64.606  12.592   9.174  1.00 78.40           C  
ANISOU 3070  C   VAL B  66    14130   8739   6920   1253    -26    314       C  
ATOM   3071  O   VAL B  66      64.974  13.715   9.538  1.00 70.08           O  
ANISOU 3071  O   VAL B  66    12968   7775   5885   1307   -117    298       O  
ATOM   3072  CB  VAL B  66      65.147  10.506  10.508  1.00 85.20           C  
ANISOU 3072  CB  VAL B  66    15251   9448   7674   1467    159    233       C  
ATOM   3073  CG1 VAL B  66      66.473  11.169  10.862  1.00 84.26           C  
ANISOU 3073  CG1 VAL B  66    14983   9482   7551   1638     26    186       C  
ATOM   3074  CG2 VAL B  66      64.661   9.636  11.649  1.00 90.50           C  
ANISOU 3074  CG2 VAL B  66    16143   9949   8295   1538    324    202       C  
ATOM   3075  N   GLU B  67      64.653  12.215   7.892  1.00 79.96           N  
ANISOU 3075  N   GLU B  67    14265   8964   7153   1165    -67    364       N  
ATOM   3076  CA  GLU B  67      65.170  13.129   6.875  1.00 78.33           C  
ANISOU 3076  CA  GLU B  67    13863   8884   7013   1137   -212    408       C  
ATOM   3077  C   GLU B  67      64.281  14.356   6.720  1.00 76.70           C  
ANISOU 3077  C   GLU B  67    13539   8677   6928   1005   -250    441       C  
ATOM   3078  O   GLU B  67      64.782  15.465   6.490  1.00 70.66           O  
ANISOU 3078  O   GLU B  67    12549   8011   6286   1013   -348    436       O  
ATOM   3079  CB  GLU B  67      65.333  12.404   5.540  1.00 78.59           C  
ANISOU 3079  CB  GLU B  67    13852   8931   7077   1076   -235    453       C  
ATOM   3080  CG  GLU B  67      66.474  11.390   5.527  1.00 83.22           C  
ANISOU 3080  CG  GLU B  67    14439   9555   7625   1198   -227    415       C  
ATOM   3081  CD  GLU B  67      66.578  10.635   4.214  1.00 82.71           C  
ANISOU 3081  CD  GLU B  67    14335   9498   7593   1134   -244    460       C  
ATOM   3082  OE1 GLU B  67      65.706  10.830   3.341  1.00 83.37           O  
ANISOU 3082  OE1 GLU B  67    14404   9550   7722   1004   -258    514       O  
ATOM   3083  OE2 GLU B  67      67.540   9.856   4.050  1.00 84.65           O  
ANISOU 3083  OE2 GLU B  67    14561   9783   7819   1220   -248    440       O  
ATOM   3084  N   ALA B  68      62.961  14.176   6.835  1.00 78.35           N  
ANISOU 3084  N   ALA B  68    13775   8773   7222    855   -153    438       N  
ATOM   3085  CA  ALA B  68      62.044  15.309   6.777  1.00 76.50           C  
ANISOU 3085  CA  ALA B  68    13310   8539   7218    708   -172    429       C  
ATOM   3086  C   ALA B  68      62.211  16.232   7.980  1.00 76.21           C  
ANISOU 3086  C   ALA B  68    13196   8527   7235    770   -178    384       C  
ATOM   3087  O   ALA B  68      62.064  17.453   7.848  1.00 77.55           O  
ANISOU 3087  O   ALA B  68    13133   8758   7574    709   -244    383       O  
ATOM   3088  CB  ALA B  68      60.600  14.816   6.684  1.00 71.43           C  
ANISOU 3088  CB  ALA B  68    12720   7773   6646    541    -62    414       C  
ATOM   3089  N   PHE B  69      62.528  15.679   9.152  1.00 75.68           N  
ANISOU 3089  N   PHE B  69    13328   8412   7016    904   -107    343       N  
ATOM   3090  CA  PHE B  69      62.709  16.524  10.324  1.00 73.89           C  
ANISOU 3090  CA  PHE B  69    13035   8208   6832    984   -119    293       C  
ATOM   3091  C   PHE B  69      63.967  17.374  10.203  1.00 75.04           C  
ANISOU 3091  C   PHE B  69    13007   8508   6999   1098   -256    268       C  
ATOM   3092  O   PHE B  69      63.957  18.557  10.556  1.00 80.12           O  
ANISOU 3092  O   PHE B  69    13450   9204   7790   1075   -306    242       O  
ATOM   3093  CB  PHE B  69      62.778  15.670  11.590  1.00 72.58           C  
ANISOU 3093  CB  PHE B  69    13150   7947   6479   1134     -7    250       C  
ATOM   3094  CG  PHE B  69      63.164  16.445  12.816  1.00 73.47           C  
ANISOU 3094  CG  PHE B  69    13218   8097   6601   1268    -37    189       C  
ATOM   3095  CD1 PHE B  69      62.248  17.268  13.448  1.00 80.97           C  
ANISOU 3095  CD1 PHE B  69    14060   8993   7713   1169     -2    183       C  
ATOM   3096  CD2 PHE B  69      64.457  16.399  13.301  1.00 79.09           C  
ANISOU 3096  CD2 PHE B  69    13978   8906   7165   1497   -111    130       C  
ATOM   3097  CE1 PHE B  69      62.604  17.995  14.569  1.00 84.16           C  
ANISOU 3097  CE1 PHE B  69    14420   9429   8126   1298    -36    128       C  
ATOM   3098  CE2 PHE B  69      64.822  17.130  14.416  1.00 85.34           C  
ANISOU 3098  CE2 PHE B  69    14715   9740   7971   1631   -149     56       C  
ATOM   3099  CZ  PHE B  69      63.894  17.928  15.051  1.00 84.10           C  
ANISOU 3099  CZ  PHE B  69    14460   9520   7974   1531   -112     60       C  
ATOM   3100  N   GLU B  70      65.056  16.803   9.690  1.00 70.43           N  
ANISOU 3100  N   GLU B  70    12489   7995   6275   1217   -311    269       N  
ATOM   3101  CA  GLU B  70      66.281  17.578   9.550  1.00 70.54           C  
ANISOU 3101  CA  GLU B  70    12330   8153   6320   1320   -427    225       C  
ATOM   3102  C   GLU B  70      66.139  18.681   8.508  1.00 66.33           C  
ANISOU 3102  C   GLU B  70    11522   7674   6007   1173   -491    266       C  
ATOM   3103  O   GLU B  70      66.948  19.614   8.493  1.00 67.33           O  
ANISOU 3103  O   GLU B  70    11463   7900   6221   1219   -561    220       O  
ATOM   3104  CB  GLU B  70      67.464  16.668   9.225  1.00 83.13           C  
ANISOU 3104  CB  GLU B  70    14064   9811   7709   1483   -467    211       C  
ATOM   3105  CG  GLU B  70      67.786  15.673  10.334  1.00 90.79           C  
ANISOU 3105  CG  GLU B  70    15250  10739   8508   1656   -398    147       C  
ATOM   3106  CD  GLU B  70      69.076  14.915  10.092  1.00 99.68           C  
ANISOU 3106  CD  GLU B  70    16332  11937   9607   1783   -429    100       C  
ATOM   3107  OE1 GLU B  70      69.827  15.299   9.170  1.00103.45           O  
ANISOU 3107  OE1 GLU B  70    16669  12518  10121   1772   -519    110       O  
ATOM   3108  OE2 GLU B  70      69.340  13.936  10.823  1.00107.11           O  
ANISOU 3108  OE2 GLU B  70    17383  12821  10493   1897   -358     57       O  
ATOM   3109  N   TYR B  71      65.141  18.579   7.629  1.00 71.66           N  
ANISOU 3109  N   TYR B  71    12174   8284   6767   1007   -460    341       N  
ATOM   3110  CA  TYR B  71      64.911  19.566   6.582  1.00 71.39           C  
ANISOU 3110  CA  TYR B  71    11915   8291   6920    888   -508    383       C  
ATOM   3111  C   TYR B  71      63.897  20.624   7.013  1.00 71.78           C  
ANISOU 3111  C   TYR B  71    11814   8313   7147    767   -484    374       C  
ATOM   3112  O   TYR B  71      64.133  21.819   6.811  1.00 75.41           O  
ANISOU 3112  O   TYR B  71    12070   8834   7749    742   -525    367       O  
ATOM   3113  CB  TYR B  71      64.427  18.871   5.301  1.00 63.58           C  
ANISOU 3113  CB  TYR B  71    10982   7261   5913    803   -504    457       C  
ATOM   3114  CG  TYR B  71      64.490  19.729   4.055  1.00 62.81           C  
ANISOU 3114  CG  TYR B  71    10694   7212   5959    742   -561    503       C  
ATOM   3115  CD1 TYR B  71      65.691  20.289   3.634  1.00 62.01           C  
ANISOU 3115  CD1 TYR B  71    10486   7195   5879    826   -616    499       C  
ATOM   3116  CD2 TYR B  71      63.348  19.973   3.294  1.00 65.17           C  
ANISOU 3116  CD2 TYR B  71    10926   7469   6368    611   -551    539       C  
ATOM   3117  CE1 TYR B  71      65.755  21.074   2.496  1.00 65.04           C  
ANISOU 3117  CE1 TYR B  71    10720   7602   6388    783   -643    543       C  
ATOM   3118  CE2 TYR B  71      63.403  20.755   2.151  1.00 68.50           C  
ANISOU 3118  CE2 TYR B  71    11199   7927   6900    585   -595    580       C  
ATOM   3119  CZ  TYR B  71      64.610  21.305   1.759  1.00 70.79           C  
ANISOU 3119  CZ  TYR B  71    11405   8284   7207    672   -632    589       C  
ATOM   3120  OH  TYR B  71      64.681  22.086   0.625  1.00 73.35           O  
ANISOU 3120  OH  TYR B  71    11606   8626   7637    659   -651    632       O  
ATOM   3121  N   TYR B  72      62.802  20.220   7.656  1.00 68.03           N  
ANISOU 3121  N   TYR B  72    11442   7742   6665    697   -408    370       N  
ATOM   3122  CA  TYR B  72      61.763  21.159   8.055  1.00 62.70           C  
ANISOU 3122  CA  TYR B  72    10634   7037   6150    579   -384    364       C  
ATOM   3123  C   TYR B  72      61.808  21.532   9.536  1.00 60.27           C  
ANISOU 3123  C   TYR B  72    10350   6714   5837    648   -356    311       C  
ATOM   3124  O   TYR B  72      61.121  22.479   9.932  1.00 60.27           O  
ANISOU 3124  O   TYR B  72    10218   6707   5973    567   -349    307       O  
ATOM   3125  CB  TYR B  72      60.371  20.589   7.742  1.00 57.64           C  
ANISOU 3125  CB  TYR B  72    10061   6299   5542    436   -314    382       C  
ATOM   3126  CG  TYR B  72      60.096  20.280   6.283  1.00 62.29           C  
ANISOU 3126  CG  TYR B  72    10614   6899   6154    363   -346    422       C  
ATOM   3127  CD1 TYR B  72      60.140  18.971   5.805  1.00 66.47           C  
ANISOU 3127  CD1 TYR B  72    11321   7379   6554    376   -314    435       C  
ATOM   3128  CD2 TYR B  72      59.762  21.289   5.389  1.00 65.45           C  
ANISOU 3128  CD2 TYR B  72    10816   7354   6698    292   -403    446       C  
ATOM   3129  CE1 TYR B  72      59.872  18.679   4.474  1.00 69.83           C  
ANISOU 3129  CE1 TYR B  72    11714   7816   7002    321   -351    466       C  
ATOM   3130  CE2 TYR B  72      59.489  21.006   4.056  1.00 71.91           C  
ANISOU 3130  CE2 TYR B  72    11612   8180   7529    252   -436    476       C  
ATOM   3131  CZ  TYR B  72      59.547  19.700   3.602  1.00 73.93           C  
ANISOU 3131  CZ  TYR B  72    12034   8392   7664    266   -417    485       C  
ATOM   3132  OH  TYR B  72      59.276  19.421   2.277  1.00 74.18           O  
ANISOU 3132  OH  TYR B  72    12042   8434   7709    237   -459    510       O  
ATOM   3133  N   HIS B  73      62.584  20.809  10.358  1.00 54.38           N  
ANISOU 3133  N   HIS B  73     9774   5963   4926    810   -341    268       N  
ATOM   3134  CA  HIS B  73      62.668  21.056  11.804  1.00 54.35           C  
ANISOU 3134  CA  HIS B  73     9823   5938   4891    914   -316    210       C  
ATOM   3135  C   HIS B  73      61.295  20.951  12.463  1.00 54.42           C  
ANISOU 3135  C   HIS B  73     9908   5819   4951    807   -212    225       C  
ATOM   3136  O   HIS B  73      60.924  21.775  13.301  1.00 51.65           O  
ANISOU 3136  O   HIS B  73     9474   5458   4692    797   -209    205       O  
ATOM   3137  CB  HIS B  73      63.322  22.400  12.117  1.00 59.53           C  
ANISOU 3137  CB  HIS B  73    10250   6700   5667    955   -400    164       C  
ATOM   3138  CG  HIS B  73      64.802  22.404  11.910  1.00 62.64           C  
ANISOU 3138  CG  HIS B  73    10602   7210   5989   1104   -480    107       C  
ATOM   3139  ND1 HIS B  73      65.624  23.392  12.404  1.00 62.97           N  
ANISOU 3139  ND1 HIS B  73    10473   7349   6105   1186   -545     26       N  
ATOM   3140  CD2 HIS B  73      65.606  21.542  11.243  1.00 60.93           C  
ANISOU 3140  CD2 HIS B  73    10483   7029   5638   1184   -504    111       C  
ATOM   3141  CE1 HIS B  73      66.872  23.140  12.050  1.00 63.54           C  
ANISOU 3141  CE1 HIS B  73    10530   7512   6099   1307   -604    -29       C  
ATOM   3142  NE2 HIS B  73      66.887  22.022  11.346  1.00 62.18           N  
ANISOU 3142  NE2 HIS B  73    10524   7306   5795   1311   -583     28       N  
ATOM   3143  N   THR B  74      60.519  19.951  12.056  1.00 57.36           N  
ANISOU 3143  N   THR B  74    10430   6090   5274    720   -124    254       N  
ATOM   3144  CA  THR B  74      59.228  19.696  12.673  1.00 64.84           C  
ANISOU 3144  CA  THR B  74    11468   6901   6268    617     -2    251       C  
ATOM   3145  C   THR B  74      58.887  18.224  12.510  1.00 66.04           C  
ANISOU 3145  C   THR B  74    11874   6936   6285    607    119    252       C  
ATOM   3146  O   THR B  74      59.305  17.577  11.549  1.00 68.67           O  
ANISOU 3146  O   THR B  74    12245   7301   6544    608     90    273       O  
ATOM   3147  CB  THR B  74      58.110  20.561  12.075  1.00 60.77           C  
ANISOU 3147  CB  THR B  74    10737   6393   5960    413    -19    273       C  
ATOM   3148  OG1 THR B  74      56.863  20.247  12.713  1.00 58.55           O  
ANISOU 3148  OG1 THR B  74    10546   5977   5725    313    108    256       O  
ATOM   3149  CG2 THR B  74      57.983  20.317  10.581  1.00 54.69           C  
ANISOU 3149  CG2 THR B  74     9889   5667   5224    314    -65    302       C  
ATOM   3150  N   THR B  75      58.124  17.701  13.465  1.00 67.72           N  
ANISOU 3150  N   THR B  75    12265   7001   6464    600    266    229       N  
ATOM   3151  CA  THR B  75      57.686  16.317  13.433  1.00 73.53           C  
ANISOU 3151  CA  THR B  75    13257   7596   7083    579    421    218       C  
ATOM   3152  C   THR B  75      56.188  16.194  13.213  1.00 80.64           C  
ANISOU 3152  C   THR B  75    14118   8384   8136    357    533    200       C  
ATOM   3153  O   THR B  75      55.646  15.091  13.314  1.00 90.91           O  
ANISOU 3153  O   THR B  75    15628   9542   9372    314    697    173       O  
ATOM   3154  CB  THR B  75      58.079  15.610  14.731  1.00 77.72           C  
ANISOU 3154  CB  THR B  75    14084   8023   7424    776    541    192       C  
ATOM   3155  OG1 THR B  75      57.464  16.276  15.841  1.00 77.69           O  
ANISOU 3155  OG1 THR B  75    14060   7950   7510    776    595    174       O  
ATOM   3156  CG2 THR B  75      59.587  15.641  14.916  1.00 77.32           C  
ANISOU 3156  CG2 THR B  75    14073   8099   7208   1013    422    184       C  
ATOM   3157  N   ASP B  76      55.509  17.297  12.939  1.00 83.42           N  
ANISOU 3157  N   ASP B  76    14213   8796   8688    220    459    201       N  
ATOM   3158  CA  ASP B  76      54.099  17.254  12.588  1.00 87.44           C  
ANISOU 3158  CA  ASP B  76    14644   9227   9352     10    539    164       C  
ATOM   3159  C   ASP B  76      53.924  16.432  11.316  1.00 81.80           C  
ANISOU 3159  C   ASP B  76    13936   8519   8623    -81    539    150       C  
ATOM   3160  O   ASP B  76      54.470  16.808  10.266  1.00 77.46           O  
ANISOU 3160  O   ASP B  76    13240   8105   8088    -70    389    185       O  
ATOM   3161  CB  ASP B  76      53.562  18.672  12.396  1.00 91.64           C  
ANISOU 3161  CB  ASP B  76    14887   9857  10076    -90    428    172       C  
ATOM   3162  CG  ASP B  76      52.045  18.732  12.348  1.00 96.13           C  
ANISOU 3162  CG  ASP B  76    15378  10344  10803   -285    518    114       C  
ATOM   3163  OD1 ASP B  76      51.401  17.705  12.041  1.00 99.11           O  
ANISOU 3163  OD1 ASP B  76    15865  10617  11174   -378    639     59       O  
ATOM   3164  OD2 ASP B  76      51.493  19.819  12.622  1.00 95.21           O  
ANISOU 3164  OD2 ASP B  76    15086  10270  10820   -346    470    116       O  
ATOM   3165  N   PRO B  77      53.201  15.311  11.357  1.00 90.48           N  
ANISOU 3165  N   PRO B  77    15207   9472   9698   -165    708     97       N  
ATOM   3166  CA  PRO B  77      53.003  14.533  10.122  1.00 96.03           C  
ANISOU 3166  CA  PRO B  77    15905  10185  10396   -253    702     73       C  
ATOM   3167  C   PRO B  77      52.204  15.283   9.070  1.00 95.41           C  
ANISOU 3167  C   PRO B  77    15541  10203  10508   -404    588     40       C  
ATOM   3168  O   PRO B  77      52.452  15.113   7.868  1.00 93.45           O  
ANISOU 3168  O   PRO B  77    15217  10038  10251   -414    487     50       O  
ATOM   3169  CB  PRO B  77      52.268  13.277  10.616  1.00 96.29           C  
ANISOU 3169  CB  PRO B  77    16179  10018  10388   -324    942      4       C  
ATOM   3170  CG  PRO B  77      51.612  13.698  11.899  1.00 92.57           C  
ANISOU 3170  CG  PRO B  77    15744   9439   9989   -343   1062    -23       C  
ATOM   3171  CD  PRO B  77      52.559  14.679  12.523  1.00 90.64           C  
ANISOU 3171  CD  PRO B  77    15445   9302   9692   -176    926     53       C  
ATOM   3172  N   SER B  78      51.266  16.126   9.493  1.00 93.43           N  
ANISOU 3172  N   SER B  78    15138   9944  10418   -505    599      0       N  
ATOM   3173  CA  SER B  78      50.414  16.903   8.604  1.00 91.06           C  
ANISOU 3173  CA  SER B  78    14574   9737  10289   -631    498    -46       C  
ATOM   3174  C   SER B  78      51.105  18.134   8.029  1.00 90.21           C  
ANISOU 3174  C   SER B  78    14270   9802  10204   -551    299     30       C  
ATOM   3175  O   SER B  78      50.430  18.958   7.405  1.00 95.41           O  
ANISOU 3175  O   SER B  78    14717  10542  10992   -627    215      0       O  
ATOM   3176  CB  SER B  78      49.144  17.329   9.341  1.00 94.96           C  
ANISOU 3176  CB  SER B  78    14991  10156  10934   -763    594   -122       C  
ATOM   3177  OG  SER B  78      49.431  18.332  10.297  1.00 95.41           O  
ANISOU 3177  OG  SER B  78    15007  10239  11005   -692    559    -59       O  
ATOM   3178  N   PHE B  79      52.414  18.294   8.238  1.00 86.25           N  
ANISOU 3178  N   PHE B  79    13834   9356   9582   -397    234    117       N  
ATOM   3179  CA  PHE B  79      53.091  19.518   7.821  1.00 81.24           C  
ANISOU 3179  CA  PHE B  79    13017   8867   8986   -327     77    179       C  
ATOM   3180  C   PHE B  79      53.150  19.631   6.302  1.00 89.57           C  
ANISOU 3180  C   PHE B  79    13949  10015  10068   -341    -34    188       C  
ATOM   3181  O   PHE B  79      52.724  20.643   5.731  1.00 98.65           O  
ANISOU 3181  O   PHE B  79    14905  11248  11328   -379   -117    184       O  
ATOM   3182  CB  PHE B  79      54.494  19.576   8.421  1.00 74.94           C  
ANISOU 3182  CB  PHE B  79    12314   8100   8059   -159     45    242       C  
ATOM   3183  CG  PHE B  79      55.228  20.855   8.128  1.00 64.91           C  
ANISOU 3183  CG  PHE B  79    10857   6963   6842    -94    -87    290       C  
ATOM   3184  CD1 PHE B  79      54.971  21.997   8.875  1.00 62.86           C  
ANISOU 3184  CD1 PHE B  79    10474   6729   6682   -109   -102    292       C  
ATOM   3185  CD2 PHE B  79      56.182  20.916   7.127  1.00 56.55           C  
ANISOU 3185  CD2 PHE B  79     9755   5994   5737    -20   -183    333       C  
ATOM   3186  CE1 PHE B  79      55.646  23.179   8.621  1.00 59.39           C  
ANISOU 3186  CE1 PHE B  79     9869   6401   6297    -57   -202    328       C  
ATOM   3187  CE2 PHE B  79      56.859  22.094   6.868  1.00 53.68           C  
ANISOU 3187  CE2 PHE B  79     9227   5735   5432     33   -275    367       C  
ATOM   3188  CZ  PHE B  79      56.593  23.226   7.616  1.00 55.79           C  
ANISOU 3188  CZ  PHE B  79     9372   6025   5801     12   -280    361       C  
ATOM   3189  N   LEU B  80      53.690  18.612   5.628  1.00 88.44           N  
ANISOU 3189  N   LEU B  80    13930   9861   9815   -297    -35    201       N  
ATOM   3190  CA  LEU B  80      53.763  18.660   4.170  1.00 85.63           C  
ANISOU 3190  CA  LEU B  80    13475   9584   9476   -292   -139    212       C  
ATOM   3191  C   LEU B  80      52.378  18.774   3.553  1.00 79.38           C  
ANISOU 3191  C   LEU B  80    12554   8790   8815   -422   -140    120       C  
ATOM   3192  O   LEU B  80      52.194  19.474   2.552  1.00 76.75           O  
ANISOU 3192  O   LEU B  80    12066   8549   8545   -409   -246    121       O  
ATOM   3193  CB  LEU B  80      54.482  17.430   3.621  1.00 89.61           C  
ANISOU 3193  CB  LEU B  80    14152  10061   9834   -230   -129    239       C  
ATOM   3194  CG  LEU B  80      56.006  17.520   3.569  1.00 94.71           C  
ANISOU 3194  CG  LEU B  80    14856  10771  10359    -74   -197    330       C  
ATOM   3195  CD1 LEU B  80      56.615  17.317   4.950  1.00 98.32           C  
ANISOU 3195  CD1 LEU B  80    15456  11182  10720      2   -123    339       C  
ATOM   3196  CD2 LEU B  80      56.568  16.527   2.565  1.00 95.29           C  
ANISOU 3196  CD2 LEU B  80    15039  10849  10318    -22   -228    363       C  
ATOM   3197  N   GLY B  81      51.388  18.108   4.143  1.00 77.88           N  
ANISOU 3197  N   GLY B  81    12430   8496   8667   -538    -16     30       N  
ATOM   3198  CA  GLY B  81      50.036  18.235   3.629  1.00 81.18           C  
ANISOU 3198  CA  GLY B  81    12705   8919   9221   -664    -15    -87       C  
ATOM   3199  C   GLY B  81      49.552  19.671   3.638  1.00 83.26           C  
ANISOU 3199  C   GLY B  81    12760   9275   9599   -675    -98    -89       C  
ATOM   3200  O   GLY B  81      49.032  20.172   2.637  1.00 85.80           O  
ANISOU 3200  O   GLY B  81    12929   9684   9988   -680   -193   -134       O  
ATOM   3201  N   ARG B  82      49.750  20.366   4.763  1.00 82.81           N  
ANISOU 3201  N   ARG B  82    12704   9202   9557   -662    -64    -39       N  
ATOM   3202  CA  ARG B  82      49.343  21.765   4.852  1.00 78.53           C  
ANISOU 3202  CA  ARG B  82    11979   8745   9115   -671   -134    -29       C  
ATOM   3203  C   ARG B  82      50.261  22.672   4.042  1.00 75.90           C  
ANISOU 3203  C   ARG B  82    11556   8530   8751   -550   -263     61       C  
ATOM   3204  O   ARG B  82      49.811  23.702   3.524  1.00 74.30           O  
ANISOU 3204  O   ARG B  82    11197   8412   8621   -547   -335     51       O  
ATOM   3205  CB  ARG B  82      49.298  22.198   6.317  1.00 74.90           C  
ANISOU 3205  CB  ARG B  82    11556   8225   8677   -689    -56     -2       C  
ATOM   3206  CG  ARG B  82      48.219  21.495   7.140  1.00 78.62           C  
ANISOU 3206  CG  ARG B  82    12101   8567   9206   -815     90    -97       C  
ATOM   3207  CD  ARG B  82      48.220  21.963   8.594  1.00 84.25           C  
ANISOU 3207  CD  ARG B  82    12864   9215   9933   -809    164    -58       C  
ATOM   3208  NE  ARG B  82      49.368  21.443   9.332  1.00 86.35           N  
ANISOU 3208  NE  ARG B  82    13323   9422  10064   -690    209     16       N  
ATOM   3209  CZ  ARG B  82      50.486  22.125   9.554  1.00 86.72           C  
ANISOU 3209  CZ  ARG B  82    13353   9545  10052   -562    123    105       C  
ATOM   3210  NH1 ARG B  82      50.611  23.361   9.091  1.00 91.12           N  
ANISOU 3210  NH1 ARG B  82    13720  10226  10676   -547      4    141       N  
ATOM   3211  NH2 ARG B  82      51.483  21.572  10.231  1.00 86.30           N  
ANISOU 3211  NH2 ARG B  82    13476   9445   9870   -442    161    147       N  
ATOM   3212  N   TYR B  83      51.540  22.304   3.914  1.00 69.91           N  
ANISOU 3212  N   TYR B  83    10903   7775   7883   -445   -283    144       N  
ATOM   3213  CA  TYR B  83      52.470  23.101   3.120  1.00 65.92           C  
ANISOU 3213  CA  TYR B  83    10322   7366   7358   -334   -383    223       C  
ATOM   3214  C   TYR B  83      52.187  22.956   1.630  1.00 65.08           C  
ANISOU 3214  C   TYR B  83    10162   7309   7255   -310   -457    199       C  
ATOM   3215  O   TYR B  83      52.273  23.934   0.879  1.00 62.68           O  
ANISOU 3215  O   TYR B  83     9746   7083   6987   -249   -527    228       O  
ATOM   3216  CB  TYR B  83      53.907  22.696   3.437  1.00 70.25           C  
ANISOU 3216  CB  TYR B  83    10993   7905   7794   -230   -380    299       C  
ATOM   3217  CG  TYR B  83      54.924  23.145   2.409  1.00 75.93           C  
ANISOU 3217  CG  TYR B  83    11666   8702   8483   -121   -463    367       C  
ATOM   3218  CD1 TYR B  83      55.155  24.491   2.169  1.00 80.88           C  
ANISOU 3218  CD1 TYR B  83    12151   9398   9183    -83   -505    401       C  
ATOM   3219  CD2 TYR B  83      55.654  22.218   1.680  1.00 78.55           C  
ANISOU 3219  CD2 TYR B  83    12107   9027   8713    -54   -485    397       C  
ATOM   3220  CE1 TYR B  83      56.088  24.899   1.231  1.00 84.57           C  
ANISOU 3220  CE1 TYR B  83    12588   9916   9631     16   -553    459       C  
ATOM   3221  CE2 TYR B  83      56.585  22.615   0.745  1.00 80.15           C  
ANISOU 3221  CE2 TYR B  83    12273   9288   8894     46   -549    460       C  
ATOM   3222  CZ  TYR B  83      56.799  23.954   0.520  1.00 83.61           C  
ANISOU 3222  CZ  TYR B  83    12572   9784   9414     81   -576    489       C  
ATOM   3223  OH  TYR B  83      57.731  24.341  -0.420  1.00 80.34           O  
ANISOU 3223  OH  TYR B  83    12133   9408   8985    181   -614    548       O  
ATOM   3224  N   MET B  84      51.849  21.744   1.179  1.00 72.42           N  
ANISOU 3224  N   MET B  84    11181   8191   8144   -346   -435    145       N  
ATOM   3225  CA  MET B  84      51.512  21.561  -0.229  1.00 75.59           C  
ANISOU 3225  CA  MET B  84    11532   8640   8550   -312   -513    108       C  
ATOM   3226  C   MET B  84      50.183  22.220  -0.578  1.00 71.81           C  
ANISOU 3226  C   MET B  84    10893   8209   8181   -369   -546      2       C  
ATOM   3227  O   MET B  84      50.022  22.731  -1.692  1.00 73.34           O  
ANISOU 3227  O   MET B  84    11003   8478   8386   -289   -634     -9       O  
ATOM   3228  CB  MET B  84      51.483  20.075  -0.587  1.00 80.99           C  
ANISOU 3228  CB  MET B  84    12349   9259   9165   -340   -479     66       C  
ATOM   3229  CG  MET B  84      52.830  19.366  -0.485  1.00 86.99           C  
ANISOU 3229  CG  MET B  84    13275   9988   9790   -257   -465    169       C  
ATOM   3230  SD  MET B  84      53.877  19.469  -1.953  1.00 93.47           S  
ANISOU 3230  SD  MET B  84    14097  10880  10537   -102   -582    263       S  
ATOM   3231  CE  MET B  84      54.712  21.036  -1.714  1.00 94.70           C  
ANISOU 3231  CE  MET B  84    14145  11106  10731    -16   -620    355       C  
ATOM   3232  N   SER B  85      49.224  22.224   0.351  1.00 71.72           N  
ANISOU 3232  N   SER B  85    10847   8156   8247   -493   -473    -81       N  
ATOM   3233  CA  SER B  85      47.970  22.928   0.104  1.00 72.42           C  
ANISOU 3233  CA  SER B  85    10775   8303   8440   -543   -507   -189       C  
ATOM   3234  C   SER B  85      48.203  24.424  -0.058  1.00 73.37           C  
ANISOU 3234  C   SER B  85    10787   8514   8578   -456   -574   -116       C  
ATOM   3235  O   SER B  85      47.659  25.051  -0.974  1.00 78.79           O  
ANISOU 3235  O   SER B  85    11367   9283   9286   -396   -651   -166       O  
ATOM   3236  CB  SER B  85      46.989  22.676   1.247  1.00 73.08           C  
ANISOU 3236  CB  SER B  85    10848   8312   8605   -695   -400   -281       C  
ATOM   3237  OG  SER B  85      46.682  21.303   1.366  1.00 78.13           O  
ANISOU 3237  OG  SER B  85    11593   8854   9238   -782   -311   -364       O  
ATOM   3238  N   ALA B  86      49.025  25.010   0.816  1.00 76.29           N  
ANISOU 3238  N   ALA B  86    11189   8867   8930   -436   -540     -6       N  
ATOM   3239  CA  ALA B  86      49.313  26.439   0.736  1.00 72.55           C  
ANISOU 3239  CA  ALA B  86    10622   8467   8478   -363   -580     63       C  
ATOM   3240  C   ALA B  86      50.113  26.787  -0.516  1.00 68.95           C  
ANISOU 3240  C   ALA B  86    10167   8064   7965   -219   -648    129       C  
ATOM   3241  O   ALA B  86      49.856  27.812  -1.157  1.00 61.93           O  
ANISOU 3241  O   ALA B  86     9193   7243   7095   -147   -689    132       O  
ATOM   3242  CB  ALA B  86      50.056  26.890   1.995  1.00 63.68           C  
ANISOU 3242  CB  ALA B  86     9530   7309   7356   -377   -525    148       C  
ATOM   3243  N   LEU B  87      51.104  25.961  -0.865  1.00 70.03           N  
ANISOU 3243  N   LEU B  87    10414   8166   8027   -166   -650    185       N  
ATOM   3244  CA  LEU B  87      51.910  26.235  -2.050  1.00 69.73           C  
ANISOU 3244  CA  LEU B  87    10391   8164   7939    -27   -702    252       C  
ATOM   3245  C   LEU B  87      51.067  26.213  -3.315  1.00 78.22           C  
ANISOU 3245  C   LEU B  87    11420   9286   9014     34   -772    177       C  
ATOM   3246  O   LEU B  87      51.406  26.880  -4.300  1.00 82.28           O  
ANISOU 3246  O   LEU B  87    11920   9839   9504    167   -810    220       O  
ATOM   3247  CB  LEU B  87      53.050  25.222  -2.154  1.00 66.94           C  
ANISOU 3247  CB  LEU B  87    10168   7765   7501     11   -694    316       C  
ATOM   3248  CG  LEU B  87      54.062  25.472  -3.270  1.00 61.86           C  
ANISOU 3248  CG  LEU B  87     9553   7144   6806    154   -733    399       C  
ATOM   3249  CD1 LEU B  87      54.663  26.850  -3.138  1.00 57.97           C  
ANISOU 3249  CD1 LEU B  87     8989   6681   6357    211   -706    463       C  
ATOM   3250  CD2 LEU B  87      55.146  24.413  -3.257  1.00 66.59           C  
ANISOU 3250  CD2 LEU B  87    10282   7702   7317    183   -726    455       C  
ATOM   3251  N   ASN B  88      49.961  25.469  -3.302  1.00 83.51           N  
ANISOU 3251  N   ASN B  88    12067   9949   9713    -52   -782     52       N  
ATOM   3252  CA  ASN B  88      49.079  25.432  -4.458  1.00 84.85           C  
ANISOU 3252  CA  ASN B  88    12175  10175   9887     13   -860    -53       C  
ATOM   3253  C   ASN B  88      48.411  26.781  -4.697  1.00 80.35           C  
ANISOU 3253  C   ASN B  88    11490   9684   9353     76   -891    -84       C  
ATOM   3254  O   ASN B  88      48.036  27.095  -5.832  1.00 84.44           O  
ANISOU 3254  O   ASN B  88    11977  10263   9844    209   -963   -133       O  
ATOM   3255  CB  ASN B  88      48.035  24.334  -4.267  1.00 92.69           C  
ANISOU 3255  CB  ASN B  88    13153  11141  10923   -113   -849   -205       C  
ATOM   3256  CG  ASN B  88      47.407  23.902  -5.565  1.00 97.47           C  
ANISOU 3256  CG  ASN B  88    13723  11797  11516    -31   -938   -321       C  
ATOM   3257  OD1 ASN B  88      46.414  24.477  -6.015  1.00103.43           O  
ANISOU 3257  OD1 ASN B  88    14360  12627  12310      9   -995   -439       O  
ATOM   3258  ND2 ASN B  88      47.992  22.885  -6.187  1.00 97.60           N  
ANISOU 3258  ND2 ASN B  88    13841  11775  11470      9   -956   -294       N  
ATOM   3259  N   HIS B  89      48.260  27.590  -3.647  1.00 77.24           N  
ANISOU 3259  N   HIS B  89    11044   9292   9010     -1   -838    -57       N  
ATOM   3260  CA  HIS B  89      47.698  28.930  -3.765  1.00 74.63           C  
ANISOU 3260  CA  HIS B  89    10619   9034   8702     57   -855    -71       C  
ATOM   3261  C   HIS B  89      48.779  29.989  -3.920  1.00 76.12           C  
ANISOU 3261  C   HIS B  89    10840   9225   8859    166   -823     73       C  
ATOM   3262  O   HIS B  89      48.640  30.899  -4.745  1.00 83.04           O  
ANISOU 3262  O   HIS B  89    11696  10152   9705    302   -845     79       O  
ATOM   3263  CB  HIS B  89      46.851  29.270  -2.536  1.00 74.28           C  
ANISOU 3263  CB  HIS B  89    10496   8992   8736    -90   -811   -125       C  
ATOM   3264  CG  HIS B  89      45.557  28.524  -2.455  1.00 77.60           C  
ANISOU 3264  CG  HIS B  89    10852   9421   9211   -193   -829   -297       C  
ATOM   3265  ND1 HIS B  89      45.483  27.204  -2.065  1.00 78.39           N  
ANISOU 3265  ND1 HIS B  89    11008   9443   9333   -310   -787   -351       N  
ATOM   3266  CD2 HIS B  89      44.284  28.922  -2.681  1.00 79.83           C  
ANISOU 3266  CD2 HIS B  89    11018   9779   9533   -199   -872   -439       C  
ATOM   3267  CE1 HIS B  89      44.220  26.815  -2.072  1.00 82.58           C  
ANISOU 3267  CE1 HIS B  89    11453   9994   9931   -394   -795   -523       C  
ATOM   3268  NE2 HIS B  89      43.472  27.840  -2.441  1.00 83.25           N  
ANISOU 3268  NE2 HIS B  89    11423  10178  10028   -328   -855   -585       N  
ATOM   3269  N   THR B  90      49.858  29.894  -3.139  1.00 74.55           N  
ANISOU 3269  N   THR B  90    10695   8968   8664    116   -763    177       N  
ATOM   3270  CA  THR B  90      50.863  30.951  -3.158  1.00 77.54           C  
ANISOU 3270  CA  THR B  90    11080   9344   9036    196   -716    289       C  
ATOM   3271  C   THR B  90      51.564  31.039  -4.505  1.00 79.50           C  
ANISOU 3271  C   THR B  90    11392   9591   9224    361   -732    341       C  
ATOM   3272  O   THR B  90      51.996  32.126  -4.902  1.00 77.23           O  
ANISOU 3272  O   THR B  90    11100   9310   8933    460   -687    400       O  
ATOM   3273  CB  THR B  90      51.887  30.747  -2.036  1.00 74.88           C  
ANISOU 3273  CB  THR B  90    10777   8956   8719    118   -659    361       C  
ATOM   3274  OG1 THR B  90      52.598  29.519  -2.229  1.00 73.49           O  
ANISOU 3274  OG1 THR B  90    10696   8735   8491    123   -673    379       O  
ATOM   3275  CG2 THR B  90      51.193  30.718  -0.681  1.00 74.43           C  
ANISOU 3275  CG2 THR B  90    10676   8888   8717    -24   -634    317       C  
ATOM   3276  N   LYS B  91      51.666  29.920  -5.227  1.00 86.51           N  
ANISOU 3276  N   LYS B  91    12345  10460  10063    397   -784    319       N  
ATOM   3277  CA  LYS B  91      52.296  29.946  -6.542  1.00 88.50           C  
ANISOU 3277  CA  LYS B  91    12668  10703  10254    566   -802    371       C  
ATOM   3278  C   LYS B  91      51.451  30.691  -7.569  1.00 80.83           C  
ANISOU 3278  C   LYS B  91    11672   9785   9256    710   -839    315       C  
ATOM   3279  O   LYS B  91      51.966  31.056  -8.630  1.00 76.52           O  
ANISOU 3279  O   LYS B  91    11192   9224   8659    880   -829    369       O  
ATOM   3280  CB  LYS B  91      52.584  28.517  -7.018  1.00 92.37           C  
ANISOU 3280  CB  LYS B  91    13239  11162  10694    568   -854    361       C  
ATOM   3281  CG  LYS B  91      51.349  27.704  -7.377  1.00 98.43           C  
ANISOU 3281  CG  LYS B  91    13979  11962  11459    538   -932    226       C  
ATOM   3282  CD  LYS B  91      51.713  26.273  -7.767  1.00101.88           C  
ANISOU 3282  CD  LYS B  91    14505  12358  11846    527   -968    224       C  
ATOM   3283  CE  LYS B  91      50.494  25.506  -8.276  1.00104.06           C  
ANISOU 3283  CE  LYS B  91    14742  12667  12130    509  -1041     69       C  
ATOM   3284  NZ  LYS B  91      50.822  24.095  -8.626  1.00102.29           N  
ANISOU 3284  NZ  LYS B  91    14610  12397  11858    488  -1065     64       N  
ATOM   3285  N   LYS B  92      50.177  30.939  -7.268  1.00 79.88           N  
ANISOU 3285  N   LYS B  92    11463   9724   9162    659   -875    204       N  
ATOM   3286  CA  LYS B  92      49.303  31.727  -8.123  1.00 78.38           C  
ANISOU 3286  CA  LYS B  92    11244   9601   8935    808   -915    133       C  
ATOM   3287  C   LYS B  92      49.276  33.203  -7.737  1.00 82.00           C  
ANISOU 3287  C   LYS B  92    11671  10079   9405    836   -839    182       C  
ATOM   3288  O   LYS B  92      48.620  33.995  -8.421  1.00 83.95           O  
ANISOU 3288  O   LYS B  92    11915  10381   9603    981   -855    134       O  
ATOM   3289  CB  LYS B  92      47.881  31.160  -8.085  1.00 81.03           C  
ANISOU 3289  CB  LYS B  92    11491  10004   9291    748  -1003    -42       C  
ATOM   3290  CG  LYS B  92      47.756  29.744  -8.628  1.00 91.50           C  
ANISOU 3290  CG  LYS B  92    12845  11316  10604    736  -1075   -117       C  
ATOM   3291  CD  LYS B  92      46.336  29.211  -8.453  1.00100.27           C  
ANISOU 3291  CD  LYS B  92    13847  12488  11763    646  -1140   -314       C  
ATOM   3292  CE  LYS B  92      46.223  27.753  -8.873  1.00103.69           C  
ANISOU 3292  CE  LYS B  92    14304  12895  12199    605  -1191   -398       C  
ATOM   3293  NZ  LYS B  92      44.879  27.190  -8.557  1.00103.75           N  
ANISOU 3293  NZ  LYS B  92    14194  12946  12280    482  -1226   -605       N  
ATOM   3294  N   TRP B  93      49.964  33.590  -6.664  1.00 79.45           N  
ANISOU 3294  N   TRP B  93    11331   9716   9141    712   -756    269       N  
ATOM   3295  CA  TRP B  93      50.003  34.984  -6.257  1.00 71.97           C  
ANISOU 3295  CA  TRP B  93    10354   8780   8211    728   -674    317       C  
ATOM   3296  C   TRP B  93      51.000  35.764  -7.107  1.00 65.35           C  
ANISOU 3296  C   TRP B  93     9604   7893   7332    891   -586    416       C  
ATOM   3297  O   TRP B  93      51.837  35.199  -7.817  1.00 68.79           O  
ANISOU 3297  O   TRP B  93    10118   8276   7741    967   -582    465       O  
ATOM   3298  CB  TRP B  93      50.388  35.122  -4.786  1.00 71.70           C  
ANISOU 3298  CB  TRP B  93    10264   8720   8258    545   -621    362       C  
ATOM   3299  CG  TRP B  93      49.331  34.737  -3.816  1.00 69.73           C  
ANISOU 3299  CG  TRP B  93     9934   8506   8055    392   -668    276       C  
ATOM   3300  CD1 TRP B  93      48.030  34.450  -4.090  1.00 69.28           C  
ANISOU 3300  CD1 TRP B  93     9826   8510   7986    390   -744    153       C  
ATOM   3301  CD2 TRP B  93      49.474  34.641  -2.396  1.00 71.08           C  
ANISOU 3301  CD2 TRP B  93    10064   8649   8295    228   -634    298       C  
ATOM   3302  NE1 TRP B  93      47.353  34.158  -2.928  1.00 66.66           N  
ANISOU 3302  NE1 TRP B  93     9426   8181   7722    219   -746    100       N  
ATOM   3303  CE2 TRP B  93      48.219  34.270  -1.874  1.00 65.81           C  
ANISOU 3303  CE2 TRP B  93     9333   8015   7658    125   -679    195       C  
ATOM   3304  CE3 TRP B  93      50.544  34.822  -1.517  1.00 72.74           C  
ANISOU 3304  CE3 TRP B  93    10284   8809   8544    168   -569    383       C  
ATOM   3305  CZ2 TRP B  93      48.005  34.080  -0.514  1.00 63.94           C  
ANISOU 3305  CZ2 TRP B  93     9061   7748   7484    -30   -652    191       C  
ATOM   3306  CZ3 TRP B  93      50.330  34.632  -0.166  1.00 73.01           C  
ANISOU 3306  CZ3 TRP B  93    10282   8827   8634     27   -557    372       C  
ATOM   3307  CH2 TRP B  93      49.071  34.264   0.322  1.00 67.77           C  
ANISOU 3307  CH2 TRP B  93     9574   8182   7994    -68   -593    286       C  
ATOM   3308  N   LYS B  94      50.918  37.084  -7.004  1.00 61.73           N  
ANISOU 3308  N   LYS B  94     9138   7443   6873    941   -501    447       N  
ATOM   3309  CA  LYS B  94      51.837  37.990  -7.677  1.00 64.48           C  
ANISOU 3309  CA  LYS B  94     9573   7728   7198   1081   -375    536       C  
ATOM   3310  C   LYS B  94      52.733  38.644  -6.636  1.00 66.77           C  
ANISOU 3310  C   LYS B  94     9817   7974   7580    953   -261    607       C  
ATOM   3311  O   LYS B  94      52.248  39.098  -5.594  1.00 74.57           O  
ANISOU 3311  O   LYS B  94    10719   9000   8613    830   -260    587       O  
ATOM   3312  CB  LYS B  94      51.074  39.041  -8.488  1.00 65.80           C  
ANISOU 3312  CB  LYS B  94     9793   7931   7280   1268   -341    508       C  
ATOM   3313  CG  LYS B  94      50.347  38.455  -9.678  1.00 69.68           C  
ANISOU 3313  CG  LYS B  94    10340   8464   7672   1443   -451    429       C  
ATOM   3314  CD  LYS B  94      51.347  37.950 -10.702  1.00 77.00           C  
ANISOU 3314  CD  LYS B  94    11383   9305   8567   1575   -422    495       C  
ATOM   3315  CE  LYS B  94      50.672  37.179 -11.816  1.00 87.46           C  
ANISOU 3315  CE  LYS B  94    12756  10672   9802   1739   -551    409       C  
ATOM   3316  NZ  LYS B  94      50.087  35.913 -11.294  1.00 92.69           N  
ANISOU 3316  NZ  LYS B  94    13316  11394  10510   1574   -696    317       N  
ATOM   3317  N   TYR B  95      54.036  38.694  -6.920  1.00 63.73           N  
ANISOU 3317  N   TYR B  95     9483   7509   7224    986   -167    679       N  
ATOM   3318  CA  TYR B  95      55.036  39.193  -5.980  1.00 65.04           C  
ANISOU 3318  CA  TYR B  95     9592   7634   7486    871    -65    722       C  
ATOM   3319  C   TYR B  95      55.770  40.370  -6.612  1.00 67.02           C  
ANISOU 3319  C   TYR B  95     9905   7812   7749    986    112    775       C  
ATOM   3320  O   TYR B  95      56.883  40.214  -7.135  1.00 75.22           O  
ANISOU 3320  O   TYR B  95    10994   8775   8810   1039    189    816       O  
ATOM   3321  CB  TYR B  95      56.000  38.083  -5.558  1.00 59.65           C  
ANISOU 3321  CB  TYR B  95     8894   6925   6844    782   -109    734       C  
ATOM   3322  CG  TYR B  95      55.287  36.906  -4.935  1.00 61.38           C  
ANISOU 3322  CG  TYR B  95     9078   7197   7047    674   -253    681       C  
ATOM   3323  CD1 TYR B  95      54.962  36.905  -3.584  1.00 66.26           C  
ANISOU 3323  CD1 TYR B  95     9611   7847   7719    522   -278    653       C  
ATOM   3324  CD2 TYR B  95      54.926  35.805  -5.695  1.00 60.32           C  
ANISOU 3324  CD2 TYR B  95     9003   7071   6845    727   -352    657       C  
ATOM   3325  CE1 TYR B  95      54.299  35.842  -3.007  1.00 67.11           C  
ANISOU 3325  CE1 TYR B  95     9703   7981   7815    425   -380    603       C  
ATOM   3326  CE2 TYR B  95      54.263  34.729  -5.124  1.00 63.95           C  
ANISOU 3326  CE2 TYR B  95     9436   7564   7297    619   -457    599       C  
ATOM   3327  CZ  TYR B  95      53.952  34.754  -3.778  1.00 64.87           C  
ANISOU 3327  CZ  TYR B  95     9477   7699   7469    468   -462    574       C  
ATOM   3328  OH  TYR B  95      53.288  33.695  -3.197  1.00 60.06           O  
ANISOU 3328  OH  TYR B  95     8859   7104   6856    363   -539    515       O  
ATOM   3329  N   PRO B  96      55.177  41.563  -6.585  1.00 57.12           N  
ANISOU 3329  N   PRO B  96     8655   6570   6477   1029    192    774       N  
ATOM   3330  CA  PRO B  96      55.830  42.718  -7.203  1.00 58.02           C  
ANISOU 3330  CA  PRO B  96     8849   6599   6597   1143    391    821       C  
ATOM   3331  C   PRO B  96      56.998  43.219  -6.375  1.00 60.97           C  
ANISOU 3331  C   PRO B  96     9144   6918   7102   1016    519    839       C  
ATOM   3332  O   PRO B  96      56.988  43.172  -5.144  1.00 63.33           O  
ANISOU 3332  O   PRO B  96     9323   7266   7475    852    469    813       O  
ATOM   3333  CB  PRO B  96      54.710  43.762  -7.265  1.00 59.58           C  
ANISOU 3333  CB  PRO B  96     9073   6843   6723   1216    422    805       C  
ATOM   3334  CG  PRO B  96      53.827  43.413  -6.121  1.00 55.84           C  
ANISOU 3334  CG  PRO B  96     8472   6471   6273   1052    276    757       C  
ATOM   3335  CD  PRO B  96      53.863  41.912  -6.014  1.00 54.02           C  
ANISOU 3335  CD  PRO B  96     8205   6268   6053    981    117    727       C  
ATOM   3336  N   GLN B  97      58.008  43.726  -7.075  1.00 66.07           N  
ANISOU 3336  N   GLN B  97     9862   7459   7781   1103    694    872       N  
ATOM   3337  CA  GLN B  97      59.178  44.345  -6.456  1.00 71.06           C  
ANISOU 3337  CA  GLN B  97    10420   8031   8550   1003    848    866       C  
ATOM   3338  C   GLN B  97      58.839  45.793  -6.141  1.00 75.50           C  
ANISOU 3338  C   GLN B  97    10978   8575   9132    997   1002    867       C  
ATOM   3339  O   GLN B  97      58.925  46.666  -7.007  1.00 85.68           O  
ANISOU 3339  O   GLN B  97    12390   9779  10386   1134   1183    897       O  
ATOM   3340  CB  GLN B  97      60.388  44.255  -7.378  1.00 76.14           C  
ANISOU 3340  CB  GLN B  97    11140   8559   9229   1094    987    890       C  
ATOM   3341  CG  GLN B  97      60.941  42.859  -7.574  1.00 81.33           C  
ANISOU 3341  CG  GLN B  97    11791   9230   9879   1082    850    891       C  
ATOM   3342  CD  GLN B  97      61.626  42.325  -6.334  1.00 92.60           C  
ANISOU 3342  CD  GLN B  97    13067  10712  11406    906    773    840       C  
ATOM   3343  OE1 GLN B  97      62.003  43.085  -5.439  1.00 95.67           O  
ANISOU 3343  OE1 GLN B  97    13349  11102  11897    802    858    798       O  
ATOM   3344  NE2 GLN B  97      61.800  41.010  -6.277  1.00 99.72           N  
ANISOU 3344  NE2 GLN B  97    13965  11655  12270    883    615    837       N  
ATOM   3345  N   VAL B  98      58.438  46.059  -4.907  1.00 75.22           N  
ANISOU 3345  N   VAL B  98    10819   8614   9146    850    940    838       N  
ATOM   3346  CA  VAL B  98      58.054  47.402  -4.489  1.00 78.92           C  
ANISOU 3346  CA  VAL B  98    11277   9078   9631    830   1069    842       C  
ATOM   3347  C   VAL B  98      59.247  48.026  -3.783  1.00 83.71           C  
ANISOU 3347  C   VAL B  98    11782   9627  10398    715   1222    808       C  
ATOM   3348  O   VAL B  98      59.554  47.674  -2.641  1.00 87.21           O  
ANISOU 3348  O   VAL B  98    12082  10124  10929    569   1128    765       O  
ATOM   3349  CB  VAL B  98      56.821  47.384  -3.582  1.00 80.53           C  
ANISOU 3349  CB  VAL B  98    11410   9397   9790    746    911    830       C  
ATOM   3350  CG1 VAL B  98      56.447  48.807  -3.197  1.00 78.40           C  
ANISOU 3350  CG1 VAL B  98    11142   9122   9526    735   1051    842       C  
ATOM   3351  CG2 VAL B  98      55.657  46.666  -4.269  1.00 84.02           C  
ANISOU 3351  CG2 VAL B  98    11928   9906  10092    850    752    831       C  
ATOM   3352  N   ASN B  99      59.915  48.961  -4.461  1.00 88.26           N  
ANISOU 3352  N   ASN B  99    12435  10087  11012    789   1467    817       N  
ATOM   3353  CA  ASN B  99      61.040  49.704  -3.888  1.00 92.36           C  
ANISOU 3353  CA  ASN B  99    12855  10542  11698    685   1649    763       C  
ATOM   3354  C   ASN B  99      62.157  48.756  -3.446  1.00 84.87           C  
ANISOU 3354  C   ASN B  99    11781   9605  10861    593   1568    702       C  
ATOM   3355  O   ASN B  99      62.621  48.789  -2.304  1.00 82.10           O  
ANISOU 3355  O   ASN B  99    11271   9302  10622    457   1528    632       O  
ATOM   3356  CB  ASN B  99      60.571  50.592  -2.729  1.00 99.66           C  
ANISOU 3356  CB  ASN B  99    13677  11522  12668    567   1659    741       C  
ATOM   3357  CG  ASN B  99      61.540  51.720  -2.419  1.00104.21           C  
ANISOU 3357  CG  ASN B  99    14191  12009  13397    498   1910    685       C  
ATOM   3358  OD1 ASN B  99      62.488  51.964  -3.166  1.00109.77           O  
ANISOU 3358  OD1 ASN B  99    14944  12595  14168    548   2108    663       O  
ATOM   3359  ND2 ASN B  99      61.296  52.423  -1.316  1.00 99.59           N  
ANISOU 3359  ND2 ASN B  99    13495  11473  12872    383   1910    656       N  
ATOM   3360  N   GLY B 100      62.594  47.903  -4.375  1.00 81.56           N  
ANISOU 3360  N   GLY B 100    11442   9144  10402    685   1542    724       N  
ATOM   3361  CA  GLY B 100      63.658  46.952  -4.122  1.00 76.22           C  
ANISOU 3361  CA  GLY B 100    10674   8479   9805    627   1468    671       C  
ATOM   3362  C   GLY B 100      63.298  45.783  -3.230  1.00 75.78           C  
ANISOU 3362  C   GLY B 100    10534   8548   9710    547   1201    654       C  
ATOM   3363  O   GLY B 100      64.105  44.854  -3.107  1.00 79.32           O  
ANISOU 3363  O   GLY B 100    10938   9013  10188    526   1123    617       O  
ATOM   3364  N   LEU B 101      62.126  45.790  -2.604  1.00 75.24           N  
ANISOU 3364  N   LEU B 101    10453   8563   9572    506   1070    677       N  
ATOM   3365  CA  LEU B 101      61.680  44.713  -1.735  1.00 70.45           C  
ANISOU 3365  CA  LEU B 101     9786   8056   8926    432    842    662       C  
ATOM   3366  C   LEU B 101      60.581  43.903  -2.415  1.00 70.83           C  
ANISOU 3366  C   LEU B 101     9946   8138   8829    507    701    721       C  
ATOM   3367  O   LEU B 101      59.914  44.368  -3.345  1.00 76.12           O  
ANISOU 3367  O   LEU B 101    10721   8779   9421    613    757    766       O  
ATOM   3368  CB  LEU B 101      61.173  45.269  -0.400  1.00 67.58           C  
ANISOU 3368  CB  LEU B 101     9314   7756   8608    318    799    632       C  
ATOM   3369  CG  LEU B 101      62.184  46.085   0.407  1.00 67.54           C  
ANISOU 3369  CG  LEU B 101     9177   7731   8753    240    921    553       C  
ATOM   3370  CD1 LEU B 101      61.504  46.767   1.580  1.00 64.06           C  
ANISOU 3370  CD1 LEU B 101     8654   7346   8341    151    886    542       C  
ATOM   3371  CD2 LEU B 101      63.326  45.202   0.884  1.00 69.33           C  
ANISOU 3371  CD2 LEU B 101     9320   7980   9043    210    851    474       C  
ATOM   3372  N   THR B 102      60.381  42.685  -1.922  1.00 63.76           N  
ANISOU 3372  N   THR B 102     9029   7304   7895    458    520    707       N  
ATOM   3373  CA  THR B 102      59.396  41.767  -2.482  1.00 59.88           C  
ANISOU 3373  CA  THR B 102     8622   6847   7284    509    381    737       C  
ATOM   3374  C   THR B 102      58.140  41.789  -1.620  1.00 63.43           C  
ANISOU 3374  C   THR B 102     9028   7369   7704    429    274    725       C  
ATOM   3375  O   THR B 102      58.158  41.332  -0.473  1.00 70.58           O  
ANISOU 3375  O   THR B 102     9861   8313   8645    324    192    694       O  
ATOM   3376  CB  THR B 102      59.962  40.354  -2.575  1.00 57.00           C  
ANISOU 3376  CB  THR B 102     8280   6487   6889    508    271    729       C  
ATOM   3377  OG1 THR B 102      61.136  40.366  -3.394  1.00 59.12           O  
ANISOU 3377  OG1 THR B 102     8588   6688   7188    584    374    741       O  
ATOM   3378  CG2 THR B 102      58.943  39.424  -3.191  1.00 61.79           C  
ANISOU 3378  CG2 THR B 102     8969   7123   7384    555    140    747       C  
ATOM   3379  N   SER B 103      57.055  42.313  -2.177  1.00 64.68           N  
ANISOU 3379  N   SER B 103     9238   7546   7793    493    278    744       N  
ATOM   3380  CA  SER B 103      55.750  42.361  -1.539  1.00 59.61           C  
ANISOU 3380  CA  SER B 103     8558   6973   7116    431    182    727       C  
ATOM   3381  C   SER B 103      54.854  41.304  -2.179  1.00 56.75           C  
ANISOU 3381  C   SER B 103     8253   6648   6662    478     47    707       C  
ATOM   3382  O   SER B 103      55.306  40.486  -2.992  1.00 61.43           O  
ANISOU 3382  O   SER B 103     8910   7212   7218    548     18    713       O  
ATOM   3383  CB  SER B 103      55.155  43.770  -1.654  1.00 60.72           C  
ANISOU 3383  CB  SER B 103     8707   7120   7242    473    284    745       C  
ATOM   3384  OG  SER B 103      53.943  43.897  -0.924  1.00 54.83           O  
ANISOU 3384  OG  SER B 103     7913   6448   6473    404    195    725       O  
ATOM   3385  N   ILE B 104      53.570  41.336  -1.831  1.00 49.19           N  
ANISOU 3385  N   ILE B 104     7267   5754   5669    441    -34    675       N  
ATOM   3386  CA  ILE B 104      52.590  40.392  -2.351  1.00 54.79           C  
ANISOU 3386  CA  ILE B 104     8005   6506   6307    470   -160    626       C  
ATOM   3387  C   ILE B 104      51.366  41.170  -2.805  1.00 61.28           C  
ANISOU 3387  C   ILE B 104     8836   7387   7062    550   -169    595       C  
ATOM   3388  O   ILE B 104      50.810  41.960  -2.032  1.00 57.62           O  
ANISOU 3388  O   ILE B 104     8315   6958   6620    485   -149    593       O  
ATOM   3389  CB  ILE B 104      52.184  39.345  -1.296  1.00 54.93           C  
ANISOU 3389  CB  ILE B 104     7966   6545   6359    321   -264    584       C  
ATOM   3390  CG1 ILE B 104      53.414  38.738  -0.626  1.00 59.82           C  
ANISOU 3390  CG1 ILE B 104     8581   7116   7034    253   -247    610       C  
ATOM   3391  CG2 ILE B 104      51.322  38.266  -1.925  1.00 53.41           C  
ANISOU 3391  CG2 ILE B 104     7802   6382   6109    345   -374    518       C  
ATOM   3392  CD1 ILE B 104      53.080  37.814   0.512  1.00 65.55           C  
ANISOU 3392  CD1 ILE B 104     9276   7845   7783    125   -321    575       C  
ATOM   3393  N   LYS B 105      50.945  40.946  -4.052  1.00 63.75           N  
ANISOU 3393  N   LYS B 105     9222   7715   7285    703   -204    565       N  
ATOM   3394  CA  LYS B 105      49.693  41.520  -4.525  1.00 60.86           C  
ANISOU 3394  CA  LYS B 105     8864   7424   6836    803   -240    507       C  
ATOM   3395  C   LYS B 105      48.535  40.952  -3.715  1.00 54.27           C  
ANISOU 3395  C   LYS B 105     7930   6663   6026    669   -361    422       C  
ATOM   3396  O   LYS B 105      48.439  39.737  -3.528  1.00 53.15           O  
ANISOU 3396  O   LYS B 105     7761   6518   5915    585   -448    376       O  
ATOM   3397  CB  LYS B 105      49.497  41.227  -6.011  1.00 68.39           C  
ANISOU 3397  CB  LYS B 105     9917   8382   7686   1011   -273    474       C  
ATOM   3398  CG  LYS B 105      48.226  41.836  -6.585  1.00 79.09           C  
ANISOU 3398  CG  LYS B 105    11288   9826   8937   1154   -316    394       C  
ATOM   3399  CD  LYS B 105      47.915  41.310  -7.979  1.00 84.13           C  
ANISOU 3399  CD  LYS B 105    12010  10483   9473   1364   -388    330       C  
ATOM   3400  CE  LYS B 105      46.581  41.851  -8.466  1.00 87.13           C  
ANISOU 3400  CE  LYS B 105    12391  10972   9743   1515   -453    220       C  
ATOM   3401  NZ  LYS B 105      45.532  41.733  -7.410  1.00 90.05           N  
ANISOU 3401  NZ  LYS B 105    12615  11431  10167   1338   -541    135       N  
ATOM   3402  N   TRP B 106      47.647  41.835  -3.254  1.00 56.23           N  
ANISOU 3402  N   TRP B 106     8132   6973   6259    653   -355    398       N  
ATOM   3403  CA  TRP B 106      46.607  41.440  -2.310  1.00 60.35           C  
ANISOU 3403  CA  TRP B 106     8553   7552   6825    505   -444    324       C  
ATOM   3404  C   TRP B 106      45.730  40.318  -2.858  1.00 62.24           C  
ANISOU 3404  C   TRP B 106     8768   7840   7040    521   -568    198       C  
ATOM   3405  O   TRP B 106      45.233  40.386  -3.986  1.00 66.25           O  
ANISOU 3405  O   TRP B 106     9313   8399   7458    689   -612    130       O  
ATOM   3406  CB  TRP B 106      45.744  42.641  -1.906  1.00 68.16           C  
ANISOU 3406  CB  TRP B 106     9506   8608   7783    515   -420    316       C  
ATOM   3407  CG  TRP B 106      44.297  42.482  -2.235  1.00 92.06           C  
ANISOU 3407  CG  TRP B 106    12486  11739  10754    559   -525    184       C  
ATOM   3408  CD1 TRP B 106      43.680  42.777  -3.421  1.00101.80           C  
ANISOU 3408  CD1 TRP B 106    13767  13043  11870    762   -562    107       C  
ATOM   3409  CD2 TRP B 106      43.304  41.851  -1.416  1.00105.26           C  
ANISOU 3409  CD2 TRP B 106    14052  13453  12489    405   -610     91       C  
ATOM   3410  NE1 TRP B 106      42.346  42.440  -3.357  1.00108.15           N  
ANISOU 3410  NE1 TRP B 106    14483  13946  12662    741   -673    -39       N  
ATOM   3411  CE2 TRP B 106      42.093  41.860  -2.142  1.00109.49           C  
ANISOU 3411  CE2 TRP B 106    14555  14094  12950    513   -696    -51       C  
ATOM   3412  CE3 TRP B 106      43.316  41.304  -0.127  1.00108.13           C  
ANISOU 3412  CE3 TRP B 106    14350  13770  12963    198   -611    106       C  
ATOM   3413  CZ2 TRP B 106      40.907  41.344  -1.622  1.00109.60           C  
ANISOU 3413  CZ2 TRP B 106    14460  14170  13014    400   -778   -184       C  
ATOM   3414  CZ3 TRP B 106      42.137  40.793   0.388  1.00110.65           C  
ANISOU 3414  CZ3 TRP B 106    14581  14134  13325     91   -680     -9       C  
ATOM   3415  CH2 TRP B 106      40.949  40.816  -0.359  1.00111.33           C  
ANISOU 3415  CH2 TRP B 106    14622  14325  13352    182   -760   -156       C  
ATOM   3416  N   ALA B 107      45.574  39.267  -2.052  1.00 60.10           N  
ANISOU 3416  N   ALA B 107     8441   7546   6849    352   -617    160       N  
ATOM   3417  CA  ALA B 107      44.753  38.112  -2.379  1.00 62.00           C  
ANISOU 3417  CA  ALA B 107     8646   7817   7094    323   -716     28       C  
ATOM   3418  C   ALA B 107      44.599  37.222  -1.153  1.00 74.28           C  
ANISOU 3418  C   ALA B 107    10153   9324   8747    113   -719      8       C  
ATOM   3419  O   ALA B 107      45.590  36.926  -0.479  1.00 83.64           O  
ANISOU 3419  O   ALA B 107    11376  10430   9974     36   -667    102       O  
ATOM   3420  CB  ALA B 107      45.371  37.311  -3.527  1.00 61.20           C  
ANISOU 3420  CB  ALA B 107     8622   7686   6945    438   -746     24       C  
ATOM   3421  N   ASP B 108      43.374  36.787  -0.857  1.00 76.22           N  
ANISOU 3421  N   ASP B 108    10319   9613   9028     28   -771   -124       N  
ATOM   3422  CA  ASP B 108      43.113  35.837   0.231  1.00 70.51           C  
ANISOU 3422  CA  ASP B 108     9569   8827   8397   -162   -755   -160       C  
ATOM   3423  C   ASP B 108      43.547  36.377   1.593  1.00 58.36           C  
ANISOU 3423  C   ASP B 108     8032   7233   6910   -269   -683    -48       C  
ATOM   3424  O   ASP B 108      44.078  35.640   2.423  1.00 56.32           O  
ANISOU 3424  O   ASP B 108     7815   6887   6698   -370   -643     -8       O  
ATOM   3425  CB  ASP B 108      43.794  34.493  -0.040  1.00 66.12           C  
ANISOU 3425  CB  ASP B 108     9082   8195   7845   -188   -757   -162       C  
ATOM   3426  CG  ASP B 108      43.422  33.916  -1.381  1.00 69.88           C  
ANISOU 3426  CG  ASP B 108     9559   8720   8273    -78   -833   -271       C  
ATOM   3427  OD1 ASP B 108      42.252  34.063  -1.792  1.00 76.70           O  
ANISOU 3427  OD1 ASP B 108    10339   9667   9135    -49   -891   -414       O  
ATOM   3428  OD2 ASP B 108      44.309  33.328  -2.031  1.00 67.89           O  
ANISOU 3428  OD2 ASP B 108     9388   8427   7981    -10   -838   -219       O  
ATOM   3429  N   ASN B 109      43.318  37.669   1.827  1.00 56.96           N  
ANISOU 3429  N   ASN B 109     7818   7107   6716   -232   -666     -2       N  
ATOM   3430  CA  ASN B 109      43.629  38.308   3.108  1.00 59.76           C  
ANISOU 3430  CA  ASN B 109     8163   7422   7121   -322   -606     95       C  
ATOM   3431  C   ASN B 109      45.106  38.154   3.481  1.00 56.80           C  
ANISOU 3431  C   ASN B 109     7856   6966   6758   -322   -553    212       C  
ATOM   3432  O   ASN B 109      45.448  37.955   4.648  1.00 50.63           O  
ANISOU 3432  O   ASN B 109     7083   6122   6031   -417   -518    256       O  
ATOM   3433  CB  ASN B 109      42.740  37.758   4.231  1.00 65.41           C  
ANISOU 3433  CB  ASN B 109     8834   8105   7916   -481   -602     31       C  
ATOM   3434  CG  ASN B 109      41.267  38.043   4.017  1.00 69.13           C  
ANISOU 3434  CG  ASN B 109     9215   8662   8389   -494   -649    -95       C  
ATOM   3435  OD1 ASN B 109      40.878  39.159   3.667  1.00 80.96           O  
ANISOU 3435  OD1 ASN B 109    10679  10249   9835   -409   -668    -88       O  
ATOM   3436  ND2 ASN B 109      40.434  37.040   4.261  1.00 65.67           N  
ANISOU 3436  ND2 ASN B 109     8741   8198   8012   -601   -658   -220       N  
ATOM   3437  N   ASN B 110      45.991  38.260   2.489  1.00 60.59           N  
ANISOU 3437  N   ASN B 110     8388   7447   7187   -202   -545    254       N  
ATOM   3438  CA  ASN B 110      47.421  38.049   2.684  1.00 58.38           C  
ANISOU 3438  CA  ASN B 110     8164   7101   6919   -190   -499    342       C  
ATOM   3439  C   ASN B 110      48.156  39.306   3.139  1.00 64.09           C  
ANISOU 3439  C   ASN B 110     8869   7820   7662   -168   -428    432       C  
ATOM   3440  O   ASN B 110      49.391  39.335   3.094  1.00 72.79           O  
ANISOU 3440  O   ASN B 110    10002   8881   8774   -133   -384    488       O  
ATOM   3441  CB  ASN B 110      48.058  37.505   1.400  1.00 51.63           C  
ANISOU 3441  CB  ASN B 110     7372   6237   6007    -77   -515    341       C  
ATOM   3442  CG  ASN B 110      47.943  38.467   0.221  1.00 62.42           C  
ANISOU 3442  CG  ASN B 110     8751   7656   7311     74   -502    350       C  
ATOM   3443  OD1 ASN B 110      47.601  39.642   0.376  1.00 64.54           O  
ANISOU 3443  OD1 ASN B 110     8989   7961   7571    100   -465    372       O  
ATOM   3444  ND2 ASN B 110      48.221  37.958  -0.975  1.00 65.00           N  
ANISOU 3444  ND2 ASN B 110     9137   7979   7582    187   -528    334       N  
ATOM   3445  N   CYS B 111      47.427  40.346   3.552  1.00 58.25           N  
ANISOU 3445  N   CYS B 111     8077   7125   6930   -186   -414    438       N  
ATOM   3446  CA  CYS B 111      48.068  41.606   3.912  1.00 57.42           C  
ANISOU 3446  CA  CYS B 111     7955   7018   6844   -164   -336    516       C  
ATOM   3447  C   CYS B 111      49.055  41.429   5.064  1.00 63.92           C  
ANISOU 3447  C   CYS B 111     8766   7781   7740   -239   -306    559       C  
ATOM   3448  O   CYS B 111      50.156  41.994   5.032  1.00 64.78           O  
ANISOU 3448  O   CYS B 111     8875   7867   7872   -200   -240    604       O  
ATOM   3449  CB  CYS B 111      47.001  42.644   4.254  1.00 56.97           C  
ANISOU 3449  CB  CYS B 111     7851   7021   6775   -180   -333    513       C  
ATOM   3450  SG  CYS B 111      45.987  42.199   5.680  1.00 70.67           S  
ANISOU 3450  SG  CYS B 111     9529   8752   8572   -336   -385    478       S  
ATOM   3451  N   TYR B 112      48.702  40.620   6.073  1.00 58.83           N  
ANISOU 3451  N   TYR B 112     8116   7106   7130   -336   -348    534       N  
ATOM   3452  CA  TYR B 112      49.629  40.377   7.173  1.00 56.49           C  
ANISOU 3452  CA  TYR B 112     7824   6756   6884   -375   -329    561       C  
ATOM   3453  C   TYR B 112      50.848  39.582   6.715  1.00 59.32           C  
ANISOU 3453  C   TYR B 112     8234   7079   7226   -321   -325    560       C  
ATOM   3454  O   TYR B 112      51.947  39.784   7.240  1.00 67.05           O  
ANISOU 3454  O   TYR B 112     9201   8036   8238   -304   -294    579       O  
ATOM   3455  CB  TYR B 112      48.922  39.652   8.325  1.00 57.68           C  
ANISOU 3455  CB  TYR B 112     7988   6868   7061   -468   -359    534       C  
ATOM   3456  CG  TYR B 112      48.696  38.170   8.104  1.00 57.38           C  
ANISOU 3456  CG  TYR B 112     8018   6787   6996   -492   -389    480       C  
ATOM   3457  CD1 TYR B 112      49.568  37.227   8.643  1.00 57.44           C  
ANISOU 3457  CD1 TYR B 112     8097   6731   6996   -485   -382    481       C  
ATOM   3458  CD2 TYR B 112      47.611  37.712   7.367  1.00 56.44           C  
ANISOU 3458  CD2 TYR B 112     7897   6694   6856   -515   -421    416       C  
ATOM   3459  CE1 TYR B 112      49.364  35.871   8.447  1.00 61.21           C  
ANISOU 3459  CE1 TYR B 112     8654   7161   7440   -506   -393    433       C  
ATOM   3460  CE2 TYR B 112      47.403  36.361   7.166  1.00 53.59           C  
ANISOU 3460  CE2 TYR B 112     7595   6287   6478   -546   -435    356       C  
ATOM   3461  CZ  TYR B 112      48.278  35.447   7.708  1.00 61.03           C  
ANISOU 3461  CZ  TYR B 112     8622   7157   7410   -545   -415    372       C  
ATOM   3462  OH  TYR B 112      48.072  34.103   7.510  1.00 68.87           O  
ANISOU 3462  OH  TYR B 112     9691   8097   8379   -575   -414    316       O  
ATOM   3463  N   LEU B 113      50.680  38.676   5.749  1.00 58.16           N  
ANISOU 3463  N   LEU B 113     8139   6929   7028   -290   -358    529       N  
ATOM   3464  CA  LEU B 113      51.836  37.984   5.190  1.00 58.42           C  
ANISOU 3464  CA  LEU B 113     8225   6934   7037   -229   -354    537       C  
ATOM   3465  C   LEU B 113      52.746  38.955   4.457  1.00 60.10           C  
ANISOU 3465  C   LEU B 113     8417   7160   7260   -145   -291    576       C  
ATOM   3466  O   LEU B 113      53.972  38.905   4.610  1.00 61.11           O  
ANISOU 3466  O   LEU B 113     8545   7263   7411   -117   -259    587       O  
ATOM   3467  CB  LEU B 113      51.381  36.871   4.247  1.00 68.20           C  
ANISOU 3467  CB  LEU B 113     9525   8169   8218   -209   -403    497       C  
ATOM   3468  CG  LEU B 113      51.149  35.488   4.855  1.00 72.68           C  
ANISOU 3468  CG  LEU B 113    10153   8688   8772   -276   -434    457       C  
ATOM   3469  CD1 LEU B 113      50.652  34.511   3.804  1.00 75.07           C  
ANISOU 3469  CD1 LEU B 113    10503   8993   9026   -258   -476    408       C  
ATOM   3470  CD2 LEU B 113      52.426  34.983   5.475  1.00 72.14           C  
ANISOU 3470  CD2 LEU B 113    10135   8578   8696   -254   -417    481       C  
ATOM   3471  N   ALA B 114      52.162  39.851   3.659  1.00 63.09           N  
ANISOU 3471  N   ALA B 114     8781   7573   7618    -97   -263    588       N  
ATOM   3472  CA  ALA B 114      52.970  40.830   2.940  1.00 57.93           C  
ANISOU 3472  CA  ALA B 114     8127   6912   6973    -13   -172    625       C  
ATOM   3473  C   ALA B 114      53.750  41.712   3.904  1.00 57.70           C  
ANISOU 3473  C   ALA B 114     8031   6868   7023    -55   -101    643       C  
ATOM   3474  O   ALA B 114      54.942  41.963   3.696  1.00 63.99           O  
ANISOU 3474  O   ALA B 114     8819   7635   7860    -18    -30    648       O  
ATOM   3475  CB  ALA B 114      52.082  41.674   2.030  1.00 54.25           C  
ANISOU 3475  CB  ALA B 114     7678   6482   6452     62   -146    631       C  
ATOM   3476  N   THR B 115      53.101  42.182   4.976  1.00 54.45           N  
ANISOU 3476  N   THR B 115     7566   6478   6644   -132   -117    643       N  
ATOM   3477  CA  THR B 115      53.801  43.014   5.952  1.00 55.87           C  
ANISOU 3477  CA  THR B 115     7677   6649   6904   -169    -60    650       C  
ATOM   3478  C   THR B 115      54.964  42.266   6.589  1.00 59.32           C  
ANISOU 3478  C   THR B 115     8101   7058   7380   -175    -81    616       C  
ATOM   3479  O   THR B 115      56.067  42.811   6.722  1.00 62.58           O  
ANISOU 3479  O   THR B 115     8462   7460   7856   -155    -13    598       O  
ATOM   3480  CB  THR B 115      52.832  43.490   7.030  1.00 57.62           C  
ANISOU 3480  CB  THR B 115     7855   6895   7143   -244    -92    661       C  
ATOM   3481  OG1 THR B 115      51.806  44.292   6.429  1.00 60.85           O  
ANISOU 3481  OG1 THR B 115     8272   7342   7506   -226    -69    684       O  
ATOM   3482  CG2 THR B 115      53.576  44.314   8.081  1.00 54.67           C  
ANISOU 3482  CG2 THR B 115     7406   6512   6852   -275    -43    661       C  
ATOM   3483  N   ALA B 116      54.738  41.010   6.981  1.00 60.24           N  
ANISOU 3483  N   ALA B 116     8266   7164   7459   -196   -168    596       N  
ATOM   3484  CA  ALA B 116      55.808  40.210   7.569  1.00 53.08           C  
ANISOU 3484  CA  ALA B 116     7371   6237   6561   -176   -193    559       C  
ATOM   3485  C   ALA B 116      56.916  39.930   6.559  1.00 57.04           C  
ANISOU 3485  C   ALA B 116     7892   6728   7053   -106   -159    549       C  
ATOM   3486  O   ALA B 116      58.103  40.040   6.890  1.00 56.24           O  
ANISOU 3486  O   ALA B 116     7747   6626   6997    -76   -131    509       O  
ATOM   3487  CB  ALA B 116      55.234  38.906   8.116  1.00 44.14           C  
ANISOU 3487  CB  ALA B 116     6317   5081   5371   -204   -270    544       C  
ATOM   3488  N   LEU B 117      56.550  39.603   5.313  1.00 57.49           N  
ANISOU 3488  N   LEU B 117     8010   6780   7054    -70   -159    576       N  
ATOM   3489  CA  LEU B 117      57.558  39.325   4.294  1.00 59.93           C  
ANISOU 3489  CA  LEU B 117     8350   7069   7350      4   -123    576       C  
ATOM   3490  C   LEU B 117      58.436  40.545   4.033  1.00 64.41           C  
ANISOU 3490  C   LEU B 117     8848   7626   7998     32     -4    572       C  
ATOM   3491  O   LEU B 117      59.656  40.417   3.860  1.00 66.76           O  
ANISOU 3491  O   LEU B 117     9127   7908   8332     69     36    541       O  
ATOM   3492  CB  LEU B 117      56.885  38.869   2.999  1.00 59.14           C  
ANISOU 3492  CB  LEU B 117     8330   6964   7175     52   -146    607       C  
ATOM   3493  CG  LEU B 117      57.785  38.626   1.781  1.00 59.15           C  
ANISOU 3493  CG  LEU B 117     8383   6937   7155    144   -105    623       C  
ATOM   3494  CD1 LEU B 117      58.715  37.445   2.006  1.00 59.65           C  
ANISOU 3494  CD1 LEU B 117     8482   6990   7193    154   -156    600       C  
ATOM   3495  CD2 LEU B 117      56.955  38.422   0.518  1.00 60.67           C  
ANISOU 3495  CD2 LEU B 117     8651   7129   7274    210   -127    649       C  
ATOM   3496  N   LEU B 118      57.837  41.740   4.011  1.00 58.68           N  
ANISOU 3496  N   LEU B 118     8086   6906   7304     15     63    596       N  
ATOM   3497  CA  LEU B 118      58.627  42.952   3.827  1.00 56.68           C  
ANISOU 3497  CA  LEU B 118     7773   6628   7133     31    203    586       C  
ATOM   3498  C   LEU B 118      59.520  43.210   5.034  1.00 60.04           C  
ANISOU 3498  C   LEU B 118     8092   7065   7655    -17    213    520       C  
ATOM   3499  O   LEU B 118      60.653  43.683   4.885  1.00 58.67           O  
ANISOU 3499  O   LEU B 118     7861   6870   7563      1    311    471       O  
ATOM   3500  CB  LEU B 118      57.707  44.147   3.563  1.00 50.28           C  
ANISOU 3500  CB  LEU B 118     6970   5822   6314     30    277    629       C  
ATOM   3501  CG  LEU B 118      56.910  44.136   2.246  1.00 50.11           C  
ANISOU 3501  CG  LEU B 118     7053   5793   6195    116    288    676       C  
ATOM   3502  CD1 LEU B 118      55.838  45.210   2.239  1.00 47.95           C  
ANISOU 3502  CD1 LEU B 118     6787   5544   5889    119    330    706       C  
ATOM   3503  CD2 LEU B 118      57.812  44.302   1.028  1.00 55.32           C  
ANISOU 3503  CD2 LEU B 118     7772   6391   6858    214    405    687       C  
ATOM   3504  N   THR B 119      59.028  42.901   6.236  1.00 60.63           N  
ANISOU 3504  N   THR B 119     8140   7173   7724    -69    116    506       N  
ATOM   3505  CA  THR B 119      59.824  43.106   7.445  1.00 61.63           C  
ANISOU 3505  CA  THR B 119     8170   7316   7929    -89    107    432       C  
ATOM   3506  C   THR B 119      61.007  42.147   7.511  1.00 66.56           C  
ANISOU 3506  C   THR B 119     8794   7945   8550    -37     66    361       C  
ATOM   3507  O   THR B 119      62.098  42.527   7.956  1.00 62.52           O  
ANISOU 3507  O   THR B 119     8186   7446   8123    -21    107    273       O  
ATOM   3508  CB  THR B 119      58.944  42.948   8.681  1.00 56.60           C  
ANISOU 3508  CB  THR B 119     7533   6702   7272   -135     15    443       C  
ATOM   3509  OG1 THR B 119      57.863  43.893   8.629  1.00 52.83           O  
ANISOU 3509  OG1 THR B 119     7048   6229   6796   -182     52    504       O  
ATOM   3510  CG2 THR B 119      59.766  43.177   9.938  1.00 48.82           C  
ANISOU 3510  CG2 THR B 119     6455   5736   6359   -128     -3    359       C  
ATOM   3511  N   LEU B 120      60.811  40.896   7.083  1.00 69.60           N  
ANISOU 3511  N   LEU B 120     9284   8325   8836     -6    -13    389       N  
ATOM   3512  CA  LEU B 120      61.888  39.911   7.155  1.00 68.14           C  
ANISOU 3512  CA  LEU B 120     9118   8150   8624     54    -58    327       C  
ATOM   3513  C   LEU B 120      63.059  40.279   6.255  1.00 75.99           C  
ANISOU 3513  C   LEU B 120    10064   9130   9679     94     38    290       C  
ATOM   3514  O   LEU B 120      64.203  39.917   6.550  1.00 86.06           O  
ANISOU 3514  O   LEU B 120    11295  10427  10978    139     26    202       O  
ATOM   3515  CB  LEU B 120      61.348  38.529   6.796  1.00 63.81           C  
ANISOU 3515  CB  LEU B 120     8705   7589   7950     73   -147    374       C  
ATOM   3516  CG  LEU B 120      60.423  37.893   7.838  1.00 60.02           C  
ANISOU 3516  CG  LEU B 120     8285   7109   7412     40   -230    384       C  
ATOM   3517  CD1 LEU B 120      59.651  36.736   7.246  1.00 59.54           C  
ANISOU 3517  CD1 LEU B 120     8351   7022   7248     34   -281    432       C  
ATOM   3518  CD2 LEU B 120      61.243  37.419   9.032  1.00 61.74           C  
ANISOU 3518  CD2 LEU B 120     8494   7346   7618     94   -278    302       C  
ATOM   3519  N   GLN B 121      62.805  41.013   5.172  1.00 73.85           N  
ANISOU 3519  N   GLN B 121     9806   8820   9434     89    141    347       N  
ATOM   3520  CA  GLN B 121      63.868  41.442   4.270  1.00 65.17           C  
ANISOU 3520  CA  GLN B 121     8674   7684   8402    127    264    317       C  
ATOM   3521  C   GLN B 121      64.616  42.670   4.773  1.00 58.57           C  
ANISOU 3521  C   GLN B 121     7697   6845   7713     93    385    229       C  
ATOM   3522  O   GLN B 121      65.528  43.140   4.082  1.00 59.06           O  
ANISOU 3522  O   GLN B 121     7721   6865   7855    113    517    188       O  
ATOM   3523  CB  GLN B 121      63.305  41.743   2.879  1.00 62.91           C  
ANISOU 3523  CB  GLN B 121     8484   7343   8075    161    343    411       C  
ATOM   3524  CG  GLN B 121      62.613  40.580   2.226  1.00 64.06           C  
ANISOU 3524  CG  GLN B 121     8759   7491   8090    200    233    481       C  
ATOM   3525  CD  GLN B 121      61.963  40.963   0.916  1.00 62.95           C  
ANISOU 3525  CD  GLN B 121     8710   7306   7904    256    299    559       C  
ATOM   3526  OE1 GLN B 121      60.739  40.931   0.784  1.00 69.04           O  
ANISOU 3526  OE1 GLN B 121     9531   8095   8605    251    242    605       O  
ATOM   3527  NE2 GLN B 121      62.780  41.323  -0.065  1.00 56.94           N  
ANISOU 3527  NE2 GLN B 121     7971   6485   7178    321    423    564       N  
ATOM   3528  N   GLN B 122      64.252  43.215   5.934  1.00 52.65           N  
ANISOU 3528  N   GLN B 122     6869   6130   7005     42    355    196       N  
ATOM   3529  CA  GLN B 122      64.891  44.424   6.434  1.00 61.51           C  
ANISOU 3529  CA  GLN B 122     7850   7250   8272      4    472    105       C  
ATOM   3530  C   GLN B 122      65.594  44.233   7.769  1.00 61.08           C  
ANISOU 3530  C   GLN B 122     7679   7259   8271     10    387    -26       C  
ATOM   3531  O   GLN B 122      66.165  45.197   8.294  1.00 58.38           O  
ANISOU 3531  O   GLN B 122     7200   6924   8059    -20    470   -126       O  
ATOM   3532  CB  GLN B 122      63.873  45.565   6.556  1.00 65.18           C  
ANISOU 3532  CB  GLN B 122     8316   7696   8754    -52    542    176       C  
ATOM   3533  CG  GLN B 122      63.289  46.024   5.232  1.00 73.34           C  
ANISOU 3533  CG  GLN B 122     9458   8668   9742    -32    657    279       C  
ATOM   3534  CD  GLN B 122      62.270  47.134   5.412  1.00 77.09           C  
ANISOU 3534  CD  GLN B 122     9942   9136  10214    -74    719    342       C  
ATOM   3535  OE1 GLN B 122      61.060  46.899   5.358  1.00 77.49           O  
ANISOU 3535  OE1 GLN B 122    10075   9209  10159    -72    632    429       O  
ATOM   3536  NE2 GLN B 122      62.758  48.356   5.632  1.00 71.83           N  
ANISOU 3536  NE2 GLN B 122     9188   8440   9663   -111    875    289       N  
ATOM   3537  N   ILE B 123      65.566  43.031   8.333  1.00 62.99           N  
ANISOU 3537  N   ILE B 123     7975   7544   8413     59    230    -36       N  
ATOM   3538  CA  ILE B 123      66.265  42.718   9.569  1.00 65.01           C  
ANISOU 3538  CA  ILE B 123     8148   7863   8691    106    139   -168       C  
ATOM   3539  C   ILE B 123      67.233  41.577   9.294  1.00 69.09           C  
ANISOU 3539  C   ILE B 123     8699   8407   9147    192     78   -235       C  
ATOM   3540  O   ILE B 123      66.941  40.681   8.493  1.00 72.78           O  
ANISOU 3540  O   ILE B 123     9298   8849   9506    212     45   -143       O  
ATOM   3541  CB  ILE B 123      65.287  42.355  10.709  1.00 58.44           C  
ANISOU 3541  CB  ILE B 123     7375   7051   7777    108     14   -123       C  
ATOM   3542  CG1 ILE B 123      64.408  41.168  10.325  1.00 59.35           C  
ANISOU 3542  CG1 ILE B 123     7667   7144   7741    119    -69     -5       C  
ATOM   3543  CG2 ILE B 123      64.408  43.533  11.057  1.00 53.15           C  
ANISOU 3543  CG2 ILE B 123     6660   6364   7171     26     71    -66       C  
ATOM   3544  CD1 ILE B 123      63.438  40.780  11.417  1.00 56.33           C  
ANISOU 3544  CD1 ILE B 123     7354   6763   7288    117   -165     35       C  
ATOM   3545  N   GLU B 124      68.387  41.614   9.955  1.00 72.32           N  
ANISOU 3545  N   GLU B 124     8984   8872   9622    249     60   -405       N  
ATOM   3546  CA  GLU B 124      69.383  40.564   9.789  1.00 83.19           C  
ANISOU 3546  CA  GLU B 124    10384  10290  10934    345     -3   -488       C  
ATOM   3547  C   GLU B 124      68.898  39.294  10.477  1.00 74.87           C  
ANISOU 3547  C   GLU B 124     9480   9263   9703    424   -159   -446       C  
ATOM   3548  O   GLU B 124      68.674  39.287  11.692  1.00 70.04           O  
ANISOU 3548  O   GLU B 124     8858   8686   9070    466   -237   -497       O  
ATOM   3549  CB  GLU B 124      70.724  41.015  10.363  1.00 96.91           C  
ANISOU 3549  CB  GLU B 124    11933  12094  12796    394     17   -708       C  
ATOM   3550  CG  GLU B 124      71.869  40.054  10.093  1.00110.37           C  
ANISOU 3550  CG  GLU B 124    13641  13849  14444    498    -34   -814       C  
ATOM   3551  CD  GLU B 124      73.171  40.509  10.728  1.00118.96           C  
ANISOU 3551  CD  GLU B 124    14523  15018  15660    554    -25  -1064       C  
ATOM   3552  OE1 GLU B 124      73.492  41.712  10.621  1.00121.19           O  
ANISOU 3552  OE1 GLU B 124    14641  15277  16128    471    110  -1145       O  
ATOM   3553  OE2 GLU B 124      73.874  39.667  11.331  1.00121.24           O  
ANISOU 3553  OE2 GLU B 124    14814  15392  15860    687   -146  -1189       O  
ATOM   3554  N   LEU B 125      68.732  38.222   9.703  1.00 74.17           N  
ANISOU 3554  N   LEU B 125     9542   9150   9488    449   -194   -354       N  
ATOM   3555  CA  LEU B 125      68.105  37.015  10.228  1.00 72.59           C  
ANISOU 3555  CA  LEU B 125     9512   8951   9119    505   -309   -294       C  
ATOM   3556  C   LEU B 125      68.551  35.809   9.410  1.00 74.42           C  
ANISOU 3556  C   LEU B 125     9867   9181   9229    565   -342   -263       C  
ATOM   3557  O   LEU B 125      68.540  35.858   8.176  1.00 76.86           O  
ANISOU 3557  O   LEU B 125    10196   9450   9558    519   -279   -187       O  
ATOM   3558  CB  LEU B 125      66.581  37.166  10.203  1.00 71.32           C  
ANISOU 3558  CB  LEU B 125     9439   8729   8930    411   -303   -145       C  
ATOM   3559  CG  LEU B 125      65.757  36.302  11.154  1.00 76.21           C  
ANISOU 3559  CG  LEU B 125    10198   9333   9425    444   -391   -107       C  
ATOM   3560  CD1 LEU B 125      66.047  36.666  12.603  1.00 79.55           C  
ANISOU 3560  CD1 LEU B 125    10553   9796   9875    512   -436   -215       C  
ATOM   3561  CD2 LEU B 125      64.284  36.477  10.852  1.00 77.77           C  
ANISOU 3561  CD2 LEU B 125    10462   9472   9616    335   -369     30       C  
ATOM   3562  N   LYS B 126      68.956  34.741  10.095  1.00 81.48           N  
ANISOU 3562  N   LYS B 126    10855  10115   9990    681   -436   -324       N  
ATOM   3563  CA  LYS B 126      69.348  33.484   9.463  1.00 90.99           C  
ANISOU 3563  CA  LYS B 126    12200  11321  11052    749   -476   -294       C  
ATOM   3564  C   LYS B 126      68.482  32.361  10.016  1.00 88.55           C  
ANISOU 3564  C   LYS B 126    12094  10977  10574    783   -540   -220       C  
ATOM   3565  O   LYS B 126      68.376  32.199  11.236  1.00 97.22           O  
ANISOU 3565  O   LYS B 126    13227  12092  11622    855   -587   -281       O  
ATOM   3566  CB  LYS B 126      70.831  33.163   9.695  1.00 98.63           C  
ANISOU 3566  CB  LYS B 126    13103  12373  11998    880   -513   -456       C  
ATOM   3567  CG  LYS B 126      71.806  34.223   9.182  1.00107.64           C  
ANISOU 3567  CG  LYS B 126    14033  13543  13321    846   -431   -560       C  
ATOM   3568  CD  LYS B 126      71.709  34.408   7.668  1.00108.83           C  
ANISOU 3568  CD  LYS B 126    14199  13627  13526    757   -336   -442       C  
ATOM   3569  CE  LYS B 126      72.776  35.370   7.150  1.00107.62           C  
ANISOU 3569  CE  LYS B 126    13857  13485  13550    734   -228   -556       C  
ATOM   3570  NZ  LYS B 126      72.645  36.734   7.745  1.00106.73           N  
ANISOU 3570  NZ  LYS B 126    13572  13370  13610    661   -153   -631       N  
ATOM   3571  N   PHE B 127      67.871  31.586   9.125  1.00 78.87           N  
ANISOU 3571  N   PHE B 127    11007   9696   9264    738   -534    -96       N  
ATOM   3572  CA  PHE B 127      66.969  30.519   9.537  1.00 72.76           C  
ANISOU 3572  CA  PHE B 127    10428   8871   8346    747   -567    -28       C  
ATOM   3573  C   PHE B 127      67.714  29.202   9.706  1.00 73.02           C  
ANISOU 3573  C   PHE B 127    10615   8928   8202    883   -617    -71       C  
ATOM   3574  O   PHE B 127      68.651  28.897   8.962  1.00 73.21           O  
ANISOU 3574  O   PHE B 127    10627   8992   8199    934   -627    -94       O  
ATOM   3575  CB  PHE B 127      65.830  30.352   8.531  1.00 65.29           C  
ANISOU 3575  CB  PHE B 127     9547   7855   7405    626   -534    109       C  
ATOM   3576  CG  PHE B 127      64.841  31.481   8.555  1.00 65.45           C  
ANISOU 3576  CG  PHE B 127     9464   7849   7557    508   -492    155       C  
ATOM   3577  CD1 PHE B 127      64.011  31.669   9.652  1.00 62.96           C  
ANISOU 3577  CD1 PHE B 127     9166   7509   7248    480   -498    153       C  
ATOM   3578  CD2 PHE B 127      64.746  32.363   7.486  1.00 64.18           C  
ANISOU 3578  CD2 PHE B 127     9200   7683   7503    438   -440    202       C  
ATOM   3579  CE1 PHE B 127      63.102  32.714   9.683  1.00 57.54           C  
ANISOU 3579  CE1 PHE B 127     8386   6805   6673    375   -463    196       C  
ATOM   3580  CE2 PHE B 127      63.840  33.410   7.510  1.00 60.09           C  
ANISOU 3580  CE2 PHE B 127     8600   7146   7086    346   -400    242       C  
ATOM   3581  CZ  PHE B 127      63.016  33.584   8.608  1.00 59.25           C  
ANISOU 3581  CZ  PHE B 127     8502   7027   6985    310   -416    239       C  
ATOM   3582  N   ASN B 128      67.296  28.432  10.706  1.00 73.24           N  
ANISOU 3582  N   ASN B 128    10798   8926   8103    950   -638    -81       N  
ATOM   3583  CA  ASN B 128      67.872  27.132  11.024  1.00 73.29           C  
ANISOU 3583  CA  ASN B 128    10991   8943   7911   1097   -672   -119       C  
ATOM   3584  C   ASN B 128      67.377  26.032  10.084  1.00 73.35           C  
ANISOU 3584  C   ASN B 128    11171   8889   7811   1047   -651     -7       C  
ATOM   3585  O   ASN B 128      68.204  25.263   9.578  1.00 77.31           O  
ANISOU 3585  O   ASN B 128    11748   9424   8201   1132   -677    -20       O  
ATOM   3586  CB  ASN B 128      67.568  26.765  12.478  1.00 78.50           C  
ANISOU 3586  CB  ASN B 128    11777   9576   8473   1203   -680   -171       C  
ATOM   3587  CG  ASN B 128      68.252  27.683  13.463  1.00 83.33           C  
ANISOU 3587  CG  ASN B 128    12234  10265   9161   1299   -721   -307       C  
ATOM   3588  OD1 ASN B 128      69.358  28.166  13.219  1.00 91.29           O  
ANISOU 3588  OD1 ASN B 128    13087  11369  10231   1352   -756   -409       O  
ATOM   3589  ND2 ASN B 128      67.580  27.956  14.575  1.00 84.32           N  
ANISOU 3589  ND2 ASN B 128    12394  10346   9296   1317   -712   -316       N  
ATOM   3590  N   PRO B 129      66.073  25.894   9.826  1.00 69.22           N  
ANISOU 3590  N   PRO B 129    10710   8276   7313    916   -607     93       N  
ATOM   3591  CA  PRO B 129      65.621  24.837   8.905  1.00 64.61           C  
ANISOU 3591  CA  PRO B 129    10275   7637   6635    869   -588    179       C  
ATOM   3592  C   PRO B 129      66.170  25.058   7.508  1.00 66.29           C  
ANISOU 3592  C   PRO B 129    10396   7889   6901    839   -607    220       C  
ATOM   3593  O   PRO B 129      66.022  26.152   6.939  1.00 61.82           O  
ANISOU 3593  O   PRO B 129     9660   7338   6491    757   -596    240       O  
ATOM   3594  CB  PRO B 129      64.089  24.969   8.929  1.00 58.06           C  
ANISOU 3594  CB  PRO B 129     9464   6721   5875    722   -539    245       C  
ATOM   3595  CG  PRO B 129      63.785  25.655  10.201  1.00 59.81           C  
ANISOU 3595  CG  PRO B 129     9635   6935   6154    733   -527    197       C  
ATOM   3596  CD  PRO B 129      64.920  26.613  10.404  1.00 65.37           C  
ANISOU 3596  CD  PRO B 129    10167   7738   6933    810   -573    121       C  
ATOM   3597  N   PRO B 130      66.818  24.049   6.923  1.00 68.31           N  
ANISOU 3597  N   PRO B 130    10775   8157   7024    913   -628    235       N  
ATOM   3598  CA  PRO B 130      67.317  24.212   5.547  1.00 63.76           C  
ANISOU 3598  CA  PRO B 130    10127   7605   6494    892   -641    285       C  
ATOM   3599  C   PRO B 130      66.219  24.532   4.553  1.00 62.01           C  
ANISOU 3599  C   PRO B 130     9870   7326   6367    758   -616    379       C  
ATOM   3600  O   PRO B 130      66.455  25.301   3.615  1.00 67.21           O  
ANISOU 3600  O   PRO B 130    10405   7998   7132    730   -608    408       O  
ATOM   3601  CB  PRO B 130      67.982  22.860   5.254  1.00 58.92           C  
ANISOU 3601  CB  PRO B 130     9697   7000   5688    995   -668    296       C  
ATOM   3602  CG  PRO B 130      68.351  22.330   6.603  1.00 61.73           C  
ANISOU 3602  CG  PRO B 130    10165   7377   5914   1116   -677    209       C  
ATOM   3603  CD  PRO B 130      67.249  22.776   7.523  1.00 64.79           C  
ANISOU 3603  CD  PRO B 130    10540   7707   6372   1040   -637    204       C  
ATOM   3604  N   ALA B 131      65.013  23.989   4.749  1.00 59.13           N  
ANISOU 3604  N   ALA B 131     9608   6893   5967    682   -595    415       N  
ATOM   3605  CA  ALA B 131      63.901  24.318   3.865  1.00 56.84           C  
ANISOU 3605  CA  ALA B 131     9269   6561   5766    566   -580    477       C  
ATOM   3606  C   ALA B 131      63.576  25.807   3.915  1.00 63.28           C  
ANISOU 3606  C   ALA B 131     9895   7398   6751    506   -563    469       C  
ATOM   3607  O   ALA B 131      63.273  26.418   2.884  1.00 61.43           O  
ANISOU 3607  O   ALA B 131     9581   7162   6597    468   -557    513       O  
ATOM   3608  CB  ALA B 131      62.674  23.488   4.233  1.00 47.71           C  
ANISOU 3608  CB  ALA B 131     8240   5332   4557    492   -552    484       C  
ATOM   3609  N   LEU B 132      63.627  26.408   5.109  1.00 69.71           N  
ANISOU 3609  N   LEU B 132    10646   8228   7610    509   -551    413       N  
ATOM   3610  CA  LEU B 132      63.369  27.841   5.231  1.00 67.25           C  
ANISOU 3610  CA  LEU B 132    10161   7938   7454    453   -528    404       C  
ATOM   3611  C   LEU B 132      64.505  28.660   4.641  1.00 72.54           C  
ANISOU 3611  C   LEU B 132    10704   8656   8199    502   -516    386       C  
ATOM   3612  O   LEU B 132      64.268  29.672   3.974  1.00 76.08           O  
ANISOU 3612  O   LEU B 132    11045   9103   8760    455   -478    415       O  
ATOM   3613  CB  LEU B 132      63.153  28.233   6.688  1.00 59.91           C  
ANISOU 3613  CB  LEU B 132     9202   7010   6549    451   -520    348       C  
ATOM   3614  CG  LEU B 132      61.696  28.313   7.128  1.00 60.75           C  
ANISOU 3614  CG  LEU B 132     9332   7062   6687    348   -498    375       C  
ATOM   3615  CD1 LEU B 132      61.607  28.792   8.563  1.00 59.61           C  
ANISOU 3615  CD1 LEU B 132     9158   6918   6574    363   -490    325       C  
ATOM   3616  CD2 LEU B 132      60.917  29.230   6.208  1.00 64.67           C  
ANISOU 3616  CD2 LEU B 132     9716   7562   7295    257   -483    423       C  
ATOM   3617  N   GLN B 133      65.746  28.256   4.899  1.00 78.46           N  
ANISOU 3617  N   GLN B 133    11471   9450   8891    602   -538    328       N  
ATOM   3618  CA  GLN B 133      66.869  29.044   4.417  1.00 80.17           C  
ANISOU 3618  CA  GLN B 133    11554   9708   9198    641   -511    287       C  
ATOM   3619  C   GLN B 133      66.888  29.091   2.896  1.00 76.13           C  
ANISOU 3619  C   GLN B 133    11052   9164   8709    627   -483    369       C  
ATOM   3620  O   GLN B 133      67.194  30.133   2.305  1.00 72.02           O  
ANISOU 3620  O   GLN B 133    10415   8639   8312    611   -419    370       O  
ATOM   3621  CB  GLN B 133      68.176  28.477   4.964  1.00 83.52           C  
ANISOU 3621  CB  GLN B 133    11998  10194   9544    760   -549    191       C  
ATOM   3622  CG  GLN B 133      69.355  29.421   4.822  1.00 94.03           C  
ANISOU 3622  CG  GLN B 133    13154  11575  10998    793   -512    101       C  
ATOM   3623  CD  GLN B 133      69.233  30.654   5.703  1.00 99.92           C  
ANISOU 3623  CD  GLN B 133    13738  12341  11886    750   -479     25       C  
ATOM   3624  OE1 GLN B 133      68.662  31.674   5.304  1.00 96.57           O  
ANISOU 3624  OE1 GLN B 133    13225  11879  11588    658   -413     71       O  
ATOM   3625  NE2 GLN B 133      69.768  30.562   6.915  1.00107.92           N  
ANISOU 3625  NE2 GLN B 133    14723  13414  12870    830   -524    -95       N  
ATOM   3626  N   ASP B 134      66.531  27.980   2.245  1.00 78.58           N  
ANISOU 3626  N   ASP B 134    11510   9445   8901    640   -520    437       N  
ATOM   3627  CA  ASP B 134      66.458  27.965   0.788  1.00 82.93           C  
ANISOU 3627  CA  ASP B 134    12086   9962   9462    644   -504    518       C  
ATOM   3628  C   ASP B 134      65.329  28.858   0.289  1.00 81.99           C  
ANISOU 3628  C   ASP B 134    11907   9806   9437    571   -466    565       C  
ATOM   3629  O   ASP B 134      65.511  29.631  -0.659  1.00 85.74           O  
ANISOU 3629  O   ASP B 134    12328  10260   9988    589   -412    598       O  
ATOM   3630  CB  ASP B 134      66.270  26.534   0.281  1.00 94.14           C  
ANISOU 3630  CB  ASP B 134    13677  11360  10730    674   -559    571       C  
ATOM   3631  CG  ASP B 134      67.468  25.641   0.581  1.00109.88           C  
ANISOU 3631  CG  ASP B 134    15748  13394  12609    768   -593    533       C  
ATOM   3632  OD1 ASP B 134      68.418  26.113   1.247  1.00113.87           O  
ANISOU 3632  OD1 ASP B 134    16163  13950  13154    814   -583    449       O  
ATOM   3633  OD2 ASP B 134      67.451  24.461   0.163  1.00112.91           O  
ANISOU 3633  OD2 ASP B 134    16281  13761  12858    802   -631    578       O  
ATOM   3634  N   ALA B 135      64.159  28.776   0.926  1.00 75.61           N  
ANISOU 3634  N   ALA B 135    11118   8988   8623    498   -486    563       N  
ATOM   3635  CA  ALA B 135      63.034  29.598   0.502  1.00 75.21           C  
ANISOU 3635  CA  ALA B 135    11011   8916   8648    438   -461    595       C  
ATOM   3636  C   ALA B 135      63.256  31.069   0.822  1.00 76.81           C  
ANISOU 3636  C   ALA B 135    11070   9133   8980    419   -392    569       C  
ATOM   3637  O   ALA B 135      62.720  31.940   0.126  1.00 81.90           O  
ANISOU 3637  O   ALA B 135    11670   9761   9686    409   -347    603       O  
ATOM   3638  CB  ALA B 135      61.750  29.102   1.161  1.00 73.19           C  
ANISOU 3638  CB  ALA B 135    10804   8647   8358    360   -495    584       C  
ATOM   3639  N   TYR B 136      64.031  31.366   1.864  1.00 74.95           N  
ANISOU 3639  N   TYR B 136    10766   8930   8782    424   -380    502       N  
ATOM   3640  CA  TYR B 136      64.330  32.757   2.186  1.00 79.96           C  
ANISOU 3640  CA  TYR B 136    11257   9576   9548    402   -307    465       C  
ATOM   3641  C   TYR B 136      65.155  33.403   1.081  1.00 82.62           C  
ANISOU 3641  C   TYR B 136    11549   9890   9951    448   -222    479       C  
ATOM   3642  O   TYR B 136      64.916  34.560   0.714  1.00 84.10           O  
ANISOU 3642  O   TYR B 136    11668  10054  10232    427   -135    494       O  
ATOM   3643  CB  TYR B 136      65.058  32.843   3.526  1.00 87.44           C  
ANISOU 3643  CB  TYR B 136    12138  10568  10518    414   -323    370       C  
ATOM   3644  CG  TYR B 136      65.123  34.236   4.116  1.00 91.19           C  
ANISOU 3644  CG  TYR B 136    12463  11056  11129    372   -257    322       C  
ATOM   3645  CD1 TYR B 136      64.277  35.246   3.672  1.00 91.33           C  
ANISOU 3645  CD1 TYR B 136    12437  11045  11218    313   -195    376       C  
ATOM   3646  CD2 TYR B 136      66.036  34.540   5.117  1.00 94.72           C  
ANISOU 3646  CD2 TYR B 136    12814  11548  11626    402   -259    213       C  
ATOM   3647  CE1 TYR B 136      64.335  36.515   4.215  1.00 92.45           C  
ANISOU 3647  CE1 TYR B 136    12453  11196  11477    273   -126    335       C  
ATOM   3648  CE2 TYR B 136      66.103  35.804   5.663  1.00 95.10           C  
ANISOU 3648  CE2 TYR B 136    12721  11608  11804    360   -197    162       C  
ATOM   3649  CZ  TYR B 136      65.253  36.789   5.209  1.00 96.32           C  
ANISOU 3649  CZ  TYR B 136    12844  11727  12028    290   -126    229       C  
ATOM   3650  OH  TYR B 136      65.325  38.049   5.758  1.00 99.97           O  
ANISOU 3650  OH  TYR B 136    13175  12196  12612    247    -55    181       O  
ATOM   3651  N   TYR B 137      66.130  32.668   0.535  1.00 82.48           N  
ANISOU 3651  N   TYR B 137    11583   9873   9883    517   -236    476       N  
ATOM   3652  CA  TYR B 137      66.943  33.216  -0.545  1.00 82.27           C  
ANISOU 3652  CA  TYR B 137    11527   9809   9922    566   -142    491       C  
ATOM   3653  C   TYR B 137      66.084  33.489  -1.769  1.00 79.89           C  
ANISOU 3653  C   TYR B 137    11296   9450   9608    583   -107    588       C  
ATOM   3654  O   TYR B 137      66.227  34.530  -2.421  1.00 81.97           O  
ANISOU 3654  O   TYR B 137    11520   9667   9958    602     10    604       O  
ATOM   3655  CB  TYR B 137      68.080  32.258  -0.905  1.00 81.58           C  
ANISOU 3655  CB  TYR B 137    11494   9736   9768    641   -175    475       C  
ATOM   3656  CG  TYR B 137      69.186  32.159   0.124  1.00 92.14           C  
ANISOU 3656  CG  TYR B 137    12745  11137  11127    660   -192    353       C  
ATOM   3657  CD1 TYR B 137      70.040  31.061   0.145  1.00 99.20           C  
ANISOU 3657  CD1 TYR B 137    13706  12069  11916    733   -260    324       C  
ATOM   3658  CD2 TYR B 137      69.382  33.160   1.070  1.00 95.66           C  
ANISOU 3658  CD2 TYR B 137    13044  11612  11690    618   -145    257       C  
ATOM   3659  CE1 TYR B 137      71.056  30.957   1.080  1.00102.23           C  
ANISOU 3659  CE1 TYR B 137    14013  12526  12306    776   -286    193       C  
ATOM   3660  CE2 TYR B 137      70.399  33.065   2.012  1.00 99.80           C  
ANISOU 3660  CE2 TYR B 137    13482  12206  12233    655   -173    122       C  
ATOM   3661  CZ  TYR B 137      71.231  31.960   2.011  1.00103.06           C  
ANISOU 3661  CZ  TYR B 137    13962  12661  12533    741   -246     86       C  
ATOM   3662  OH  TYR B 137      72.244  31.850   2.938  1.00105.39           O  
ANISOU 3662  OH  TYR B 137    14173  13037  12832    802   -283    -65       O  
ATOM   3663  N   ARG B 138      65.175  32.565  -2.085  1.00 73.36           N  
ANISOU 3663  N   ARG B 138    10579   8623   8672    586   -200    644       N  
ATOM   3664  CA  ARG B 138      64.308  32.742  -3.240  1.00 78.81           C  
ANISOU 3664  CA  ARG B 138    11335   9272   9338    624   -188    715       C  
ATOM   3665  C   ARG B 138      63.316  33.879  -3.051  1.00 82.37           C  
ANISOU 3665  C   ARG B 138    11724   9721   9851    581   -140    714       C  
ATOM   3666  O   ARG B 138      62.849  34.459  -4.037  1.00 77.07           O  
ANISOU 3666  O   ARG B 138    11087   9013   9183    641    -88    757       O  
ATOM   3667  CB  ARG B 138      63.553  31.449  -3.516  1.00 84.78           C  
ANISOU 3667  CB  ARG B 138    12203  10036   9972    627   -304    746       C  
ATOM   3668  CG  ARG B 138      64.449  30.277  -3.774  1.00 89.08           C  
ANISOU 3668  CG  ARG B 138    12832  10582  10433    677   -353    759       C  
ATOM   3669  CD  ARG B 138      63.666  29.178  -4.423  1.00 92.16           C  
ANISOU 3669  CD  ARG B 138    13339  10961  10715    694   -440    799       C  
ATOM   3670  NE  ARG B 138      64.566  28.258  -5.096  1.00 98.42           N  
ANISOU 3670  NE  ARG B 138    14225  11741  11430    770   -467    837       N  
ATOM   3671  CZ  ARG B 138      64.172  27.287  -5.909  1.00103.34           C  
ANISOU 3671  CZ  ARG B 138    14959  12347  11959    811   -533    880       C  
ATOM   3672  NH1 ARG B 138      62.880  27.111  -6.161  1.00 98.79           N  
ANISOU 3672  NH1 ARG B 138    14403  11769  11366    781   -578    874       N  
ATOM   3673  NH2 ARG B 138      65.075  26.500  -6.477  1.00108.04           N  
ANISOU 3673  NH2 ARG B 138    15639  12930  12481    882   -555    921       N  
ATOM   3674  N   ALA B 139      62.986  34.217  -1.806  1.00 87.88           N  
ANISOU 3674  N   ALA B 139    12342  10457  10591    493   -154    665       N  
ATOM   3675  CA  ALA B 139      62.053  35.312  -1.568  1.00 89.76           C  
ANISOU 3675  CA  ALA B 139    12522  10700  10884    450   -110    666       C  
ATOM   3676  C   ALA B 139      62.683  36.655  -1.909  1.00 91.24           C  
ANISOU 3676  C   ALA B 139    12644  10850  11172    479     37    664       C  
ATOM   3677  O   ALA B 139      62.031  37.526  -2.497  1.00 96.58           O  
ANISOU 3677  O   ALA B 139    13334  11503  11859    509    104    697       O  
ATOM   3678  CB  ALA B 139      61.577  35.284  -0.117  1.00 94.17           C  
ANISOU 3678  CB  ALA B 139    13019  11300  11460    354   -162    620       C  
ATOM   3679  N   ARG B 140      63.954  36.833  -1.552  1.00 89.14           N  
ANISOU 3679  N   ARG B 140    12312  10580  10978    476     97    614       N  
ATOM   3680  CA  ARG B 140      64.678  38.050  -1.891  1.00 91.31           C  
ANISOU 3680  CA  ARG B 140    12523  10806  11364    494    262    594       C  
ATOM   3681  C   ARG B 140      64.882  38.191  -3.395  1.00 92.76           C  
ANISOU 3681  C   ARG B 140    12806  10912  11527    599    353    658       C  
ATOM   3682  O   ARG B 140      64.932  39.314  -3.911  1.00 95.10           O  
ANISOU 3682  O   ARG B 140    13101  11147  11886    631    508    671       O  
ATOM   3683  CB  ARG B 140      66.015  38.028  -1.160  1.00 93.67           C  
ANISOU 3683  CB  ARG B 140    12717  11127  11747    469    289    499       C  
ATOM   3684  CG  ARG B 140      65.902  38.228   0.340  1.00 95.85           C  
ANISOU 3684  CG  ARG B 140    12886  11468  12063    389    233    422       C  
ATOM   3685  CD  ARG B 140      67.254  37.996   0.994  1.00100.38           C  
ANISOU 3685  CD  ARG B 140    13365  12079  12695    397    231    308       C  
ATOM   3686  NE  ARG B 140      67.269  38.335   2.414  1.00104.59           N  
ANISOU 3686  NE  ARG B 140    13788  12671  13279    346    190    219       N  
ATOM   3687  CZ  ARG B 140      67.675  39.509   2.891  1.00109.62           C  
ANISOU 3687  CZ  ARG B 140    14289  13307  14053    305    294    139       C  
ATOM   3688  NH1 ARG B 140      68.127  40.440   2.062  1.00109.93           N  
ANISOU 3688  NH1 ARG B 140    14292  13281  14196    303    462    135       N  
ATOM   3689  NH2 ARG B 140      67.652  39.745   4.198  1.00111.14           N  
ANISOU 3689  NH2 ARG B 140    14389  13556  14281    273    239     59       N  
ATOM   3690  N   ALA B 141      64.991  37.071  -4.113  1.00 89.46           N  
ANISOU 3690  N   ALA B 141    12488  10488  11015    664    269    701       N  
ATOM   3691  CA  ALA B 141      65.103  37.132  -5.566  1.00 87.05           C  
ANISOU 3691  CA  ALA B 141    12294  10105  10675    784    341    769       C  
ATOM   3692  C   ALA B 141      63.782  37.557  -6.197  1.00 95.72           C  
ANISOU 3692  C   ALA B 141    13468  11192  11709    841    335    822       C  
ATOM   3693  O   ALA B 141      63.739  38.488  -7.012  1.00102.93           O  
ANISOU 3693  O   ALA B 141    14433  12035  12642    928    474    853       O  
ATOM   3694  CB  ALA B 141      65.556  35.776  -6.110  1.00 79.67           C  
ANISOU 3694  CB  ALA B 141    11446   9175   9652    839    238    801       C  
ATOM   3695  N   GLY B 142      62.692  36.890  -5.826  1.00 92.41           N  
ANISOU 3695  N   GLY B 142    13061  10840  11212    801    184    821       N  
ATOM   3696  CA  GLY B 142      61.383  37.197  -6.363  1.00 84.13           C  
ANISOU 3696  CA  GLY B 142    12066   9801  10098    856    154    844       C  
ATOM   3697  C   GLY B 142      60.442  36.017  -6.265  1.00 82.47           C  
ANISOU 3697  C   GLY B 142    11886   9651   9797    829    -21    833       C  
ATOM   3698  O   GLY B 142      59.222  36.191  -6.207  1.00 78.96           O  
ANISOU 3698  O   GLY B 142    11436   9248   9319    820    -76    813       O  
ATOM   3699  N   GLU B 143      61.007  34.805  -6.258  1.00 86.96           N  
ANISOU 3699  N   GLU B 143    12490  10224  10328    816   -101    837       N  
ATOM   3700  CA  GLU B 143      60.240  33.566  -6.109  1.00 87.28           C  
ANISOU 3700  CA  GLU B 143    12566  10308  10289    776   -247    818       C  
ATOM   3701  C   GLU B 143      59.944  33.329  -4.626  1.00 83.92           C  
ANISOU 3701  C   GLU B 143    12064   9930   9893    630   -293    767       C  
ATOM   3702  O   GLU B 143      60.498  32.448  -3.965  1.00 88.25           O  
ANISOU 3702  O   GLU B 143    12622  10488  10420    578   -337    753       O  
ATOM   3703  CB  GLU B 143      60.989  32.397  -6.730  1.00 92.84           C  
ANISOU 3703  CB  GLU B 143    13358  10988  10928    831   -297    850       C  
ATOM   3704  CG  GLU B 143      61.216  32.535  -8.229  1.00100.23           C  
ANISOU 3704  CG  GLU B 143    14388  11868  11826    991   -260    906       C  
ATOM   3705  CD  GLU B 143      61.973  31.357  -8.823  1.00106.24           C  
ANISOU 3705  CD  GLU B 143    15238  12607  12520   1044   -315    945       C  
ATOM   3706  OE1 GLU B 143      62.435  30.487  -8.050  1.00106.25           O  
ANISOU 3706  OE1 GLU B 143    15231  12637  12502    960   -369    928       O  
ATOM   3707  OE2 GLU B 143      62.100  31.301 -10.065  1.00107.64           O  
ANISOU 3707  OE2 GLU B 143    15507  12736  12656   1184   -302    995       O  
ATOM   3708  N   ALA B 144      59.024  34.136  -4.111  1.00 76.49           N  
ANISOU 3708  N   ALA B 144    11058   9017   8990    577   -279    741       N  
ATOM   3709  CA  ALA B 144      58.621  34.080  -2.718  1.00 69.66           C  
ANISOU 3709  CA  ALA B 144    10124   8186   8158    450   -311    698       C  
ATOM   3710  C   ALA B 144      57.451  33.142  -2.480  1.00 70.81           C  
ANISOU 3710  C   ALA B 144    10298   8356   8252    390   -410    661       C  
ATOM   3711  O   ALA B 144      57.077  32.928  -1.324  1.00 74.57           O  
ANISOU 3711  O   ALA B 144    10739   8846   8747    289   -431    628       O  
ATOM   3712  CB  ALA B 144      58.258  35.483  -2.220  1.00 63.75           C  
ANISOU 3712  CB  ALA B 144     9287   7451   7483    417   -237    691       C  
ATOM   3713  N   ALA B 145      56.867  32.579  -3.539  1.00 76.15           N  
ANISOU 3713  N   ALA B 145    11035   9032   8866    453   -463    658       N  
ATOM   3714  CA  ALA B 145      55.704  31.714  -3.372  1.00 75.69           C  
ANISOU 3714  CA  ALA B 145    10989   8995   8776    389   -544    599       C  
ATOM   3715  C   ALA B 145      56.029  30.504  -2.511  1.00 71.97           C  
ANISOU 3715  C   ALA B 145    10564   8503   8279    302   -572    584       C  
ATOM   3716  O   ALA B 145      55.218  30.095  -1.671  1.00 72.39           O  
ANISOU 3716  O   ALA B 145    10603   8558   8344    200   -589    532       O  
ATOM   3717  CB  ALA B 145      55.175  31.273  -4.736  1.00 77.13           C  
ANISOU 3717  CB  ALA B 145    11226   9183   8898    490   -601    583       C  
ATOM   3718  N   ASN B 146      57.212  29.918  -2.702  1.00 70.63           N  
ANISOU 3718  N   ASN B 146    10460   8309   8069    350   -566    626       N  
ATOM   3719  CA  ASN B 146      57.597  28.775  -1.884  1.00 68.05           C  
ANISOU 3719  CA  ASN B 146    10199   7962   7694    294   -584    612       C  
ATOM   3720  C   ASN B 146      57.818  29.187  -0.435  1.00 68.73           C  
ANISOU 3720  C   ASN B 146    10236   8053   7825    225   -547    592       C  
ATOM   3721  O   ASN B 146      57.516  28.415   0.481  1.00 71.25           O  
ANISOU 3721  O   ASN B 146    10605   8352   8114    160   -554    559       O  
ATOM   3722  CB  ASN B 146      58.847  28.119  -2.459  1.00 71.75           C  
ANISOU 3722  CB  ASN B 146    10749   8415   8097    378   -591    659       C  
ATOM   3723  CG  ASN B 146      58.821  26.619  -2.321  1.00 83.20           C  
ANISOU 3723  CG  ASN B 146    12316   9842   9453    354   -631    646       C  
ATOM   3724  OD1 ASN B 146      59.308  26.065  -1.336  1.00 94.54           O  
ANISOU 3724  OD1 ASN B 146    13801  11270  10851    326   -618    632       O  
ATOM   3725  ND2 ASN B 146      58.243  25.945  -3.312  1.00 85.60           N  
ANISOU 3725  ND2 ASN B 146    12675  10136   9714    377   -676    642       N  
ATOM   3726  N   PHE B 147      58.319  30.406  -0.213  1.00 70.62           N  
ANISOU 3726  N   PHE B 147    10385   8310   8136    244   -500    608       N  
ATOM   3727  CA  PHE B 147      58.591  30.882   1.142  1.00 65.52           C  
ANISOU 3727  CA  PHE B 147     9683   7675   7539    194   -471    583       C  
ATOM   3728  C   PHE B 147      57.307  31.185   1.903  1.00 63.15           C  
ANISOU 3728  C   PHE B 147     9341   7375   7276    101   -475    553       C  
ATOM   3729  O   PHE B 147      57.204  30.885   3.098  1.00 64.80           O  
ANISOU 3729  O   PHE B 147     9565   7571   7484     51   -472    526       O  
ATOM   3730  CB  PHE B 147      59.465  32.128   1.073  1.00 66.07           C  
ANISOU 3730  CB  PHE B 147     9658   7760   7686    235   -410    596       C  
ATOM   3731  CG  PHE B 147      59.856  32.673   2.407  1.00 67.76           C  
ANISOU 3731  CG  PHE B 147     9800   7991   7956    198   -387    558       C  
ATOM   3732  CD1 PHE B 147      60.608  31.919   3.284  1.00 73.43           C  
ANISOU 3732  CD1 PHE B 147    10558   8712   8629    217   -412    522       C  
ATOM   3733  CD2 PHE B 147      59.490  33.955   2.776  1.00 68.02           C  
ANISOU 3733  CD2 PHE B 147     9730   8037   8077    161   -340    555       C  
ATOM   3734  CE1 PHE B 147      60.980  32.430   4.513  1.00 70.71           C  
ANISOU 3734  CE1 PHE B 147    10148   8387   8332    207   -400    475       C  
ATOM   3735  CE2 PHE B 147      59.861  34.473   3.999  1.00 67.31           C  
ANISOU 3735  CE2 PHE B 147     9569   7963   8042    134   -324    516       C  
ATOM   3736  CZ  PHE B 147      60.604  33.708   4.869  1.00 68.55           C  
ANISOU 3736  CZ  PHE B 147     9762   8126   8159    161   -358    472       C  
ATOM   3737  N   CYS B 148      56.319  31.786   1.236  1.00 62.91           N  
ANISOU 3737  N   CYS B 148     9266   7362   7275     90   -478    553       N  
ATOM   3738  CA  CYS B 148      55.062  32.089   1.911  1.00 64.52           C  
ANISOU 3738  CA  CYS B 148     9423   7574   7517      2   -483    517       C  
ATOM   3739  C   CYS B 148      54.312  30.826   2.300  1.00 67.56           C  
ANISOU 3739  C   CYS B 148     9881   7926   7863    -69   -510    469       C  
ATOM   3740  O   CYS B 148      53.576  30.827   3.293  1.00 66.83           O  
ANISOU 3740  O   CYS B 148     9773   7817   7803   -152   -495    437       O  
ATOM   3741  CB  CYS B 148      54.175  32.970   1.032  1.00 68.35           C  
ANISOU 3741  CB  CYS B 148     9849   8096   8024     27   -486    513       C  
ATOM   3742  SG  CYS B 148      54.861  34.592   0.668  1.00 71.34           S  
ANISOU 3742  SG  CYS B 148    10159   8495   8451    101   -414    565       S  
ATOM   3743  N   ALA B 149      54.451  29.755   1.517  1.00 68.21           N  
ANISOU 3743  N   ALA B 149    10046   7989   7880    -37   -539    462       N  
ATOM   3744  CA  ALA B 149      53.803  28.500   1.879  1.00 67.71           C  
ANISOU 3744  CA  ALA B 149    10065   7880   7782   -109   -542    410       C  
ATOM   3745  C   ALA B 149      54.410  27.918   3.147  1.00 65.40           C  
ANISOU 3745  C   ALA B 149     9853   7539   7456   -130   -502    416       C  
ATOM   3746  O   ALA B 149      53.689  27.391   4.004  1.00 63.90           O  
ANISOU 3746  O   ALA B 149     9708   7299   7272   -210   -465    372       O  
ATOM   3747  CB  ALA B 149      53.901  27.507   0.723  1.00 69.91           C  
ANISOU 3747  CB  ALA B 149    10419   8151   7994    -63   -579    403       C  
ATOM   3748  N   LEU B 150      55.735  28.001   3.284  1.00 67.07           N  
ANISOU 3748  N   LEU B 150    10091   7762   7631    -49   -502    460       N  
ATOM   3749  CA  LEU B 150      56.380  27.536   4.505  1.00 60.85           C  
ANISOU 3749  CA  LEU B 150     9381   6942   6799    -34   -473    453       C  
ATOM   3750  C   LEU B 150      55.926  28.354   5.709  1.00 58.87           C  
ANISOU 3750  C   LEU B 150     9063   6687   6619    -82   -444    436       C  
ATOM   3751  O   LEU B 150      55.650  27.798   6.778  1.00 59.14           O  
ANISOU 3751  O   LEU B 150     9179   6664   6625   -107   -408    410       O  
ATOM   3752  CB  LEU B 150      57.898  27.602   4.353  1.00 55.36           C  
ANISOU 3752  CB  LEU B 150     8695   6280   6060     74   -489    480       C  
ATOM   3753  CG  LEU B 150      58.542  26.520   3.492  1.00 61.16           C  
ANISOU 3753  CG  LEU B 150     9539   7006   6693    135   -512    500       C  
ATOM   3754  CD1 LEU B 150      60.032  26.774   3.402  1.00 70.47           C  
ANISOU 3754  CD1 LEU B 150    10700   8227   7849    237   -525    515       C  
ATOM   3755  CD2 LEU B 150      58.272  25.142   4.069  1.00 61.35           C  
ANISOU 3755  CD2 LEU B 150     9727   6968   6616    117   -488    474       C  
ATOM   3756  N   ILE B 151      55.829  29.675   5.550  1.00 52.05           N  
ANISOU 3756  N   ILE B 151     8062   5873   5842    -89   -451    454       N  
ATOM   3757  CA  ILE B 151      55.348  30.521   6.641  1.00 54.64           C  
ANISOU 3757  CA  ILE B 151     8321   6200   6240   -137   -429    445       C  
ATOM   3758  C   ILE B 151      53.966  30.066   7.095  1.00 58.98           C  
ANISOU 3758  C   ILE B 151     8906   6699   6804   -236   -407    411       C  
ATOM   3759  O   ILE B 151      53.726  29.851   8.288  1.00 62.80           O  
ANISOU 3759  O   ILE B 151     9440   7132   7289   -261   -372    395       O  
ATOM   3760  CB  ILE B 151      55.339  32.000   6.204  1.00 53.03           C  
ANISOU 3760  CB  ILE B 151     7975   6056   6119   -134   -429    471       C  
ATOM   3761  CG1 ILE B 151      56.762  32.494   5.949  1.00 53.52           C  
ANISOU 3761  CG1 ILE B 151     7997   6151   6188    -48   -423    487       C  
ATOM   3762  CG2 ILE B 151      54.640  32.874   7.233  1.00 43.02           C  
ANISOU 3762  CG2 ILE B 151     6636   4788   4920   -195   -411    466       C  
ATOM   3763  CD1 ILE B 151      56.800  33.922   5.492  1.00 52.86           C  
ANISOU 3763  CD1 ILE B 151     7793   6106   6184    -44   -393    510       C  
ATOM   3764  N   LEU B 152      53.045  29.887   6.144  1.00 62.15           N  
ANISOU 3764  N   LEU B 152     9285   7112   7220   -284   -422    389       N  
ATOM   3765  CA  LEU B 152      51.698  29.441   6.482  1.00 58.29           C  
ANISOU 3765  CA  LEU B 152     8809   6578   6760   -387   -395    332       C  
ATOM   3766  C   LEU B 152      51.718  28.080   7.168  1.00 64.21           C  
ANISOU 3766  C   LEU B 152     9712   7232   7451   -410   -339    302       C  
ATOM   3767  O   LEU B 152      50.967  27.848   8.124  1.00 66.85           O  
ANISOU 3767  O   LEU B 152    10085   7500   7816   -481   -279    268       O  
ATOM   3768  CB  LEU B 152      50.833  29.398   5.218  1.00 57.99           C  
ANISOU 3768  CB  LEU B 152     8713   6581   6739   -411   -433    287       C  
ATOM   3769  CG  LEU B 152      50.447  30.742   4.586  1.00 58.74           C  
ANISOU 3769  CG  LEU B 152     8676   6761   6883   -386   -472    300       C  
ATOM   3770  CD1 LEU B 152      49.975  30.585   3.147  1.00 57.17           C  
ANISOU 3770  CD1 LEU B 152     8450   6608   6663   -346   -523    259       C  
ATOM   3771  CD2 LEU B 152      49.363  31.419   5.400  1.00 60.38           C  
ANISOU 3771  CD2 LEU B 152     8808   6974   7160   -471   -452    270       C  
ATOM   3772  N   ALA B 153      52.578  27.170   6.703  1.00 65.07           N  
ANISOU 3772  N   ALA B 153     9925   7327   7471   -345   -346    315       N  
ATOM   3773  CA  ALA B 153      52.632  25.835   7.292  1.00 67.68           C  
ANISOU 3773  CA  ALA B 153    10428   7562   7725   -353   -279    288       C  
ATOM   3774  C   ALA B 153      53.209  25.876   8.702  1.00 66.28           C  
ANISOU 3774  C   ALA B 153    10332   7339   7512   -297   -235    306       C  
ATOM   3775  O   ALA B 153      52.706  25.200   9.608  1.00 66.24           O  
ANISOU 3775  O   ALA B 153    10446   7235   7486   -331   -148    275       O  
ATOM   3776  CB  ALA B 153      53.451  24.904   6.399  1.00 72.59           C  
ANISOU 3776  CB  ALA B 153    11143   8190   8247   -285   -304    305       C  
ATOM   3777  N   TYR B 154      54.254  26.674   8.912  1.00 66.94           N  
ANISOU 3777  N   TYR B 154    10354   7489   7590   -205   -285    346       N  
ATOM   3778  CA  TYR B 154      54.856  26.758  10.235  1.00 64.59           C  
ANISOU 3778  CA  TYR B 154    10121   7163   7256   -127   -260    346       C  
ATOM   3779  C   TYR B 154      53.914  27.414  11.239  1.00 68.01           C  
ANISOU 3779  C   TYR B 154    10510   7557   7775   -195   -220    338       C  
ATOM   3780  O   TYR B 154      53.875  27.019  12.411  1.00 79.81           O  
ANISOU 3780  O   TYR B 154    12123   8971   9228   -157   -161    324       O  
ATOM   3781  CB  TYR B 154      56.171  27.523  10.159  1.00 54.79           C  
ANISOU 3781  CB  TYR B 154     8794   6012   6011    -20   -325    366       C  
ATOM   3782  CG  TYR B 154      57.353  26.689   9.733  1.00 53.86           C  
ANISOU 3782  CG  TYR B 154     8773   5914   5778     87   -348    364       C  
ATOM   3783  CD1 TYR B 154      57.912  25.750  10.596  1.00 55.46           C  
ANISOU 3783  CD1 TYR B 154     9149   6068   5857    187   -316    337       C  
ATOM   3784  CD2 TYR B 154      57.925  26.849   8.477  1.00 52.04           C  
ANISOU 3784  CD2 TYR B 154     8472   5748   5553    103   -397    388       C  
ATOM   3785  CE1 TYR B 154      59.008  24.993  10.219  1.00 55.56           C  
ANISOU 3785  CE1 TYR B 154     9253   6108   5750    296   -342    331       C  
ATOM   3786  CE2 TYR B 154      59.017  26.096   8.088  1.00 57.25           C  
ANISOU 3786  CE2 TYR B 154     9218   6427   6107    201   -419    388       C  
ATOM   3787  CZ  TYR B 154      59.557  25.170   8.961  1.00 59.56           C  
ANISOU 3787  CZ  TYR B 154     9673   6683   6273    295   -396    358       C  
ATOM   3788  OH  TYR B 154      60.649  24.425   8.565  1.00 55.69           O  
ANISOU 3788  OH  TYR B 154     9271   6223   5667    401   -423    355       O  
ATOM   3789  N   CYS B 155      53.161  28.421  10.811  1.00 57.28           N  
ANISOU 3789  N   CYS B 155     8992   6249   6524   -280   -250    347       N  
ATOM   3790  CA  CYS B 155      52.243  29.099  11.715  1.00 58.26           C  
ANISOU 3790  CA  CYS B 155     9065   6344   6729   -347   -218    344       C  
ATOM   3791  C   CYS B 155      50.897  28.396  11.851  1.00 63.76           C  
ANISOU 3791  C   CYS B 155     9821   6951   7455   -463   -143    298       C  
ATOM   3792  O   CYS B 155      50.043  28.885  12.598  1.00 67.32           O  
ANISOU 3792  O   CYS B 155    10236   7368   7976   -527   -109    292       O  
ATOM   3793  CB  CYS B 155      52.028  30.543  11.264  1.00 57.02           C  
ANISOU 3793  CB  CYS B 155     8718   6283   6663   -379   -275    372       C  
ATOM   3794  SG  CYS B 155      53.550  31.489  11.125  1.00 58.86           S  
ANISOU 3794  SG  CYS B 155     8863   6608   6895   -265   -332    407       S  
ATOM   3795  N   ASN B 156      50.691  27.279  11.154  1.00 64.69           N  
ANISOU 3795  N   ASN B 156    10024   7028   7527   -494   -113    260       N  
ATOM   3796  CA  ASN B 156      49.407  26.576  11.124  1.00 66.19           C  
ANISOU 3796  CA  ASN B 156    10250   7136   7762   -618    -33    189       C  
ATOM   3797  C   ASN B 156      48.282  27.526  10.702  1.00 64.17           C  
ANISOU 3797  C   ASN B 156     9812   6947   7622   -718    -73    159       C  
ATOM   3798  O   ASN B 156      47.321  27.766  11.433  1.00 62.09           O  
ANISOU 3798  O   ASN B 156     9526   6633   7432   -799    -17    128       O  
ATOM   3799  CB  ASN B 156      49.097  25.921  12.475  1.00 68.25           C  
ANISOU 3799  CB  ASN B 156    10675   7253   8004   -626     94    172       C  
ATOM   3800  CG  ASN B 156      49.801  24.586  12.655  1.00 77.37           C  
ANISOU 3800  CG  ASN B 156    12049   8318   9031   -550    168    166       C  
ATOM   3801  OD1 ASN B 156      50.877  24.512  13.253  1.00 83.85           O  
ANISOU 3801  OD1 ASN B 156    12968   9137   9755   -413    156    208       O  
ATOM   3802  ND2 ASN B 156      49.191  23.520  12.139  1.00 78.76           N  
ANISOU 3802  ND2 ASN B 156    12301   8422   9201   -634    246    101       N  
ATOM   3803  N   LYS B 157      48.448  28.113   9.517  1.00 58.47           N  
ANISOU 3803  N   LYS B 157     8967   6340   6910   -695   -169    169       N  
ATOM   3804  CA  LYS B 157      47.458  29.027   8.960  1.00 58.30           C  
ANISOU 3804  CA  LYS B 157     8783   6400   6970   -755   -217    135       C  
ATOM   3805  C   LYS B 157      47.225  28.670   7.500  1.00 60.34           C  
ANISOU 3805  C   LYS B 157     8994   6718   7213   -750   -273     81       C  
ATOM   3806  O   LYS B 157      48.167  28.665   6.702  1.00 63.15           O  
ANISOU 3806  O   LYS B 157     9364   7121   7509   -658   -327    129       O  
ATOM   3807  CB  LYS B 157      47.912  30.484   9.100  1.00 61.23           C  
ANISOU 3807  CB  LYS B 157     9047   6858   7362   -697   -276    212       C  
ATOM   3808  CG  LYS B 157      48.040  30.950  10.543  1.00 62.85           C  
ANISOU 3808  CG  LYS B 157     9277   7012   7590   -698   -233    256       C  
ATOM   3809  CD  LYS B 157      47.892  32.452  10.652  1.00 68.58           C  
ANISOU 3809  CD  LYS B 157     9867   7821   8368   -691   -277    301       C  
ATOM   3810  CE  LYS B 157      46.505  32.904  10.246  1.00 68.82           C  
ANISOU 3810  CE  LYS B 157     9795   7896   8458   -777   -290    246       C  
ATOM   3811  NZ  LYS B 157      45.445  32.296  11.098  1.00 69.90           N  
ANISOU 3811  NZ  LYS B 157     9975   7940   8645   -881   -218    186       N  
ATOM   3812  N   THR B 158      45.979  28.367   7.155  1.00 63.40           N  
ANISOU 3812  N   THR B 158     9326   7104   7660   -842   -261    -28       N  
ATOM   3813  CA  THR B 158      45.618  28.062   5.780  1.00 69.02           C  
ANISOU 3813  CA  THR B 158     9980   7881   8364   -826   -324   -103       C  
ATOM   3814  C   THR B 158      45.354  29.346   4.993  1.00 67.53           C  
ANISOU 3814  C   THR B 158     9649   7821   8187   -761   -418    -94       C  
ATOM   3815  O   THR B 158      45.022  30.395   5.553  1.00 67.57           O  
ANISOU 3815  O   THR B 158     9581   7861   8231   -774   -420    -65       O  
ATOM   3816  CB  THR B 158      44.395  27.152   5.742  1.00 73.15           C  
ANISOU 3816  CB  THR B 158    10493   8351   8950   -947   -268   -254       C  
ATOM   3817  OG1 THR B 158      43.420  27.661   6.654  1.00 76.82           O  
ANISOU 3817  OG1 THR B 158    10892   8794   9503  -1041   -218   -298       O  
ATOM   3818  CG2 THR B 158      44.765  25.720   6.118  1.00 77.33           C  
ANISOU 3818  CG2 THR B 158    11190   8751   9442   -986   -168   -269       C  
ATOM   3819  N   VAL B 159      45.510  29.252   3.670  1.00 62.42           N  
ANISOU 3819  N   VAL B 159     8979   7241   7498   -678   -490   -118       N  
ATOM   3820  CA  VAL B 159      45.309  30.419   2.824  1.00 60.88           C  
ANISOU 3820  CA  VAL B 159     8682   7158   7292   -585   -565   -110       C  
ATOM   3821  C   VAL B 159      43.889  30.941   2.999  1.00 62.07           C  
ANISOU 3821  C   VAL B 159     8715   7361   7508   -651   -578   -220       C  
ATOM   3822  O   VAL B 159      42.930  30.169   3.116  1.00 66.57           O  
ANISOU 3822  O   VAL B 159     9258   7904   8133   -749   -556   -352       O  
ATOM   3823  CB  VAL B 159      45.600  30.052   1.360  1.00 63.45           C  
ANISOU 3823  CB  VAL B 159     9022   7529   7556   -473   -634   -134       C  
ATOM   3824  CG1 VAL B 159      45.515  31.275   0.468  1.00 66.22           C  
ANISOU 3824  CG1 VAL B 159     9304   7981   7875   -342   -694   -115       C  
ATOM   3825  CG2 VAL B 159      46.970  29.396   1.247  1.00 61.33           C  
ANISOU 3825  CG2 VAL B 159     8874   7202   7225   -421   -616    -33       C  
ATOM   3826  N   GLY B 160      43.749  32.264   3.029  1.00 59.89           N  
ANISOU 3826  N   GLY B 160     8367   7159   7228   -598   -603   -173       N  
ATOM   3827  CA  GLY B 160      42.458  32.902   3.171  1.00 61.84           C  
ANISOU 3827  CA  GLY B 160     8503   7473   7520   -639   -624   -268       C  
ATOM   3828  C   GLY B 160      42.092  33.312   4.581  1.00 60.56           C  
ANISOU 3828  C   GLY B 160     8323   7264   7422   -752   -561   -233       C  
ATOM   3829  O   GLY B 160      41.148  34.091   4.757  1.00 62.09           O  
ANISOU 3829  O   GLY B 160     8424   7523   7643   -773   -580   -283       O  
ATOM   3830  N   GLU B 161      42.810  32.834   5.589  1.00 64.27           N  
ANISOU 3830  N   GLU B 161     8884   7626   7908   -810   -491   -151       N  
ATOM   3831  CA  GLU B 161      42.493  33.176   6.967  1.00 66.66           C  
ANISOU 3831  CA  GLU B 161     9188   7873   8268   -899   -429   -115       C  
ATOM   3832  C   GLU B 161      43.175  34.478   7.355  1.00 60.18           C  
ANISOU 3832  C   GLU B 161     8348   7093   7423   -831   -443     18       C  
ATOM   3833  O   GLU B 161      44.286  34.768   6.902  1.00 55.28           O  
ANISOU 3833  O   GLU B 161     7762   6492   6750   -735   -462    101       O  
ATOM   3834  CB  GLU B 161      42.923  32.057   7.919  1.00 70.11           C  
ANISOU 3834  CB  GLU B 161     9750   8169   8721   -966   -341    -97       C  
ATOM   3835  CG  GLU B 161      42.067  30.798   7.846  1.00 78.34           C  
ANISOU 3835  CG  GLU B 161    10816   9140   9810  -1069   -284   -237       C  
ATOM   3836  CD  GLU B 161      40.637  31.034   8.306  1.00 89.51           C  
ANISOU 3836  CD  GLU B 161    12135  10556  11319  -1181   -252   -347       C  
ATOM   3837  OE1 GLU B 161      40.442  31.802   9.274  1.00 92.24           O  
ANISOU 3837  OE1 GLU B 161    12465  10887  11695  -1207   -228   -283       O  
ATOM   3838  OE2 GLU B 161      39.708  30.448   7.706  1.00 96.38           O  
ANISOU 3838  OE2 GLU B 161    12941  11444  12236  -1243   -252   -505       O  
ATOM   3839  N   LEU B 162      42.482  35.273   8.171  1.00 59.53           N  
ANISOU 3839  N   LEU B 162     8209   7024   7385   -885   -428     28       N  
ATOM   3840  CA  LEU B 162      43.066  36.481   8.732  1.00 64.44           C  
ANISOU 3840  CA  LEU B 162     8816   7672   7997   -839   -427    148       C  
ATOM   3841  C   LEU B 162      44.179  36.120   9.707  1.00 69.84           C  
ANISOU 3841  C   LEU B 162     9593   8259   8683   -834   -380    234       C  
ATOM   3842  O   LEU B 162      44.143  35.074  10.361  1.00 77.50           O  
ANISOU 3842  O   LEU B 162    10644   9130   9672   -888   -331    206       O  
ATOM   3843  CB  LEU B 162      42.001  37.316   9.437  1.00 59.27           C  
ANISOU 3843  CB  LEU B 162     8086   7046   7386   -902   -423    138       C  
ATOM   3844  CG  LEU B 162      40.784  37.720   8.609  1.00 55.14           C  
ANISOU 3844  CG  LEU B 162     7464   6631   6855   -899   -474     32       C  
ATOM   3845  CD1 LEU B 162      39.722  38.357   9.503  1.00 54.87           C  
ANISOU 3845  CD1 LEU B 162     7367   6610   6872   -979   -460     17       C  
ATOM   3846  CD2 LEU B 162      41.212  38.669   7.496  1.00 55.60           C  
ANISOU 3846  CD2 LEU B 162     7498   6796   6831   -763   -523     71       C  
ATOM   3847  N   GLY B 163      45.170  37.008   9.817  1.00 67.74           N  
ANISOU 3847  N   GLY B 163     9317   8023   8396   -760   -388    328       N  
ATOM   3848  CA  GLY B 163      46.370  36.713  10.572  1.00 62.49           C  
ANISOU 3848  CA  GLY B 163     8726   7292   7724   -724   -361    388       C  
ATOM   3849  C   GLY B 163      46.848  37.891  11.398  1.00 57.02           C  
ANISOU 3849  C   GLY B 163     7990   6618   7057   -698   -353    465       C  
ATOM   3850  O   GLY B 163      46.305  38.999  11.326  1.00 53.08           O  
ANISOU 3850  O   GLY B 163     7411   6181   6575   -709   -362    487       O  
ATOM   3851  N   ASP B 164      47.894  37.622  12.175  1.00 60.22           N  
ANISOU 3851  N   ASP B 164     8452   6970   7459   -654   -337    496       N  
ATOM   3852  CA  ASP B 164      48.534  38.588  13.059  1.00 57.90           C  
ANISOU 3852  CA  ASP B 164     8119   6686   7195   -619   -332    549       C  
ATOM   3853  C   ASP B 164      50.008  38.673  12.683  1.00 56.38           C  
ANISOU 3853  C   ASP B 164     7923   6516   6984   -529   -337    559       C  
ATOM   3854  O   ASP B 164      50.673  37.644  12.546  1.00 55.88           O  
ANISOU 3854  O   ASP B 164     7937   6417   6879   -488   -340    532       O  
ATOM   3855  CB  ASP B 164      48.352  38.153  14.519  1.00 57.29           C  
ANISOU 3855  CB  ASP B 164     8112   6519   7135   -633   -310    553       C  
ATOM   3856  CG  ASP B 164      48.884  39.162  15.516  1.00 65.40           C  
ANISOU 3856  CG  ASP B 164     9094   7558   8198   -591   -315    597       C  
ATOM   3857  OD1 ASP B 164      48.143  39.505  16.463  1.00 66.13           O  
ANISOU 3857  OD1 ASP B 164     9188   7616   8323   -630   -305    621       O  
ATOM   3858  OD2 ASP B 164      50.040  39.610  15.363  1.00 71.91           O  
ANISOU 3858  OD2 ASP B 164     9877   8423   9022   -521   -327    602       O  
ATOM   3859  N   VAL B 165      50.510  39.897  12.490  1.00 61.28           N  
ANISOU 3859  N   VAL B 165     8455   7195   7635   -501   -328    590       N  
ATOM   3860  CA  VAL B 165      51.906  40.063  12.085  1.00 59.48           C  
ANISOU 3860  CA  VAL B 165     8205   6987   7408   -425   -316    583       C  
ATOM   3861  C   VAL B 165      52.845  39.721  13.234  1.00 60.77           C  
ANISOU 3861  C   VAL B 165     8394   7115   7581   -373   -326    558       C  
ATOM   3862  O   VAL B 165      53.833  39.000  13.053  1.00 63.94           O  
ANISOU 3862  O   VAL B 165     8837   7508   7950   -308   -335    523       O  
ATOM   3863  CB  VAL B 165      52.146  41.486  11.556  1.00 53.84           C  
ANISOU 3863  CB  VAL B 165     7395   6329   6732   -415   -275    612       C  
ATOM   3864  CG1 VAL B 165      53.634  41.752  11.400  1.00 51.18           C  
ANISOU 3864  CG1 VAL B 165     7020   6000   6425   -350   -244    588       C  
ATOM   3865  CG2 VAL B 165      51.452  41.659  10.231  1.00 55.95           C  
ANISOU 3865  CG2 VAL B 165     7667   6631   6960   -418   -265    623       C  
ATOM   3866  N   ARG B 166      52.540  40.210  14.437  1.00 56.00           N  
ANISOU 3866  N   ARG B 166     7771   6493   7013   -386   -330    571       N  
ATOM   3867  CA  ARG B 166      53.371  39.898  15.593  1.00 53.51           C  
ANISOU 3867  CA  ARG B 166     7488   6147   6697   -308   -348    535       C  
ATOM   3868  C   ARG B 166      53.375  38.404  15.875  1.00 60.29           C  
ANISOU 3868  C   ARG B 166     8492   6937   7479   -270   -357    507       C  
ATOM   3869  O   ARG B 166      54.419  37.828  16.202  1.00 63.83           O  
ANISOU 3869  O   ARG B 166     8987   7378   7887   -172   -373    459       O  
ATOM   3870  CB  ARG B 166      52.866  40.640  16.827  1.00 53.41           C  
ANISOU 3870  CB  ARG B 166     7446   6117   6729   -322   -353    561       C  
ATOM   3871  CG  ARG B 166      53.700  40.382  18.061  1.00 57.55           C  
ANISOU 3871  CG  ARG B 166     8006   6613   7247   -214   -379    514       C  
ATOM   3872  CD  ARG B 166      53.008  40.886  19.313  1.00 61.63           C  
ANISOU 3872  CD  ARG B 166     8531   7091   7794   -220   -385    548       C  
ATOM   3873  NE  ARG B 166      51.786  40.121  19.536  1.00 62.83           N  
ANISOU 3873  NE  ARG B 166     8798   7164   7912   -280   -362    585       N  
ATOM   3874  CZ  ARG B 166      51.750  38.947  20.155  1.00 64.89           C  
ANISOU 3874  CZ  ARG B 166     9210   7334   8111   -220   -347    561       C  
ATOM   3875  NH1 ARG B 166      52.871  38.400  20.605  1.00 60.09           N  
ANISOU 3875  NH1 ARG B 166     8662   6717   7452    -84   -368    503       N  
ATOM   3876  NH2 ARG B 166      50.596  38.312  20.311  1.00 71.20           N  
ANISOU 3876  NH2 ARG B 166    10104   8050   8897   -292   -302    585       N  
ATOM   3877  N   GLU B 167      52.217  37.766  15.746  1.00 60.87           N  
ANISOU 3877  N   GLU B 167     8639   6960   7530   -344   -340    525       N  
ATOM   3878  CA  GLU B 167      52.130  36.339  16.013  1.00 61.71           C  
ANISOU 3878  CA  GLU B 167     8897   6983   7565   -319   -322    496       C  
ATOM   3879  C   GLU B 167      52.958  35.549  15.004  1.00 59.54           C  
ANISOU 3879  C   GLU B 167     8661   6732   7231   -275   -333    469       C  
ATOM   3880  O   GLU B 167      53.633  34.579  15.373  1.00 51.88           O  
ANISOU 3880  O   GLU B 167     7805   5719   6186   -191   -329    436       O  
ATOM   3881  CB  GLU B 167      50.671  35.905  16.019  1.00 72.85           C  
ANISOU 3881  CB  GLU B 167    10357   8335   8988   -427   -284    504       C  
ATOM   3882  CG  GLU B 167      50.428  34.552  16.643  1.00 88.01           C  
ANISOU 3882  CG  GLU B 167    12450  10138  10851   -411   -230    475       C  
ATOM   3883  CD  GLU B 167      48.956  34.172  16.677  1.00 97.32           C  
ANISOU 3883  CD  GLU B 167    13660  11250  12067   -533   -174    463       C  
ATOM   3884  OE1 GLU B 167      48.104  35.024  16.325  1.00 92.15           O  
ANISOU 3884  OE1 GLU B 167    12885  10651  11477   -620   -193    476       O  
ATOM   3885  OE2 GLU B 167      48.656  33.032  17.109  1.00108.32           O  
ANISOU 3885  OE2 GLU B 167    15203  12530  13422   -536   -101    431       O  
ATOM   3886  N   THR B 168      52.948  35.983  13.729  1.00 59.16           N  
ANISOU 3886  N   THR B 168     8527   6750   7203   -314   -345    482       N  
ATOM   3887  CA  THR B 168      53.724  35.315  12.672  1.00 59.22           C  
ANISOU 3887  CA  THR B 168     8565   6778   7158   -270   -356    465       C  
ATOM   3888  C   THR B 168      55.227  35.483  12.899  1.00 59.61           C  
ANISOU 3888  C   THR B 168     8590   6862   7197   -163   -373    437       C  
ATOM   3889  O   THR B 168      55.994  34.530  12.727  1.00 57.25           O  
ANISOU 3889  O   THR B 168     8375   6551   6826    -93   -384    409       O  
ATOM   3890  CB  THR B 168      53.327  35.848  11.292  1.00 58.00           C  
ANISOU 3890  CB  THR B 168     8331   6679   7027   -315   -360    486       C  
ATOM   3891  OG1 THR B 168      51.939  35.600  11.034  1.00 58.88           O  
ANISOU 3891  OG1 THR B 168     8457   6772   7143   -401   -355    483       O  
ATOM   3892  CG2 THR B 168      54.142  35.195  10.187  1.00 56.16           C  
ANISOU 3892  CG2 THR B 168     8135   6461   6742   -260   -371    477       C  
ATOM   3893  N   MET B 169      55.672  36.683  13.288  1.00 62.28           N  
ANISOU 3893  N   MET B 169     8809   7246   7608   -147   -373    435       N  
ATOM   3894  CA  MET B 169      57.101  36.890  13.509  1.00 58.61           C  
ANISOU 3894  CA  MET B 169     8295   6820   7153    -51   -386    380       C  
ATOM   3895  C   MET B 169      57.613  36.005  14.642  1.00 51.99           C  
ANISOU 3895  C   MET B 169     7563   5949   6244     52   -414    327       C  
ATOM   3896  O   MET B 169      58.649  35.343  14.505  1.00 53.94           O  
ANISOU 3896  O   MET B 169     7851   6213   6431    145   -434    275       O  
ATOM   3897  CB  MET B 169      57.403  38.362  13.809  1.00 55.05           C  
ANISOU 3897  CB  MET B 169     7692   6418   6807    -63   -367    372       C  
ATOM   3898  CG  MET B 169      57.046  39.360  12.703  1.00 60.34           C  
ANISOU 3898  CG  MET B 169     8272   7118   7535   -136   -319    419       C  
ATOM   3899  SD  MET B 169      57.850  39.084  11.113  1.00 69.31           S  
ANISOU 3899  SD  MET B 169     9409   8274   8653   -106   -289    414       S  
ATOM   3900  CE  MET B 169      59.546  39.418  11.546  1.00 59.11           C  
ANISOU 3900  CE  MET B 169     8025   7016   7417    -22   -276    317       C  
ATOM   3901  N   SER B 170      56.893  35.966  15.769  1.00 48.22           N  
ANISOU 3901  N   SER B 170     7142   5419   5761     49   -412    339       N  
ATOM   3902  CA  SER B 170      57.384  35.194  16.910  1.00 60.71           C  
ANISOU 3902  CA  SER B 170     8845   6960   7264    178   -429    286       C  
ATOM   3903  C   SER B 170      57.421  33.699  16.610  1.00 63.83           C  
ANISOU 3903  C   SER B 170     9419   7300   7536    217   -412    280       C  
ATOM   3904  O   SER B 170      58.306  32.994  17.110  1.00 64.28           O  
ANISOU 3904  O   SER B 170     9570   7354   7501    358   -431    220       O  
ATOM   3905  CB  SER B 170      56.539  35.470  18.152  1.00 60.00           C  
ANISOU 3905  CB  SER B 170     8797   6807   7193    173   -416    309       C  
ATOM   3906  OG  SER B 170      55.224  35.003  17.959  1.00 77.47           O  
ANISOU 3906  OG  SER B 170    11092   8944   9398     62   -368    369       O  
ATOM   3907  N   TYR B 171      56.486  33.195  15.800  1.00 57.92           N  
ANISOU 3907  N   TYR B 171     8719   6510   6779    105   -377    331       N  
ATOM   3908  CA  TYR B 171      56.581  31.807  15.365  1.00 64.36           C  
ANISOU 3908  CA  TYR B 171     9693   7277   7484    132   -355    321       C  
ATOM   3909  C   TYR B 171      57.837  31.592  14.535  1.00 62.79           C  
ANISOU 3909  C   TYR B 171     9463   7151   7243    206   -396    292       C  
ATOM   3910  O   TYR B 171      58.584  30.633  14.751  1.00 58.87           O  
ANISOU 3910  O   TYR B 171     9094   6642   6634    319   -401    253       O  
ATOM   3911  CB  TYR B 171      55.349  31.413  14.550  1.00 79.41           C  
ANISOU 3911  CB  TYR B 171    11623   9139   9411    -10   -316    362       C  
ATOM   3912  CG  TYR B 171      54.232  30.759  15.329  1.00 93.55           C  
ANISOU 3912  CG  TYR B 171    13544  10815  11186    -61   -245    364       C  
ATOM   3913  CD1 TYR B 171      53.045  31.436  15.587  1.00101.84           C  
ANISOU 3913  CD1 TYR B 171    14521  11844  12329   -173   -223    388       C  
ATOM   3914  CD2 TYR B 171      54.355  29.454  15.785  1.00 99.82           C  
ANISOU 3914  CD2 TYR B 171    14543  11515  11868      5   -188    338       C  
ATOM   3915  CE1 TYR B 171      52.015  30.834  16.291  1.00107.87           C  
ANISOU 3915  CE1 TYR B 171    15401  12493  13093   -227   -143    381       C  
ATOM   3916  CE2 TYR B 171      53.333  28.843  16.488  1.00107.12           C  
ANISOU 3916  CE2 TYR B 171    15599  12315  12787    -44    -94    335       C  
ATOM   3917  CZ  TYR B 171      52.165  29.536  16.738  1.00111.23           C  
ANISOU 3917  CZ  TYR B 171    16032  12813  13418   -165    -70    353       C  
ATOM   3918  OH  TYR B 171      51.150  28.923  17.439  1.00114.78           O  
ANISOU 3918  OH  TYR B 171    16609  13128  13874   -220     38    341       O  
ATOM   3919  N   LEU B 172      58.098  32.495  13.589  1.00 67.50           N  
ANISOU 3919  N   LEU B 172     9901   7822   7925    154   -416    308       N  
ATOM   3920  CA  LEU B 172      59.263  32.343  12.728  1.00 62.76           C  
ANISOU 3920  CA  LEU B 172     9266   7282   7299    215   -440    282       C  
ATOM   3921  C   LEU B 172      60.561  32.560  13.491  1.00 64.55           C  
ANISOU 3921  C   LEU B 172     9452   7560   7514    349   -473    198       C  
ATOM   3922  O   LEU B 172      61.580  31.947  13.159  1.00 72.75           O  
ANISOU 3922  O   LEU B 172    10528   8632   8482    441   -496    153       O  
ATOM   3923  CB  LEU B 172      59.162  33.304  11.547  1.00 56.93           C  
ANISOU 3923  CB  LEU B 172     8385   6590   6658    135   -429    321       C  
ATOM   3924  CG  LEU B 172      58.055  32.997  10.541  1.00 53.39           C  
ANISOU 3924  CG  LEU B 172     7972   6111   6203     37   -414    381       C  
ATOM   3925  CD1 LEU B 172      58.030  34.042   9.440  1.00 45.73           C  
ANISOU 3925  CD1 LEU B 172     6877   5187   5313     -3   -398    413       C  
ATOM   3926  CD2 LEU B 172      58.241  31.604   9.957  1.00 54.13           C  
ANISOU 3926  CD2 LEU B 172     8207   6175   6188     69   -423    381       C  
ATOM   3927  N   PHE B 173      60.548  33.428  14.505  1.00 60.65           N  
ANISOU 3927  N   PHE B 173     8875   7080   7088    369   -481    165       N  
ATOM   3928  CA  PHE B 173      61.744  33.639  15.319  1.00 54.47           C  
ANISOU 3928  CA  PHE B 173     8043   6354   6298    510   -522     58       C  
ATOM   3929  C   PHE B 173      62.157  32.367  16.053  1.00 56.67           C  
ANISOU 3929  C   PHE B 173     8511   6604   6418    663   -545      7       C  
ATOM   3930  O   PHE B 173      63.338  32.194  16.375  1.00 55.27           O  
ANISOU 3930  O   PHE B 173     8318   6489   6192    807   -589    -96       O  
ATOM   3931  CB  PHE B 173      61.505  34.769  16.315  1.00 46.31           C  
ANISOU 3931  CB  PHE B 173     6898   5333   5365    504   -528     35       C  
ATOM   3932  CG  PHE B 173      61.456  36.130  15.696  1.00 47.44           C  
ANISOU 3932  CG  PHE B 173     6848   5520   5656    392   -498     56       C  
ATOM   3933  CD1 PHE B 173      60.807  37.172  16.340  1.00 55.11           C  
ANISOU 3933  CD1 PHE B 173     7736   6485   6719    333   -486     81       C  
ATOM   3934  CD2 PHE B 173      62.037  36.368  14.465  1.00 46.70           C  
ANISOU 3934  CD2 PHE B 173     6673   5465   5606    352   -471     55       C  
ATOM   3935  CE1 PHE B 173      60.752  38.433  15.774  1.00 58.15           C  
ANISOU 3935  CE1 PHE B 173     7964   6905   7227    237   -443    102       C  
ATOM   3936  CE2 PHE B 173      61.990  37.628  13.891  1.00 49.67           C  
ANISOU 3936  CE2 PHE B 173     6898   5866   6110    262   -418     74       C  
ATOM   3937  CZ  PHE B 173      61.347  38.661  14.545  1.00 56.30           C  
ANISOU 3937  CZ  PHE B 173     7660   6701   7031    205   -402     97       C  
ATOM   3938  N   GLN B 174      61.199  31.474  16.329  1.00 54.96           N  
ANISOU 3938  N   GLN B 174     8477   6291   6115    639   -508     68       N  
ATOM   3939  CA  GLN B 174      61.524  30.199  16.954  1.00 53.29           C  
ANISOU 3939  CA  GLN B 174     8483   6032   5734    787   -502     30       C  
ATOM   3940  C   GLN B 174      62.453  29.375  16.075  1.00 62.42           C  
ANISOU 3940  C   GLN B 174     9690   7235   6794    848   -523      4       C  
ATOM   3941  O   GLN B 174      63.297  28.630  16.586  1.00 71.11           O  
ANISOU 3941  O   GLN B 174    10908   8352   7757   1023   -548    -71       O  
ATOM   3942  CB  GLN B 174      60.247  29.398  17.213  1.00 52.33           C  
ANISOU 3942  CB  GLN B 174     8546   5781   5558    717   -424    103       C  
ATOM   3943  CG  GLN B 174      59.217  30.067  18.106  1.00 52.09           C  
ANISOU 3943  CG  GLN B 174     8493   5687   5611    656   -392    136       C  
ATOM   3944  CD  GLN B 174      59.773  30.447  19.450  1.00 59.10           C  
ANISOU 3944  CD  GLN B 174     9392   6587   6476    824   -427     66       C  
ATOM   3945  OE1 GLN B 174      60.600  29.732  20.017  1.00 62.54           O  
ANISOU 3945  OE1 GLN B 174     9959   7026   6777   1014   -444     -7       O  
ATOM   3946  NE2 GLN B 174      59.300  31.564  19.989  1.00 60.30           N  
ANISOU 3946  NE2 GLN B 174     9415   6748   6749    769   -440     83       N  
ATOM   3947  N   HIS B 175      62.315  29.498  14.756  1.00 60.23           N  
ANISOU 3947  N   HIS B 175     9332   6978   6576    721   -516     62       N  
ATOM   3948  CA  HIS B 175      63.158  28.800  13.801  1.00 56.68           C  
ANISOU 3948  CA  HIS B 175     8919   6569   6048    765   -536     52       C  
ATOM   3949  C   HIS B 175      64.315  29.647  13.304  1.00 55.45           C  
ANISOU 3949  C   HIS B 175     8569   6519   5981    796   -577    -11       C  
ATOM   3950  O   HIS B 175      64.966  29.270  12.327  1.00 64.97           O  
ANISOU 3950  O   HIS B 175     9772   7758   7156    807   -587     -7       O  
ATOM   3951  CB  HIS B 175      62.329  28.306  12.618  1.00 58.70           C  
ANISOU 3951  CB  HIS B 175     9225   6773   6304    629   -500    149       C  
ATOM   3952  CG  HIS B 175      61.353  27.227  12.966  1.00 56.60           C  
ANISOU 3952  CG  HIS B 175     9163   6400   5941    602   -444    187       C  
ATOM   3953  ND1 HIS B 175      61.723  25.905  13.092  1.00 54.87           N  
ANISOU 3953  ND1 HIS B 175     9153   6142   5553    702   -424    172       N  
ATOM   3954  CD2 HIS B 175      60.021  27.270  13.206  1.00 57.17           C  
ANISOU 3954  CD2 HIS B 175     9266   6391   6066    483   -389    232       C  
ATOM   3955  CE1 HIS B 175      60.660  25.180  13.395  1.00 55.28           C  
ANISOU 3955  CE1 HIS B 175     9358   6082   5563    641   -347    205       C  
ATOM   3956  NE2 HIS B 175      59.614  25.983  13.469  1.00 54.77           N  
ANISOU 3956  NE2 HIS B 175     9182   5991   5638    505   -327    237       N  
ATOM   3957  N   ALA B 176      64.592  30.774  13.942  1.00 48.90           N  
ANISOU 3957  N   ALA B 176     7578   5736   5266    808   -592    -74       N  
ATOM   3958  CA  ALA B 176      65.718  31.610  13.548  1.00 51.65           C  
ANISOU 3958  CA  ALA B 176     7734   6176   5715    831   -610   -158       C  
ATOM   3959  C   ALA B 176      66.874  31.428  14.531  1.00 60.31           C  
ANISOU 3959  C   ALA B 176     8819   7345   6750   1020   -669   -313       C  
ATOM   3960  O   ALA B 176      66.681  31.033  15.684  1.00 54.03           O  
ANISOU 3960  O   ALA B 176     8137   6529   5865   1130   -695   -350       O  
ATOM   3961  CB  ALA B 176      65.307  33.080  13.473  1.00 49.23           C  
ANISOU 3961  CB  ALA B 176     7236   5877   5593    709   -573   -139       C  
ATOM   3962  N   ASN B 177      68.089  31.706  14.059  1.00 69.22           N  
ANISOU 3962  N   ASN B 177     9816   8558   7925   1069   -687   -413       N  
ATOM   3963  CA  ASN B 177      69.275  31.546  14.898  1.00 78.54           C  
ANISOU 3963  CA  ASN B 177    10962   9830   9052   1261   -753   -591       C  
ATOM   3964  C   ASN B 177      69.438  32.812  15.732  1.00 77.71           C  
ANISOU 3964  C   ASN B 177    10659   9768   9101   1261   -761   -695       C  
ATOM   3965  O   ASN B 177      70.218  33.716  15.421  1.00 79.43           O  
ANISOU 3965  O   ASN B 177    10664  10050   9467   1229   -744   -796       O  
ATOM   3966  CB  ASN B 177      70.507  31.258  14.044  1.00 85.47           C  
ANISOU 3966  CB  ASN B 177    11775  10782   9917   1312   -766   -670       C  
ATOM   3967  CG  ASN B 177      71.692  30.742  14.865  1.00 85.03           C  
ANISOU 3967  CG  ASN B 177    11732  10826   9748   1541   -848   -859       C  
ATOM   3968  OD1 ASN B 177      71.836  31.048  16.052  1.00 80.07           O  
ANISOU 3968  OD1 ASN B 177    11071  10236   9117   1658   -895   -975       O  
ATOM   3969  ND2 ASN B 177      72.537  29.936  14.228  1.00 86.12           N  
ANISOU 3969  ND2 ASN B 177    11927  11012   9784   1619   -871   -895       N  
ATOM   3970  N   LEU B 178      68.665  32.873  16.819  1.00 76.31           N  
ANISOU 3970  N   LEU B 178    10560   9545   8890   1296   -778   -672       N  
ATOM   3971  CA  LEU B 178      68.698  33.994  17.751  1.00 71.14           C  
ANISOU 3971  CA  LEU B 178     9745   8922   8361   1311   -795   -760       C  
ATOM   3972  C   LEU B 178      69.146  33.575  19.146  1.00 78.38           C  
ANISOU 3972  C   LEU B 178    10741   9877   9161   1546   -877   -898       C  
ATOM   3973  O   LEU B 178      68.948  34.329  20.103  1.00 78.03           O  
ANISOU 3973  O   LEU B 178    10619   9839   9189   1580   -900   -950       O  
ATOM   3974  CB  LEU B 178      67.337  34.685  17.826  1.00 66.39           C  
ANISOU 3974  CB  LEU B 178     9142   8234   7849   1143   -740   -611       C  
ATOM   3975  CG  LEU B 178      66.827  35.330  16.540  1.00 69.18           C  
ANISOU 3975  CG  LEU B 178     9403   8556   8326    931   -660   -490       C  
ATOM   3976  CD1 LEU B 178      65.556  36.112  16.817  1.00 78.52           C  
ANISOU 3976  CD1 LEU B 178    10569   9676   9588    799   -621   -376       C  
ATOM   3977  CD2 LEU B 178      67.888  36.229  15.931  1.00 67.75           C  
ANISOU 3977  CD2 LEU B 178     9001   8449   8291    900   -628   -598       C  
ATOM   3978  N   ASP B 179      69.736  32.383  19.288  1.00 91.60           N  
ANISOU 3978  N   ASP B 179    12582  11576  10645   1724   -922   -956       N  
ATOM   3979  CA  ASP B 179      70.184  31.921  20.600  1.00100.41           C  
ANISOU 3979  CA  ASP B 179    13804  12728  11620   1986   -998  -1094       C  
ATOM   3980  C   ASP B 179      71.313  32.775  21.171  1.00 94.24           C  
ANISOU 3980  C   ASP B 179    12784  12081  10944   2108  -1073  -1327       C  
ATOM   3981  O   ASP B 179      71.494  32.806  22.393  1.00 92.47           O  
ANISOU 3981  O   ASP B 179    12594  11885  10656   2308  -1139  -1446       O  
ATOM   3982  CB  ASP B 179      70.619  30.455  20.522  1.00112.86           C  
ANISOU 3982  CB  ASP B 179    15621  14306  12954   2158  -1018  -1109       C  
ATOM   3983  CG  ASP B 179      71.459  30.160  19.293  1.00128.00           C  
ANISOU 3983  CG  ASP B 179    17461  16293  14878   2105  -1018  -1132       C  
ATOM   3984  OD1 ASP B 179      71.192  29.142  18.619  1.00134.05           O  
ANISOU 3984  OD1 ASP B 179    18417  17004  15514   2076   -982  -1016       O  
ATOM   3985  OD2 ASP B 179      72.361  30.965  18.977  1.00133.81           O  
ANISOU 3985  OD2 ASP B 179    17948  17132  15761   2084  -1044  -1266       O  
ATOM   3986  N   SER B 180      72.062  33.477  20.323  1.00 92.62           N  
ANISOU 3986  N   SER B 180    12339  11953  10901   1998  -1056  -1405       N  
ATOM   3987  CA  SER B 180      73.123  34.364  20.783  1.00 95.27           C  
ANISOU 3987  CA  SER B 180    12416  12412  11372   2081  -1107  -1644       C  
ATOM   3988  C   SER B 180      72.617  35.745  21.190  1.00 93.82           C  
ANISOU 3988  C   SER B 180    12046  12205  11395   1949  -1073  -1638       C  
ATOM   3989  O   SER B 180      73.432  36.598  21.550  1.00 94.97           O  
ANISOU 3989  O   SER B 180    11957  12445  11683   1991  -1100  -1841       O  
ATOM   3990  CB  SER B 180      74.188  34.510  19.696  1.00102.44           C  
ANISOU 3990  CB  SER B 180    13149  13399  12375   2017  -1080  -1744       C  
ATOM   3991  OG  SER B 180      73.597  34.904  18.470  1.00106.81           O  
ANISOU 3991  OG  SER B 180    13669  13869  13046   1760   -967  -1558       O  
ATOM   3992  N   CYS B 181      71.311  35.996  21.118  1.00 89.27           N  
ANISOU 3992  N   CYS B 181    11562  11512  10845   1789  -1011  -1423       N  
ATOM   3993  CA  CYS B 181      70.755  37.280  21.528  1.00 83.84           C  
ANISOU 3993  CA  CYS B 181    10722  10801  10334   1669   -978  -1400       C  
ATOM   3994  C   CYS B 181      70.539  37.321  23.037  1.00 83.33           C  
ANISOU 3994  C   CYS B 181    10720  10737  10203   1854  -1061  -1471       C  
ATOM   3995  O   CYS B 181      70.134  36.328  23.648  1.00 88.80           O  
ANISOU 3995  O   CYS B 181    11658  11378  10705   2002  -1099  -1418       O  
ATOM   3996  CB  CYS B 181      69.434  37.550  20.807  1.00 82.19           C  
ANISOU 3996  CB  CYS B 181    10583  10475  10171   1431   -882  -1148       C  
ATOM   3997  SG  CYS B 181      69.580  37.756  19.020  1.00 79.25           S  
ANISOU 3997  SG  CYS B 181    10127  10089   9897   1217   -774  -1057       S  
ATOM   3998  N   LYS B 182      70.801  38.484  23.632  1.00 73.35           N  
ANISOU 3998  N   LYS B 182     8414  10463   8994   -118     20   -925       N  
ATOM   3999  CA  LYS B 182      70.780  38.641  25.079  1.00 65.33           C  
ANISOU 3999  CA  LYS B 182     7453   9436   7935    -31    -11   -912       C  
ATOM   4000  C   LYS B 182      70.167  39.985  25.442  1.00 65.18           C  
ANISOU 4000  C   LYS B 182     7479   9384   7903    -85    -60   -916       C  
ATOM   4001  O   LYS B 182      70.480  41.007  24.824  1.00 66.23           O  
ANISOU 4001  O   LYS B 182     7585   9542   8036   -182   -112   -937       O  
ATOM   4002  CB  LYS B 182      72.199  38.528  25.647  1.00 62.23           C  
ANISOU 4002  CB  LYS B 182     7009   9133   7504     17    -63   -934       C  
ATOM   4003  CG  LYS B 182      72.327  38.611  27.152  1.00 65.62           C  
ANISOU 4003  CG  LYS B 182     7488   9562   7883    105    -98   -918       C  
ATOM   4004  CD  LYS B 182      73.804  38.510  27.521  1.00 71.10           C  
ANISOU 4004  CD  LYS B 182     8118  10353   8544    147   -154   -948       C  
ATOM   4005  CE  LYS B 182      74.050  38.643  29.010  1.00 72.49           C  
ANISOU 4005  CE  LYS B 182     8338  10540   8664    228   -197   -932       C  
ATOM   4006  NZ  LYS B 182      75.512  38.630  29.296  1.00 71.57           N  
ANISOU 4006  NZ  LYS B 182     8151  10526   8516    265   -257   -971       N  
ATOM   4007  N   ARG B 183      69.286  39.977  26.438  1.00 65.05           N  
ANISOU 4007  N   ARG B 183     7533   9309   7875    -29    -46   -902       N  
ATOM   4008  CA  ARG B 183      68.658  41.189  26.944  1.00 63.44           C  
ANISOU 4008  CA  ARG B 183     7369   9071   7665    -67    -93   -917       C  
ATOM   4009  C   ARG B 183      68.703  41.172  28.463  1.00 62.71           C  
ANISOU 4009  C   ARG B 183     7317   8986   7526      7   -108   -913       C  
ATOM   4010  O   ARG B 183      68.438  40.140  29.090  1.00 57.31           O  
ANISOU 4010  O   ARG B 183     6671   8280   6824     84    -57   -894       O  
ATOM   4011  CB  ARG B 183      67.203  41.326  26.476  1.00 56.91           C  
ANISOU 4011  CB  ARG B 183     6585   8154   6884   -100    -56   -923       C  
ATOM   4012  CG  ARG B 183      66.420  42.415  27.207  1.00 46.04           C  
ANISOU 4012  CG  ARG B 183     5251   6732   5509   -117   -102   -951       C  
ATOM   4013  CD  ARG B 183      65.029  42.577  26.637  1.00 50.12           C  
ANISOU 4013  CD  ARG B 183     5800   7164   6077   -148    -75   -972       C  
ATOM   4014  NE  ARG B 183      65.022  43.190  25.314  1.00 54.72           N  
ANISOU 4014  NE  ARG B 183     6358   7733   6699   -237   -112   -972       N  
ATOM   4015  CZ  ARG B 183      63.942  43.268  24.539  1.00 61.50           C  
ANISOU 4015  CZ  ARG B 183     7236   8524   7608   -271    -94   -986       C  
ATOM   4016  NH1 ARG B 183      62.787  42.762  24.955  1.00 64.66           N  
ANISOU 4016  NH1 ARG B 183     7673   8871   8024   -221    -34  -1010       N  
ATOM   4017  NH2 ARG B 183      64.015  43.840  23.342  1.00 65.66           N  
ANISOU 4017  NH2 ARG B 183     7747   9039   8164   -359   -138   -980       N  
ATOM   4018  N   VAL B 184      69.057  42.311  29.050  1.00 63.66           N  
ANISOU 4018  N   VAL B 184     7432   9136   7622    -22   -176   -932       N  
ATOM   4019  CA  VAL B 184      69.119  42.467  30.497  1.00 62.49           C  
ANISOU 4019  CA  VAL B 184     7314   9002   7426     31   -195   -933       C  
ATOM   4020  C   VAL B 184      68.129  43.553  30.881  1.00 63.03           C  
ANISOU 4020  C   VAL B 184     7416   9019   7515    -15   -220   -964       C  
ATOM   4021  O   VAL B 184      68.236  44.689  30.407  1.00 60.86           O  
ANISOU 4021  O   VAL B 184     7117   8746   7259    -87   -276   -985       O  
ATOM   4022  CB  VAL B 184      70.538  42.810  30.975  1.00 57.51           C  
ANISOU 4022  CB  VAL B 184     6636   8468   6747     45   -253   -936       C  
ATOM   4023  CG1 VAL B 184      70.570  42.936  32.485  1.00 57.11           C  
ANISOU 4023  CG1 VAL B 184     6619   8434   6646     96   -270   -933       C  
ATOM   4024  CG2 VAL B 184      71.502  41.750  30.510  1.00 55.57           C  
ANISOU 4024  CG2 VAL B 184     6348   8273   6495     92   -236   -923       C  
ATOM   4025  N   LEU B 185      67.143  43.189  31.695  1.00 69.15           N  
ANISOU 4025  N   LEU B 185     8246   9744   8286     19   -180   -973       N  
ATOM   4026  CA  LEU B 185      66.113  44.096  32.179  1.00 72.23           C  
ANISOU 4026  CA  LEU B 185     8662  10085   8699    -17   -198  -1020       C  
ATOM   4027  C   LEU B 185      66.303  44.378  33.663  1.00 72.14           C  
ANISOU 4027  C   LEU B 185     8665  10108   8636      7   -217  -1033       C  
ATOM   4028  O   LEU B 185      66.921  43.595  34.386  1.00 76.86           O  
ANISOU 4028  O   LEU B 185     9277  10748   9177     62   -200  -1000       O  
ATOM   4029  CB  LEU B 185      64.717  43.512  31.943  1.00 75.07           C  
ANISOU 4029  CB  LEU B 185     9066  10364   9093    -13   -130  -1044       C  
ATOM   4030  CG  LEU B 185      64.372  43.256  30.481  1.00 81.03           C  
ANISOU 4030  CG  LEU B 185     9806  11081   9902    -41   -106  -1035       C  
ATOM   4031  CD1 LEU B 185      62.931  42.787  30.343  1.00 88.10           C  
ANISOU 4031  CD1 LEU B 185    10743  11903  10829    -37    -39  -1071       C  
ATOM   4032  CD2 LEU B 185      64.625  44.513  29.678  1.00 80.41           C  
ANISOU 4032  CD2 LEU B 185     9691  11000   9862   -114   -187  -1047       C  
ATOM   4033  N   ASN B 186      65.750  45.504  34.115  1.00 71.53           N  
ANISOU 4033  N   ASN B 186     8585  10012   8581    -38   -257  -1083       N  
ATOM   4034  CA  ASN B 186      65.794  45.873  35.526  1.00 74.07           C  
ANISOU 4034  CA  ASN B 186     8916  10367   8861    -32   -272  -1107       C  
ATOM   4035  C   ASN B 186      64.488  46.548  35.920  1.00 70.15           C  
ANISOU 4035  C   ASN B 186     8435   9810   8408    -72   -272  -1183       C  
ATOM   4036  O   ASN B 186      64.073  47.521  35.284  1.00 67.67           O  
ANISOU 4036  O   ASN B 186     8098   9456   8157   -117   -318  -1221       O  
ATOM   4037  CB  ASN B 186      66.971  46.809  35.832  1.00 75.97           C  
ANISOU 4037  CB  ASN B 186     9108  10684   9074    -50   -341  -1098       C  
ATOM   4038  CG  ASN B 186      67.213  46.979  37.325  1.00 75.10           C  
ANISOU 4038  CG  ASN B 186     9002  10624   8906    -36   -347  -1109       C  
ATOM   4039  OD1 ASN B 186      67.006  46.053  38.109  1.00 74.61           O  
ANISOU 4039  OD1 ASN B 186     8984  10564   8800      4   -303  -1094       O  
ATOM   4040  ND2 ASN B 186      67.637  48.173  37.724  1.00 76.03           N  
ANISOU 4040  ND2 ASN B 186     9081  10783   9023    -75   -403  -1137       N  
ATOM   4041  N   VAL B 187      63.856  46.040  36.975  1.00 67.65           N  
ANISOU 4041  N   VAL B 187     8158   9488   8057    -60   -225  -1211       N  
ATOM   4042  CA  VAL B 187      62.639  46.617  37.529  1.00 67.49           C  
ANISOU 4042  CA  VAL B 187     8146   9426   8073   -101   -220  -1303       C  
ATOM   4043  C   VAL B 187      62.964  47.184  38.903  1.00 70.53           C  
ANISOU 4043  C   VAL B 187     8516   9867   8414   -122   -245  -1328       C  
ATOM   4044  O   VAL B 187      63.491  46.471  39.766  1.00 74.45           O  
ANISOU 4044  O   VAL B 187     9043  10413   8832    -96   -219  -1287       O  
ATOM   4045  CB  VAL B 187      61.515  45.571  37.620  1.00 65.52           C  
ANISOU 4045  CB  VAL B 187     7953   9127   7814    -92   -135  -1335       C  
ATOM   4046  CG1 VAL B 187      60.228  46.210  38.140  1.00 64.22           C  
ANISOU 4046  CG1 VAL B 187     7785   8925   7692   -142   -132  -1453       C  
ATOM   4047  CG2 VAL B 187      61.301  44.916  36.263  1.00 65.36           C  
ANISOU 4047  CG2 VAL B 187     7942   9061   7831    -70   -102  -1300       C  
ATOM   4048  N   VAL B 188      62.620  48.453  39.117  1.00 65.76           N  
ANISOU 4048  N   VAL B 188     7870   9254   7862   -169   -299  -1398       N  
ATOM   4049  CA  VAL B 188      62.938  49.160  40.349  1.00 70.62           C  
ANISOU 4049  CA  VAL B 188     8458   9927   8446   -199   -326  -1430       C  
ATOM   4050  C   VAL B 188      61.651  49.670  40.984  1.00 75.23           C  
ANISOU 4050  C   VAL B 188     9034  10474   9077   -249   -317  -1549       C  
ATOM   4051  O   VAL B 188      60.845  50.337  40.323  1.00 68.18           O  
ANISOU 4051  O   VAL B 188     8119   9515   8272   -270   -348  -1617       O  
ATOM   4052  CB  VAL B 188      63.903  50.336  40.093  1.00 69.34           C  
ANISOU 4052  CB  VAL B 188     8241   9804   8304   -215   -405  -1411       C  
ATOM   4053  CG1 VAL B 188      64.123  51.127  41.371  1.00 69.50           C  
ANISOU 4053  CG1 VAL B 188     8225   9883   8299   -251   -426  -1454       C  
ATOM   4054  CG2 VAL B 188      65.226  49.839  39.534  1.00 70.98           C  
ANISOU 4054  CG2 VAL B 188     8447  10064   8460   -173   -412  -1312       C  
ATOM   4055  N   CYS B 189      61.471  49.372  42.268  1.00 83.22           N  
ANISOU 4055  N   CYS B 189    10062  11529  10029   -274   -279  -1581       N  
ATOM   4056  CA  CYS B 189      60.401  49.963  43.052  1.00 88.72           C  
ANISOU 4056  CA  CYS B 189    10736  12213  10763   -336   -273  -1709       C  
ATOM   4057  C   CYS B 189      61.013  50.862  44.120  1.00 91.87           C  
ANISOU 4057  C   CYS B 189    11084  12684  11140   -375   -311  -1727       C  
ATOM   4058  O   CYS B 189      62.125  50.617  44.597  1.00 90.45           O  
ANISOU 4058  O   CYS B 189    10911  12575  10883   -355   -314  -1641       O  
ATOM   4059  CB  CYS B 189      59.528  48.887  43.705  1.00 85.95           C  
ANISOU 4059  CB  CYS B 189    10447  11855  10356   -359   -187  -1753       C  
ATOM   4060  SG  CYS B 189      58.163  49.536  44.699  1.00 83.78           S  
ANISOU 4060  SG  CYS B 189    10137  11575  10120   -452   -171  -1937       S  
ATOM   4061  N   LYS B 190      60.274  51.905  44.499  1.00 94.46           N  
ANISOU 4061  N   LYS B 190    11355  12995  11539   -431   -341  -1846       N  
ATOM   4062  CA  LYS B 190      60.816  52.857  45.462  1.00 95.30           C  
ANISOU 4062  CA  LYS B 190    11403  13170  11636   -473   -377  -1872       C  
ATOM   4063  C   LYS B 190      60.922  52.258  46.857  1.00 93.62           C  
ANISOU 4063  C   LYS B 190    11214  13034  11324   -514   -320  -1876       C  
ATOM   4064  O   LYS B 190      61.756  52.703  47.651  1.00 94.19           O  
ANISOU 4064  O   LYS B 190    11252  13184  11351   -533   -338  -1847       O  
ATOM   4065  CB  LYS B 190      60.008  54.153  45.460  1.00 99.16           C  
ANISOU 4065  CB  LYS B 190    11822  13615  12238   -520   -431  -2003       C  
ATOM   4066  CG  LYS B 190      60.136  54.903  44.143  1.00 98.82           C  
ANISOU 4066  CG  LYS B 190    11764  13501  12282   -486   -508  -1981       C  
ATOM   4067  CD  LYS B 190      59.226  56.105  44.054  1.00 99.34           C  
ANISOU 4067  CD  LYS B 190    11773  13503  12469   -522   -573  -2115       C  
ATOM   4068  CE  LYS B 190      59.374  56.775  42.698  1.00 97.45           C  
ANISOU 4068  CE  LYS B 190    11538  13183  12304   -492   -658  -2079       C  
ATOM   4069  NZ  LYS B 190      58.466  57.942  42.549  1.00 99.30           N  
ANISOU 4069  NZ  LYS B 190    11725  13339  12664   -517   -738  -2208       N  
ATOM   4070  N   THR B 191      60.111  51.256  47.174  1.00 96.34           N  
ANISOU 4070  N   THR B 191    11618  13359  11627   -533   -252  -1910       N  
ATOM   4071  CA  THR B 191      60.190  50.633  48.490  1.00100.25           C  
ANISOU 4071  CA  THR B 191    12153  13922  12017   -585   -201  -1909       C  
ATOM   4072  C   THR B 191      60.593  49.168  48.441  1.00108.61           C  
ANISOU 4072  C   THR B 191    13314  14980  12972   -538   -155  -1797       C  
ATOM   4073  O   THR B 191      61.316  48.711  49.329  1.00113.41           O  
ANISOU 4073  O   THR B 191    13958  15651  13481   -545   -147  -1730       O  
ATOM   4074  CB  THR B 191      58.844  50.765  49.220  1.00 98.16           C  
ANISOU 4074  CB  THR B 191    11875  13647  11774   -680   -159  -2071       C  
ATOM   4075  OG1 THR B 191      57.793  50.253  48.394  1.00 99.11           O  
ANISOU 4075  OG1 THR B 191    12030  13688  11941   -665   -126  -2128       O  
ATOM   4076  CG2 THR B 191      58.551  52.226  49.531  1.00 97.87           C  
ANISOU 4076  CG2 THR B 191    11729  13623  11834   -732   -210  -2188       C  
ATOM   4077  N   CYS B 192      60.154  48.416  47.428  1.00112.48           N  
ANISOU 4077  N   CYS B 192    13854  15400  13484   -489   -127  -1774       N  
ATOM   4078  CA  CYS B 192      60.541  47.010  47.328  1.00116.59           C  
ANISOU 4078  CA  CYS B 192    14472  15913  13914   -440    -85  -1668       C  
ATOM   4079  C   CYS B 192      62.037  46.861  47.074  1.00110.30           C  
ANISOU 4079  C   CYS B 192    13670  15157  13081   -360   -132  -1531       C  
ATOM   4080  O   CYS B 192      62.671  45.928  47.582  1.00108.77           O  
ANISOU 4080  O   CYS B 192    13544  14991  12792   -333   -120  -1446       O  
ATOM   4081  CB  CYS B 192      59.743  46.314  46.228  1.00126.18           C  
ANISOU 4081  CB  CYS B 192    15727  17045  15169   -406    -42  -1680       C  
ATOM   4082  SG  CYS B 192      57.985  46.136  46.580  1.00140.04           S  
ANISOU 4082  SG  CYS B 192    17508  18761  16941   -496     30  -1846       S  
ATOM   4083  N   GLY B 193      62.619  47.777  46.296  1.00108.37           N  
ANISOU 4083  N   GLY B 193    13350  14916  12908   -327   -190  -1513       N  
ATOM   4084  CA  GLY B 193      64.025  47.729  45.955  1.00108.49           C  
ANISOU 4084  CA  GLY B 193    13348  14977  12895   -259   -234  -1405       C  
ATOM   4085  C   GLY B 193      64.235  47.553  44.460  1.00105.53           C  
ANISOU 4085  C   GLY B 193    12966  14553  12579   -200   -247  -1360       C  
ATOM   4086  O   GLY B 193      63.422  48.004  43.644  1.00107.23           O  
ANISOU 4086  O   GLY B 193    13161  14705  12878   -218   -249  -1417       O  
ATOM   4087  N   GLN B 194      65.327  46.872  44.114  1.00 99.61           N  
ANISOU 4087  N   GLN B 194    12232  13832  11783   -131   -259  -1262       N  
ATOM   4088  CA  GLN B 194      65.736  46.710  42.727  1.00 88.70           C  
ANISOU 4088  CA  GLN B 194    10833  12422  10448    -84   -274  -1217       C  
ATOM   4089  C   GLN B 194      65.876  45.225  42.414  1.00 86.04           C  
ANISOU 4089  C   GLN B 194    10563  12059  10068    -22   -231  -1149       C  
ATOM   4090  O   GLN B 194      66.314  44.441  43.262  1.00 82.67           O  
ANISOU 4090  O   GLN B 194    10186  11664   9562      6   -222  -1104       O  
ATOM   4091  CB  GLN B 194      67.065  47.430  42.493  1.00 82.92           C  
ANISOU 4091  CB  GLN B 194    10036  11760   9710    -66   -336  -1179       C  
ATOM   4092  CG  GLN B 194      67.543  47.467  41.069  1.00 82.97           C  
ANISOU 4092  CG  GLN B 194    10014  11748   9761    -42   -357  -1148       C  
ATOM   4093  CD  GLN B 194      68.934  48.033  40.964  1.00 81.30           C  
ANISOU 4093  CD  GLN B 194     9747  11622   9523    -31   -410  -1119       C  
ATOM   4094  OE1 GLN B 194      69.283  48.968  41.684  1.00 77.96           O  
ANISOU 4094  OE1 GLN B 194     9286  11252   9082    -64   -442  -1146       O  
ATOM   4095  NE2 GLN B 194      69.703  47.546  39.991  1.00 83.87           N  
ANISOU 4095  NE2 GLN B 194    10058  11961   9848      7   -418  -1075       N  
ATOM   4096  N   GLN B 195      65.508  44.844  41.188  1.00 89.58           N  
ANISOU 4096  N   GLN B 195    11016  12450  10571     -3   -208  -1141       N  
ATOM   4097  CA  GLN B 195      65.568  43.452  40.755  1.00 93.36           C  
ANISOU 4097  CA  GLN B 195    11552  12897  11022     54   -163  -1083       C  
ATOM   4098  C   GLN B 195      65.787  43.414  39.247  1.00 87.91           C  
ANISOU 4098  C   GLN B 195    10823  12181  10397     75   -167  -1061       C  
ATOM   4099  O   GLN B 195      65.013  44.026  38.505  1.00 90.44           O  
ANISOU 4099  O   GLN B 195    11120  12456  10788     34   -164  -1109       O  
ATOM   4100  CB  GLN B 195      64.269  42.720  41.130  1.00 99.67           C  
ANISOU 4100  CB  GLN B 195    12430  13635  11805     28    -90  -1123       C  
ATOM   4101  CG  GLN B 195      64.123  41.302  40.593  1.00103.83           C  
ANISOU 4101  CG  GLN B 195    13023  14116  12311     78    -32  -1073       C  
ATOM   4102  CD  GLN B 195      65.026  40.313  41.304  1.00111.26           C  
ANISOU 4102  CD  GLN B 195    14020  15086  13167    135    -43   -995       C  
ATOM   4103  OE1 GLN B 195      65.276  40.438  42.504  1.00114.10           O  
ANISOU 4103  OE1 GLN B 195    14408  15485  13462    118    -67   -993       O  
ATOM   4104  NE2 GLN B 195      65.511  39.316  40.571  1.00113.03           N  
ANISOU 4104  NE2 GLN B 195    14261  15290  13393    202    -30   -934       N  
ATOM   4105  N   GLN B 196      66.819  42.700  38.789  1.00 83.14           N  
ANISOU 4105  N   GLN B 196    10210  11606   9773    134   -177   -996       N  
ATOM   4106  CA  GLN B 196      67.125  42.631  37.363  1.00 78.55           C  
ANISOU 4106  CA  GLN B 196     9586  11013   9247    142   -179   -979       C  
ATOM   4107  C   GLN B 196      67.023  41.194  36.863  1.00 78.00           C  
ANISOU 4107  C   GLN B 196     9559  10906   9171    196   -122   -937       C  
ATOM   4108  O   GLN B 196      67.355  40.249  37.584  1.00 80.23           O  
ANISOU 4108  O   GLN B 196     9893  11197   9396    249   -110   -899       O  
ATOM   4109  CB  GLN B 196      68.515  43.208  37.038  1.00 75.99           C  
ANISOU 4109  CB  GLN B 196     9188  10767   8917    150   -244   -959       C  
ATOM   4110  CG  GLN B 196      69.698  42.312  37.321  1.00 81.76           C  
ANISOU 4110  CG  GLN B 196     9916  11554   9596    225   -259   -911       C  
ATOM   4111  CD  GLN B 196      70.980  42.887  36.753  1.00 83.50           C  
ANISOU 4111  CD  GLN B 196    10054  11853   9819    221   -315   -913       C  
ATOM   4112  OE1 GLN B 196      70.976  43.978  36.185  1.00 81.65           O  
ANISOU 4112  OE1 GLN B 196     9777  11629   9618    154   -341   -945       O  
ATOM   4113  NE2 GLN B 196      72.081  42.156  36.895  1.00 87.82           N  
ANISOU 4113  NE2 GLN B 196    10582  12455  10330    289   -336   -887       N  
ATOM   4114  N   THR B 197      66.544  41.034  35.632  1.00 77.04           N  
ANISOU 4114  N   THR B 197     9422  10740   9110    179    -89   -943       N  
ATOM   4115  CA  THR B 197      66.427  39.724  35.006  1.00 79.97           C  
ANISOU 4115  CA  THR B 197     9822  11076   9485    223    -28   -909       C  
ATOM   4116  C   THR B 197      67.152  39.722  33.664  1.00 74.93           C  
ANISOU 4116  C   THR B 197     9113  10462   8896    221    -43   -892       C  
ATOM   4117  O   THR B 197      67.409  40.773  33.070  1.00 72.16           O  
ANISOU 4117  O   THR B 197     8703  10133   8580    167    -89   -914       O  
ATOM   4118  CB  THR B 197      64.958  39.317  34.802  1.00 82.49           C  
ANISOU 4118  CB  THR B 197    10198  11318   9826    198     50   -941       C  
ATOM   4119  OG1 THR B 197      64.354  40.180  33.831  1.00 86.24           O  
ANISOU 4119  OG1 THR B 197    10628  11767  10373    141     43   -982       O  
ATOM   4120  CG2 THR B 197      64.180  39.417  36.112  1.00 79.73           C  
ANISOU 4120  CG2 THR B 197     9914  10952   9427    178     66   -978       C  
ATOM   4121  N   THR B 198      67.485  38.516  33.198  1.00 70.93           N  
ANISOU 4121  N   THR B 198     8613   9948   8390    272     -4   -856       N  
ATOM   4122  CA  THR B 198      68.214  38.318  31.951  1.00 64.78           C  
ANISOU 4122  CA  THR B 198     7761   9197   7654    268     -9   -847       C  
ATOM   4123  C   THR B 198      67.443  37.363  31.054  1.00 61.86           C  
ANISOU 4123  C   THR B 198     7411   8769   7323    270     74   -838       C  
ATOM   4124  O   THR B 198      67.011  36.296  31.503  1.00 61.67           O  
ANISOU 4124  O   THR B 198     7455   8705   7274    321    129   -818       O  
ATOM   4125  CB  THR B 198      69.620  37.766  32.206  1.00 64.97           C  
ANISOU 4125  CB  THR B 198     7749   9287   7648    334    -52   -823       C  
ATOM   4126  OG1 THR B 198      70.349  38.679  33.035  1.00 73.06           O  
ANISOU 4126  OG1 THR B 198     8752  10375   8633    330   -126   -835       O  
ATOM   4127  CG2 THR B 198      70.370  37.561  30.889  1.00 58.57           C  
ANISOU 4127  CG2 THR B 198     6854   8515   6884    316    -54   -832       C  
ATOM   4128  N   LEU B 199      67.306  37.737  29.786  1.00 55.75           N  
ANISOU 4128  N   LEU B 199     6583   7994   6607    210     83   -853       N  
ATOM   4129  CA  LEU B 199      66.574  36.979  28.783  1.00 60.44           C  
ANISOU 4129  CA  LEU B 199     7180   8540   7243    198    163   -850       C  
ATOM   4130  C   LEU B 199      67.513  36.593  27.646  1.00 65.88           C  
ANISOU 4130  C   LEU B 199     7787   9276   7967    185    161   -841       C  
ATOM   4131  O   LEU B 199      68.411  37.362  27.283  1.00 66.99           O  
ANISOU 4131  O   LEU B 199     7863   9477   8112    142     96   -855       O  
ATOM   4132  CB  LEU B 199      65.391  37.789  28.242  1.00 55.99           C  
ANISOU 4132  CB  LEU B 199     6627   7928   6720    125    177   -883       C  
ATOM   4133  CG  LEU B 199      64.340  38.140  29.291  1.00 49.88           C  
ANISOU 4133  CG  LEU B 199     5923   7108   5922    129    187   -914       C  
ATOM   4134  CD1 LEU B 199      63.311  39.075  28.707  1.00 48.46           C  
ANISOU 4134  CD1 LEU B 199     5737   6884   5791     62    178   -960       C  
ATOM   4135  CD2 LEU B 199      63.688  36.864  29.777  1.00 49.83           C  
ANISOU 4135  CD2 LEU B 199     5989   7061   5882    181    275   -905       C  
ATOM   4136  N   LYS B 200      67.318  35.391  27.101  1.00 66.51           N  
ANISOU 4136  N   LYS B 200     7870   9332   8070    217    236   -825       N  
ATOM   4137  CA  LYS B 200      68.114  34.894  25.988  1.00 66.51           C  
ANISOU 4137  CA  LYS B 200     7786   9375   8109    201    247   -827       C  
ATOM   4138  C   LYS B 200      67.196  34.350  24.901  1.00 69.55           C  
ANISOU 4138  C   LYS B 200     8167   9716   8542    161    337   -826       C  
ATOM   4139  O   LYS B 200      66.084  33.892  25.176  1.00 74.26           O  
ANISOU 4139  O   LYS B 200     8834  10248   9133    183    405   -820       O  
ATOM   4140  CB  LYS B 200      69.050  33.781  26.465  1.00 69.29           C  
ANISOU 4140  CB  LYS B 200     8130   9752   8444    296    242   -811       C  
ATOM   4141  CG  LYS B 200      70.130  34.258  27.407  1.00 77.53           C  
ANISOU 4141  CG  LYS B 200     9160  10854   9443    337    149   -816       C  
ATOM   4142  CD  LYS B 200      70.866  33.086  28.043  1.00 85.66           C  
ANISOU 4142  CD  LYS B 200    10206  11889  10454    447    137   -797       C  
ATOM   4143  CE  LYS B 200      71.758  33.554  29.195  1.00 91.41           C  
ANISOU 4143  CE  LYS B 200    10939  12665  11126    496     46   -799       C  
ATOM   4144  NZ  LYS B 200      72.364  32.416  29.946  1.00 93.12           N  
ANISOU 4144  NZ  LYS B 200    11191  12871  11318    611     21   -775       N  
ATOM   4145  N   GLY B 201      67.679  34.376  23.662  1.00 69.87           N  
ANISOU 4145  N   GLY B 201     8123   9798   8628     97    342   -839       N  
ATOM   4146  CA  GLY B 201      66.912  33.827  22.560  1.00 68.63           C  
ANISOU 4146  CA  GLY B 201     7951   9609   8517     54    429   -839       C  
ATOM   4147  C   GLY B 201      65.848  34.753  22.009  1.00 68.90           C  
ANISOU 4147  C   GLY B 201     8005   9603   8570    -30    431   -850       C  
ATOM   4148  O   GLY B 201      66.038  35.972  21.952  1.00 71.60           O  
ANISOU 4148  O   GLY B 201     8338   9961   8907    -92    351   -863       O  
ATOM   4149  N   VAL B 202      64.712  34.175  21.609  1.00 64.33           N  
ANISOU 4149  N   VAL B 202     7459   8970   8013    -30    521   -848       N  
ATOM   4150  CA  VAL B 202      63.633  34.953  21.002  1.00 58.00           C  
ANISOU 4150  CA  VAL B 202     6674   8126   7237   -103    524   -865       C  
ATOM   4151  C   VAL B 202      63.103  35.989  21.982  1.00 59.58           C  
ANISOU 4151  C   VAL B 202     6936   8292   7411    -93    458   -885       C  
ATOM   4152  O   VAL B 202      62.752  37.110  21.594  1.00 57.36           O  
ANISOU 4152  O   VAL B 202     6652   7993   7150   -160    396   -903       O  
ATOM   4153  CB  VAL B 202      62.512  34.013  20.517  1.00 58.87           C  
ANISOU 4153  CB  VAL B 202     6807   8191   7369    -91    643   -869       C  
ATOM   4154  CG1 VAL B 202      61.380  34.803  19.878  1.00 55.14           C  
ANISOU 4154  CG1 VAL B 202     6348   7675   6926   -159    639   -895       C  
ATOM   4155  CG2 VAL B 202      63.072  32.991  19.551  1.00 62.84           C  
ANISOU 4155  CG2 VAL B 202     7240   8732   7903   -104    710   -853       C  
ATOM   4156  N   GLU B 203      63.032  35.634  23.267  1.00 64.00           N  
ANISOU 4156  N   GLU B 203     7553   8837   7926    -12    466   -884       N  
ATOM   4157  CA  GLU B 203      62.496  36.561  24.254  1.00 54.54           C  
ANISOU 4157  CA  GLU B 203     6407   7611   6704     -7    411   -912       C  
ATOM   4158  C   GLU B 203      63.338  37.824  24.373  1.00 55.50           C  
ANISOU 4158  C   GLU B 203     6495   7771   6823    -49    296   -914       C  
ATOM   4159  O   GLU B 203      62.834  38.848  24.847  1.00 56.78           O  
ANISOU 4159  O   GLU B 203     6683   7906   6986    -71    240   -944       O  
ATOM   4160  CB  GLU B 203      62.395  35.871  25.614  1.00 51.45           C  
ANISOU 4160  CB  GLU B 203     6085   7208   6256     73    442   -908       C  
ATOM   4161  CG  GLU B 203      61.243  34.882  25.740  1.00 60.31           C  
ANISOU 4161  CG  GLU B 203     7270   8280   7367    101    553   -925       C  
ATOM   4162  CD  GLU B 203      61.210  34.178  27.095  1.00 67.29           C  
ANISOU 4162  CD  GLU B 203     8235   9150   8180    165    578   -918       C  
ATOM   4163  OE1 GLU B 203      62.182  33.466  27.432  1.00 69.51           O  
ANISOU 4163  OE1 GLU B 203     8518   9457   8435    219    568   -873       O  
ATOM   4164  OE2 GLU B 203      60.215  34.352  27.833  1.00 66.40           O  
ANISOU 4164  OE2 GLU B 203     8185   9003   8040    159    603   -963       O  
ATOM   4165  N   ALA B 204      64.587  37.793  23.906  1.00 59.13           N  
ANISOU 4165  N   ALA B 204     6893   8294   7281    -68    260   -892       N  
ATOM   4166  CA  ALA B 204      65.480  38.939  24.027  1.00 64.48           C  
ANISOU 4166  CA  ALA B 204     7539   9017   7944   -113    157   -898       C  
ATOM   4167  C   ALA B 204      65.246  40.006  22.973  1.00 64.72           C  
ANISOU 4167  C   ALA B 204     7549   9033   8009   -220    105   -911       C  
ATOM   4168  O   ALA B 204      65.821  41.092  23.087  1.00 73.45           O  
ANISOU 4168  O   ALA B 204     8645  10164   9100   -269     18   -920       O  
ATOM   4169  CB  ALA B 204      66.940  38.487  23.963  1.00 63.16           C  
ANISOU 4169  CB  ALA B 204     7312   8932   7756    -96    139   -885       C  
ATOM   4170  N   VAL B 205      64.452  39.731  21.941  1.00 60.12           N  
ANISOU 4170  N   VAL B 205     6964   8411   7469   -263    154   -911       N  
ATOM   4171  CA  VAL B 205      64.271  40.668  20.839  1.00 60.21           C  
ANISOU 4171  CA  VAL B 205     6962   8405   7511   -372     98   -917       C  
ATOM   4172  C   VAL B 205      62.835  41.149  20.698  1.00 62.98           C  
ANISOU 4172  C   VAL B 205     7362   8669   7899   -383     95   -940       C  
ATOM   4173  O   VAL B 205      62.541  41.917  19.777  1.00 62.30           O  
ANISOU 4173  O   VAL B 205     7277   8553   7841   -469     41   -943       O  
ATOM   4174  CB  VAL B 205      64.765  40.066  19.508  1.00 51.86           C  
ANISOU 4174  CB  VAL B 205     5844   7389   6473   -441    140   -901       C  
ATOM   4175  CG1 VAL B 205      66.213  39.581  19.648  1.00 48.29           C  
ANISOU 4175  CG1 VAL B 205     5331   7027   5990   -429    139   -898       C  
ATOM   4176  CG2 VAL B 205      63.845  38.948  19.068  1.00 47.03           C  
ANISOU 4176  CG2 VAL B 205     5235   6742   5893   -407    252   -896       C  
ATOM   4177  N   MET B 206      61.931  40.720  21.577  1.00 63.66           N  
ANISOU 4177  N   MET B 206     7491   8715   7983   -302    146   -963       N  
ATOM   4178  CA  MET B 206      60.535  41.125  21.524  1.00 65.79           C  
ANISOU 4178  CA  MET B 206     7800   8908   8289   -304    146  -1006       C  
ATOM   4179  C   MET B 206      60.113  41.703  22.865  1.00 67.03           C  
ANISOU 4179  C   MET B 206     7998   9041   8431   -254    108  -1049       C  
ATOM   4180  O   MET B 206      60.488  41.183  23.921  1.00 67.77           O  
ANISOU 4180  O   MET B 206     8104   9165   8479   -193    140  -1044       O  
ATOM   4181  CB  MET B 206      59.633  39.948  21.182  1.00 65.27           C  
ANISOU 4181  CB  MET B 206     7742   8820   8237   -269    268  -1015       C  
ATOM   4182  CG  MET B 206      59.958  39.291  19.870  1.00 67.41           C  
ANISOU 4182  CG  MET B 206     7966   9118   8527   -319    320   -978       C  
ATOM   4183  SD  MET B 206      58.813  37.946  19.580  1.00 72.17           S  
ANISOU 4183  SD  MET B 206     8583   9694   9143   -275    470   -996       S  
ATOM   4184  CE  MET B 206      57.272  38.857  19.561  1.00 77.61           C  
ANISOU 4184  CE  MET B 206     9313  10304   9870   -288    431  -1066       C  
ATOM   4185  N   TYR B 207      59.322  42.773  22.815  1.00 66.62           N  
ANISOU 4185  N   TYR B 207     7965   8930   8417   -284     34  -1096       N  
ATOM   4186  CA  TYR B 207      58.699  43.338  24.002  1.00 64.87           C  
ANISOU 4186  CA  TYR B 207     7774   8679   8195   -246      3  -1157       C  
ATOM   4187  C   TYR B 207      57.267  43.728  23.661  1.00 66.28           C  
ANISOU 4187  C   TYR B 207     7970   8782   8431   -254     -7  -1230       C  
ATOM   4188  O   TYR B 207      56.990  44.222  22.566  1.00 68.81           O  
ANISOU 4188  O   TYR B 207     8283   9065   8797   -306    -57  -1225       O  
ATOM   4189  CB  TYR B 207      59.476  44.552  24.555  1.00 60.74           C  
ANISOU 4189  CB  TYR B 207     7244   8172   7661   -272   -111  -1155       C  
ATOM   4190  CG  TYR B 207      58.842  45.112  25.809  1.00 60.14           C  
ANISOU 4190  CG  TYR B 207     7190   8072   7588   -237   -138  -1224       C  
ATOM   4191  CD1 TYR B 207      59.060  44.519  27.046  1.00 63.20           C  
ANISOU 4191  CD1 TYR B 207     7591   8502   7922   -184    -83  -1229       C  
ATOM   4192  CD2 TYR B 207      58.009  46.220  25.753  1.00 63.11           C  
ANISOU 4192  CD2 TYR B 207     7574   8382   8022   -262   -221  -1291       C  
ATOM   4193  CE1 TYR B 207      58.462  45.012  28.196  1.00 65.65           C  
ANISOU 4193  CE1 TYR B 207     7916   8796   8231   -167   -102  -1300       C  
ATOM   4194  CE2 TYR B 207      57.412  46.724  26.896  1.00 67.52           C  
ANISOU 4194  CE2 TYR B 207     8142   8924   8590   -237   -243  -1369       C  
ATOM   4195  CZ  TYR B 207      57.640  46.117  28.113  1.00 69.59           C  
ANISOU 4195  CZ  TYR B 207     8412   9237   8794   -195   -179  -1374       C  
ATOM   4196  OH  TYR B 207      57.044  46.620  29.246  1.00 74.48           O  
ANISOU 4196  OH  TYR B 207     9035   9845   9419   -184   -197  -1458       O  
ATOM   4197  N   MET B 208      56.358  43.481  24.599  1.00 61.21           N  
ANISOU 4197  N   MET B 208     7352   8121   7784   -206     40  -1301       N  
ATOM   4198  CA  MET B 208      54.941  43.773  24.429  1.00 58.58           C  
ANISOU 4198  CA  MET B 208     7030   7725   7505   -204     39  -1395       C  
ATOM   4199  C   MET B 208      54.532  44.783  25.492  1.00 64.35           C  
ANISOU 4199  C   MET B 208     7767   8431   8254   -196    -39  -1478       C  
ATOM   4200  O   MET B 208      54.400  44.432  26.671  1.00 67.53           O  
ANISOU 4200  O   MET B 208     8184   8861   8614   -164     11  -1517       O  
ATOM   4201  CB  MET B 208      54.111  42.495  24.527  1.00 65.46           C  
ANISOU 4201  CB  MET B 208     7919   8601   8352   -167    179  -1429       C  
ATOM   4202  CG  MET B 208      52.620  42.727  24.402  1.00 82.42           C  
ANISOU 4202  CG  MET B 208    10072  10695  10549   -162    188  -1544       C  
ATOM   4203  SD  MET B 208      52.057  43.331  22.795  1.00 91.49           S  
ANISOU 4203  SD  MET B 208    11199  11784  11779   -204    119  -1547       S  
ATOM   4204  CE  MET B 208      50.501  44.033  23.304  1.00 88.49           C  
ANISOU 4204  CE  MET B 208    10822  11344  11459   -181     77  -1713       C  
ATOM   4205  N   GLY B 209      54.345  46.038  25.080  1.00 62.30           N  
ANISOU 4205  N   GLY B 209     7496   8118   8055   -229   -164  -1506       N  
ATOM   4206  CA  GLY B 209      53.942  47.070  26.014  1.00 61.23           C  
ANISOU 4206  CA  GLY B 209     7358   7955   7950   -224   -246  -1594       C  
ATOM   4207  C   GLY B 209      54.047  48.483  25.481  1.00 61.92           C  
ANISOU 4207  C   GLY B 209     7441   7983   8100   -264   -399  -1598       C  
ATOM   4208  O   GLY B 209      53.210  49.337  25.792  1.00 66.70           O  
ANISOU 4208  O   GLY B 209     8042   8531   8769   -258   -475  -1698       O  
ATOM   4209  N   THR B 210      55.078  48.748  24.686  1.00 57.30           N  
ANISOU 4209  N   THR B 210     6861   7412   7499   -311   -449  -1497       N  
ATOM   4210  CA  THR B 210      55.269  50.069  24.111  1.00 57.91           C  
ANISOU 4210  CA  THR B 210     6951   7431   7622   -364   -597  -1490       C  
ATOM   4211  C   THR B 210      55.893  49.911  22.735  1.00 63.65           C  
ANISOU 4211  C   THR B 210     7690   8161   8334   -428   -611  -1394       C  
ATOM   4212  O   THR B 210      56.631  48.956  22.480  1.00 69.23           O  
ANISOU 4212  O   THR B 210     8383   8938   8985   -433   -520  -1324       O  
ATOM   4213  CB  THR B 210      56.146  50.958  25.012  1.00 57.31           C  
ANISOU 4213  CB  THR B 210     6871   7384   7521   -378   -668  -1481       C  
ATOM   4214  OG1 THR B 210      56.411  52.211  24.364  1.00 59.28           O  
ANISOU 4214  OG1 THR B 210     7144   7574   7806   -439   -810  -1465       O  
ATOM   4215  CG2 THR B 210      57.454  50.272  25.325  1.00 56.30           C  
ANISOU 4215  CG2 THR B 210     6730   7355   7306   -380   -595  -1394       C  
ATOM   4216  N   LEU B 211      55.580  50.852  21.847  1.00 61.25           N  
ANISOU 4216  N   LEU B 211     7414   7778   8082   -480   -732  -1398       N  
ATOM   4217  CA  LEU B 211      56.164  50.851  20.514  1.00 55.14           C  
ANISOU 4217  CA  LEU B 211     6657   7002   7290   -563   -761  -1312       C  
ATOM   4218  C   LEU B 211      57.517  51.534  20.475  1.00 64.56           C  
ANISOU 4218  C   LEU B 211     7864   8236   8432   -635   -829  -1246       C  
ATOM   4219  O   LEU B 211      58.333  51.225  19.597  1.00 67.97           O  
ANISOU 4219  O   LEU B 211     8296   8711   8820   -708   -811  -1172       O  
ATOM   4220  CB  LEU B 211      55.229  51.545  19.520  1.00 49.28           C  
ANISOU 4220  CB  LEU B 211     5952   6154   6618   -597   -868  -1340       C  
ATOM   4221  CG  LEU B 211      53.856  50.914  19.300  1.00 55.35           C  
ANISOU 4221  CG  LEU B 211     6706   6882   7440   -538   -808  -1412       C  
ATOM   4222  CD1 LEU B 211      53.059  51.709  18.265  1.00 51.67           C  
ANISOU 4222  CD1 LEU B 211     6280   6310   7044   -575   -938  -1434       C  
ATOM   4223  CD2 LEU B 211      53.997  49.444  18.891  1.00 57.40           C  
ANISOU 4223  CD2 LEU B 211     6936   7218   7655   -529   -645  -1365       C  
ATOM   4224  N   SER B 212      57.769  52.456  21.402  1.00 62.72           N  
ANISOU 4224  N   SER B 212     7637   7993   8200   -623   -903  -1278       N  
ATOM   4225  CA  SER B 212      58.977  53.270  21.374  1.00 64.35           C  
ANISOU 4225  CA  SER B 212     7862   8231   8358   -698   -979  -1229       C  
ATOM   4226  C   SER B 212      60.138  52.502  21.985  1.00 68.12           C  
ANISOU 4226  C   SER B 212     8297   8831   8755   -681   -877  -1187       C  
ATOM   4227  O   SER B 212      60.096  52.143  23.166  1.00 68.68           O  
ANISOU 4227  O   SER B 212     8339   8943   8815   -603   -817  -1220       O  
ATOM   4228  CB  SER B 212      58.752  54.579  22.123  1.00 67.52           C  
ANISOU 4228  CB  SER B 212     8285   8572   8797   -690  -1097  -1286       C  
ATOM   4229  OG  SER B 212      59.939  55.348  22.144  1.00 74.32           O  
ANISOU 4229  OG  SER B 212     9165   9471   9603   -764  -1160  -1241       O  
ATOM   4230  N   TYR B 213      61.184  52.267  21.188  1.00 68.90           N  
ANISOU 4230  N   TYR B 213     8393   8990   8798   -758   -865  -1120       N  
ATOM   4231  CA  TYR B 213      62.396  51.671  21.740  1.00 68.21           C  
ANISOU 4231  CA  TYR B 213     8262   9018   8636   -744   -791  -1090       C  
ATOM   4232  C   TYR B 213      63.023  52.602  22.763  1.00 77.32           C  
ANISOU 4232  C   TYR B 213     9418  10198   9762   -741   -852  -1110       C  
ATOM   4233  O   TYR B 213      63.548  52.151  23.789  1.00 76.32           O  
ANISOU 4233  O   TYR B 213     9255  10148   9597   -678   -790  -1114       O  
ATOM   4234  CB  TYR B 213      63.394  51.361  20.623  1.00 63.19           C  
ANISOU 4234  CB  TYR B 213     7615   8442   7951   -841   -777  -1035       C  
ATOM   4235  CG  TYR B 213      64.538  50.454  21.035  1.00 66.50           C  
ANISOU 4235  CG  TYR B 213     7977   8982   8307   -812   -687  -1014       C  
ATOM   4236  CD1 TYR B 213      64.454  49.657  22.171  1.00 68.89           C  
ANISOU 4236  CD1 TYR B 213     8249   9324   8604   -696   -605  -1028       C  
ATOM   4237  CD2 TYR B 213      65.710  50.402  20.287  1.00 64.98           C  
ANISOU 4237  CD2 TYR B 213     7764   8866   8061   -906   -689   -987       C  
ATOM   4238  CE1 TYR B 213      65.495  48.833  22.545  1.00 63.80           C  
ANISOU 4238  CE1 TYR B 213     7557   8780   7906   -663   -537  -1009       C  
ATOM   4239  CE2 TYR B 213      66.759  49.578  20.656  1.00 62.72           C  
ANISOU 4239  CE2 TYR B 213     7418   8690   7725   -873   -616   -981       C  
ATOM   4240  CZ  TYR B 213      66.643  48.795  21.785  1.00 62.56           C  
ANISOU 4240  CZ  TYR B 213     7369   8695   7704   -745   -544   -989       C  
ATOM   4241  OH  TYR B 213      67.677  47.971  22.166  1.00 65.18           O  
ANISOU 4241  OH  TYR B 213     7647   9127   7990   -703   -485   -983       O  
ATOM   4242  N   GLU B 214      62.947  53.912  22.518  1.00 83.66           N  
ANISOU 4242  N   GLU B 214    10267  10936  10585   -807   -975  -1123       N  
ATOM   4243  CA  GLU B 214      63.506  54.855  23.476  1.00 83.17           C  
ANISOU 4243  CA  GLU B 214    10206  10898  10499   -809  -1032  -1146       C  
ATOM   4244  C   GLU B 214      62.782  54.755  24.808  1.00 80.27           C  
ANISOU 4244  C   GLU B 214     9811  10519  10169   -703   -999  -1204       C  
ATOM   4245  O   GLU B 214      63.417  54.563  25.849  1.00 87.47           O  
ANISOU 4245  O   GLU B 214    10687  11512  11035   -661   -951  -1209       O  
ATOM   4246  CB  GLU B 214      63.433  56.278  22.918  1.00 87.41           C  
ANISOU 4246  CB  GLU B 214    10807  11349  11056   -900  -1176  -1151       C  
ATOM   4247  CG  GLU B 214      64.483  56.599  21.847  1.00 96.85           C  
ANISOU 4247  CG  GLU B 214    12036  12580  12183  -1033  -1217  -1099       C  
ATOM   4248  CD  GLU B 214      65.883  56.810  22.425  1.00108.32           C  
ANISOU 4248  CD  GLU B 214    13461  14149  13547  -1064  -1196  -1091       C  
ATOM   4249  OE1 GLU B 214      66.477  55.840  22.949  1.00110.68           O  
ANISOU 4249  OE1 GLU B 214    13695  14552  13806  -1005  -1091  -1085       O  
ATOM   4250  OE2 GLU B 214      66.390  57.954  22.371  1.00110.64           O  
ANISOU 4250  OE2 GLU B 214    13800  14429  13811  -1147  -1288  -1096       O  
ATOM   4251  N   GLN B 215      61.447  54.739  24.777  1.00 79.44           N  
ANISOU 4251  N   GLN B 215     9718  10324  10143   -659  -1011  -1254       N  
ATOM   4252  CA  GLN B 215      60.683  54.655  26.016  1.00 79.79           C  
ANISOU 4252  CA  GLN B 215     9734  10359  10221   -574   -978  -1327       C  
ATOM   4253  C   GLN B 215      61.058  53.406  26.800  1.00 77.44           C  
ANISOU 4253  C   GLN B 215     9397  10159   9866   -509   -845  -1309       C  
ATOM   4254  O   GLN B 215      60.996  53.403  28.035  1.00 80.62           O  
ANISOU 4254  O   GLN B 215     9777  10596  10259   -462   -816  -1350       O  
ATOM   4255  CB  GLN B 215      59.182  54.640  25.704  1.00 77.55           C  
ANISOU 4255  CB  GLN B 215     9464   9974  10027   -540   -998  -1394       C  
ATOM   4256  CG  GLN B 215      58.281  54.926  26.886  1.00 74.20           C  
ANISOU 4256  CG  GLN B 215     9014   9524   9654   -479   -999  -1497       C  
ATOM   4257  CD  GLN B 215      58.249  56.406  27.208  1.00 84.37           C  
ANISOU 4257  CD  GLN B 215    10314  10754  10989   -509  -1133  -1545       C  
ATOM   4258  OE1 GLN B 215      57.955  57.233  26.340  1.00 92.95           O  
ANISOU 4258  OE1 GLN B 215    11442  11749  12126   -552  -1248  -1546       O  
ATOM   4259  NE2 GLN B 215      58.559  56.752  28.451  1.00 87.29           N  
ANISOU 4259  NE2 GLN B 215    10650  11174  11342   -490  -1122  -1582       N  
ATOM   4260  N   PHE B 216      61.483  52.349  26.104  1.00 72.44           N  
ANISOU 4260  N   PHE B 216     8758   9571   9195   -511   -768  -1249       N  
ATOM   4261  CA  PHE B 216      61.932  51.130  26.775  1.00 70.95           C  
ANISOU 4261  CA  PHE B 216     8540   9467   8950   -449   -653  -1225       C  
ATOM   4262  C   PHE B 216      63.228  51.346  27.541  1.00 76.04           C  
ANISOU 4262  C   PHE B 216     9161  10205   9526   -452   -659  -1198       C  
ATOM   4263  O   PHE B 216      63.469  50.680  28.555  1.00 76.22           O  
ANISOU 4263  O   PHE B 216     9166  10286   9509   -390   -593  -1198       O  
ATOM   4264  CB  PHE B 216      62.100  50.013  25.745  1.00 66.14           C  
ANISOU 4264  CB  PHE B 216     7926   8878   8327   -455   -579  -1172       C  
ATOM   4265  CG  PHE B 216      62.261  48.650  26.351  1.00 64.51           C  
ANISOU 4265  CG  PHE B 216     7700   8730   8079   -381   -462  -1155       C  
ATOM   4266  CD1 PHE B 216      63.134  47.734  25.790  1.00 67.48           C  
ANISOU 4266  CD1 PHE B 216     8054   9169   8416   -384   -405  -1097       C  
ATOM   4267  CD2 PHE B 216      61.561  48.288  27.487  1.00 60.43           C  
ANISOU 4267  CD2 PHE B 216     7192   8206   7562   -314   -413  -1200       C  
ATOM   4268  CE1 PHE B 216      63.297  46.480  26.341  1.00 64.55           C  
ANISOU 4268  CE1 PHE B 216     7673   8842   8010   -312   -309  -1080       C  
ATOM   4269  CE2 PHE B 216      61.717  47.032  28.042  1.00 58.91           C  
ANISOU 4269  CE2 PHE B 216     6999   8060   7325   -253   -313  -1179       C  
ATOM   4270  CZ  PHE B 216      62.585  46.129  27.468  1.00 61.03           C  
ANISOU 4270  CZ  PHE B 216     7250   8381   7559   -247   -265  -1115       C  
ATOM   4271  N   LYS B 217      64.072  52.276  27.085  1.00 72.32           N  
ANISOU 4271  N   LYS B 217     8695   9751   9034   -526   -739  -1177       N  
ATOM   4272  CA  LYS B 217      65.319  52.569  27.772  1.00 64.12           C  
ANISOU 4272  CA  LYS B 217     7631   8806   7927   -533   -747  -1162       C  
ATOM   4273  C   LYS B 217      65.107  53.539  28.934  1.00 76.85           C  
ANISOU 4273  C   LYS B 217     9241  10408   9551   -519   -796  -1212       C  
ATOM   4274  O   LYS B 217      65.802  53.418  29.957  1.00 84.47           O  
ANISOU 4274  O   LYS B 217    10176  11454  10463   -485   -766  -1211       O  
ATOM   4275  CB  LYS B 217      66.338  53.134  26.788  1.00 58.90           C  
ANISOU 4275  CB  LYS B 217     6975   8176   7228   -631   -803  -1129       C  
ATOM   4276  CG  LYS B 217      66.619  52.233  25.590  1.00 60.25           C  
ANISOU 4276  CG  LYS B 217     7139   8367   7388   -664   -756  -1089       C  
ATOM   4277  CD  LYS B 217      67.505  52.929  24.565  1.00 62.06           C  
ANISOU 4277  CD  LYS B 217     7382   8621   7579   -786   -820  -1071       C  
ATOM   4278  CE  LYS B 217      67.811  52.026  23.397  1.00 61.03           C  
ANISOU 4278  CE  LYS B 217     7233   8520   7437   -829   -769  -1040       C  
ATOM   4279  NZ  LYS B 217      68.629  52.749  22.392  1.00 67.05           N  
ANISOU 4279  NZ  LYS B 217     8013   9306   8156   -969   -833  -1033       N  
ATOM   4280  N   LYS B 218      64.186  54.500  28.801  1.00 77.78           N  
ANISOU 4280  N   LYS B 218     9386  10429   9738   -545   -873  -1259       N  
ATOM   4281  CA  LYS B 218      63.928  55.437  29.894  1.00 80.04           C  
ANISOU 4281  CA  LYS B 218     9661  10703  10047   -534   -920  -1317       C  
ATOM   4282  C   LYS B 218      63.181  54.755  31.031  1.00 78.28           C  
ANISOU 4282  C   LYS B 218     9415  10492   9838   -457   -845  -1364       C  
ATOM   4283  O   LYS B 218      63.441  55.034  32.207  1.00 83.45           O  
ANISOU 4283  O   LYS B 218    10043  11198  10468   -440   -836  -1392       O  
ATOM   4284  CB  LYS B 218      63.120  56.661  29.416  1.00 83.17           C  
ANISOU 4284  CB  LYS B 218    10092  10984  10525   -579  -1035  -1365       C  
ATOM   4285  CG  LYS B 218      63.903  57.684  28.582  1.00 91.62           C  
ANISOU 4285  CG  LYS B 218    11200  12040  11573   -673  -1131  -1329       C  
ATOM   4286  CD  LYS B 218      64.318  56.971  27.317  1.00103.63           C  
ANISOU 4286  CD  LYS B 218    12741  13574  13058   -715  -1104  -1263       C  
ATOM   4287  CE  LYS B 218      65.245  57.628  26.324  1.00111.81           C  
ANISOU 4287  CE  LYS B 218    13816  14620  14046   -826  -1172  -1219       C  
ATOM   4288  NZ  LYS B 218      65.625  56.507  25.382  1.00116.51           N  
ANISOU 4288  NZ  LYS B 218    14402  15262  14604   -844  -1099  -1167       N  
ATOM   4289  N   GLY B 219      62.283  53.830  30.705  1.00 72.00           N  
ANISOU 4289  N   GLY B 219     8629   9656   9071   -418   -785  -1375       N  
ATOM   4290  CA  GLY B 219      61.527  53.135  31.726  1.00 68.86           C  
ANISOU 4290  CA  GLY B 219     8219   9268   8676   -360   -709  -1425       C  
ATOM   4291  C   GLY B 219      60.049  53.142  31.409  1.00 64.32           C  
ANISOU 4291  C   GLY B 219     7657   8597   8183   -348   -715  -1502       C  
ATOM   4292  O   GLY B 219      59.508  54.156  30.965  1.00 70.53           O  
ANISOU 4292  O   GLY B 219     8450   9306   9042   -378   -810  -1548       O  
ATOM   4293  N   VAL B 220      59.390  52.009  31.613  1.00 58.71           N  
ANISOU 4293  N   VAL B 220     6954   7892   7462   -305   -619  -1519       N  
ATOM   4294  CA  VAL B 220      57.955  51.883  31.407  1.00 61.46           C  
ANISOU 4294  CA  VAL B 220     7309   8165   7879   -290   -607  -1607       C  
ATOM   4295  C   VAL B 220      57.344  51.512  32.748  1.00 75.06           C  
ANISOU 4295  C   VAL B 220     9019   9916   9583   -266   -542  -1688       C  
ATOM   4296  O   VAL B 220      57.940  50.752  33.521  1.00 82.79           O  
ANISOU 4296  O   VAL B 220    10005  10970  10483   -248   -468  -1646       O  
ATOM   4297  CB  VAL B 220      57.609  50.841  30.316  1.00 55.77           C  
ANISOU 4297  CB  VAL B 220     6611   7421   7157   -276   -542  -1565       C  
ATOM   4298  CG1 VAL B 220      58.151  51.288  28.968  1.00 52.48           C  
ANISOU 4298  CG1 VAL B 220     6205   6974   6759   -319   -612  -1494       C  
ATOM   4299  CG2 VAL B 220      58.160  49.468  30.670  1.00 55.43           C  
ANISOU 4299  CG2 VAL B 220     6577   7452   7030   -241   -424  -1501       C  
ATOM   4300  N   GLN B 221      56.176  52.074  33.041  1.00 77.78           N  
ANISOU 4300  N   GLN B 221     9348  10204  10000   -271   -574  -1812       N  
ATOM   4301  CA  GLN B 221      55.556  51.836  34.336  1.00 85.44           C  
ANISOU 4301  CA  GLN B 221    10304  11207  10954   -268   -517  -1909       C  
ATOM   4302  C   GLN B 221      54.962  50.436  34.385  1.00 90.77           C  
ANISOU 4302  C   GLN B 221    11010  11897  11581   -244   -393  -1917       C  
ATOM   4303  O   GLN B 221      54.236  50.020  33.476  1.00 87.99           O  
ANISOU 4303  O   GLN B 221    10673  11495  11265   -230   -370  -1936       O  
ATOM   4304  CB  GLN B 221      54.497  52.895  34.628  1.00 89.73           C  
ANISOU 4304  CB  GLN B 221    10809  11689  11596   -284   -593  -2057       C  
ATOM   4305  CG  GLN B 221      55.072  54.302  34.723  1.00 98.06           C  
ANISOU 4305  CG  GLN B 221    11837  12726  12697   -310   -715  -2055       C  
ATOM   4306  CD  GLN B 221      56.197  54.404  35.749  1.00107.50           C  
ANISOU 4306  CD  GLN B 221    13019  14014  13813   -326   -694  -1997       C  
ATOM   4307  OE1 GLN B 221      57.375  54.480  35.392  1.00106.62           O  
ANISOU 4307  OE1 GLN B 221    12921  13938  13652   -331   -713  -1881       O  
ATOM   4308  NE2 GLN B 221      55.835  54.403  37.031  1.00111.74           N  
ANISOU 4308  NE2 GLN B 221    13525  14595  14335   -341   -654  -2085       N  
ATOM   4309  N   ILE B 222      55.282  49.711  35.451  1.00 94.46           N  
ANISOU 4309  N   ILE B 222    11493  12433  11963   -243   -313  -1903       N  
ATOM   4310  CA  ILE B 222      54.876  48.320  35.619  1.00 95.82           C  
ANISOU 4310  CA  ILE B 222    11712  12625  12070   -227   -193  -1897       C  
ATOM   4311  C   ILE B 222      54.381  48.137  37.047  1.00100.07           C  
ANISOU 4311  C   ILE B 222    12257  13204  12563   -258   -142  -1990       C  
ATOM   4312  O   ILE B 222      55.036  48.604  37.990  1.00105.88           O  
ANISOU 4312  O   ILE B 222    12975  13990  13265   -278   -172  -1978       O  
ATOM   4313  CB  ILE B 222      56.049  47.371  35.315  1.00 98.84           C  
ANISOU 4313  CB  ILE B 222    12129  13053  12374   -196   -148  -1746       C  
ATOM   4314  CG1 ILE B 222      56.245  47.222  33.801  1.00104.78           C  
ANISOU 4314  CG1 ILE B 222    12880  13765  13166   -178   -165  -1676       C  
ATOM   4315  CG2 ILE B 222      55.861  46.021  36.006  1.00 95.65           C  
ANISOU 4315  CG2 ILE B 222    11781  12682  11881   -184    -34  -1736       C  
ATOM   4316  CD1 ILE B 222      55.013  46.739  33.051  1.00105.32           C  
ANISOU 4316  CD1 ILE B 222    12962  13776  13278   -172   -114  -1741       C  
ATOM   4317  N   PRO B 223      53.235  47.497  37.261  1.00 97.87           N  
ANISOU 4317  N   PRO B 223    12001  12911  12276   -272    -64  -2092       N  
ATOM   4318  CA  PRO B 223      52.766  47.285  38.632  1.00 97.30           C  
ANISOU 4318  CA  PRO B 223    11940  12882  12147   -321    -11  -2187       C  
ATOM   4319  C   PRO B 223      53.701  46.360  39.392  1.00101.91           C  
ANISOU 4319  C   PRO B 223    12583  13529  12609   -319     48  -2074       C  
ATOM   4320  O   PRO B 223      54.282  45.427  38.832  1.00105.87           O  
ANISOU 4320  O   PRO B 223    13132  14031  13063   -276     89  -1955       O  
ATOM   4321  CB  PRO B 223      51.382  46.652  38.441  1.00 90.82           C  
ANISOU 4321  CB  PRO B 223    11141  12032  11334   -337     69  -2311       C  
ATOM   4322  CG  PRO B 223      51.430  46.052  37.081  1.00 89.81           C  
ANISOU 4322  CG  PRO B 223    11037  11862  11226   -285     91  -2226       C  
ATOM   4323  CD  PRO B 223      52.285  46.974  36.267  1.00 94.43           C  
ANISOU 4323  CD  PRO B 223    11579  12422  11879   -254    -20  -2135       C  
ATOM   4324  N   CYS B 224      53.837  46.628  40.684  1.00103.31           N  
ANISOU 4324  N   CYS B 224    12756  13758  12740   -367     47  -2117       N  
ATOM   4325  CA  CYS B 224      54.662  45.835  41.583  1.00107.48           C  
ANISOU 4325  CA  CYS B 224    13343  14345  13149   -373     90  -2024       C  
ATOM   4326  C   CYS B 224      53.770  44.928  42.417  1.00111.99           C  
ANISOU 4326  C   CYS B 224    13983  14930  13640   -431    188  -2108       C  
ATOM   4327  O   CYS B 224      52.547  45.075  42.439  1.00114.86           O  
ANISOU 4327  O   CYS B 224    14330  15271  14041   -476    220  -2257       O  
ATOM   4328  CB  CYS B 224      55.515  46.735  42.488  1.00106.86           C  
ANISOU 4328  CB  CYS B 224    13219  14323  13060   -396     22  -2004       C  
ATOM   4329  SG  CYS B 224      56.586  45.851  43.686  1.00108.07           S  
ANISOU 4329  SG  CYS B 224    13444  14552  13067   -402     56  -1891       S  
ATOM   4330  N   THR B 225      54.391  43.951  43.082  1.00113.38           N  
ANISOU 4330  N   THR B 225    14240  15141  13700   -433    234  -2015       N  
ATOM   4331  CA  THR B 225      53.608  43.091  43.960  1.00112.85           C  
ANISOU 4331  CA  THR B 225    14253  15087  13538   -505    324  -2090       C  
ATOM   4332  C   THR B 225      53.036  43.872  45.136  1.00114.00           C  
ANISOU 4332  C   THR B 225    14358  15276  13681   -605    314  -2234       C  
ATOM   4333  O   THR B 225      52.109  43.388  45.793  1.00116.95           O  
ANISOU 4333  O   THR B 225    14780  15662  13995   -688    387  -2347       O  
ATOM   4334  CB  THR B 225      54.456  41.923  44.468  1.00110.60           C  
ANISOU 4334  CB  THR B 225    14073  14822  13127   -487    358  -1953       C  
ATOM   4335  OG1 THR B 225      55.542  42.423  45.258  1.00109.87           O  
ANISOU 4335  OG1 THR B 225    13958  14784  13003   -486    290  -1880       O  
ATOM   4336  CG2 THR B 225      55.007  41.114  43.299  1.00109.28           C  
ANISOU 4336  CG2 THR B 225    13936  14614  12970   -390    370  -1823       C  
ATOM   4337  N   CYS B 226      53.575  45.055  45.418  1.00114.54           N  
ANISOU 4337  N   CYS B 226    14339  15372  13809   -605    228  -2239       N  
ATOM   4338  CA  CYS B 226      52.971  45.983  46.357  1.00113.42           C  
ANISOU 4338  CA  CYS B 226    14131  15267  13697   -696    210  -2394       C  
ATOM   4339  C   CYS B 226      51.979  46.865  45.602  1.00116.19           C  
ANISOU 4339  C   CYS B 226    14394  15567  14186   -690    175  -2537       C  
ATOM   4340  O   CYS B 226      51.860  46.802  44.378  1.00117.14           O  
ANISOU 4340  O   CYS B 226    14508  15628  14372   -617    159  -2500       O  
ATOM   4341  CB  CYS B 226      54.031  46.836  47.058  1.00111.58           C  
ANISOU 4341  CB  CYS B 226    13845  15089  13462   -701    136  -2333       C  
ATOM   4342  SG  CYS B 226      54.856  48.061  46.007  1.00115.02           S  
ANISOU 4342  SG  CYS B 226    14184  15496  14023   -612     23  -2260       S  
ATOM   4343  N   GLY B 227      51.277  47.711  46.343  1.00117.67           N  
ANISOU 4343  N   GLY B 227    14510  15779  14420   -768    157  -2705       N  
ATOM   4344  CA  GLY B 227      50.312  48.614  45.747  1.00118.96           C  
ANISOU 4344  CA  GLY B 227    14585  15893  14721   -762    110  -2859       C  
ATOM   4345  C   GLY B 227      50.803  49.477  44.598  1.00117.63           C  
ANISOU 4345  C   GLY B 227    14361  15665  14667   -670      7  -2784       C  
ATOM   4346  O   GLY B 227      50.216  49.464  43.512  1.00116.65           O  
ANISOU 4346  O   GLY B 227    14231  15474  14616   -620     -7  -2812       O  
ATOM   4347  N   LYS B 228      51.878  50.230  44.822  1.00116.59           N  
ANISOU 4347  N   LYS B 228    14195  15559  14548   -653    -66  -2689       N  
ATOM   4348  CA  LYS B 228      52.307  51.251  43.878  1.00113.62           C  
ANISOU 4348  CA  LYS B 228    13763  15129  14278   -590   -173  -2643       C  
ATOM   4349  C   LYS B 228      53.027  50.659  42.660  1.00110.84           C  
ANISOU 4349  C   LYS B 228    13467  14741  13908   -508   -176  -2471       C  
ATOM   4350  O   LYS B 228      53.329  49.463  42.579  1.00109.54           O  
ANISOU 4350  O   LYS B 228    13377  14594  13650   -488   -100  -2376       O  
ATOM   4351  CB  LYS B 228      53.209  52.265  44.583  1.00112.05           C  
ANISOU 4351  CB  LYS B 228    13508  14977  14088   -612   -241  -2611       C  
ATOM   4352  CG  LYS B 228      54.404  51.631  45.279  1.00115.48           C  
ANISOU 4352  CG  LYS B 228    13993  15491  14395   -615   -200  -2464       C  
ATOM   4353  CD  LYS B 228      55.259  52.662  46.003  1.00117.15           C  
ANISOU 4353  CD  LYS B 228    14141  15757  14612   -640   -261  -2445       C  
ATOM   4354  CE  LYS B 228      54.576  53.175  47.259  1.00116.93           C  
ANISOU 4354  CE  LYS B 228    14057  15776  14596   -736   -245  -2606       C  
ATOM   4355  NZ  LYS B 228      55.439  54.144  47.992  1.00117.47           N  
ANISOU 4355  NZ  LYS B 228    14062  15905  14666   -764   -296  -2584       N  
ATOM   4356  N   GLN B 229      53.290  51.543  41.697  1.00106.51           N  
ANISOU 4356  N   GLN B 229    12879  14137  13453   -465   -272  -2439       N  
ATOM   4357  CA  GLN B 229      53.821  51.195  40.385  1.00104.74           C  
ANISOU 4357  CA  GLN B 229    12692  13871  13235   -401   -289  -2307       C  
ATOM   4358  C   GLN B 229      55.347  51.246  40.380  1.00100.66           C  
ANISOU 4358  C   GLN B 229    12186  13401  12657   -378   -316  -2144       C  
ATOM   4359  O   GLN B 229      55.941  52.217  40.860  1.00104.35           O  
ANISOU 4359  O   GLN B 229    12609  13898  13142   -398   -381  -2143       O  
ATOM   4360  CB  GLN B 229      53.259  52.140  39.321  1.00107.81           C  
ANISOU 4360  CB  GLN B 229    13041  14171  13750   -380   -384  -2364       C  
ATOM   4361  CG  GLN B 229      51.757  51.997  39.103  1.00108.55           C  
ANISOU 4361  CG  GLN B 229    13122  14213  13908   -387   -361  -2524       C  
ATOM   4362  CD  GLN B 229      51.379  50.679  38.447  1.00107.54           C  
ANISOU 4362  CD  GLN B 229    13057  14076  13730   -360   -263  -2482       C  
ATOM   4363  OE1 GLN B 229      51.965  50.279  37.439  1.00112.68           O  
ANISOU 4363  OE1 GLN B 229    13741  14705  14367   -318   -265  -2351       O  
ATOM   4364  NE2 GLN B 229      50.406  49.987  39.031  1.00102.04           N  
ANISOU 4364  NE2 GLN B 229    12373  13398  12999   -392   -173  -2600       N  
ATOM   4365  N   ALA B 230      55.976  50.211  39.828  1.00 89.13           N  
ANISOU 4365  N   ALA B 230    10781  11954  11131   -336   -266  -2016       N  
ATOM   4366  CA  ALA B 230      57.421  50.176  39.658  1.00 78.24           C  
ANISOU 4366  CA  ALA B 230     9408  10620   9699   -308   -292  -1872       C  
ATOM   4367  C   ALA B 230      57.783  50.581  38.225  1.00 73.60           C  
ANISOU 4367  C   ALA B 230     8812   9981   9170   -281   -355  -1808       C  
ATOM   4368  O   ALA B 230      56.917  50.855  37.390  1.00 73.07           O  
ANISOU 4368  O   ALA B 230     8739   9841   9183   -281   -380  -1866       O  
ATOM   4369  CB  ALA B 230      57.969  48.791  40.009  1.00 73.78           C  
ANISOU 4369  CB  ALA B 230     8905  10103   9024   -281   -207  -1779       C  
ATOM   4370  N   THR B 231      59.088  50.642  37.943  1.00 72.60           N  
ANISOU 4370  N   THR B 231     8684   9898   9003   -264   -383  -1694       N  
ATOM   4371  CA  THR B 231      59.599  51.059  36.639  1.00 71.29           C  
ANISOU 4371  CA  THR B 231     8513   9699   8877   -258   -444  -1631       C  
ATOM   4372  C   THR B 231      60.556  50.022  36.074  1.00 70.59           C  
ANISOU 4372  C   THR B 231     8450   9650   8721   -223   -398  -1512       C  
ATOM   4373  O   THR B 231      61.551  49.675  36.719  1.00 74.28           O  
ANISOU 4373  O   THR B 231     8918  10193   9114   -206   -380  -1453       O  
ATOM   4374  CB  THR B 231      60.309  52.413  36.725  1.00 68.78           C  
ANISOU 4374  CB  THR B 231     8156   9395   8582   -290   -540  -1629       C  
ATOM   4375  OG1 THR B 231      59.372  53.420  37.129  1.00 77.04           O  
ANISOU 4375  OG1 THR B 231     9173  10392   9708   -320   -593  -1746       O  
ATOM   4376  CG2 THR B 231      60.914  52.786  35.377  1.00 66.46           C  
ANISOU 4376  CG2 THR B 231     7869   9072   8311   -300   -600  -1559       C  
ATOM   4377  N   LYS B 232      60.263  49.556  34.858  1.00 64.25           N  
ANISOU 4377  N   LYS B 232     7664   8798   7949   -212   -383  -1484       N  
ATOM   4378  CA  LYS B 232      61.093  48.600  34.130  1.00 58.58           C  
ANISOU 4378  CA  LYS B 232     6961   8110   7186   -184   -343  -1385       C  
ATOM   4379  C   LYS B 232      61.785  49.314  32.977  1.00 58.61           C  
ANISOU 4379  C   LYS B 232     6944   8105   7219   -216   -416  -1339       C  
ATOM   4380  O   LYS B 232      61.126  50.005  32.193  1.00 61.24           O  
ANISOU 4380  O   LYS B 232     7278   8369   7622   -249   -469  -1375       O  
ATOM   4381  CB  LYS B 232      60.238  47.443  33.604  1.00 60.27           C  
ANISOU 4381  CB  LYS B 232     7210   8284   7407   -158   -258  -1389       C  
ATOM   4382  CG  LYS B 232      60.970  46.471  32.689  1.00 69.60           C  
ANISOU 4382  CG  LYS B 232     8399   9486   8561   -133   -217  -1297       C  
ATOM   4383  CD  LYS B 232      60.010  45.777  31.711  1.00 72.25           C  
ANISOU 4383  CD  LYS B 232     8754   9762   8937   -128   -159  -1311       C  
ATOM   4384  CE  LYS B 232      59.166  44.690  32.369  1.00 72.82           C  
ANISOU 4384  CE  LYS B 232     8870   9825   8975    -97    -59  -1346       C  
ATOM   4385  NZ  LYS B 232      59.879  43.385  32.500  1.00 70.68           N  
ANISOU 4385  NZ  LYS B 232     8626   9594   8635    -53     11  -1267       N  
ATOM   4386  N   TYR B 233      63.110  49.162  32.885  1.00 59.24           N  
ANISOU 4386  N   TYR B 233     7009   8257   7244   -213   -425  -1268       N  
ATOM   4387  CA  TYR B 233      63.900  49.781  31.823  1.00 62.71           C  
ANISOU 4387  CA  TYR B 233     7431   8703   7692   -259   -487  -1229       C  
ATOM   4388  C   TYR B 233      64.909  48.774  31.272  1.00 63.97           C  
ANISOU 4388  C   TYR B 233     7581   8924   7802   -238   -442  -1157       C  
ATOM   4389  O   TYR B 233      65.265  47.789  31.928  1.00 64.27           O  
ANISOU 4389  O   TYR B 233     7621   9009   7791   -181   -382  -1132       O  
ATOM   4390  CB  TYR B 233      64.629  51.054  32.306  1.00 61.02           C  
ANISOU 4390  CB  TYR B 233     7195   8526   7464   -299   -568  -1242       C  
ATOM   4391  CG  TYR B 233      65.757  50.799  33.286  1.00 63.92           C  
ANISOU 4391  CG  TYR B 233     7538   8996   7752   -270   -548  -1213       C  
ATOM   4392  CD1 TYR B 233      65.509  50.645  34.648  1.00 68.05           C  
ANISOU 4392  CD1 TYR B 233     8061   9545   8249   -235   -518  -1241       C  
ATOM   4393  CD2 TYR B 233      67.074  50.712  32.847  1.00 65.95           C  
ANISOU 4393  CD2 TYR B 233     7773   9328   7959   -282   -560  -1165       C  
ATOM   4394  CE1 TYR B 233      66.546  50.405  35.546  1.00 66.54           C  
ANISOU 4394  CE1 TYR B 233     7851   9447   7983   -207   -507  -1212       C  
ATOM   4395  CE2 TYR B 233      68.113  50.475  33.734  1.00 72.11           C  
ANISOU 4395  CE2 TYR B 233     8527  10203   8668   -248   -548  -1145       C  
ATOM   4396  CZ  TYR B 233      67.843  50.321  35.082  1.00 70.80           C  
ANISOU 4396  CZ  TYR B 233     8366  10058   8477   -207   -523  -1164       C  
ATOM   4397  OH  TYR B 233      68.877  50.087  35.962  1.00 75.32           O  
ANISOU 4397  OH  TYR B 233     8916  10724   8977   -173   -518  -1142       O  
ATOM   4398  N   LEU B 234      65.396  49.058  30.064  1.00 62.09           N  
ANISOU 4398  N   LEU B 234     7331   8684   7577   -291   -477  -1130       N  
ATOM   4399  CA  LEU B 234      66.370  48.206  29.386  1.00 60.44           C  
ANISOU 4399  CA  LEU B 234     7099   8535   7331   -287   -441  -1078       C  
ATOM   4400  C   LEU B 234      67.790  48.543  29.832  1.00 63.50           C  
ANISOU 4400  C   LEU B 234     7451   9021   7655   -294   -475  -1065       C  
ATOM   4401  O   LEU B 234      68.249  49.679  29.669  1.00 70.48           O  
ANISOU 4401  O   LEU B 234     8328   9920   8533   -359   -545  -1080       O  
ATOM   4402  CB  LEU B 234      66.232  48.363  27.872  1.00 58.53           C  
ANISOU 4402  CB  LEU B 234     6859   8254   7127   -357   -461  -1065       C  
ATOM   4403  CG  LEU B 234      67.280  47.614  27.049  1.00 59.90           C  
ANISOU 4403  CG  LEU B 234     6996   8496   7268   -375   -430  -1027       C  
ATOM   4404  CD1 LEU B 234      67.141  46.111  27.258  1.00 61.69           C  
ANISOU 4404  CD1 LEU B 234     7217   8735   7488   -291   -335  -1006       C  
ATOM   4405  CD2 LEU B 234      67.180  47.978  25.577  1.00 55.00           C  
ANISOU 4405  CD2 LEU B 234     6378   7841   6678   -471   -461  -1019       C  
ATOM   4406  N   VAL B 235      68.492  47.548  30.368  1.00 62.78           N  
ANISOU 4406  N   VAL B 235     7341   8995   7516   -227   -427  -1040       N  
ATOM   4407  CA  VAL B 235      69.862  47.719  30.847  1.00 53.55           C  
ANISOU 4407  CA  VAL B 235     6132   7928   6284   -219   -454  -1035       C  
ATOM   4408  C   VAL B 235      70.848  47.476  29.710  1.00 58.94           C  
ANISOU 4408  C   VAL B 235     6774   8666   6955   -262   -459  -1026       C  
ATOM   4409  O   VAL B 235      71.613  48.372  29.334  1.00 61.77           O  
ANISOU 4409  O   VAL B 235     7110   9072   7290   -336   -512  -1044       O  
ATOM   4410  CB  VAL B 235      70.156  46.763  32.020  1.00 49.85           C  
ANISOU 4410  CB  VAL B 235     5667   7502   5771   -122   -413  -1018       C  
ATOM   4411  CG1 VAL B 235      71.629  46.788  32.370  1.00 51.23           C  
ANISOU 4411  CG1 VAL B 235     5794   7787   5885   -104   -441  -1016       C  
ATOM   4412  CG2 VAL B 235      69.302  47.104  33.225  1.00 49.43           C  
ANISOU 4412  CG2 VAL B 235     5651   7413   5718   -101   -410  -1038       C  
ATOM   4413  N   GLN B 236      70.823  46.276  29.137  1.00 61.58           N  
ANISOU 4413  N   GLN B 236     7099   8995   7304   -226   -402  -1004       N  
ATOM   4414  CA  GLN B 236      71.749  45.918  28.073  1.00 68.70           C  
ANISOU 4414  CA  GLN B 236     7950   9955   8198   -268   -399  -1006       C  
ATOM   4415  C   GLN B 236      71.007  45.144  26.990  1.00 73.70           C  
ANISOU 4415  C   GLN B 236     8592  10528   8884   -283   -346   -988       C  
ATOM   4416  O   GLN B 236      70.110  44.349  27.287  1.00 77.94           O  
ANISOU 4416  O   GLN B 236     9162  11005   9446   -217   -290   -969       O  
ATOM   4417  CB  GLN B 236      72.929  45.099  28.615  1.00 70.03           C  
ANISOU 4417  CB  GLN B 236     8071  10218   8321   -193   -387  -1009       C  
ATOM   4418  CG  GLN B 236      74.005  44.819  27.582  1.00 75.57           C  
ANISOU 4418  CG  GLN B 236     8705  10996   9013   -243   -390  -1035       C  
ATOM   4419  CD  GLN B 236      75.257  44.222  28.185  1.00 81.40           C  
ANISOU 4419  CD  GLN B 236     9387  11833   9707   -169   -398  -1057       C  
ATOM   4420  OE1 GLN B 236      75.325  43.971  29.386  1.00 83.82           O  
ANISOU 4420  OE1 GLN B 236     9714  12148   9987    -77   -403  -1041       O  
ATOM   4421  NE2 GLN B 236      76.257  43.983  27.346  1.00 89.60           N  
ANISOU 4421  NE2 GLN B 236    10355  12950  10738   -213   -402  -1099       N  
ATOM   4422  N   GLN B 237      71.375  45.391  25.733  1.00 66.95           N  
ANISOU 4422  N   GLN B 237     7708   9691   8040   -380   -360   -998       N  
ATOM   4423  CA  GLN B 237      70.745  44.738  24.591  1.00 63.96           C  
ANISOU 4423  CA  GLN B 237     7329   9265   7710   -413   -312   -983       C  
ATOM   4424  C   GLN B 237      71.815  44.371  23.574  1.00 62.36           C  
ANISOU 4424  C   GLN B 237     7058   9142   7494   -478   -304  -1002       C  
ATOM   4425  O   GLN B 237      72.547  45.246  23.101  1.00 59.39           O  
ANISOU 4425  O   GLN B 237     6662   8816   7086   -580   -360  -1029       O  
ATOM   4426  CB  GLN B 237      69.695  45.653  23.944  1.00 61.75           C  
ANISOU 4426  CB  GLN B 237     7099   8896   7469   -494   -347   -980       C  
ATOM   4427  CG  GLN B 237      69.005  45.052  22.717  1.00 54.37           C  
ANISOU 4427  CG  GLN B 237     6164   7913   6582   -536   -299   -965       C  
ATOM   4428  CD  GLN B 237      68.013  43.969  23.090  1.00 57.96           C  
ANISOU 4428  CD  GLN B 237     6639   8313   7070   -436   -215   -949       C  
ATOM   4429  OE1 GLN B 237      67.476  43.961  24.200  1.00 60.15           O  
ANISOU 4429  OE1 GLN B 237     6953   8559   7343   -358   -208   -953       O  
ATOM   4430  NE2 GLN B 237      67.768  43.045  22.170  1.00 62.73           N  
ANISOU 4430  NE2 GLN B 237     7220   8909   7704   -448   -148   -937       N  
ATOM   4431  N   GLU B 238      71.881  43.091  23.213  1.00 62.34           N  
ANISOU 4431  N   GLU B 238     7019   9151   7515   -429   -235   -994       N  
ATOM   4432  CA  GLU B 238      72.827  42.593  22.214  1.00 69.70           C  
ANISOU 4432  CA  GLU B 238     7874  10161   8447   -490   -218  -1024       C  
ATOM   4433  C   GLU B 238      72.046  41.698  21.256  1.00 67.84           C  
ANISOU 4433  C   GLU B 238     7633   9875   8268   -503   -145  -1003       C  
ATOM   4434  O   GLU B 238      71.720  40.552  21.584  1.00 67.62           O  
ANISOU 4434  O   GLU B 238     7604   9823   8265   -400    -80   -984       O  
ATOM   4435  CB  GLU B 238      73.992  41.846  22.863  1.00 82.38           C  
ANISOU 4435  CB  GLU B 238     9419  11856  10025   -402   -214  -1052       C  
ATOM   4436  CG  GLU B 238      74.944  42.749  23.653  1.00 98.03           C  
ANISOU 4436  CG  GLU B 238    11390  13912  11946   -406   -285  -1085       C  
ATOM   4437  CD  GLU B 238      76.175  42.018  24.170  1.00108.51           C  
ANISOU 4437  CD  GLU B 238    12648  15335  13248   -324   -289  -1125       C  
ATOM   4438  OE1 GLU B 238      76.140  40.772  24.254  1.00111.37           O  
ANISOU 4438  OE1 GLU B 238    12990  15683  13642   -230   -244  -1113       O  
ATOM   4439  OE2 GLU B 238      77.176  42.694  24.499  1.00110.57           O  
ANISOU 4439  OE2 GLU B 238    12874  15682  13456   -352   -341  -1172       O  
ATOM   4440  N   SER B 239      71.744  42.236  20.083  1.00 64.94           N  
ANISOU 4440  N   SER B 239     8076   7949   8650    374   -401   -553       N  
ATOM   4441  CA  SER B 239      70.960  41.548  19.069  1.00 60.16           C  
ANISOU 4441  CA  SER B 239     7497   7376   7986    367   -390   -502       C  
ATOM   4442  C   SER B 239      70.993  42.384  17.796  1.00 61.49           C  
ANISOU 4442  C   SER B 239     7590   7594   8177    324   -316   -449       C  
ATOM   4443  O   SER B 239      71.186  43.600  17.860  1.00 63.29           O  
ANISOU 4443  O   SER B 239     7770   7815   8464    287   -274   -427       O  
ATOM   4444  CB  SER B 239      69.513  41.338  19.531  1.00 58.15           C  
ANISOU 4444  CB  SER B 239     7321   7078   7695    351   -396   -439       C  
ATOM   4445  OG  SER B 239      68.874  42.588  19.703  1.00 60.07           O  
ANISOU 4445  OG  SER B 239     7541   7299   7983    311   -343   -381       O  
ATOM   4446  N   PRO B 240      70.784  41.761  16.636  1.00 63.27           N  
ANISOU 4446  N   PRO B 240     7814   7868   8356    326   -304   -425       N  
ATOM   4447  CA  PRO B 240      70.760  42.540  15.390  1.00 65.21           C  
ANISOU 4447  CA  PRO B 240     7999   8160   8618    280   -234   -370       C  
ATOM   4448  C   PRO B 240      69.554  43.461  15.266  1.00 69.28           C  
ANISOU 4448  C   PRO B 240     8534   8637   9151    231   -191   -279       C  
ATOM   4449  O   PRO B 240      69.588  44.391  14.447  1.00 74.91           O  
ANISOU 4449  O   PRO B 240     9201   9370   9891    185   -137   -235       O  
ATOM   4450  CB  PRO B 240      70.757  41.458  14.299  1.00 64.14           C  
ANISOU 4450  CB  PRO B 240     7874   8078   8418    308   -246   -373       C  
ATOM   4451  CG  PRO B 240      70.179  40.250  14.967  1.00 65.25           C  
ANISOU 4451  CG  PRO B 240     8105   8180   8508    352   -319   -391       C  
ATOM   4452  CD  PRO B 240      70.643  40.313  16.393  1.00 63.72           C  
ANISOU 4452  CD  PRO B 240     7929   7939   8343    371   -362   -451       C  
ATOM   4453  N   PHE B 241      68.503  43.251  16.055  1.00 64.83           N  
ANISOU 4453  N   PHE B 241     8038   8020   8572    238   -215   -254       N  
ATOM   4454  CA  PHE B 241      67.294  44.057  15.952  1.00 61.68           C  
ANISOU 4454  CA  PHE B 241     7657   7592   8187    201   -180   -177       C  
ATOM   4455  C   PHE B 241      66.501  43.916  17.243  1.00 60.29           C  
ANISOU 4455  C   PHE B 241     7538   7365   8003    215   -212   -179       C  
ATOM   4456  O   PHE B 241      66.780  43.050  18.076  1.00 60.47           O  
ANISOU 4456  O   PHE B 241     7600   7375   8000    248   -263   -229       O  
ATOM   4457  CB  PHE B 241      66.443  43.620  14.753  1.00 59.55           C  
ANISOU 4457  CB  PHE B 241     7408   7346   7874    189   -160   -117       C  
ATOM   4458  CG  PHE B 241      65.914  42.213  14.875  1.00 60.21           C  
ANISOU 4458  CG  PHE B 241     7556   7428   7891    222   -208   -123       C  
ATOM   4459  CD1 PHE B 241      64.659  41.971  15.411  1.00 62.42           C  
ANISOU 4459  CD1 PHE B 241     7895   7676   8148    215   -223    -84       C  
ATOM   4460  CD2 PHE B 241      66.684  41.130  14.476  1.00 61.83           C  
ANISOU 4460  CD2 PHE B 241     7766   7669   8057    260   -245   -171       C  
ATOM   4461  CE1 PHE B 241      64.180  40.673  15.540  1.00 65.16           C  
ANISOU 4461  CE1 PHE B 241     8306   8020   8431    236   -273    -84       C  
ATOM   4462  CE2 PHE B 241      66.208  39.832  14.600  1.00 64.04           C  
ANISOU 4462  CE2 PHE B 241     8117   7942   8275    289   -303   -175       C  
ATOM   4463  CZ  PHE B 241      64.956  39.606  15.134  1.00 64.81           C  
ANISOU 4463  CZ  PHE B 241     8275   8001   8348    272   -317   -129       C  
ATOM   4464  N   VAL B 242      65.485  44.765  17.385  1.00 56.95           N  
ANISOU 4464  N   VAL B 242     7123   6916   7599    189   -186   -125       N  
ATOM   4465  CA  VAL B 242      64.494  44.631  18.445  1.00 56.44           C  
ANISOU 4465  CA  VAL B 242     7110   6819   7516    197   -206   -116       C  
ATOM   4466  C   VAL B 242      63.126  44.879  17.834  1.00 65.31           C  
ANISOU 4466  C   VAL B 242     8246   7946   8621    173   -178    -46       C  
ATOM   4467  O   VAL B 242      62.988  45.624  16.859  1.00 70.61           O  
ANISOU 4467  O   VAL B 242     8885   8625   9317    148   -141     -6       O  
ATOM   4468  CB  VAL B 242      64.730  45.601  19.624  1.00 52.70           C  
ANISOU 4468  CB  VAL B 242     6625   6308   7093    203   -212   -144       C  
ATOM   4469  CG1 VAL B 242      65.990  45.243  20.378  1.00 53.00           C  
ANISOU 4469  CG1 VAL B 242     6659   6335   7145    232   -249   -218       C  
ATOM   4470  CG2 VAL B 242      64.793  47.028  19.121  1.00 52.31           C  
ANISOU 4470  CG2 VAL B 242     6525   6249   7100    175   -175   -113       C  
ATOM   4471  N   MET B 243      62.109  44.251  18.416  1.00 65.06           N  
ANISOU 4471  N   MET B 243     8265   7910   8546    176   -197    -31       N  
ATOM   4472  CA  MET B 243      60.735  44.385  17.953  1.00 60.09           C  
ANISOU 4472  CA  MET B 243     7647   7287   7896    156   -175     29       C  
ATOM   4473  C   MET B 243      59.876  44.865  19.110  1.00 56.58           C  
ANISOU 4473  C   MET B 243     7215   6828   7453    157   -176     28       C  
ATOM   4474  O   MET B 243      59.712  44.150  20.104  1.00 58.56           O  
ANISOU 4474  O   MET B 243     7506   7079   7667    165   -206      5       O  
ATOM   4475  CB  MET B 243      60.209  43.062  17.397  1.00 58.35           C  
ANISOU 4475  CB  MET B 243     7471   7088   7612    154   -195     54       C  
ATOM   4476  CG  MET B 243      58.765  43.108  16.948  1.00 56.66           C  
ANISOU 4476  CG  MET B 243     7269   6883   7377    132   -177    114       C  
ATOM   4477  SD  MET B 243      58.197  41.484  16.407  1.00 67.35           S  
ANISOU 4477  SD  MET B 243     8682   8254   8653    128   -214    143       S  
ATOM   4478  CE  MET B 243      56.488  41.843  16.016  1.00 57.17           C  
ANISOU 4478  CE  MET B 243     7391   6975   7355    100   -186    209       C  
ATOM   4479  N   MET B 244      59.325  46.065  18.978  1.00 56.08           N  
ANISOU 4479  N   MET B 244     7122   6757   7430    149   -149     51       N  
ATOM   4480  CA  MET B 244      58.456  46.650  19.988  1.00 59.30           C  
ANISOU 4480  CA  MET B 244     7533   7160   7839    157   -150     47       C  
ATOM   4481  C   MET B 244      57.016  46.575  19.496  1.00 59.70           C  
ANISOU 4481  C   MET B 244     7589   7235   7861    142   -133     94       C  
ATOM   4482  O   MET B 244      56.707  47.045  18.394  1.00 67.42           O  
ANISOU 4482  O   MET B 244     8549   8211   8858    130   -113    129       O  
ATOM   4483  CB  MET B 244      58.844  48.103  20.273  1.00 65.77           C  
ANISOU 4483  CB  MET B 244     8316   7949   8723    168   -144     30       C  
ATOM   4484  CG  MET B 244      60.326  48.339  20.568  1.00 68.44           C  
ANISOU 4484  CG  MET B 244     8639   8263   9102    177   -158    -12       C  
ATOM   4485  SD  MET B 244      60.923  47.587  22.096  1.00 64.00           S  
ANISOU 4485  SD  MET B 244     8110   7688   8518    206   -195    -73       S  
ATOM   4486  CE  MET B 244      59.935  48.477  23.291  1.00 61.22           C  
ANISOU 4486  CE  MET B 244     7762   7326   8171    226   -198    -80       C  
ATOM   4487  N   SER B 245      56.142  45.999  20.315  1.00 49.09           N  
ANISOU 4487  N   SER B 245     6269   5914   6468    140   -141     93       N  
ATOM   4488  CA  SER B 245      54.760  45.765  19.934  1.00 51.93           C  
ANISOU 4488  CA  SER B 245     6631   6306   6794    123   -128    133       C  
ATOM   4489  C   SER B 245      53.822  46.331  20.990  1.00 57.71           C  
ANISOU 4489  C   SER B 245     7349   7061   7516    132   -122    117       C  
ATOM   4490  O   SER B 245      54.188  46.473  22.162  1.00 61.17           O  
ANISOU 4490  O   SER B 245     7794   7495   7952    148   -134     78       O  
ATOM   4491  CB  SER B 245      54.476  44.277  19.742  1.00 59.94           C  
ANISOU 4491  CB  SER B 245     7689   7342   7742     99   -146    156       C  
ATOM   4492  OG  SER B 245      55.280  43.748  18.706  1.00 66.95           O  
ANISOU 4492  OG  SER B 245     8588   8215   8634     99   -155    168       O  
ATOM   4493  N   ALA B 246      52.622  46.682  20.544  1.00 57.66           N  
ANISOU 4493  N   ALA B 246     7322   7082   7506    127   -105    145       N  
ATOM   4494  CA  ALA B 246      51.573  47.240  21.386  1.00 59.20           C  
ANISOU 4494  CA  ALA B 246     7493   7314   7688    139    -98    127       C  
ATOM   4495  C   ALA B 246      50.262  47.192  20.599  1.00 58.58           C  
ANISOU 4495  C   ALA B 246     7396   7270   7592    125    -83    164       C  
ATOM   4496  O   ALA B 246      50.284  47.136  19.367  1.00 56.94           O  
ANISOU 4496  O   ALA B 246     7191   7040   7403    115    -80    198       O  
ATOM   4497  CB  ALA B 246      51.901  48.685  21.807  1.00 58.08           C  
ANISOU 4497  CB  ALA B 246     7321   7143   7604    180   -102     91       C  
ATOM   4498  N   PRO B 247      49.120  47.194  21.287  1.00 61.16           N  
ANISOU 4498  N   PRO B 247     7702   7654   7881    123    -74    154       N  
ATOM   4499  CA  PRO B 247      47.847  47.245  20.575  1.00 62.06           C  
ANISOU 4499  CA  PRO B 247     7791   7803   7985    114    -63    181       C  
ATOM   4500  C   PRO B 247      47.768  48.498  19.727  1.00 65.45           C  
ANISOU 4500  C   PRO B 247     8195   8195   8479    147    -66    176       C  
ATOM   4501  O   PRO B 247      48.366  49.536  20.063  1.00 68.02           O  
ANISOU 4501  O   PRO B 247     8511   8485   8849    181    -77    143       O  
ATOM   4502  CB  PRO B 247      46.808  47.261  21.706  1.00 56.44           C  
ANISOU 4502  CB  PRO B 247     7049   7167   7227    114    -52    154       C  
ATOM   4503  CG  PRO B 247      47.493  46.614  22.846  1.00 59.01           C  
ANISOU 4503  CG  PRO B 247     7408   7498   7514    100    -58    136       C  
ATOM   4504  CD  PRO B 247      48.924  47.049  22.740  1.00 59.59           C  
ANISOU 4504  CD  PRO B 247     7504   7496   7643    126    -74    119       C  
ATOM   4505  N   PRO B 248      47.052  48.441  18.606  1.00 66.91           N  
ANISOU 4505  N   PRO B 248     8375   8378   8669    136    -63    210       N  
ATOM   4506  CA  PRO B 248      47.031  49.576  17.665  1.00 67.62           C  
ANISOU 4506  CA  PRO B 248     8455   8420   8817    161    -73    211       C  
ATOM   4507  C   PRO B 248      46.611  50.865  18.350  1.00 65.60           C  
ANISOU 4507  C   PRO B 248     8165   8171   8588    208    -88    160       C  
ATOM   4508  O   PRO B 248      45.511  50.973  18.891  1.00 66.33           O  
ANISOU 4508  O   PRO B 248     8224   8324   8655    224    -86    135       O  
ATOM   4509  CB  PRO B 248      46.012  49.138  16.613  1.00 72.00           C  
ANISOU 4509  CB  PRO B 248     9010   8989   9358    144    -70    249       C  
ATOM   4510  CG  PRO B 248      46.051  47.650  16.660  1.00 71.19           C  
ANISOU 4510  CG  PRO B 248     8933   8916   9202    102    -60    284       C  
ATOM   4511  CD  PRO B 248      46.271  47.298  18.101  1.00 68.65           C  
ANISOU 4511  CD  PRO B 248     8607   8635   8843     98    -56    253       C  
ATOM   4512  N   ALA B 249      47.522  51.838  18.341  1.00 66.44           N  
ANISOU 4512  N   ALA B 249     8281   8219   8744    230   -108    142       N  
ATOM   4513  CA  ALA B 249      47.266  53.162  18.885  1.00 68.37           C  
ANISOU 4513  CA  ALA B 249     8504   8454   9020    279   -137     94       C  
ATOM   4514  C   ALA B 249      47.941  54.205  18.001  1.00 71.98           C  
ANISOU 4514  C   ALA B 249     8984   8829   9536    283   -165    104       C  
ATOM   4515  O   ALA B 249      48.919  53.918  17.303  1.00 61.03           O  
ANISOU 4515  O   ALA B 249     7623   7401   8166    248   -156    140       O  
ATOM   4516  CB  ALA B 249      47.756  53.280  20.333  1.00 60.91           C  
ANISOU 4516  CB  ALA B 249     7551   7528   8065    303   -139     51       C  
ATOM   4517  N   GLN B 250      47.404  55.427  18.043  1.00 78.61           N  
ANISOU 4517  N   GLN B 250     9814   9650  10404    326   -205     70       N  
ATOM   4518  CA  GLN B 250      47.987  56.536  17.296  1.00 78.78           C  
ANISOU 4518  CA  GLN B 250     9864   9591  10477    326   -245     79       C  
ATOM   4519  C   GLN B 250      49.425  56.760  17.730  1.00 76.02           C  
ANISOU 4519  C   GLN B 250     9530   9200  10154    311   -248     79       C  
ATOM   4520  O   GLN B 250      49.706  56.953  18.916  1.00 81.01           O  
ANISOU 4520  O   GLN B 250    10148   9846  10785    341   -258     41       O  
ATOM   4521  CB  GLN B 250      47.177  57.816  17.517  1.00 85.59           C  
ANISOU 4521  CB  GLN B 250    10720  10441  11361    383   -302     31       C  
ATOM   4522  CG  GLN B 250      47.266  58.834  16.382  1.00 95.13           C  
ANISOU 4522  CG  GLN B 250    11967  11567  12609    375   -350     48       C  
ATOM   4523  CD  GLN B 250      46.461  58.443  15.162  1.00104.89           C  
ANISOU 4523  CD  GLN B 250    13215  12803  13836    354   -339     81       C  
ATOM   4524  OE1 GLN B 250      45.702  57.477  15.191  1.00111.37           O  
ANISOU 4524  OE1 GLN B 250    14008  13687  14621    351   -300     87       O  
ATOM   4525  NE2 GLN B 250      46.629  59.190  14.076  1.00108.39           N  
ANISOU 4525  NE2 GLN B 250    13703  13171  14309    336   -376    105       N  
ATOM   4526  N   TYR B 251      50.336  56.735  16.760  1.00 67.77           N  
ANISOU 4526  N   TYR B 251     8512   8107   9132    265   -241    122       N  
ATOM   4527  CA  TYR B 251      51.763  56.800  17.029  1.00 65.54           C  
ANISOU 4527  CA  TYR B 251     8237   7793   8873    241   -238    126       C  
ATOM   4528  C   TYR B 251      52.432  57.500  15.860  1.00 65.08           C  
ANISOU 4528  C   TYR B 251     8205   7672   8849    200   -254    162       C  
ATOM   4529  O   TYR B 251      52.056  57.284  14.705  1.00 64.89           O  
ANISOU 4529  O   TYR B 251     8198   7642   8817    173   -242    200       O  
ATOM   4530  CB  TYR B 251      52.349  55.397  17.237  1.00 62.82           C  
ANISOU 4530  CB  TYR B 251     7885   7489   8496    216   -190    140       C  
ATOM   4531  CG  TYR B 251      53.807  55.359  17.636  1.00 61.10           C  
ANISOU 4531  CG  TYR B 251     7668   7249   8300    199   -187    132       C  
ATOM   4532  CD1 TYR B 251      54.219  55.750  18.907  1.00 61.92           C  
ANISOU 4532  CD1 TYR B 251     7763   7346   8418    231   -209     88       C  
ATOM   4533  CD2 TYR B 251      54.770  54.900  16.752  1.00 59.42           C  
ANISOU 4533  CD2 TYR B 251     7461   7025   8092    154   -164    164       C  
ATOM   4534  CE1 TYR B 251      55.562  55.700  19.274  1.00 55.37           C  
ANISOU 4534  CE1 TYR B 251     6932   6494   7612    217   -210     78       C  
ATOM   4535  CE2 TYR B 251      56.105  54.848  17.107  1.00 59.17           C  
ANISOU 4535  CE2 TYR B 251     7422   6979   8080    140   -163    151       C  
ATOM   4536  CZ  TYR B 251      56.497  55.246  18.364  1.00 57.58           C  
ANISOU 4536  CZ  TYR B 251     7213   6768   7898    171   -186    108       C  
ATOM   4537  OH  TYR B 251      57.835  55.183  18.690  1.00 61.17           O  
ANISOU 4537  OH  TYR B 251     7659   7207   8376    158   -187     92       O  
ATOM   4538  N   GLU B 252      53.409  58.348  16.161  1.00 65.26           N  
ANISOU 4538  N   GLU B 252     8236   7650   8910    192   -284    153       N  
ATOM   4539  CA  GLU B 252      54.107  59.104  15.135  1.00 69.51           C  
ANISOU 4539  CA  GLU B 252     8801   8132   9478    142   -303    189       C  
ATOM   4540  C   GLU B 252      55.439  58.441  14.828  1.00 70.60           C  
ANISOU 4540  C   GLU B 252     8927   8282   9618     91   -260    212       C  
ATOM   4541  O   GLU B 252      56.226  58.165  15.739  1.00 70.38           O  
ANISOU 4541  O   GLU B 252     8877   8266   9596    101   -252    186       O  
ATOM   4542  CB  GLU B 252      54.325  60.555  15.562  1.00 79.28           C  
ANISOU 4542  CB  GLU B 252    10057   9308  10756    157   -373    167       C  
ATOM   4543  CG  GLU B 252      55.071  61.385  14.523  1.00 89.00           C  
ANISOU 4543  CG  GLU B 252    11322  10479  12014     93   -398    209       C  
ATOM   4544  CD  GLU B 252      55.264  62.825  14.948  1.00 96.77           C  
ANISOU 4544  CD  GLU B 252    12335  11396  13036    105   -481    190       C  
ATOM   4545  OE1 GLU B 252      54.967  63.141  16.119  1.00101.24           O  
ANISOU 4545  OE1 GLU B 252    12890  11966  13610    169   -515    141       O  
ATOM   4546  OE2 GLU B 252      55.712  63.639  14.112  1.00 99.90           O  
ANISOU 4546  OE2 GLU B 252    12770  11738  13451     49   -515    225       O  
ATOM   4547  N   LEU B 253      55.680  58.179  13.549  1.00 73.10           N  
ANISOU 4547  N   LEU B 253     9256   8594   9925     40   -233    258       N  
ATOM   4548  CA  LEU B 253      56.929  57.589  13.088  1.00 72.90           C  
ANISOU 4548  CA  LEU B 253     9214   8588   9895     -8   -193    278       C  
ATOM   4549  C   LEU B 253      57.738  58.687  12.413  1.00 75.26           C  
ANISOU 4549  C   LEU B 253     9530   8840  10226    -65   -216    304       C  
ATOM   4550  O   LEU B 253      57.373  59.159  11.330  1.00 76.20           O  
ANISOU 4550  O   LEU B 253     9682   8930  10341    -99   -226    341       O  
ATOM   4551  CB  LEU B 253      56.669  56.429  12.132  1.00 66.93           C  
ANISOU 4551  CB  LEU B 253     8460   7872   9099    -23   -146    309       C  
ATOM   4552  CG  LEU B 253      56.043  55.177  12.743  1.00 60.58           C  
ANISOU 4552  CG  LEU B 253     7643   7117   8257     19   -123    290       C  
ATOM   4553  CD1 LEU B 253      55.597  54.221  11.648  1.00 60.36           C  
ANISOU 4553  CD1 LEU B 253     7628   7115   8192      4    -92    327       C  
ATOM   4554  CD2 LEU B 253      57.031  54.507  13.677  1.00 51.48           C  
ANISOU 4554  CD2 LEU B 253     6464   5993   7101     28   -110    256       C  
ATOM   4555  N   LYS B 254      58.828  59.095  13.055  1.00 75.60           N  
ANISOU 4555  N   LYS B 254     9552   8873  10298    -80   -228    286       N  
ATOM   4556  CA  LYS B 254      59.731  60.086  12.488  1.00 78.04           C  
ANISOU 4556  CA  LYS B 254     9873   9144  10635   -146   -250    313       C  
ATOM   4557  C   LYS B 254      60.764  59.387  11.616  1.00 73.99           C  
ANISOU 4557  C   LYS B 254     9331   8677  10103   -204   -191    338       C  
ATOM   4558  O   LYS B 254      61.331  58.366  12.016  1.00 75.32           O  
ANISOU 4558  O   LYS B 254     9461   8898  10260   -186   -153    312       O  
ATOM   4559  CB  LYS B 254      60.402  60.905  13.594  1.00 84.99           C  
ANISOU 4559  CB  LYS B 254    10744   9991  11558   -134   -296    281       C  
ATOM   4560  CG  LYS B 254      59.395  61.581  14.520  1.00 89.29           C  
ANISOU 4560  CG  LYS B 254    11313  10497  12116    -66   -357    248       C  
ATOM   4561  CD  LYS B 254      59.911  62.889  15.096  1.00 94.81           C  
ANISOU 4561  CD  LYS B 254    12030  11133  12859    -72   -429    238       C  
ATOM   4562  CE  LYS B 254      60.813  62.669  16.290  1.00100.66           C  
ANISOU 4562  CE  LYS B 254    12735  11886  13624    -47   -427    199       C  
ATOM   4563  NZ  LYS B 254      61.416  63.949  16.755  1.00102.03           N  
ANISOU 4563  NZ  LYS B 254    12929  11994  13843    -61   -501    195       N  
ATOM   4564  N   HIS B 255      61.006  59.943  10.431  1.00 70.74           N  
ANISOU 4564  N   HIS B 255     8943   8249   9688   -274   -189    385       N  
ATOM   4565  CA  HIS B 255      61.902  59.319   9.464  1.00 68.90           C  
ANISOU 4565  CA  HIS B 255     8681   8068   9428   -331   -131    410       C  
ATOM   4566  C   HIS B 255      63.312  59.171  10.029  1.00 67.08           C  
ANISOU 4566  C   HIS B 255     8395   7875   9217   -352   -114    382       C  
ATOM   4567  O   HIS B 255      63.827  60.061  10.714  1.00 68.17           O  
ANISOU 4567  O   HIS B 255     8529   7977   9395   -366   -155    369       O  
ATOM   4568  CB  HIS B 255      61.923  60.149   8.175  1.00 75.16           C  
ANISOU 4568  CB  HIS B 255     9515   8830  10213   -410   -140    466       C  
ATOM   4569  CG  HIS B 255      63.042  59.806   7.241  1.00 82.07           C  
ANISOU 4569  CG  HIS B 255    10356   9762  11064   -482    -85    490       C  
ATOM   4570  ND1 HIS B 255      64.141  60.620   7.067  1.00 85.70           N  
ANISOU 4570  ND1 HIS B 255    10800  10221  11541   -563    -91    507       N  
ATOM   4571  CD2 HIS B 255      63.234  58.739   6.430  1.00 84.49           C  
ANISOU 4571  CD2 HIS B 255    10640  10134  11328   -485    -24    499       C  
ATOM   4572  CE1 HIS B 255      64.960  60.070   6.189  1.00 87.41           C  
ANISOU 4572  CE1 HIS B 255    10980  10508  11726   -614    -31    523       C  
ATOM   4573  NE2 HIS B 255      64.434  58.927   5.788  1.00 84.72           N  
ANISOU 4573  NE2 HIS B 255    10636  10207  11348   -563      9    516       N  
ATOM   4574  N   GLY B 256      63.929  58.023   9.753  1.00 65.00           N  
ANISOU 4574  N   GLY B 256     8088   7682   8925   -348    -59    367       N  
ATOM   4575  CA  GLY B 256      65.284  57.746  10.177  1.00 65.09           C  
ANISOU 4575  CA  GLY B 256     8041   7739   8951   -363    -40    333       C  
ATOM   4576  C   GLY B 256      65.435  57.251  11.600  1.00 68.20           C  
ANISOU 4576  C   GLY B 256     8414   8134   9365   -293    -58    274       C  
ATOM   4577  O   GLY B 256      66.559  56.934  12.007  1.00 69.42           O  
ANISOU 4577  O   GLY B 256     8519   8324   9531   -297    -47    237       O  
ATOM   4578  N   THR B 257      64.349  57.155  12.366  1.00 71.57           N  
ANISOU 4578  N   THR B 257     8874   8525   9792   -230    -86    260       N  
ATOM   4579  CA  THR B 257      64.412  56.754  13.766  1.00 71.20           C  
ANISOU 4579  CA  THR B 257     8817   8475   9760   -167   -106    206       C  
ATOM   4580  C   THR B 257      63.991  55.306  13.987  1.00 63.18           C  
ANISOU 4580  C   THR B 257     7803   7503   8701   -114    -81    182       C  
ATOM   4581  O   THR B 257      63.852  54.881  15.139  1.00 55.25           O  
ANISOU 4581  O   THR B 257     6801   6494   7698    -62    -99    140       O  
ATOM   4582  CB  THR B 257      63.542  57.678  14.630  1.00 74.28           C  
ANISOU 4582  CB  THR B 257     9243   8803  10177   -131   -159    200       C  
ATOM   4583  OG1 THR B 257      62.164  57.547  14.252  1.00 79.47           O  
ANISOU 4583  OG1 THR B 257     9937   9453  10806   -107   -159    223       O  
ATOM   4584  CG2 THR B 257      63.970  59.128  14.468  1.00 68.78           C  
ANISOU 4584  CG2 THR B 257     8556   8053   9522   -181   -199    223       C  
ATOM   4585  N   PHE B 258      63.780  54.547  12.914  1.00 64.87           N  
ANISOU 4585  N   PHE B 258     8019   7756   8873   -128    -46    208       N  
ATOM   4586  CA  PHE B 258      63.339  53.161  13.003  1.00 59.27           C  
ANISOU 4586  CA  PHE B 258     7318   7084   8118    -84    -31    193       C  
ATOM   4587  C   PHE B 258      63.643  52.477  11.679  1.00 59.54           C  
ANISOU 4587  C   PHE B 258     7343   7165   8115   -110      6    218       C  
ATOM   4588  O   PHE B 258      63.988  53.123  10.688  1.00 67.46           O  
ANISOU 4588  O   PHE B 258     8337   8171   9124   -164     24    252       O  
ATOM   4589  CB  PHE B 258      61.846  53.071  13.328  1.00 59.45           C  
ANISOU 4589  CB  PHE B 258     7382   7082   8124    -48    -47    208       C  
ATOM   4590  CG  PHE B 258      60.954  53.498  12.191  1.00 64.44           C  
ANISOU 4590  CG  PHE B 258     8041   7699   8746    -74    -38    261       C  
ATOM   4591  CD1 PHE B 258      60.298  52.556  11.412  1.00 67.89           C  
ANISOU 4591  CD1 PHE B 258     8495   8161   9138    -66    -18    286       C  
ATOM   4592  CD2 PHE B 258      60.781  54.839  11.892  1.00 61.41           C  
ANISOU 4592  CD2 PHE B 258     7670   7269   8396   -105    -58    285       C  
ATOM   4593  CE1 PHE B 258      59.483  52.947  10.363  1.00 66.44           C  
ANISOU 4593  CE1 PHE B 258     8339   7957   8946    -87    -14    333       C  
ATOM   4594  CE2 PHE B 258      59.972  55.232  10.845  1.00 64.35           C  
ANISOU 4594  CE2 PHE B 258     8073   7619   8757   -128    -58    330       C  
ATOM   4595  CZ  PHE B 258      59.322  54.286  10.080  1.00 66.53           C  
ANISOU 4595  CZ  PHE B 258     8365   7922   8992   -117    -33    353       C  
ATOM   4596  N   THR B 259      63.517  51.154  11.675  1.00 57.23           N  
ANISOU 4596  N   THR B 259     7056   6908   7779    -73     12    200       N  
ATOM   4597  CA  THR B 259      63.679  50.388  10.443  1.00 61.59           C  
ANISOU 4597  CA  THR B 259     7606   7506   8290    -84     40    221       C  
ATOM   4598  C   THR B 259      62.370  50.310   9.658  1.00 63.85           C  
ANISOU 4598  C   THR B 259     7937   7774   8551    -85     45    275       C  
ATOM   4599  O   THR B 259      62.279  50.824   8.539  1.00 67.73           O  
ANISOU 4599  O   THR B 259     8434   8262   9040   -125     65    317       O  
ATOM   4600  CB  THR B 259      64.202  48.986  10.771  1.00 65.74           C  
ANISOU 4600  CB  THR B 259     8124   8076   8779    -39     32    174       C  
ATOM   4601  OG1 THR B 259      65.472  49.098  11.421  1.00 76.57           O  
ANISOU 4601  OG1 THR B 259     9450   9465  10176    -37     26    119       O  
ATOM   4602  CG2 THR B 259      64.350  48.154   9.508  1.00 59.87           C  
ANISOU 4602  CG2 THR B 259     7379   7380   7987    -40     53    191       C  
ATOM   4603  N   CYS B 260      61.353  49.667  10.231  1.00 65.77           N  
ANISOU 4603  N   CYS B 260     8211   8003   8773    -44     25    273       N  
ATOM   4604  CA  CYS B 260      60.046  49.540   9.593  1.00 63.72           C  
ANISOU 4604  CA  CYS B 260     7990   7727   8492    -41     25    318       C  
ATOM   4605  C   CYS B 260      58.997  49.276  10.666  1.00 58.81           C  
ANISOU 4605  C   CYS B 260     7390   7089   7865     -6      0    306       C  
ATOM   4606  O   CYS B 260      59.318  48.940  11.809  1.00 65.90           O  
ANISOU 4606  O   CYS B 260     8280   7994   8765     17    -16    264       O  
ATOM   4607  CB  CYS B 260      60.032  48.421   8.549  1.00 65.18           C  
ANISOU 4607  CB  CYS B 260     8189   7946   8628    -34     38    338       C  
ATOM   4608  SG  CYS B 260      60.404  46.785   9.210  1.00 62.39           S  
ANISOU 4608  SG  CYS B 260     7841   7633   8230     14     15    294       S  
ATOM   4609  N   ALA B 261      57.730  49.414  10.277  1.00 45.08           N  
ANISOU 4609  N   ALA B 261     5678   5332   6118     -4     -3    341       N  
ATOM   4610  CA  ALA B 261      56.637  49.287  11.229  1.00 48.23           C  
ANISOU 4610  CA  ALA B 261     6089   5725   6510     23    -22    331       C  
ATOM   4611  C   ALA B 261      55.426  48.643  10.562  1.00 57.90           C  
ANISOU 4611  C   ALA B 261     7342   6957   7702     28    -23    368       C  
ATOM   4612  O   ALA B 261      55.350  48.520   9.336  1.00 60.47           O  
ANISOU 4612  O   ALA B 261     7682   7278   8017     13    -11    404       O  
ATOM   4613  CB  ALA B 261      56.255  50.642  11.831  1.00 44.14           C  
ANISOU 4613  CB  ALA B 261     5562   5173   6035     24    -37    319       C  
ATOM   4614  N   SER B 262      54.470  48.241  11.402  1.00 57.58           N  
ANISOU 4614  N   SER B 262     7308   6929   7641     47    -36    359       N  
ATOM   4615  CA  SER B 262      53.236  47.594  10.978  1.00 57.17           C  
ANISOU 4615  CA  SER B 262     7277   6888   7558     50    -41    390       C  
ATOM   4616  C   SER B 262      52.045  48.450  11.387  1.00 61.27           C  
ANISOU 4616  C   SER B 262     7786   7398   8096     60    -49    386       C  
ATOM   4617  O   SER B 262      51.796  48.652  12.581  1.00 61.50           O  
ANISOU 4617  O   SER B 262     7799   7443   8126     75    -56    353       O  
ATOM   4618  CB  SER B 262      53.118  46.194  11.582  1.00 57.76           C  
ANISOU 4618  CB  SER B 262     7369   6997   7581     57    -54    384       C  
ATOM   4619  OG  SER B 262      54.199  45.382  11.164  1.00 67.68           O  
ANISOU 4619  OG  SER B 262     8637   8261   8817     58    -58    380       O  
ATOM   4620  N   GLU B 263      51.301  48.928  10.394  1.00 65.76           N  
ANISOU 4620  N   GLU B 263     8365   7943   8676     55    -49    416       N  
ATOM   4621  CA  GLU B 263      50.068  49.661  10.620  1.00 66.47           C  
ANISOU 4621  CA  GLU B 263     8446   8028   8781     71    -63    408       C  
ATOM   4622  C   GLU B 263      48.885  48.703  10.627  1.00 66.25           C  
ANISOU 4622  C   GLU B 263     8422   8036   8715     74    -65    425       C  
ATOM   4623  O   GLU B 263      48.808  47.787   9.803  1.00 66.10           O  
ANISOU 4623  O   GLU B 263     8427   8019   8669     62    -62    461       O  
ATOM   4624  CB  GLU B 263      49.864  50.721   9.540  1.00 64.38           C  
ANISOU 4624  CB  GLU B 263     8198   7713   8552     65    -73    426       C  
ATOM   4625  CG  GLU B 263      48.554  51.471   9.665  1.00 77.59           C  
ANISOU 4625  CG  GLU B 263     9864   9378  10239     89    -97    411       C  
ATOM   4626  CD  GLU B 263      48.264  52.355   8.465  1.00 88.99           C  
ANISOU 4626  CD  GLU B 263    11339  10764  11710     81   -116    432       C  
ATOM   4627  OE1 GLU B 263      48.921  52.179   7.417  1.00 91.61           O  
ANISOU 4627  OE1 GLU B 263    11698  11069  12039     53   -103    470       O  
ATOM   4628  OE2 GLU B 263      47.371  53.222   8.567  1.00 95.17           O  
ANISOU 4628  OE2 GLU B 263    12118  11528  12513    106   -147    409       O  
ATOM   4629  N   TYR B 264      47.968  48.914  11.567  1.00 59.94           N  
ANISOU 4629  N   TYR B 264     7597   7268   7909     91    -72    397       N  
ATOM   4630  CA  TYR B 264      46.763  48.106  11.665  1.00 54.28           C  
ANISOU 4630  CA  TYR B 264     6874   6594   7154     87    -74    411       C  
ATOM   4631  C   TYR B 264      45.564  49.033  11.791  1.00 53.17           C  
ANISOU 4631  C   TYR B 264     6706   6463   7034    111    -85    387       C  
ATOM   4632  O   TYR B 264      45.510  49.867  12.704  1.00 50.67           O  
ANISOU 4632  O   TYR B 264     6360   6158   6733    134    -91    342       O  
ATOM   4633  CB  TYR B 264      46.828  47.141  12.848  1.00 48.63           C  
ANISOU 4633  CB  TYR B 264     6152   5931   6392     75    -69    398       C  
ATOM   4634  CG  TYR B 264      45.661  46.182  12.890  1.00 48.44           C  
ANISOU 4634  CG  TYR B 264     6128   5954   6322     56    -72    421       C  
ATOM   4635  CD1 TYR B 264      44.591  46.392  13.749  1.00 48.94           C  
ANISOU 4635  CD1 TYR B 264     6152   6073   6369     60    -69    396       C  
ATOM   4636  CD2 TYR B 264      45.618  45.077  12.048  1.00 46.77           C  
ANISOU 4636  CD2 TYR B 264     5953   5735   6082     34    -81    469       C  
ATOM   4637  CE1 TYR B 264      43.525  45.516  13.784  1.00 55.84           C  
ANISOU 4637  CE1 TYR B 264     7021   6996   7199     33    -70    420       C  
ATOM   4638  CE2 TYR B 264      44.559  44.198  12.079  1.00 50.49           C  
ANISOU 4638  CE2 TYR B 264     6426   6247   6512     11    -90    495       C  
ATOM   4639  CZ  TYR B 264      43.516  44.420  12.944  1.00 60.98           C  
ANISOU 4639  CZ  TYR B 264     7712   7632   7824      6    -83    472       C  
ATOM   4640  OH  TYR B 264      42.463  43.534  12.961  1.00 75.27           O  
ANISOU 4640  OH  TYR B 264     9520   9488   9591    -26    -91    500       O  
ATOM   4641  N   THR B 265      44.626  48.911  10.854  1.00 54.08           N  
ANISOU 4641  N   THR B 265     6828   6570   7149    110    -93    413       N  
ATOM   4642  CA  THR B 265      43.419  49.720  10.832  1.00 60.58           C  
ANISOU 4642  CA  THR B 265     7625   7402   7991    137   -111    385       C  
ATOM   4643  C   THR B 265      42.190  48.821  10.879  1.00 61.09           C  
ANISOU 4643  C   THR B 265     7668   7524   8017    125   -107    399       C  
ATOM   4644  O   THR B 265      42.133  47.796  10.191  1.00 59.73           O  
ANISOU 4644  O   THR B 265     7525   7347   7822     99   -104    448       O  
ATOM   4645  CB  THR B 265      43.378  50.588   9.583  1.00 59.38           C  
ANISOU 4645  CB  THR B 265     7504   7178   7881    147   -133    398       C  
ATOM   4646  OG1 THR B 265      43.723  49.796   8.438  1.00 65.66           O  
ANISOU 4646  OG1 THR B 265     8341   7941   8665    121   -124    454       O  
ATOM   4647  CG2 THR B 265      44.396  51.711   9.720  1.00 51.74           C  
ANISOU 4647  CG2 THR B 265     6548   6162   6950    155   -144    377       C  
ATOM   4648  N   GLY B 266      41.217  49.199  11.707  1.00 61.55           N  
ANISOU 4648  N   GLY B 266     7677   7641   8069    145   -110    356       N  
ATOM   4649  CA  GLY B 266      39.981  48.451  11.825  1.00 66.21           C  
ANISOU 4649  CA  GLY B 266     8236   8298   8622    130   -106    364       C  
ATOM   4650  C   GLY B 266      39.794  47.919  13.227  1.00 82.18           C  
ANISOU 4650  C   GLY B 266    10221  10407  10596    111    -85    342       C  
ATOM   4651  O   GLY B 266      40.464  48.375  14.159  1.00 88.09           O  
ANISOU 4651  O   GLY B 266    10961  11164  11347    126    -78    307       O  
ATOM   4652  N   ASN B 267      38.904  46.945  13.399  1.00 90.36           N  
ANISOU 4652  N   ASN B 267    11238  11509  11586     75    -77    364       N  
ATOM   4653  CA  ASN B 267      38.712  46.322  14.696  1.00 95.74           C  
ANISOU 4653  CA  ASN B 267    11892  12275  12210     44    -57    351       C  
ATOM   4654  C   ASN B 267      39.483  45.007  14.740  1.00 96.18           C  
ANISOU 4654  C   ASN B 267    12004  12315  12223     -8    -57    405       C  
ATOM   4655  O   ASN B 267      40.082  44.570  13.757  1.00 93.64           O  
ANISOU 4655  O   ASN B 267    11736  11928  11917    -15    -71    448       O  
ATOM   4656  CB  ASN B 267      37.231  46.088  15.003  1.00100.16           C  
ANISOU 4656  CB  ASN B 267    12390  12929  12735     27    -50    339       C  
ATOM   4657  CG  ASN B 267      36.538  45.282  13.934  1.00107.11           C  
ANISOU 4657  CG  ASN B 267    13288  13798  13609     -5    -64    393       C  
ATOM   4658  OD1 ASN B 267      37.114  44.992  12.888  1.00111.96           O  
ANISOU 4658  OD1 ASN B 267    13961  14331  14248     -6    -80    437       O  
ATOM   4659  ND2 ASN B 267      35.318  44.842  14.226  1.00109.70           N  
ANISOU 4659  ND2 ASN B 267    13565  14214  13900    -36    -57    392       N  
ATOM   4660  N   TYR B 268      39.454  44.362  15.908  1.00100.65           N  
ANISOU 4660  N   TYR B 268    12564  12947  12733    -45    -46    399       N  
ATOM   4661  CA  TYR B 268      40.138  43.085  16.071  1.00105.83           C  
ANISOU 4661  CA  TYR B 268    13279  13588  13341    -94    -58    443       C  
ATOM   4662  C   TYR B 268      39.492  41.957  15.271  1.00109.02           C  
ANISOU 4662  C   TYR B 268    13712  13997  13715   -140    -78    505       C  
ATOM   4663  O   TYR B 268      40.147  40.934  15.044  1.00110.47           O  
ANISOU 4663  O   TYR B 268    13959  14145  13869   -169   -103    545       O  
ATOM   4664  CB  TYR B 268      40.168  42.677  17.540  1.00111.48           C  
ANISOU 4664  CB  TYR B 268    13988  14372  13999   -127    -46    422       C  
ATOM   4665  CG  TYR B 268      38.798  42.330  18.079  1.00117.84           C  
ANISOU 4665  CG  TYR B 268    14743  15279  14751   -170    -32    424       C  
ATOM   4666  CD1 TYR B 268      38.373  41.006  18.127  1.00119.89           C  
ANISOU 4666  CD1 TYR B 268    15036  15572  14946   -245    -48    477       C  
ATOM   4667  CD2 TYR B 268      37.911  43.315  18.496  1.00117.93           C  
ANISOU 4667  CD2 TYR B 268    14675  15357  14776   -138     -8    372       C  
ATOM   4668  CE1 TYR B 268      37.122  40.667  18.604  1.00119.17           C  
ANISOU 4668  CE1 TYR B 268    14896  15581  14803   -295    -34    483       C  
ATOM   4669  CE2 TYR B 268      36.651  42.984  18.977  1.00119.73           C  
ANISOU 4669  CE2 TYR B 268    14848  15692  14952   -180      8    369       C  
ATOM   4670  CZ  TYR B 268      36.264  41.656  19.026  1.00120.42           C  
ANISOU 4670  CZ  TYR B 268    14965  15814  14974   -263     -2    427       C  
ATOM   4671  OH  TYR B 268      35.017  41.310  19.497  1.00122.69           O  
ANISOU 4671  OH  TYR B 268    15195  16215  15208   -315     16    429       O  
ATOM   4672  N   GLN B 269      38.228  42.101  14.852  1.00108.30           N  
ANISOU 4672  N   GLN B 269    13576  13946  13627   -146    -75    511       N  
ATOM   4673  CA  GLN B 269      37.578  40.992  14.157  1.00106.39           C  
ANISOU 4673  CA  GLN B 269    13361  13708  13353   -193    -99    572       C  
ATOM   4674  C   GLN B 269      37.992  40.953  12.696  1.00102.96           C  
ANISOU 4674  C   GLN B 269    12975  13181  12964   -164   -123    607       C  
ATOM   4675  O   GLN B 269      38.104  39.873  12.102  1.00102.80           O  
ANISOU 4675  O   GLN B 269    13011  13132  12917   -194   -154    662       O  
ATOM   4676  CB  GLN B 269      36.053  41.090  14.249  1.00113.43           C  
ANISOU 4676  CB  GLN B 269    14184  14682  14231   -214    -89    564       C  
ATOM   4677  CG  GLN B 269      35.485  41.172  15.658  1.00121.75           C  
ANISOU 4677  CG  GLN B 269    15179  15848  15235   -245    -60    526       C  
ATOM   4678  CD  GLN B 269      33.966  41.298  15.665  1.00128.56           C  
ANISOU 4678  CD  GLN B 269    15961  16802  16085   -263    -47    513       C  
ATOM   4679  OE1 GLN B 269      33.382  41.931  14.784  1.00131.88           O  
ANISOU 4679  OE1 GLN B 269    16351  17200  16557   -219    -54    498       O  
ATOM   4680  NE2 GLN B 269      33.334  40.796  16.726  1.00128.22           N  
ANISOU 4680  NE2 GLN B 269    15879  16867  15971   -325    -28    510       N  
ATOM   4681  N   CYS B 270      38.187  42.118  12.092  1.00 97.63           N  
ANISOU 4681  N   CYS B 270    12284  12459  12354   -106   -113    576       N  
ATOM   4682  CA  CYS B 270      38.711  42.182  10.738  1.00 90.78           C  
ANISOU 4682  CA  CYS B 270    11465  11503  11525    -79   -131    606       C  
ATOM   4683  C   CYS B 270      39.427  43.511  10.591  1.00 85.16           C  
ANISOU 4683  C   CYS B 270    10742  10743  10870    -27   -116    563       C  
ATOM   4684  O   CYS B 270      38.841  44.566  10.843  1.00 91.28           O  
ANISOU 4684  O   CYS B 270    11469  11538  11676      3   -108    517       O  
ATOM   4685  CB  CYS B 270      37.599  42.037   9.701  1.00 92.70           C  
ANISOU 4685  CB  CYS B 270    11703  11736  11783    -79   -149    635       C  
ATOM   4686  SG  CYS B 270      38.220  41.993   8.014  1.00101.02           S  
ANISOU 4686  SG  CYS B 270    12827  12682  12875    -49   -171    678       S  
ATOM   4687  N   GLY B 271      40.690  43.455  10.175  1.00 73.38           N  
ANISOU 4687  N   GLY B 271     9297   9191   9391    -17   -119    576       N  
ATOM   4688  CA  GLY B 271      41.519  44.636  10.080  1.00 61.94           C  
ANISOU 4688  CA  GLY B 271     7845   7698   7992     20   -107    542       C  
ATOM   4689  C   GLY B 271      42.358  44.597   8.822  1.00 58.92           C  
ANISOU 4689  C   GLY B 271     7513   7242   7632     29   -115    575       C  
ATOM   4690  O   GLY B 271      42.273  43.663   8.025  1.00 59.76           O  
ANISOU 4690  O   GLY B 271     7658   7333   7717     15   -130    621       O  
ATOM   4691  N   HIS B 272      43.198  45.617   8.677  1.00 60.72           N  
ANISOU 4691  N   HIS B 272     7741   7429   7900     50   -105    551       N  
ATOM   4692  CA  HIS B 272      44.008  45.772   7.480  1.00 66.38           C  
ANISOU 4692  CA  HIS B 272     8499   8083   8637     55   -107    578       C  
ATOM   4693  C   HIS B 272      45.428  46.126   7.886  1.00 64.41           C  
ANISOU 4693  C   HIS B 272     8251   7822   8399     55    -92    556       C  
ATOM   4694  O   HIS B 272      45.641  47.083   8.635  1.00 67.59           O  
ANISOU 4694  O   HIS B 272     8625   8227   8828     66    -86    516       O  
ATOM   4695  CB  HIS B 272      43.413  46.860   6.574  1.00 73.40           C  
ANISOU 4695  CB  HIS B 272     9393   8924   9570     74   -117    576       C  
ATOM   4696  CG  HIS B 272      44.081  46.984   5.243  1.00 76.31           C  
ANISOU 4696  CG  HIS B 272     9808   9232   9953     71   -117    610       C  
ATOM   4697  ND1 HIS B 272      44.177  45.934   4.356  1.00 80.22           N  
ANISOU 4697  ND1 HIS B 272    10343   9717  10421     63   -122    656       N  
ATOM   4698  CD2 HIS B 272      44.673  48.041   4.640  1.00 79.72           C  
ANISOU 4698  CD2 HIS B 272    10258   9613  10420     73   -116    605       C  
ATOM   4699  CE1 HIS B 272      44.810  46.337   3.268  1.00 82.46           C  
ANISOU 4699  CE1 HIS B 272    10661   9950  10720     62   -118    676       C  
ATOM   4700  NE2 HIS B 272      45.121  47.612   3.415  1.00 79.83           N  
ANISOU 4700  NE2 HIS B 272    10317   9592  10423     63   -114    648       N  
ATOM   4701  N   TYR B 273      46.392  45.348   7.399  1.00 56.13           N  
ANISOU 4701  N   TYR B 273     7235   6763   7331     46    -90    580       N  
ATOM   4702  CA  TYR B 273      47.796  45.548   7.717  1.00 49.94           C  
ANISOU 4702  CA  TYR B 273     6448   5973   6554     45    -77    558       C  
ATOM   4703  C   TYR B 273      48.478  46.299   6.585  1.00 56.41           C  
ANISOU 4703  C   TYR B 273     7282   6747   7404     44    -66    572       C  
ATOM   4704  O   TYR B 273      48.309  45.952   5.412  1.00 61.27           O  
ANISOU 4704  O   TYR B 273     7929   7340   8010     42    -70    609       O  
ATOM   4705  CB  TYR B 273      48.506  44.216   7.946  1.00 48.67           C  
ANISOU 4705  CB  TYR B 273     6309   5838   6348     40    -86    565       C  
ATOM   4706  CG  TYR B 273      48.546  43.753   9.383  1.00 57.59           C  
ANISOU 4706  CG  TYR B 273     7424   7006   7451     35    -93    534       C  
ATOM   4707  CD1 TYR B 273      47.854  42.620   9.783  1.00 60.81           C  
ANISOU 4707  CD1 TYR B 273     7851   7445   7810     20   -115    552       C  
ATOM   4708  CD2 TYR B 273      49.295  44.436  10.337  1.00 62.25           C  
ANISOU 4708  CD2 TYR B 273     7989   7601   8064     41    -81    490       C  
ATOM   4709  CE1 TYR B 273      47.899  42.178  11.096  1.00 66.66           C  
ANISOU 4709  CE1 TYR B 273     8587   8220   8520      8   -124    526       C  
ATOM   4710  CE2 TYR B 273      49.343  44.004  11.658  1.00 58.96           C  
ANISOU 4710  CE2 TYR B 273     7566   7216   7621     37    -89    462       C  
ATOM   4711  CZ  TYR B 273      48.645  42.873  12.028  1.00 60.68           C  
ANISOU 4711  CZ  TYR B 273     7805   7464   7785     19   -109    480       C  
ATOM   4712  OH  TYR B 273      48.681  42.426  13.326  1.00 53.79           O  
ANISOU 4712  OH  TYR B 273     6935   6624   6880      7   -119    455       O  
ATOM   4713  N   LYS B 274      49.266  47.305   6.942  1.00 63.16           N  
ANISOU 4713  N   LYS B 274     8118   7588   8291     41    -55    544       N  
ATOM   4714  CA  LYS B 274      50.113  48.015   5.998  1.00 64.89           C  
ANISOU 4714  CA  LYS B 274     8350   7771   8534     27    -44    556       C  
ATOM   4715  C   LYS B 274      51.516  48.120   6.575  1.00 65.49           C  
ANISOU 4715  C   LYS B 274     8404   7863   8616     18    -29    528       C  
ATOM   4716  O   LYS B 274      51.704  48.176   7.792  1.00 66.48           O  
ANISOU 4716  O   LYS B 274     8504   8008   8745     27    -33    492       O  
ATOM   4717  CB  LYS B 274      49.570  49.417   5.675  1.00 61.69           C  
ANISOU 4717  CB  LYS B 274     7949   7320   8170     24    -55    554       C  
ATOM   4718  CG  LYS B 274      48.267  49.419   4.894  1.00 61.40           C  
ANISOU 4718  CG  LYS B 274     7937   7259   8133     34    -73    578       C  
ATOM   4719  CD  LYS B 274      47.832  50.841   4.573  1.00 71.34           C  
ANISOU 4719  CD  LYS B 274     9209   8466   9432     35    -96    568       C  
ATOM   4720  CE  LYS B 274      46.474  50.880   3.881  1.00 77.23           C  
ANISOU 4720  CE  LYS B 274     9977   9186  10181     52   -121    582       C  
ATOM   4721  NZ  LYS B 274      45.986  52.283   3.722  1.00 81.08           N  
ANISOU 4721  NZ  LYS B 274    10479   9622  10707     61   -156    560       N  
ATOM   4722  N   HIS B 275      52.497  48.151   5.682  1.00 62.54           N  
ANISOU 4722  N   HIS B 275     8039   7484   8240      0    -13    544       N  
ATOM   4723  CA  HIS B 275      53.903  48.144   6.052  1.00 59.07           C  
ANISOU 4723  CA  HIS B 275     7574   7067   7803     -9      2    517       C  
ATOM   4724  C   HIS B 275      54.509  49.517   5.788  1.00 61.23           C  
ANISOU 4724  C   HIS B 275     7837   7309   8117    -41     11    516       C  
ATOM   4725  O   HIS B 275      54.517  49.986   4.647  1.00 62.21           O  
ANISOU 4725  O   HIS B 275     7984   7410   8244    -66     19    549       O  
ATOM   4726  CB  HIS B 275      54.646  47.059   5.273  1.00 56.79           C  
ANISOU 4726  CB  HIS B 275     7295   6809   7475     -6     13    528       C  
ATOM   4727  CG  HIS B 275      56.103  46.979   5.598  1.00 56.68           C  
ANISOU 4727  CG  HIS B 275     7248   6826   7461    -12     26    493       C  
ATOM   4728  ND1 HIS B 275      56.575  46.400   6.755  1.00 57.64           N  
ANISOU 4728  ND1 HIS B 275     7352   6973   7576      9     13    450       N  
ATOM   4729  CD2 HIS B 275      57.194  47.396   4.914  1.00 57.35           C  
ANISOU 4729  CD2 HIS B 275     7314   6924   7551    -38     51    493       C  
ATOM   4730  CE1 HIS B 275      57.893  46.470   6.775  1.00 57.77           C  
ANISOU 4730  CE1 HIS B 275     7339   7015   7598      1     26    421       C  
ATOM   4731  NE2 HIS B 275      58.294  47.068   5.668  1.00 59.50           N  
ANISOU 4731  NE2 HIS B 275     7552   7232   7824    -29     52    446       N  
ATOM   4732  N   ILE B 276      55.039  50.143   6.835  1.00 63.63           N  
ANISOU 4732  N   ILE B 276     8114   7614   8450    -42      6    479       N  
ATOM   4733  CA  ILE B 276      55.741  51.417   6.728  1.00 62.96           C  
ANISOU 4733  CA  ILE B 276     8020   7500   8402    -76      6    477       C  
ATOM   4734  C   ILE B 276      57.231  51.137   6.855  1.00 64.82           C  
ANISOU 4734  C   ILE B 276     8222   7772   8635    -93     28    456       C  
ATOM   4735  O   ILE B 276      57.655  50.437   7.780  1.00 70.55           O  
ANISOU 4735  O   ILE B 276     8926   8529   9353    -67     26    420       O  
ATOM   4736  CB  ILE B 276      55.282  52.419   7.802  1.00 64.25           C  
ANISOU 4736  CB  ILE B 276     8176   7633   8603    -61    -23    449       C  
ATOM   4737  CG1 ILE B 276      53.928  53.023   7.440  1.00 65.91           C  
ANISOU 4737  CG1 ILE B 276     8417   7804   8823    -50    -49    465       C  
ATOM   4738  CG2 ILE B 276      56.305  53.528   7.984  1.00 65.12           C  
ANISOU 4738  CG2 ILE B 276     8272   7720   8750    -94    -30    438       C  
ATOM   4739  CD1 ILE B 276      52.768  52.192   7.883  1.00 64.45           C  
ANISOU 4739  CD1 ILE B 276     8231   7645   8614    -10    -54    458       C  
ATOM   4740  N   THR B 277      58.021  51.669   5.924  1.00 64.93           N  
ANISOU 4740  N   THR B 277     8234   7785   8653   -138     47    478       N  
ATOM   4741  CA  THR B 277      59.468  51.512   5.932  1.00 64.96           C  
ANISOU 4741  CA  THR B 277     8196   7831   8655   -161     70    456       C  
ATOM   4742  C   THR B 277      60.130  52.877   5.789  1.00 69.67           C  
ANISOU 4742  C   THR B 277     8783   8401   9287   -218     69    466       C  
ATOM   4743  O   THR B 277      59.577  53.789   5.167  1.00 70.11           O  
ANISOU 4743  O   THR B 277     8875   8409   9354   -249     56    502       O  
ATOM   4744  CB  THR B 277      59.951  50.583   4.808  1.00 57.69           C  
ANISOU 4744  CB  THR B 277     7272   6958   7687   -165    100    472       C  
ATOM   4745  OG1 THR B 277      61.384  50.567   4.774  1.00 58.97           O  
ANISOU 4745  OG1 THR B 277     7386   7171   7849   -190    124    445       O  
ATOM   4746  CG2 THR B 277      59.440  51.060   3.476  1.00 56.31           C  
ANISOU 4746  CG2 THR B 277     7136   6757   7501   -200    111    526       C  
ATOM   4747  N   SER B 278      61.319  53.012   6.374  1.00 69.24           N  
ANISOU 4747  N   SER B 278     8683   8375   9250   -232     77    432       N  
ATOM   4748  CA  SER B 278      62.064  54.266   6.366  1.00 72.71           C  
ANISOU 4748  CA  SER B 278     9110   8793   9725   -291     71    440       C  
ATOM   4749  C   SER B 278      63.308  54.106   5.502  1.00 72.01           C  
ANISOU 4749  C   SER B 278     8982   8764   9615   -344    112    446       C  
ATOM   4750  O   SER B 278      64.179  53.282   5.805  1.00 68.84           O  
ANISOU 4750  O   SER B 278     8533   8422   9200   -322    132    405       O  
ATOM   4751  CB  SER B 278      62.443  54.694   7.785  1.00 76.25           C  
ANISOU 4751  CB  SER B 278     9534   9223  10215   -271     42    395       C  
ATOM   4752  OG  SER B 278      63.341  55.792   7.766  1.00 77.44           O  
ANISOU 4752  OG  SER B 278     9666   9358  10398   -331     34    402       O  
ATOM   4753  N   LYS B 279      63.379  54.879   4.419  1.00 74.26           N  
ANISOU 4753  N   LYS B 279     9289   9035   9892   -412    123    494       N  
ATOM   4754  CA  LYS B 279      64.550  54.877   3.551  1.00 80.88           C  
ANISOU 4754  CA  LYS B 279    10089   9937  10706   -474    167    504       C  
ATOM   4755  C   LYS B 279      65.030  56.308   3.332  1.00 86.24           C  
ANISOU 4755  C   LYS B 279    10775  10581  11411   -564    153    536       C  
ATOM   4756  O   LYS B 279      65.429  56.974   4.293  1.00 89.10           O  
ANISOU 4756  O   LYS B 279    11119  10918  11817   -573    124    514       O  
ATOM   4757  CB  LYS B 279      64.228  54.175   2.231  1.00 78.89           C  
ANISOU 4757  CB  LYS B 279     9858   9717  10398   -475    200    536       C  
ATOM   4758  CG  LYS B 279      63.693  52.766   2.437  1.00 83.24           C  
ANISOU 4758  CG  LYS B 279    10411  10293  10922   -387    201    509       C  
ATOM   4759  CD  LYS B 279      63.552  52.009   1.130  1.00 96.22           C  
ANISOU 4759  CD  LYS B 279    12073  11976  12511   -384    231    536       C  
ATOM   4760  CE  LYS B 279      63.444  50.505   1.374  1.00 99.89           C  
ANISOU 4760  CE  LYS B 279    12527  12484  12944   -302    228    500       C  
ATOM   4761  NZ  LYS B 279      63.802  49.695   0.168  1.00102.60           N  
ANISOU 4761  NZ  LYS B 279    12864  12890  13229   -296    259    509       N  
ATOM   4762  N   GLU B 280      65.019  56.796   2.086  1.00 85.97           N  
ANISOU 4762  N   GLU B 280    10773  10545  11349   -635    171    589       N  
ATOM   4763  CA  GLU B 280      65.300  58.215   1.887  1.00 84.58           C  
ANISOU 4763  CA  GLU B 280    10623  10319  11193   -726    143    627       C  
ATOM   4764  C   GLU B 280      64.144  59.060   2.400  1.00 89.13           C  
ANISOU 4764  C   GLU B 280    11271  10787  11806   -701     73    639       C  
ATOM   4765  O   GLU B 280      64.345  60.210   2.802  1.00101.98           O  
ANISOU 4765  O   GLU B 280    12917  12361  13468   -747     26    649       O  
ATOM   4766  CB  GLU B 280      65.570  58.529   0.414  1.00 88.11           C  
ANISOU 4766  CB  GLU B 280    11095  10789  11594   -816    176    682       C  
ATOM   4767  CG  GLU B 280      64.337  58.533  -0.480  1.00 92.31           C  
ANISOU 4767  CG  GLU B 280    11712  11261  12101   -802    161    725       C  
ATOM   4768  CD  GLU B 280      63.946  57.162  -0.993  1.00 98.33           C  
ANISOU 4768  CD  GLU B 280    12464  12074  12821   -732    201    714       C  
ATOM   4769  OE1 GLU B 280      64.396  56.146  -0.422  1.00100.87           O  
ANISOU 4769  OE1 GLU B 280    12723  12463  13141   -672    227    665       O  
ATOM   4770  OE2 GLU B 280      63.172  57.106  -1.971  1.00 99.78           O  
ANISOU 4770  OE2 GLU B 280    12710  12226  12977   -735    201    753       O  
ATOM   4771  N   THR B 281      62.934  58.503   2.393  1.00 83.11           N  
ANISOU 4771  N   THR B 281    10547   9995  11036   -628     61    636       N  
ATOM   4772  CA  THR B 281      61.758  59.106   3.007  1.00 79.55           C  
ANISOU 4772  CA  THR B 281    10149   9458  10617   -582     -3    631       C  
ATOM   4773  C   THR B 281      60.883  57.973   3.547  1.00 77.25           C  
ANISOU 4773  C   THR B 281     9847   9185  10319   -484      5    598       C  
ATOM   4774  O   THR B 281      61.288  56.807   3.557  1.00 74.28           O  
ANISOU 4774  O   THR B 281     9427   8879   9918   -454     51    578       O  
ATOM   4775  CB  THR B 281      61.024  60.003   1.996  1.00 78.88           C  
ANISOU 4775  CB  THR B 281    10147   9301  10522   -630    -40    681       C  
ATOM   4776  OG1 THR B 281      59.952  60.700   2.646  1.00 79.99           O  
ANISOU 4776  OG1 THR B 281    10334   9361  10696   -583   -111    666       O  
ATOM   4777  CG2 THR B 281      60.464  59.180   0.833  1.00 76.34           C  
ANISOU 4777  CG2 THR B 281     9852   9000  10155   -619     -2    709       C  
ATOM   4778  N   LEU B 282      59.674  58.316   3.993  1.00 76.99           N  
ANISOU 4778  N   LEU B 282     9855   9092  10305   -435    -43    590       N  
ATOM   4779  CA  LEU B 282      58.736  57.344   4.540  1.00 68.34           C  
ANISOU 4779  CA  LEU B 282     8752   8013   9202   -351    -39    563       C  
ATOM   4780  C   LEU B 282      57.892  56.741   3.424  1.00 71.15           C  
ANISOU 4780  C   LEU B 282     9145   8367   9522   -341    -23    596       C  
ATOM   4781  O   LEU B 282      57.278  57.470   2.639  1.00 81.55           O  
ANISOU 4781  O   LEU B 282    10519   9627  10840   -368    -51    628       O  
ATOM   4782  CB  LEU B 282      57.834  57.994   5.589  1.00 60.66           C  
ANISOU 4782  CB  LEU B 282     7794   6990   8263   -301    -96    533       C  
ATOM   4783  CG  LEU B 282      58.571  58.361   6.878  1.00 60.57           C  
ANISOU 4783  CG  LEU B 282     7744   6985   8285   -290   -113    493       C  
ATOM   4784  CD1 LEU B 282      57.615  58.852   7.954  1.00 63.18           C  
ANISOU 4784  CD1 LEU B 282     8086   7278   8641   -228   -165    457       C  
ATOM   4785  CD2 LEU B 282      59.374  57.183   7.378  1.00 61.68           C  
ANISOU 4785  CD2 LEU B 282     7828   7197   8411   -270    -65    465       C  
ATOM   4786  N   TYR B 283      57.876  55.414   3.350  1.00 67.14           N  
ANISOU 4786  N   TYR B 283     8612   7915   8983   -304     14    588       N  
ATOM   4787  CA  TYR B 283      57.088  54.682   2.370  1.00 65.74           C  
ANISOU 4787  CA  TYR B 283     8469   7739   8772   -286     27    617       C  
ATOM   4788  C   TYR B 283      56.009  53.862   3.069  1.00 65.53           C  
ANISOU 4788  C   TYR B 283     8439   7718   8742   -215     13    595       C  
ATOM   4789  O   TYR B 283      56.200  53.379   4.189  1.00 66.20           O  
ANISOU 4789  O   TYR B 283     8486   7834   8832   -180     14    557       O  
ATOM   4790  CB  TYR B 283      57.977  53.757   1.534  1.00 68.10           C  
ANISOU 4790  CB  TYR B 283     8746   8101   9028   -303     77    630       C  
ATOM   4791  CG  TYR B 283      58.811  54.473   0.496  1.00 78.01           C  
ANISOU 4791  CG  TYR B 283    10012   9358  10272   -381     98    664       C  
ATOM   4792  CD1 TYR B 283      60.022  55.063   0.835  1.00 79.84           C  
ANISOU 4792  CD1 TYR B 283    10202   9616  10518   -432    111    651       C  
ATOM   4793  CD2 TYR B 283      58.397  54.541  -0.828  1.00 85.31           C  
ANISOU 4793  CD2 TYR B 283    10988  10260  11167   -408    105    710       C  
ATOM   4794  CE1 TYR B 283      60.791  55.713  -0.113  1.00 83.17           C  
ANISOU 4794  CE1 TYR B 283    10631  10048  10923   -515    132    686       C  
ATOM   4795  CE2 TYR B 283      59.161  55.185  -1.784  1.00 88.46           C  
ANISOU 4795  CE2 TYR B 283    11399  10664  11546   -487    126    744       C  
ATOM   4796  CZ  TYR B 283      60.355  55.771  -1.422  1.00 85.80           C  
ANISOU 4796  CZ  TYR B 283    11018  10360  11222   -544    141    733       C  
ATOM   4797  OH  TYR B 283      61.112  56.416  -2.376  1.00 86.90           O  
ANISOU 4797  OH  TYR B 283    11168  10512  11337   -634    164    769       O  
ATOM   4798  N   CYS B 284      54.861  53.722   2.408  1.00 60.47           N  
ANISOU 4798  N   CYS B 284     7840   7045   8090   -196     -2    619       N  
ATOM   4799  CA  CYS B 284      53.764  52.907   2.916  1.00 54.67           C  
ANISOU 4799  CA  CYS B 284     7103   6321   7347   -139    -14    605       C  
ATOM   4800  C   CYS B 284      53.374  51.909   1.836  1.00 57.13           C  
ANISOU 4800  C   CYS B 284     7441   6644   7621   -130      2    640       C  
ATOM   4801  O   CYS B 284      52.803  52.290   0.809  1.00 60.94           O  
ANISOU 4801  O   CYS B 284     7970   7083   8101   -143     -9    672       O  
ATOM   4802  CB  CYS B 284      52.564  53.756   3.321  1.00 58.56           C  
ANISOU 4802  CB  CYS B 284     7616   6765   7869   -116    -59    592       C  
ATOM   4803  SG  CYS B 284      51.182  52.763   3.949  1.00 60.97           S  
ANISOU 4803  SG  CYS B 284     7908   7098   8160    -55    -69    575       S  
ATOM   4804  N   ILE B 285      53.671  50.637   2.080  1.00 59.19           N  
ANISOU 4804  N   ILE B 285     7680   6959   7851   -104     21    631       N  
ATOM   4805  CA  ILE B 285      53.411  49.559   1.139  1.00 53.81           C  
ANISOU 4805  CA  ILE B 285     7023   6292   7129    -88     29    661       C  
ATOM   4806  C   ILE B 285      52.175  48.804   1.600  1.00 58.98           C  
ANISOU 4806  C   ILE B 285     7687   6947   7776    -47      5    659       C  
ATOM   4807  O   ILE B 285      52.137  48.293   2.726  1.00 63.30           O  
ANISOU 4807  O   ILE B 285     8205   7525   8320    -26     -2    629       O  
ATOM   4808  CB  ILE B 285      54.616  48.618   1.014  1.00 45.16           C  
ANISOU 4808  CB  ILE B 285     5903   5257   6000    -86     56    650       C  
ATOM   4809  CG1 ILE B 285      55.873  49.420   0.693  1.00 44.73           C  
ANISOU 4809  CG1 ILE B 285     5826   5216   5954   -133     84    646       C  
ATOM   4810  CG2 ILE B 285      54.357  47.589  -0.064  1.00 49.24           C  
ANISOU 4810  CG2 ILE B 285     6452   5784   6473    -66     57    681       C  
ATOM   4811  CD1 ILE B 285      57.104  48.575   0.580  1.00 45.28           C  
ANISOU 4811  CD1 ILE B 285     5860   5354   5991   -128    109    625       C  
ATOM   4812  N   ASP B 286      51.149  48.781   0.752  1.00 60.34           N  
ANISOU 4812  N   ASP B 286     7899   7082   7945    -39    -11    691       N  
ATOM   4813  CA  ASP B 286      49.910  48.036   0.972  1.00 64.38           C  
ANISOU 4813  CA  ASP B 286     8420   7595   8447     -7    -35    697       C  
ATOM   4814  C   ASP B 286      49.804  47.009  -0.152  1.00 67.04           C  
ANISOU 4814  C   ASP B 286     8794   7932   8746      4    -36    736       C  
ATOM   4815  O   ASP B 286      49.079  47.204  -1.131  1.00 70.55           O  
ANISOU 4815  O   ASP B 286     9278   8333   9194      5    -48    767       O  
ATOM   4816  CB  ASP B 286      48.697  48.970   0.998  1.00 70.61           C  
ANISOU 4816  CB  ASP B 286     9220   8338   9270     -1    -61    693       C  
ATOM   4817  CG  ASP B 286      47.402  48.229   1.249  1.00 76.18           C  
ANISOU 4817  CG  ASP B 286     9925   9054   9965     26    -83    697       C  
ATOM   4818  OD1 ASP B 286      47.465  47.110   1.798  1.00 78.67           O  
ANISOU 4818  OD1 ASP B 286    10224   9416  10249     36    -79    696       O  
ATOM   4819  OD2 ASP B 286      46.327  48.753   0.882  1.00 78.32           O  
ANISOU 4819  OD2 ASP B 286    10213   9289  10257     37   -107    700       O  
ATOM   4820  N   GLY B 287      50.530  45.908  -0.006  1.00 67.50           N  
ANISOU 4820  N   GLY B 287     8843   8037   8768     16    -29    732       N  
ATOM   4821  CA  GLY B 287      50.587  44.930  -1.071  1.00 64.28           C  
ANISOU 4821  CA  GLY B 287     8470   7631   8320     33    -35    764       C  
ATOM   4822  C   GLY B 287      51.341  45.452  -2.277  1.00 63.74           C  
ANISOU 4822  C   GLY B 287     8421   7550   8246     13     -9    784       C  
ATOM   4823  O   GLY B 287      52.567  45.573  -2.253  1.00 67.52           O  
ANISOU 4823  O   GLY B 287     8873   8066   8715     -2     18    765       O  
ATOM   4824  N   ALA B 288      50.613  45.773  -3.342  1.00 67.19           N  
ANISOU 4824  N   ALA B 288     8904   7937   8687     10    -18    820       N  
ATOM   4825  CA  ALA B 288      51.217  46.319  -4.549  1.00 67.58           C  
ANISOU 4825  CA  ALA B 288     8982   7970   8727    -17      6    844       C  
ATOM   4826  C   ALA B 288      51.192  47.841  -4.613  1.00 67.40           C  
ANISOU 4826  C   ALA B 288     8966   7902   8743    -62     12    844       C  
ATOM   4827  O   ALA B 288      51.756  48.413  -5.551  1.00 69.62           O  
ANISOU 4827  O   ALA B 288     9272   8169   9012    -98     32    865       O  
ATOM   4828  CB  ALA B 288      50.518  45.749  -5.784  1.00 63.59           C  
ANISOU 4828  CB  ALA B 288     8536   7430   8197      6    -13    886       C  
ATOM   4829  N   LEU B 289      50.566  48.507  -3.653  1.00 62.93           N  
ANISOU 4829  N   LEU B 289     8382   7313   8217    -62     -8    820       N  
ATOM   4830  CA  LEU B 289      50.406  49.950  -3.697  1.00 61.95           C  
ANISOU 4830  CA  LEU B 289     8275   7136   8130    -96    -19    817       C  
ATOM   4831  C   LEU B 289      51.470  50.610  -2.830  1.00 66.67           C  
ANISOU 4831  C   LEU B 289     8826   7763   8743   -127      0    787       C  
ATOM   4832  O   LEU B 289      51.933  50.036  -1.842  1.00 72.79           O  
ANISOU 4832  O   LEU B 289     9551   8592   9515   -110     12    757       O  
ATOM   4833  CB  LEU B 289      48.999  50.346  -3.235  1.00 66.21           C  
ANISOU 4833  CB  LEU B 289     8824   7631   8703    -69    -62    803       C  
ATOM   4834  CG  LEU B 289      47.849  49.500  -3.814  1.00 65.43           C  
ANISOU 4834  CG  LEU B 289     8755   7512   8591    -31    -84    826       C  
ATOM   4835  CD1 LEU B 289      46.491  50.056  -3.421  1.00 68.75           C  
ANISOU 4835  CD1 LEU B 289     9180   7895   9048     -8   -125    805       C  
ATOM   4836  CD2 LEU B 289      47.944  49.372  -5.335  1.00 57.77           C  
ANISOU 4836  CD2 LEU B 289     7848   6504   7597    -42    -81    870       C  
ATOM   4837  N   LEU B 290      51.846  51.832  -3.203  1.00 70.41           N  
ANISOU 4837  N   LEU B 290     9321   8197   9234   -176     -3    795       N  
ATOM   4838  CA  LEU B 290      52.949  52.545  -2.572  1.00 67.16           C  
ANISOU 4838  CA  LEU B 290     8872   7808   8837   -216     12    775       C  
ATOM   4839  C   LEU B 290      52.572  53.995  -2.313  1.00 67.20           C  
ANISOU 4839  C   LEU B 290     8905   7747   8882   -242    -29    768       C  
ATOM   4840  O   LEU B 290      51.848  54.600  -3.106  1.00 72.59           O  
ANISOU 4840  O   LEU B 290     9648   8363   9570   -252    -61    790       O  
ATOM   4841  CB  LEU B 290      54.198  52.497  -3.460  1.00 69.01           C  
ANISOU 4841  CB  LEU B 290     9105   8079   9038   -267     55    798       C  
ATOM   4842  CG  LEU B 290      55.482  53.056  -2.868  1.00 68.77           C  
ANISOU 4842  CG  LEU B 290     9025   8086   9017   -312     77    778       C  
ATOM   4843  CD1 LEU B 290      55.834  52.296  -1.606  1.00 77.86           C  
ANISOU 4843  CD1 LEU B 290    10112   9294  10177   -268     85    732       C  
ATOM   4844  CD2 LEU B 290      56.583  52.961  -3.887  1.00 70.17           C  
ANISOU 4844  CD2 LEU B 290     9197   8309   9154   -364    122    802       C  
ATOM   4845  N   THR B 291      53.062  54.551  -1.206  1.00 66.99           N  
ANISOU 4845  N   THR B 291     8837   7732   8883   -248    -36    734       N  
ATOM   4846  CA  THR B 291      52.770  55.935  -0.853  1.00 71.33           C  
ANISOU 4846  CA  THR B 291     9413   8219   9470   -267    -86    722       C  
ATOM   4847  C   THR B 291      53.973  56.529  -0.136  1.00 79.46           C  
ANISOU 4847  C   THR B 291    10405   9272  10516   -306    -77    705       C  
ATOM   4848  O   THR B 291      54.489  55.924   0.808  1.00 88.11           O  
ANISOU 4848  O   THR B 291    11440  10423  11613   -281    -52    675       O  
ATOM   4849  CB  THR B 291      51.528  56.040   0.042  1.00 74.41           C  
ANISOU 4849  CB  THR B 291     9796   8590   9888   -203   -129    684       C  
ATOM   4850  OG1 THR B 291      50.382  55.546  -0.660  1.00 84.41           O  
ANISOU 4850  OG1 THR B 291    11096   9833  11142   -170   -141    699       O  
ATOM   4851  CG2 THR B 291      51.278  57.491   0.449  1.00 69.35           C  
ANISOU 4851  CG2 THR B 291     9181   7885   9282   -212   -190    663       C  
ATOM   4852  N   LYS B 292      54.403  57.713  -0.569  1.00 80.37           N  
ANISOU 4852  N   LYS B 292    10558   9338  10641   -369   -103    725       N  
ATOM   4853  CA  LYS B 292      55.500  58.435   0.062  1.00 75.76           C  
ANISOU 4853  CA  LYS B 292     9945   8764  10077   -414   -105    714       C  
ATOM   4854  C   LYS B 292      54.958  59.630   0.834  1.00 73.62           C  
ANISOU 4854  C   LYS B 292     9701   8426   9848   -400   -179    688       C  
ATOM   4855  O   LYS B 292      53.887  60.157   0.530  1.00 77.19           O  
ANISOU 4855  O   LYS B 292    10208   8813  10308   -378   -233    688       O  
ATOM   4856  CB  LYS B 292      56.517  58.915  -0.976  1.00 80.52           C  
ANISOU 4856  CB  LYS B 292    10571   9368  10655   -508    -82    758       C  
ATOM   4857  CG  LYS B 292      56.976  57.843  -1.937  1.00 83.30           C  
ANISOU 4857  CG  LYS B 292    10906   9784  10960   -520    -15    784       C  
ATOM   4858  CD  LYS B 292      57.998  58.395  -2.917  1.00 88.57           C  
ANISOU 4858  CD  LYS B 292    11591  10464  11598   -620     10    825       C  
ATOM   4859  CE  LYS B 292      57.447  59.597  -3.679  1.00 91.14           C  
ANISOU 4859  CE  LYS B 292    12010  10693  11925   -675    -46    863       C  
ATOM   4860  NZ  LYS B 292      58.443  60.156  -4.639  1.00 91.04           N  
ANISOU 4860  NZ  LYS B 292    12018  10694  11877   -785    -22    909       N  
ATOM   4861  N   SER B 293      55.722  60.059   1.834  1.00 73.69           N  
ANISOU 4861  N   SER B 293     9669   8449   9882   -408   -187    662       N  
ATOM   4862  CA  SER B 293      55.415  61.251   2.618  1.00 81.19           C  
ANISOU 4862  CA  SER B 293    10643   9337  10869   -396   -263    636       C  
ATOM   4863  C   SER B 293      56.612  61.550   3.508  1.00 83.32           C  
ANISOU 4863  C   SER B 293    10864   9634  11161   -423   -256    619       C  
ATOM   4864  O   SER B 293      57.447  60.680   3.770  1.00 79.07           O  
ANISOU 4864  O   SER B 293    10264   9167  10611   -426   -193    613       O  
ATOM   4865  CB  SER B 293      54.137  61.090   3.458  1.00 88.96           C  
ANISOU 4865  CB  SER B 293    11619  10313  11871   -302   -297    589       C  
ATOM   4866  OG  SER B 293      54.201  59.966   4.319  1.00 97.40           O  
ANISOU 4866  OG  SER B 293    12618  11455  12933   -251   -247    560       O  
ATOM   4867  N   SER B 294      56.702  62.806   3.946  1.00 87.73           N  
ANISOU 4867  N   SER B 294    11454  10129  11749   -441   -327    612       N  
ATOM   4868  CA  SER B 294      57.809  63.196   4.814  1.00 87.18           C  
ANISOU 4868  CA  SER B 294    11344  10075  11705   -467   -331    596       C  
ATOM   4869  C   SER B 294      57.613  62.672   6.230  1.00 79.88           C  
ANISOU 4869  C   SER B 294    10363   9187  10802   -380   -325    539       C  
ATOM   4870  O   SER B 294      58.580  62.265   6.883  1.00 78.47           O  
ANISOU 4870  O   SER B 294    10127   9057  10632   -385   -289    522       O  
ATOM   4871  CB  SER B 294      57.962  64.715   4.819  1.00 97.56           C  
ANISOU 4871  CB  SER B 294    12720  11305  13043   -515   -420    609       C  
ATOM   4872  OG  SER B 294      58.162  65.206   3.503  1.00108.63           O  
ANISOU 4872  OG  SER B 294    14182  12671  14420   -605   -427    666       O  
ATOM   4873  N   GLU B 295      56.375  62.663   6.720  1.00 78.36           N  
ANISOU 4873  N   GLU B 295    10183   8975  10614   -301   -361    506       N  
ATOM   4874  CA  GLU B 295      56.079  62.188   8.062  1.00 82.13           C  
ANISOU 4874  CA  GLU B 295    10612   9490  11105   -222   -356    452       C  
ATOM   4875  C   GLU B 295      54.872  61.258   8.051  1.00 79.10           C  
ANISOU 4875  C   GLU B 295    10218   9141  10697   -158   -331    436       C  
ATOM   4876  O   GLU B 295      54.139  61.146   7.064  1.00 74.19           O  
ANISOU 4876  O   GLU B 295     9631   8500  10056   -165   -332    462       O  
ATOM   4877  CB  GLU B 295      55.815  63.345   9.036  1.00 89.15           C  
ANISOU 4877  CB  GLU B 295    11519  10325  12028   -184   -440    414       C  
ATOM   4878  CG  GLU B 295      54.962  64.467   8.481  1.00 96.97           C  
ANISOU 4878  CG  GLU B 295    12582  11236  13025   -183   -523    419       C  
ATOM   4879  CD  GLU B 295      54.706  65.556   9.508  1.00106.07           C  
ANISOU 4879  CD  GLU B 295    13752  12341  14209   -132   -614    374       C  
ATOM   4880  OE1 GLU B 295      55.253  65.465  10.630  1.00107.51           O  
ANISOU 4880  OE1 GLU B 295    13890  12549  14408   -104   -607    343       O  
ATOM   4881  OE2 GLU B 295      53.933  66.490   9.206  1.00111.24           O  
ANISOU 4881  OE2 GLU B 295    14467  12930  14870   -114   -697    364       O  
ATOM   4882  N   TYR B 296      54.689  60.573   9.178  1.00 80.21           N  
ANISOU 4882  N   TYR B 296    10310   9331  10836   -100   -310    395       N  
ATOM   4883  CA  TYR B 296      53.617  59.610   9.361  1.00 74.03           C  
ANISOU 4883  CA  TYR B 296     9509   8592  10028    -45   -285    379       C  
ATOM   4884  C   TYR B 296      53.040  59.743  10.760  1.00 68.72           C  
ANISOU 4884  C   TYR B 296     8809   7938   9365     24   -311    323       C  
ATOM   4885  O   TYR B 296      53.779  59.904  11.734  1.00 62.37           O  
ANISOU 4885  O   TYR B 296     7980   7141   8576     32   -315    298       O  
ATOM   4886  CB  TYR B 296      54.117  58.173   9.150  1.00 72.38           C  
ANISOU 4886  CB  TYR B 296     9267   8447   9787    -59   -212    396       C  
ATOM   4887  CG  TYR B 296      53.042  57.127   9.328  1.00 62.10           C  
ANISOU 4887  CG  TYR B 296     7951   7189   8455    -13   -190    387       C  
ATOM   4888  CD1 TYR B 296      52.352  56.619   8.240  1.00 65.41           C  
ANISOU 4888  CD1 TYR B 296     8394   7607   8851    -21   -176    421       C  
ATOM   4889  CD2 TYR B 296      52.718  56.653  10.593  1.00 56.56           C  
ANISOU 4889  CD2 TYR B 296     7215   6529   7746     34   -186    346       C  
ATOM   4890  CE1 TYR B 296      51.369  55.669   8.410  1.00 71.47           C  
ANISOU 4890  CE1 TYR B 296     9148   8414   9592     15   -160    415       C  
ATOM   4891  CE2 TYR B 296      51.742  55.718  10.773  1.00 63.58           C  
ANISOU 4891  CE2 TYR B 296     8092   7462   8605     65   -168    341       C  
ATOM   4892  CZ  TYR B 296      51.069  55.221   9.682  1.00 71.25           C  
ANISOU 4892  CZ  TYR B 296     9084   8432   9556     54   -156    376       C  
ATOM   4893  OH  TYR B 296      50.093  54.272   9.876  1.00 72.75           O  
ANISOU 4893  OH  TYR B 296     9262   8666   9715     79   -142    374       O  
ATOM   4894  N   LYS B 297      51.716  59.649  10.857  1.00 71.77           N  
ANISOU 4894  N   LYS B 297     9195   8335   9738     74   -327    302       N  
ATOM   4895  CA  LYS B 297      51.047  59.614  12.154  1.00 74.22           C  
ANISOU 4895  CA  LYS B 297     9472   8682  10045    140   -342    248       C  
ATOM   4896  C   LYS B 297      49.816  58.730  11.994  1.00 68.99           C  
ANISOU 4896  C   LYS B 297     8793   8070   9350    168   -315    245       C  
ATOM   4897  O   LYS B 297      48.845  59.132  11.349  1.00 68.13           O  
ANISOU 4897  O   LYS B 297     8705   7939   9243    184   -346    244       O  
ATOM   4898  CB  LYS B 297      50.686  61.022  12.621  1.00 81.90           C  
ANISOU 4898  CB  LYS B 297    10465   9605  11047    178   -422    209       C  
ATOM   4899  CG  LYS B 297      50.049  61.087  13.993  1.00 91.24           C  
ANISOU 4899  CG  LYS B 297    11611  10832  12225    251   -439    147       C  
ATOM   4900  CD  LYS B 297      49.758  62.528  14.393  1.00 98.04           C  
ANISOU 4900  CD  LYS B 297    12497  11640  13114    296   -529    105       C  
ATOM   4901  CE  LYS B 297      49.101  62.597  15.765  1.00101.13           C  
ANISOU 4901  CE  LYS B 297    12847  12083  13493    375   -545     38       C  
ATOM   4902  NZ  LYS B 297      49.959  61.992  16.829  1.00101.97           N  
ANISOU 4902  NZ  LYS B 297    12922  12228  13595    373   -501     31       N  
ATOM   4903  N   GLY B 298      49.853  57.534  12.580  1.00 68.33           N  
ANISOU 4903  N   GLY B 298     8674   8053   9237    173   -264    242       N  
ATOM   4904  CA  GLY B 298      48.765  56.595  12.453  1.00 63.89           C  
ANISOU 4904  CA  GLY B 298     8095   7541   8639    188   -238    246       C  
ATOM   4905  C   GLY B 298      48.799  55.471  13.472  1.00 61.60           C  
ANISOU 4905  C   GLY B 298     7769   7321   8314    197   -199    232       C  
ATOM   4906  O   GLY B 298      49.662  55.418  14.356  1.00 59.94           O  
ANISOU 4906  O   GLY B 298     7548   7119   8108    198   -192    213       O  
ATOM   4907  N   PRO B 299      47.837  54.542  13.366  1.00 59.67           N  
ANISOU 4907  N   PRO B 299     7512   7127   8034    200   -177    242       N  
ATOM   4908  CA  PRO B 299      47.760  53.434  14.329  1.00 55.38           C  
ANISOU 4908  CA  PRO B 299     6944   6650   7449    200   -146    232       C  
ATOM   4909  C   PRO B 299      48.749  52.324  14.020  1.00 58.81           C  
ANISOU 4909  C   PRO B 299     7396   7086   7863    161   -115    268       C  
ATOM   4910  O   PRO B 299      48.554  51.538  13.085  1.00 64.23           O  
ANISOU 4910  O   PRO B 299     8100   7775   8531    137   -100    308       O  
ATOM   4911  CB  PRO B 299      46.309  52.958  14.196  1.00 58.61           C  
ANISOU 4911  CB  PRO B 299     7334   7108   7828    210   -141    233       C  
ATOM   4912  CG  PRO B 299      45.949  53.289  12.787  1.00 61.35           C  
ANISOU 4912  CG  PRO B 299     7708   7406   8195    201   -156    265       C  
ATOM   4913  CD  PRO B 299      46.714  54.532  12.411  1.00 56.96           C  
ANISOU 4913  CD  PRO B 299     7177   6778   7685    204   -187    259       C  
ATOM   4914  N   ILE B 300      49.821  52.266  14.803  1.00 56.76           N  
ANISOU 4914  N   ILE B 300     7133   6824   7609    159   -110    249       N  
ATOM   4915  CA  ILE B 300      50.887  51.287  14.636  1.00 55.14           C  
ANISOU 4915  CA  ILE B 300     6942   6621   7387    131    -90    268       C  
ATOM   4916  C   ILE B 300      50.770  50.231  15.726  1.00 61.39           C  
ANISOU 4916  C   ILE B 300     7729   7463   8133    134    -81    250       C  
ATOM   4917  O   ILE B 300      50.328  50.508  16.847  1.00 65.68           O  
ANISOU 4917  O   ILE B 300     8255   8032   8669    157    -88    215       O  
ATOM   4918  CB  ILE B 300      52.275  51.960  14.653  1.00 52.64           C  
ANISOU 4918  CB  ILE B 300     6626   6264   7110    123    -95    257       C  
ATOM   4919  CG1 ILE B 300      52.352  53.049  13.578  1.00 53.67           C  
ANISOU 4919  CG1 ILE B 300     6769   6345   7279    108   -108    279       C  
ATOM   4920  CG2 ILE B 300      53.368  50.944  14.423  1.00 57.57           C  
ANISOU 4920  CG2 ILE B 300     7258   6898   7716    100    -77    268       C  
ATOM   4921  CD1 ILE B 300      52.166  52.530  12.162  1.00 50.61           C  
ANISOU 4921  CD1 ILE B 300     6403   5951   6876     80    -92    327       C  
ATOM   4922  N   THR B 301      51.126  49.000  15.379  1.00 60.93           N  
ANISOU 4922  N   THR B 301     7691   7419   8040    112    -71    275       N  
ATOM   4923  CA  THR B 301      51.121  47.914  16.346  1.00 61.74           C  
ANISOU 4923  CA  THR B 301     7805   7560   8094    107    -72    262       C  
ATOM   4924  C   THR B 301      52.476  47.251  16.533  1.00 68.03           C  
ANISOU 4924  C   THR B 301     8620   8343   8884    101    -78    250       C  
ATOM   4925  O   THR B 301      52.723  46.695  17.606  1.00 72.81           O  
ANISOU 4925  O   THR B 301     9237   8965   9462    104    -88    223       O  
ATOM   4926  CB  THR B 301      50.096  46.839  15.951  1.00 62.81           C  
ANISOU 4926  CB  THR B 301     7955   7730   8179     86    -71    298       C  
ATOM   4927  OG1 THR B 301      50.157  45.761  16.894  1.00 70.98           O  
ANISOU 4927  OG1 THR B 301     9010   8798   9161     72    -80    288       O  
ATOM   4928  CG2 THR B 301      50.379  46.312  14.548  1.00 55.41           C  
ANISOU 4928  CG2 THR B 301     7042   6771   7241     72    -70    340       C  
ATOM   4929  N   ASP B 302      53.355  47.287  15.529  1.00 67.88           N  
ANISOU 4929  N   ASP B 302     8606   8298   8888     93    -73    265       N  
ATOM   4930  CA  ASP B 302      54.703  46.741  15.630  1.00 63.68           C  
ANISOU 4930  CA  ASP B 302     8082   7759   8354     93    -80    244       C  
ATOM   4931  C   ASP B 302      55.678  47.736  15.030  1.00 60.62           C  
ANISOU 4931  C   ASP B 302     7672   7342   8019     89    -69    240       C  
ATOM   4932  O   ASP B 302      55.391  48.333  13.991  1.00 66.94           O  
ANISOU 4932  O   ASP B 302     8467   8127   8839     76    -57    272       O  
ATOM   4933  CB  ASP B 302      54.832  45.398  14.897  1.00 72.97           C  
ANISOU 4933  CB  ASP B 302     9290   8952   9485     83    -89    269       C  
ATOM   4934  CG  ASP B 302      53.811  44.373  15.361  1.00 82.71           C  
ANISOU 4934  CG  ASP B 302    10553  10212  10662     75   -105    284       C  
ATOM   4935  OD1 ASP B 302      53.810  44.030  16.565  1.00 80.68           O  
ANISOU 4935  OD1 ASP B 302    10307   9966  10380     77   -121    255       O  
ATOM   4936  OD2 ASP B 302      53.002  43.918  14.520  1.00 86.11           O  
ANISOU 4936  OD2 ASP B 302    10997  10650  11069     63   -105    326       O  
ATOM   4937  N   VAL B 303      56.821  47.926  15.691  1.00 58.10           N  
ANISOU 4937  N   VAL B 303     7340   7013   7722     97    -77    200       N  
ATOM   4938  CA  VAL B 303      57.903  48.773  15.193  1.00 56.33           C  
ANISOU 4938  CA  VAL B 303     7091   6768   7545     84    -68    194       C  
ATOM   4939  C   VAL B 303      59.210  48.012  15.346  1.00 60.02           C  
ANISOU 4939  C   VAL B 303     7552   7249   8003     89    -74    161       C  
ATOM   4940  O   VAL B 303      59.468  47.423  16.401  1.00 66.62           O  
ANISOU 4940  O   VAL B 303     8401   8089   8823    109    -95    123       O  
ATOM   4941  CB  VAL B 303      57.982  50.125  15.922  1.00 55.16           C  
ANISOU 4941  CB  VAL B 303     6924   6587   7446     91    -78    174       C  
ATOM   4942  CG1 VAL B 303      59.006  51.018  15.252  1.00 49.61           C  
ANISOU 4942  CG1 VAL B 303     6199   5862   6788     64    -72    180       C  
ATOM   4943  CG2 VAL B 303      56.624  50.811  15.926  1.00 55.61           C  
ANISOU 4943  CG2 VAL B 303     6988   6635   7507     99    -83    193       C  
ATOM   4944  N   PHE B 304      60.032  48.028  14.298  1.00 54.83           N  
ANISOU 4944  N   PHE B 304     6878   6602   7355     70    -57    171       N  
ATOM   4945  CA  PHE B 304      61.289  47.295  14.269  1.00 58.36           C  
ANISOU 4945  CA  PHE B 304     7310   7073   7791     78    -63    134       C  
ATOM   4946  C   PHE B 304      62.462  48.266  14.234  1.00 64.60           C  
ANISOU 4946  C   PHE B 304     8057   7857   8633     59    -52    113       C  
ATOM   4947  O   PHE B 304      62.496  49.175  13.397  1.00 66.16           O  
ANISOU 4947  O   PHE B 304     8237   8047   8855     24    -29    147       O  
ATOM   4948  CB  PHE B 304      61.333  46.364  13.058  1.00 56.55           C  
ANISOU 4948  CB  PHE B 304     7090   6875   7519     76    -54    158       C  
ATOM   4949  CG  PHE B 304      60.358  45.230  13.140  1.00 55.39           C  
ANISOU 4949  CG  PHE B 304     6991   6735   7319     94    -75    174       C  
ATOM   4950  CD1 PHE B 304      60.766  43.987  13.584  1.00 51.62           C  
ANISOU 4950  CD1 PHE B 304     6539   6274   6800    120   -110    140       C  
ATOM   4951  CD2 PHE B 304      59.030  45.410  12.785  1.00 57.33           C  
ANISOU 4951  CD2 PHE B 304     7257   6969   7555     83    -67    224       C  
ATOM   4952  CE1 PHE B 304      59.873  42.939  13.664  1.00 54.97           C  
ANISOU 4952  CE1 PHE B 304     7013   6702   7172    128   -138    160       C  
ATOM   4953  CE2 PHE B 304      58.128  44.365  12.867  1.00 57.16           C  
ANISOU 4953  CE2 PHE B 304     7276   6957   7484     92    -88    242       C  
ATOM   4954  CZ  PHE B 304      58.551  43.127  13.303  1.00 55.26           C  
ANISOU 4954  CZ  PHE B 304     7065   6732   7201    111   -124    214       C  
ATOM   4955  N   TYR B 305      63.432  48.054  15.120  1.00 61.63           N  
ANISOU 4955  N   TYR B 305     7665   7482   8269     78    -71     57       N  
ATOM   4956  CA  TYR B 305      64.589  48.929  15.234  1.00 63.64           C  
ANISOU 4956  CA  TYR B 305     7874   7731   8574     59    -66     32       C  
ATOM   4957  C   TYR B 305      65.872  48.144  15.004  1.00 66.90           C  
ANISOU 4957  C   TYR B 305     8257   8188   8975     69    -68    -15       C  
ATOM   4958  O   TYR B 305      65.976  46.972  15.384  1.00 67.91           O  
ANISOU 4958  O   TYR B 305     8407   8330   9065    107    -94    -51       O  
ATOM   4959  CB  TYR B 305      64.661  49.579  16.616  1.00 62.76           C  
ANISOU 4959  CB  TYR B 305     7767   7579   8502     78    -93      0       C  
ATOM   4960  CG  TYR B 305      63.449  50.388  17.018  1.00 59.35           C  
ANISOU 4960  CG  TYR B 305     7359   7109   8081     79    -99     31       C  
ATOM   4961  CD1 TYR B 305      63.429  51.768  16.866  1.00 54.78           C  
ANISOU 4961  CD1 TYR B 305     6766   6498   7549     54   -100     53       C  
ATOM   4962  CD2 TYR B 305      62.339  49.774  17.589  1.00 57.39           C  
ANISOU 4962  CD2 TYR B 305     7150   6862   7795    107   -109     35       C  
ATOM   4963  CE1 TYR B 305      62.334  52.507  17.250  1.00 57.34           C  
ANISOU 4963  CE1 TYR B 305     7114   6791   7882     66   -114     72       C  
ATOM   4964  CE2 TYR B 305      61.239  50.505  17.971  1.00 56.88           C  
ANISOU 4964  CE2 TYR B 305     7099   6775   7737    114   -114     55       C  
ATOM   4965  CZ  TYR B 305      61.240  51.869  17.802  1.00 63.16           C  
ANISOU 4965  CZ  TYR B 305     7880   7539   8581     98   -118     69       C  
ATOM   4966  OH  TYR B 305      60.137  52.598  18.184  1.00 75.71           O  
ANISOU 4966  OH  TYR B 305     9482   9108  10175    115   -131     80       O  
ATOM   4967  N   LYS B 306      66.864  48.818  14.421  1.00 64.00           N  
ANISOU 4967  N   LYS B 306     7837   7841   8639     34    -46    -18       N  
ATOM   4968  CA  LYS B 306      68.187  48.230  14.276  1.00 70.88           C  
ANISOU 4968  CA  LYS B 306     8665   8762   9506     45    -47    -74       C  
ATOM   4969  C   LYS B 306      68.988  48.398  15.561  1.00 68.80           C  
ANISOU 4969  C   LYS B 306     8385   8473   9281     69    -80   -137       C  
ATOM   4970  O   LYS B 306      68.968  49.460  16.195  1.00 62.53           O  
ANISOU 4970  O   LYS B 306     7587   7636   8536     51    -87   -129       O  
ATOM   4971  CB  LYS B 306      68.951  48.866  13.116  1.00 76.04           C  
ANISOU 4971  CB  LYS B 306     9261   9461  10172    -10     -5    -53       C  
ATOM   4972  CG  LYS B 306      68.898  48.071  11.836  1.00 83.07           C  
ANISOU 4972  CG  LYS B 306    10147  10408  11007    -11     20    -35       C  
ATOM   4973  CD  LYS B 306      69.961  48.537  10.853  1.00 89.15           C  
ANISOU 4973  CD  LYS B 306    10849  11240  11782    -61     61    -35       C  
ATOM   4974  CE  LYS B 306      71.357  48.370  11.435  1.00 87.78           C  
ANISOU 4974  CE  LYS B 306    10613  11107  11631    -46     48   -114       C  
ATOM   4975  NZ  LYS B 306      71.637  46.951  11.798  1.00 86.86           N  
ANISOU 4975  NZ  LYS B 306    10509  11018  11476     29     11   -182       N  
ATOM   4976  N   GLU B 307      69.708  47.342  15.931  1.00 63.42           N  
ANISOU 4976  N   GLU B 307     7702   7819   8578    112   -108   -204       N  
ATOM   4977  CA  GLU B 307      70.496  47.333  17.150  1.00 65.42           C  
ANISOU 4977  CA  GLU B 307     7948   8046   8864    143   -147   -272       C  
ATOM   4978  C   GLU B 307      71.740  46.491  16.912  1.00 74.31           C  
ANISOU 4978  C   GLU B 307     9032   9228   9975    170   -162   -345       C  
ATOM   4979  O   GLU B 307      71.789  45.653  16.006  1.00 75.27           O  
ANISOU 4979  O   GLU B 307     9149   9402  10048    182   -155   -348       O  
ATOM   4980  CB  GLU B 307      69.677  46.798  18.338  1.00 66.82           C  
ANISOU 4980  CB  GLU B 307     8197   8170   9020    185   -189   -284       C  
ATOM   4981  CG  GLU B 307      70.331  46.920  19.725  1.00 70.87           C  
ANISOU 4981  CG  GLU B 307     8718   8641   9569    216   -232   -348       C  
ATOM   4982  CD  GLU B 307      70.682  48.350  20.104  1.00 76.41           C  
ANISOU 4982  CD  GLU B 307     9382   9310  10341    188   -221   -338       C  
ATOM   4983  OE1 GLU B 307      71.797  48.798  19.763  1.00 80.84           O  
ANISOU 4983  OE1 GLU B 307     9879   9896  10940    167   -211   -363       O  
ATOM   4984  OE2 GLU B 307      69.845  49.029  20.740  1.00 78.80           O  
ANISOU 4984  OE2 GLU B 307     9717   9564  10658    187   -226   -306       O  
ATOM   4985  N   ASN B 308      72.759  46.747  17.723  1.00 82.49           N  
ANISOU 4985  N   ASN B 308    10036  10253  11055    185   -187   -409       N  
ATOM   4986  CA  ASN B 308      73.978  45.955  17.706  1.00 84.21           C  
ANISOU 4986  CA  ASN B 308    10213  10520  11263    221   -213   -495       C  
ATOM   4987  C   ASN B 308      74.372  45.629  19.140  1.00 78.32           C  
ANISOU 4987  C   ASN B 308     9502   9719  10538    272   -276   -567       C  
ATOM   4988  O   ASN B 308      74.371  44.465  19.555  1.00 69.54           O  
ANISOU 4988  O   ASN B 308     8440   8600   9383    326   -327   -617       O  
ATOM   4989  CB  ASN B 308      75.093  46.712  16.985  1.00 90.85           C  
ANISOU 4989  CB  ASN B 308    10955  11422  12141    175   -173   -506       C  
ATOM   4990  CG  ASN B 308      76.395  45.952  16.973  1.00102.30           C  
ANISOU 4990  CG  ASN B 308    12350  12934  13585    216   -199   -606       C  
ATOM   4991  OD1 ASN B 308      77.259  46.165  17.824  1.00112.40           O  
ANISOU 4991  OD1 ASN B 308    13601  14195  14909    234   -230   -670       O  
ATOM   4992  ND2 ASN B 308      76.545  45.052  16.006  1.00103.96           N  
ANISOU 4992  ND2 ASN B 308    12544  13218  13738    238   -191   -623       N  
ATOM   4993  N   SER B 309      74.693  46.669  19.904  1.00 78.58           N  
ANISOU 4993  N   SER B 309     9514   9707  10634    254   -277   -569       N  
ATOM   4994  CA  SER B 309      75.003  46.517  21.317  1.00 74.46           C  
ANISOU 4994  CA  SER B 309     9032   9123  10138    299   -335   -631       C  
ATOM   4995  C   SER B 309      74.679  47.829  22.008  1.00 73.60           C  
ANISOU 4995  C   SER B 309     8927   8952  10087    271   -327   -590       C  
ATOM   4996  O   SER B 309      75.187  48.882  21.609  1.00 78.01           O  
ANISOU 4996  O   SER B 309     9422   9523  10695    224   -298   -568       O  
ATOM   4997  CB  SER B 309      76.469  46.140  21.527  1.00 78.28           C  
ANISOU 4997  CB  SER B 309     9461   9637  10645    331   -369   -730       C  
ATOM   4998  OG  SER B 309      76.720  45.838  22.891  1.00 84.83           O  
ANISOU 4998  OG  SER B 309    10342  10399  11492    382   -433   -793       O  
ATOM   4999  N   TYR B 310      73.818  47.769  23.018  1.00 69.87           N  
ANISOU 4999  N   TYR B 310     8530   8414   9603    297   -355   -579       N  
ATOM   5000  CA  TYR B 310      73.426  48.942  23.784  1.00 70.23           C  
ANISOU 5000  CA  TYR B 310     8588   8399   9697    286   -357   -548       C  
ATOM   5001  C   TYR B 310      73.623  48.642  25.259  1.00 77.29           C  
ANISOU 5001  C   TYR B 310     9536   9231  10601    339   -415   -609       C  
ATOM   5002  O   TYR B 310      73.233  47.571  25.733  1.00 76.91           O  
ANISOU 5002  O   TYR B 310     9551   9172  10498    375   -445   -635       O  
ATOM   5003  CB  TYR B 310      71.973  49.336  23.513  1.00 62.96           C  
ANISOU 5003  CB  TYR B 310     7706   7467   8749    263   -327   -466       C  
ATOM   5004  CG  TYR B 310      71.364  50.228  24.576  1.00 62.04           C  
ANISOU 5004  CG  TYR B 310     7625   7285   8661    276   -346   -450       C  
ATOM   5005  CD1 TYR B 310      71.562  51.603  24.556  1.00 59.48           C  
ANISOU 5005  CD1 TYR B 310     7268   6934   8398    248   -342   -423       C  
ATOM   5006  CD2 TYR B 310      70.579  49.696  25.594  1.00 68.50           C  
ANISOU 5006  CD2 TYR B 310     8514   8070   9442    315   -372   -462       C  
ATOM   5007  CE1 TYR B 310      71.001  52.424  25.523  1.00 59.45           C  
ANISOU 5007  CE1 TYR B 310     7298   6872   8419    269   -367   -413       C  
ATOM   5008  CE2 TYR B 310      70.013  50.510  26.565  1.00 71.10           C  
ANISOU 5008  CE2 TYR B 310     8873   8350   9793    333   -389   -453       C  
ATOM   5009  CZ  TYR B 310      70.229  51.876  26.525  1.00 63.22           C  
ANISOU 5009  CZ  TYR B 310     7839   7325   8858    314   -388   -431       C  
ATOM   5010  OH  TYR B 310      69.667  52.691  27.488  1.00 58.72           O  
ANISOU 5010  OH  TYR B 310     7299   6705   8306    341   -412   -426       O  
ATOM   5011  N   THR B 311      74.233  49.580  25.976  1.00 82.98           N  
ANISOU 5011  N   THR B 311    10235   9906  11387    342   -435   -630       N  
ATOM   5012  CA  THR B 311      74.380  49.486  27.423  1.00 81.04           C  
ANISOU 5012  CA  THR B 311    10044   9592  11157    393   -490   -683       C  
ATOM   5013  C   THR B 311      73.889  50.790  28.030  1.00 74.59           C  
ANISOU 5013  C   THR B 311     9236   8720  10383    385   -492   -642       C  
ATOM   5014  O   THR B 311      74.297  51.872  27.600  1.00 76.51           O  
ANISOU 5014  O   THR B 311     9425   8965  10683    348   -477   -615       O  
ATOM   5015  CB  THR B 311      75.835  49.210  27.839  1.00 81.90           C  
ANISOU 5015  CB  THR B 311    10120   9693  11307    421   -533   -772       C  
ATOM   5016  OG1 THR B 311      76.704  50.168  27.224  1.00 88.68           O  
ANISOU 5016  OG1 THR B 311    10889  10577  12229    379   -510   -764       O  
ATOM   5017  CG2 THR B 311      76.263  47.801  27.424  1.00 78.87           C  
ANISOU 5017  CG2 THR B 311     9741   9355  10870    447   -550   -828       C  
ATOM   5018  N   THR B 312      73.014  50.685  29.024  1.00 73.39           N  
ANISOU 5018  N   THR B 312     9156   8525  10204    419   -512   -639       N  
ATOM   5019  CA  THR B 312      72.444  51.866  29.651  1.00 75.40           C  
ANISOU 5019  CA  THR B 312     9425   8732  10491    425   -519   -607       C  
ATOM   5020  C   THR B 312      73.479  52.595  30.499  1.00 76.54           C  
ANISOU 5020  C   THR B 312     9555   8817  10708    449   -566   -654       C  
ATOM   5021  O   THR B 312      74.491  52.032  30.925  1.00 76.20           O  
ANISOU 5021  O   THR B 312     9509   8759  10683    474   -599   -722       O  
ATOM   5022  CB  THR B 312      71.261  51.487  30.543  1.00 79.82           C  
ANISOU 5022  CB  THR B 312    10061   9273  10995    458   -528   -599       C  
ATOM   5023  OG1 THR B 312      70.614  52.678  31.011  1.00 84.31           O  
ANISOU 5023  OG1 THR B 312    10636   9808  11589    468   -532   -567       O  
ATOM   5024  CG2 THR B 312      71.735  50.681  31.741  1.00 79.46           C  
ANISOU 5024  CG2 THR B 312    10073   9186  10933    506   -578   -670       C  
ATOM   5025  N   THR B 313      73.215  53.875  30.734  1.00 82.02           N  
ANISOU 5025  N   THR B 313    10243   9475  11448    443   -575   -619       N  
ATOM   5026  CA  THR B 313      74.008  54.636  31.684  1.00 85.98           C  
ANISOU 5026  CA  THR B 313    10745   9908  12016    472   -628   -658       C  
ATOM   5027  C   THR B 313      73.280  54.777  33.011  1.00 87.61           C  
ANISOU 5027  C   THR B 313    11024  10058  12204    532   -663   -673       C  
ATOM   5028  O   THR B 313      73.828  55.358  33.951  1.00 85.61           O  
ANISOU 5028  O   THR B 313    10785   9740  12001    568   -713   -708       O  
ATOM   5029  CB  THR B 313      74.349  56.023  31.111  1.00 81.48           C  
ANISOU 5029  CB  THR B 313    10123   9326  11511    426   -630   -614       C  
ATOM   5030  OG1 THR B 313      73.147  56.775  30.898  1.00 81.10           O  
ANISOU 5030  OG1 THR B 313    10098   9274  11444    418   -618   -550       O  
ATOM   5031  CG2 THR B 313      75.085  55.884  29.784  1.00 78.89           C  
ANISOU 5031  CG2 THR B 313     9720   9062  11193    359   -590   -597       C  
ATOM   5032  N   ILE B 314      72.076  54.207  33.109  1.00 89.93           N  
ANISOU 5032  N   ILE B 314    11364  10381  12426    542   -637   -650       N  
ATOM   5033  CA  ILE B 314      71.261  54.290  34.314  1.00 88.55           C  
ANISOU 5033  CA  ILE B 314    11254  10171  12219    594   -660   -662       C  
ATOM   5034  C   ILE B 314      71.875  53.423  35.407  1.00 93.21           C  
ANISOU 5034  C   ILE B 314    11897  10721  12797    637   -701   -733       C  
ATOM   5035  O   ILE B 314      72.317  52.294  35.155  1.00 90.19           O  
ANISOU 5035  O   ILE B 314    11523  10361  12385    627   -699   -764       O  
ATOM   5036  CB  ILE B 314      69.814  53.874  33.990  1.00 80.09           C  
ANISOU 5036  CB  ILE B 314    10206   9155  11070    581   -615   -616       C  
ATOM   5037  CG1 ILE B 314      69.195  54.873  33.002  1.00 75.78           C  
ANISOU 5037  CG1 ILE B 314     9615   8635  10542    547   -586   -551       C  
ATOM   5038  CG2 ILE B 314      68.979  53.785  35.256  1.00 78.90           C  
ANISOU 5038  CG2 ILE B 314    10119   8986  10872    629   -633   -634       C  
ATOM   5039  CD1 ILE B 314      67.828  54.487  32.463  1.00 73.60           C  
ANISOU 5039  CD1 ILE B 314     9349   8420  10197    528   -540   -505       C  
ATOM   5040  N   LYS B 315      71.904  53.943  36.634  1.00101.44           N  
ANISOU 5040  N   LYS B 315    12982  11702  13860    688   -746   -764       N  
ATOM   5041  CA  LYS B 315      72.383  53.186  37.792  1.00106.70           C  
ANISOU 5041  CA  LYS B 315    13713  12319  14509    733   -791   -831       C  
ATOM   5042  C   LYS B 315      71.477  53.543  38.969  1.00107.07           C  
ANISOU 5042  C   LYS B 315    13822  12339  14521    779   -807   -832       C  
ATOM   5043  O   LYS B 315      71.621  54.621  39.568  1.00104.68           O  
ANISOU 5043  O   LYS B 315    13518  11986  14270    816   -841   -838       O  
ATOM   5044  CB  LYS B 315      73.850  53.498  38.090  1.00111.35           C  
ANISOU 5044  CB  LYS B 315    14278  12847  15182    753   -842   -887       C  
ATOM   5045  CG  LYS B 315      74.651  52.412  38.845  1.00119.54           C  
ANISOU 5045  CG  LYS B 315    15368  13845  16205    786   -889   -967       C  
ATOM   5046  CD  LYS B 315      73.856  51.660  39.915  1.00122.85           C  
ANISOU 5046  CD  LYS B 315    15888  14246  16545    819   -904   -985       C  
ATOM   5047  CE  LYS B 315      74.757  50.796  40.789  1.00121.08           C  
ANISOU 5047  CE  LYS B 315    15727  13960  16318    857   -968  -1069       C  
ATOM   5048  NZ  LYS B 315      73.980  49.998  41.783  1.00119.30           N  
ANISOU 5048  NZ  LYS B 315    15606  13718  16003    876   -984  -1081       N  
ATOM   5049  N   PRO B 316      70.534  52.664  39.330  1.00112.14           N  
ANISOU 5049  N   PRO B 316    14520  13016  15073    777   -786   -826       N  
ATOM   5050  CA  PRO B 316      69.557  53.036  40.373  1.00116.10           C  
ANISOU 5050  CA  PRO B 316    15070  13513  15531    816   -790   -822       C  
ATOM   5051  C   PRO B 316      70.130  53.120  41.781  1.00122.48           C  
ANISOU 5051  C   PRO B 316    15941  14241  16354    875   -850   -884       C  
ATOM   5052  O   PRO B 316      69.765  54.039  42.524  1.00125.10           O  
ANISOU 5052  O   PRO B 316    16285  14548  16700    921   -869   -886       O  
ATOM   5053  CB  PRO B 316      68.495  51.930  40.263  1.00114.03           C  
ANISOU 5053  CB  PRO B 316    14844  13319  15163    781   -748   -798       C  
ATOM   5054  CG  PRO B 316      68.698  51.322  38.907  1.00112.88           C  
ANISOU 5054  CG  PRO B 316    14653  13219  15018    726   -716   -769       C  
ATOM   5055  CD  PRO B 316      70.169  51.408  38.656  1.00112.34           C  
ANISOU 5055  CD  PRO B 316    14556  13100  15028    733   -752   -810       C  
ATOM   5056  N   LEU B 317      70.988  52.175  42.174  1.00123.92           N  
ANISOU 5056  N   LEU B 317    16169  14383  16532    880   -886   -937       N  
ATOM   5057  CA  LEU B 317      71.595  52.086  43.513  1.00122.50           C  
ANISOU 5057  CA  LEU B 317    16062  14120  16362    936   -950  -1002       C  
ATOM   5058  C   LEU B 317      70.553  52.219  44.630  1.00119.65           C  
ANISOU 5058  C   LEU B 317    15767  13764  15933    967   -947   -998       C  
ATOM   5059  O   LEU B 317      70.513  53.187  45.386  1.00118.48           O  
ANISOU 5059  O   LEU B 317    15625  13574  15816   1020   -974  -1009       O  
ATOM   5060  CB  LEU B 317      72.722  53.111  43.702  1.00116.48           C  
ANISOU 5060  CB  LEU B 317    15262  13282  15711    974   -999  -1032       C  
ATOM   5061  CG  LEU B 317      72.625  54.623  43.487  1.00105.94           C  
ANISOU 5061  CG  LEU B 317    13868  11937  14445    990  -1000   -997       C  
ATOM   5062  CD1 LEU B 317      72.226  55.397  44.726  1.00107.19           C  
ANISOU 5062  CD1 LEU B 317    14078  12046  14603   1057  -1038  -1013       C  
ATOM   5063  CD2 LEU B 317      73.980  55.046  43.051  1.00106.88           C  
ANISOU 5063  CD2 LEU B 317    13934  12011  14665    983  -1035  -1020       C  
ATOM   5064  N   GLU B 318      69.725  51.189  44.744  1.00114.02           N  
ANISOU 5064  N   GLU B 318    15103  13102  15118    933   -918   -984       N  
ATOM   5065  CA  GLU B 318      68.784  51.170  45.852  1.00108.10           C  
ANISOU 5065  CA  GLU B 318    14417  12366  14290    955   -914   -985       C  
ATOM   5066  C   GLU B 318      68.344  49.747  46.129  1.00107.23           C  
ANISOU 5066  C   GLU B 318    14385  12285  14073    910   -908   -988       C  
ATOM   5067  O   GLU B 318      68.318  48.901  45.231  1.00113.08           O  
ANISOU 5067  O   GLU B 318    15113  13064  14788    856   -888   -966       O  
ATOM   5068  CB  GLU B 318      67.566  52.053  45.578  1.00106.98           C  
ANISOU 5068  CB  GLU B 318    14219  12300  14128    957   -861   -933       C  
ATOM   5069  CG  GLU B 318      67.075  52.016  44.150  1.00108.54           C  
ANISOU 5069  CG  GLU B 318    14340  12573  14327    900   -805   -875       C  
ATOM   5070  CD  GLU B 318      65.802  52.809  43.976  1.00107.77           C  
ANISOU 5070  CD  GLU B 318    14198  12549  14201    906   -761   -833       C  
ATOM   5071  OE1 GLU B 318      64.880  52.630  44.797  1.00108.10           O  
ANISOU 5071  OE1 GLU B 318    14278  12633  14163    917   -745   -836       O  
ATOM   5072  OE2 GLU B 318      65.728  53.624  43.034  1.00105.79           O  
ANISOU 5072  OE2 GLU B 318    13875  12316  14006    900   -744   -799       O  
ATOM   5073  N   HIS B 319      67.992  49.505  47.385  1.00103.79           N  
ANISOU 5073  N   HIS B 319    14034  11829  13573    932   -929  -1014       N  
ATOM   5074  CA  HIS B 319      67.504  48.209  47.814  1.00 99.39           C  
ANISOU 5074  CA  HIS B 319    13566  11295  12904    883   -930  -1013       C  
ATOM   5075  C   HIS B 319      66.875  48.295  49.202  1.00101.00           C  
ANISOU 5075  C   HIS B 319    13845  11497  13033    907   -936  -1030       C  
ATOM   5076  O   HIS B 319      65.651  48.359  49.337  1.00100.89           O  
ANISOU 5076  O   HIS B 319    13818  11573  12941    880   -882   -990       O  
ATOM   5077  CB  HIS B 319      68.638  47.188  47.800  1.00 97.26           C  
ANISOU 5077  CB  HIS B 319    13358  10949  12646    875   -995  -1063       C  
ATOM   5078  CG  HIS B 319      68.377  46.019  46.906  1.00 94.08           C  
ANISOU 5078  CG  HIS B 319    12964  10596  12185    804   -980  -1033       C  
ATOM   5079  ND1 HIS B 319      69.386  45.270  46.343  1.00 94.68           N  
ANISOU 5079  ND1 HIS B 319    13052  10630  12293    799  -1028  -1069       N  
ATOM   5080  CD2 HIS B 319      67.216  45.468  46.480  1.00 95.01           C  
ANISOU 5080  CD2 HIS B 319    13080  10804  12214    739   -929   -974       C  
ATOM   5081  CE1 HIS B 319      68.859  44.305  45.610  1.00 93.74           C  
ANISOU 5081  CE1 HIS B 319    12943  10567  12105    736  -1009  -1032       C  
ATOM   5082  NE2 HIS B 319      67.543  44.403  45.677  1.00 94.98           N  
ANISOU 5082  NE2 HIS B 319    13095  10804  12191    696   -949   -971       N  
TER    5083      HIS B 319                                                      
ATOM   5084  N   GLU C   1      73.536  89.693 -34.942  1.00122.34           N  
ATOM   5085  CA  GLU C   1      72.404  90.019 -35.795  1.00121.98           C  
ATOM   5086  C   GLU C   1      71.540  88.776 -36.038  1.00120.44           C  
ATOM   5087  O   GLU C   1      71.966  87.836 -36.711  1.00118.51           O  
ATOM   5088  CB  GLU C   1      72.899  90.591 -37.111  1.00124.11           C  
ATOM   5089  CG  GLU C   1      71.826  91.348 -37.839  1.00127.27           C  
ATOM   5090  CD  GLU C   1      72.360  92.042 -39.048  1.00130.47           C  
ATOM   5091  OE1 GLU C   1      73.553  91.826 -39.366  1.00132.11           O  
ATOM   5092  OE2 GLU C   1      71.623  92.898 -39.588  1.00125.06           O  
ATOM   5093  N   VAL C   2      70.330  88.774 -35.475  1.00120.91           N  
ATOM   5094  CA  VAL C   2      69.393  87.665 -35.628  1.00117.66           C  
ATOM   5095  C   VAL C   2      68.267  88.100 -36.556  1.00118.12           C  
ATOM   5096  O   VAL C   2      68.284  89.219 -37.079  1.00116.43           O  
ATOM   5097  CB  VAL C   2      68.853  87.207 -34.261  1.00109.88           C  
ATOM   5098  CG1 VAL C   2      69.958  86.522 -33.457  1.00105.07           C  
ATOM   5099  CG2 VAL C   2      68.287  88.391 -33.492  1.00105.11           C  
ATOM   5100  N   ARG C   3      67.268  87.245 -36.749  1.00156.45           N  
ANISOU 5100  N   ARG C   3    19314  20109  20022   1013     39    200       N  
ATOM   5101  CA  ARG C   3      66.117  87.609 -37.563  1.00136.73           C  
ANISOU 5101  CA  ARG C   3    16869  17603  17480   1083      3     34       C  
ATOM   5102  C   ARG C   3      64.864  87.628 -36.704  1.00122.29           C  
ANISOU 5102  C   ARG C   3    15034  15767  15662   1045    -32    -66       C  
ATOM   5103  O   ARG C   3      64.612  86.695 -35.933  1.00122.20           O  
ANISOU 5103  O   ARG C   3    14957  15741  15733   1009     -2    -64       O  
ATOM   5104  CB  ARG C   3      65.922  86.667 -38.753  1.00132.14           C  
ANISOU 5104  CB  ARG C   3    16272  16998  16936   1173     50    -52       C  
ATOM   5105  CG  ARG C   3      67.037  86.715 -39.785  1.00131.44           C  
ANISOU 5105  CG  ARG C   3    16199  16918  16823   1231     83     30       C  
ATOM   5106  CD  ARG C   3      66.489  86.404 -41.169  1.00128.60           C  
ANISOU 5106  CD  ARG C   3    15862  16557  16444   1334     95   -104       C  
ATOM   5107  NE  ARG C   3      65.794  85.124 -41.274  1.00127.13           N  
ANISOU 5107  NE  ARG C   3    15629  16333  16340   1351    140   -216       N  
ATOM   5108  CZ  ARG C   3      65.032  84.799 -42.314  1.00129.52           C  
ANISOU 5108  CZ  ARG C   3    15947  16638  16626   1424    141   -365       C  
ATOM   5109  NH1 ARG C   3      64.878  85.670 -43.303  1.00131.66           N  
ANISOU 5109  NH1 ARG C   3    16272  16954  16799   1488    102   -411       N  
ATOM   5110  NH2 ARG C   3      64.415  83.626 -42.368  1.00128.99           N  
ANISOU 5110  NH2 ARG C   3    15836  16533  16642   1433    182   -468       N  
ATOM   5111  N   THR C   4      64.087  88.697 -36.851  1.00112.24           N  
ANISOU 5111  N   THR C   4    13827  14507  14312   1057    -91   -146       N  
ATOM   5112  CA  THR C   4      62.931  88.974 -36.021  1.00100.98           C  
ANISOU 5112  CA  THR C   4    12411  13078  12880   1021   -130   -227       C  
ATOM   5113  C   THR C   4      61.754  89.384 -36.894  1.00 98.91           C  
ANISOU 5113  C   THR C   4    12197  12814  12570   1093   -160   -372       C  
ATOM   5114  O   THR C   4      61.928  89.957 -37.971  1.00 99.10           O  
ANISOU 5114  O   THR C   4    12263  12854  12536   1153   -168   -389       O  
ATOM   5115  CB  THR C   4      63.233  90.088 -35.006  1.00 94.17           C  
ANISOU 5115  CB  THR C   4    11582  12237  11963    939   -170   -151       C  
ATOM   5116  OG1 THR C   4      63.684  91.258 -35.700  1.00 94.70           O  
ANISOU 5116  OG1 THR C   4    11715  12315  11950    963   -196   -125       O  
ATOM   5117  CG2 THR C   4      64.313  89.646 -34.024  1.00 88.74           C  
ANISOU 5117  CG2 THR C   4    10835  11564  11318    857   -143     -7       C  
ATOM   5118  N   ILE C   5      60.549  89.073 -36.416  1.00 96.59           N  
ANISOU 5118  N   ILE C   5    11891  12508  12301   1087   -176   -468       N  
ATOM   5119  CA  ILE C   5      59.314  89.578 -36.997  1.00 93.04           C  
ANISOU 5119  CA  ILE C   5    11486  12063  11801   1139   -210   -592       C  
ATOM   5120  C   ILE C   5      58.448  90.128 -35.870  1.00 93.80           C  
ANISOU 5120  C   ILE C   5    11601  12155  11883   1087   -247   -613       C  
ATOM   5121  O   ILE C   5      58.629  89.798 -34.696  1.00 93.39           O  
ANISOU 5121  O   ILE C   5    11512  12096  11875   1020   -243   -557       O  
ATOM   5122  CB  ILE C   5      58.543  88.503 -37.791  1.00 91.57           C  
ANISOU 5122  CB  ILE C   5    11264  11865  11662   1201   -190   -709       C  
ATOM   5123  CG1 ILE C   5      58.085  87.377 -36.864  1.00 93.39           C  
ANISOU 5123  CG1 ILE C   5    11427  12063  11994   1163   -171   -727       C  
ATOM   5124  CG2 ILE C   5      59.400  87.959 -38.917  1.00 93.21           C  
ANISOU 5124  CG2 ILE C   5    11458  12078  11880   1255   -149   -696       C  
ATOM   5125  CD1 ILE C   5      57.108  86.417 -37.505  1.00 94.20           C  
ANISOU 5125  CD1 ILE C   5    11498  12148  12146   1215   -161   -856       C  
ATOM   5126  N   LYS C   6      57.516  91.002 -36.242  1.00 92.96           N  
ANISOU 5126  N   LYS C   6    11551  12058  11711   1120   -280   -687       N  
ATOM   5127  CA  LYS C   6      56.582  91.609 -35.301  1.00 87.60           C  
ANISOU 5127  CA  LYS C   6    10900  11373  11011   1083   -311   -715       C  
ATOM   5128  C   LYS C   6      55.257  90.862 -35.352  1.00 81.72           C  
ANISOU 5128  C   LYS C   6    10128  10617  10306   1118   -318   -821       C  
ATOM   5129  O   LYS C   6      54.709  90.632 -36.435  1.00 82.07           O  
ANISOU 5129  O   LYS C   6    10174  10671  10337   1185   -317   -903       O  
ATOM   5130  CB  LYS C   6      56.366  93.087 -35.625  1.00 88.67           C  
ANISOU 5130  CB  LYS C   6    11113  11520  11056   1097   -335   -719       C  
ATOM   5131  CG  LYS C   6      57.555  93.976 -35.292  1.00 92.61           C  
ANISOU 5131  CG  LYS C   6    11643  12023  11520   1046   -336   -613       C  
ATOM   5132  CD  LYS C   6      57.196  95.452 -35.410  1.00 95.18           C  
ANISOU 5132  CD  LYS C   6    12042  12349  11772   1052   -355   -621       C  
ATOM   5133  CE  LYS C   6      58.373  96.344 -35.049  1.00 93.98           C  
ANISOU 5133  CE  LYS C   6    11919  12195  11592    994   -357   -520       C  
ATOM   5134  NZ  LYS C   6      58.160  97.742 -35.512  1.00 95.98           N  
ANISOU 5134  NZ  LYS C   6    12236  12447  11787   1019   -364   -526       N  
ATOM   5135  N   VAL C   7      54.751  90.480 -34.184  1.00 75.24           N  
ANISOU 5135  N   VAL C   7     9277   9780   9531   1073   -326   -818       N  
ATOM   5136  CA  VAL C   7      53.478  89.794 -34.054  1.00 67.92           C  
ANISOU 5136  CA  VAL C   7     8319   8837   8649   1099   -335   -905       C  
ATOM   5137  C   VAL C   7      52.686  90.464 -32.938  1.00 60.54           C  
ANISOU 5137  C   VAL C   7     7415   7899   7690   1063   -364   -900       C  
ATOM   5138  O   VAL C   7      53.155  91.403 -32.301  1.00 69.86           O  
ANISOU 5138  O   VAL C   7     8638   9086   8818   1016   -373   -839       O  
ATOM   5139  CB  VAL C   7      53.646  88.287 -33.778  1.00 66.83           C  
ANISOU 5139  CB  VAL C   7     8089   8678   8626   1092   -304   -903       C  
ATOM   5140  CG1 VAL C   7      54.423  87.625 -34.905  1.00 77.05           C  
ANISOU 5140  CG1 VAL C   7     9359   9971   9945   1130   -268   -911       C  
ATOM   5141  CG2 VAL C   7      54.321  88.067 -32.439  1.00 52.82           C  
ANISOU 5141  CG2 VAL C   7     6270   6904   6896   1019   -292   -799       C  
ATOM   5142  N   PHE C   8      51.463  89.990 -32.728  1.00 53.98           N  
ANISOU 5142  N   PHE C   8     6561   7055   6893   1088   -378   -968       N  
ATOM   5143  CA  PHE C   8      50.595  90.504 -31.680  1.00 53.08           C  
ANISOU 5143  CA  PHE C   8     6472   6936   6762   1064   -403   -966       C  
ATOM   5144  C   PHE C   8      50.172  89.364 -30.766  1.00 57.71           C  
ANISOU 5144  C   PHE C   8     6974   7507   7446   1049   -400   -961       C  
ATOM   5145  O   PHE C   8      49.755  88.301 -31.238  1.00 58.32           O  
ANISOU 5145  O   PHE C   8     6993   7570   7597   1085   -390  -1013       O  
ATOM   5146  CB  PHE C   8      49.355  91.189 -32.258  1.00 50.94           C  
ANISOU 5146  CB  PHE C   8     6256   6666   6431   1116   -425  -1040       C  
ATOM   5147  CG  PHE C   8      49.661  92.391 -33.104  1.00 52.53           C  
ANISOU 5147  CG  PHE C   8     6533   6887   6541   1137   -423  -1037       C  
ATOM   5148  CD1 PHE C   8      49.996  93.595 -32.518  1.00 56.20           C  
ANISOU 5148  CD1 PHE C   8     7061   7348   6944   1097   -425   -985       C  
ATOM   5149  CD2 PHE C   8      49.582  92.323 -34.485  1.00 48.33           C  
ANISOU 5149  CD2 PHE C   8     6004   6377   5984   1197   -418  -1088       C  
ATOM   5150  CE1 PHE C   8      50.270  94.701 -33.292  1.00 57.25           C  
ANISOU 5150  CE1 PHE C   8     7254   7493   7005   1118   -418   -978       C  
ATOM   5151  CE2 PHE C   8      49.853  93.419 -35.258  1.00 48.94           C  
ANISOU 5151  CE2 PHE C   8     6137   6476   5981   1222   -413  -1076       C  
ATOM   5152  CZ  PHE C   8      50.196  94.613 -34.664  1.00 54.11           C  
ANISOU 5152  CZ  PHE C   8     6851   7122   6588   1184   -412  -1018       C  
ATOM   5153  N   THR C   9      50.273  89.587 -29.464  1.00 54.55           N  
ANISOU 5153  N   THR C   9     6563   7113   7048    995   -406   -900       N  
ATOM   5154  CA  THR C   9      49.766  88.649 -28.478  1.00 53.92           C  
ANISOU 5154  CA  THR C   9     6402   7027   7056    985   -405   -885       C  
ATOM   5155  C   THR C   9      48.529  89.245 -27.823  1.00 57.94           C  
ANISOU 5155  C   THR C   9     6952   7533   7530    997   -436   -913       C  
ATOM   5156  O   THR C   9      48.378  90.468 -27.751  1.00 62.82           O  
ANISOU 5156  O   THR C   9     7659   8156   8053    986   -450   -915       O  
ATOM   5157  CB  THR C   9      50.819  88.327 -27.420  1.00 47.47           C  
ANISOU 5157  CB  THR C   9     5526   6236   6276    917   -384   -783       C  
ATOM   5158  OG1 THR C   9      51.237  89.542 -26.785  1.00 52.55           O  
ANISOU 5158  OG1 THR C   9     6239   6904   6824    864   -400   -738       O  
ATOM   5159  CG2 THR C   9      52.020  87.666 -28.068  1.00 41.19           C  
ANISOU 5159  CG2 THR C   9     4685   5441   5524    910   -346   -743       C  
ATOM   5160  N   THR C  10      47.632  88.376 -27.365  1.00 55.33           N  
ANISOU 5160  N   THR C  10     6554   7189   7278   1022   -443   -932       N  
ATOM   5161  CA  THR C  10      46.394  88.841 -26.759  1.00 52.82           C  
ANISOU 5161  CA  THR C  10     6270   6866   6934   1042   -471   -953       C  
ATOM   5162  C   THR C  10      45.829  87.739 -25.874  1.00 57.77           C  
ANISOU 5162  C   THR C  10     6793   7488   7668   1051   -472   -931       C  
ATOM   5163  O   THR C  10      46.187  86.564 -26.002  1.00 60.03           O  
ANISOU 5163  O   THR C  10     6985   7766   8058   1055   -450   -923       O  
ATOM   5164  CB  THR C  10      45.372  89.253 -27.822  1.00 51.65           C  
ANISOU 5164  CB  THR C  10     6183   6703   6741   1102   -488  -1034       C  
ATOM   5165  OG1 THR C  10      44.284  89.944 -27.200  1.00 65.55           O  
ANISOU 5165  OG1 THR C  10     7991   8459   8457   1117   -510  -1037       O  
ATOM   5166  CG2 THR C  10      44.824  88.025 -28.522  1.00 49.75           C  
ANISOU 5166  CG2 THR C  10     5867   6443   6591   1147   -488  -1093       C  
ATOM   5167  N   VAL C  11      44.931  88.134 -24.978  1.00 53.94           N  
ANISOU 5167  N   VAL C  11     6326   7007   7163   1057   -494   -919       N  
ATOM   5168  CA  VAL C  11      44.169  87.185 -24.177  1.00 50.90           C  
ANISOU 5168  CA  VAL C  11     5846   6616   6876   1081   -501   -900       C  
ATOM   5169  C   VAL C  11      42.679  87.261 -24.455  1.00 59.24           C  
ANISOU 5169  C   VAL C  11     6930   7646   7931   1142   -530   -955       C  
ATOM   5170  O   VAL C  11      41.927  86.405 -23.963  1.00 69.16           O  
ANISOU 5170  O   VAL C  11     8105   8891   9280   1173   -539   -945       O  
ATOM   5171  CB  VAL C  11      44.427  87.384 -22.665  1.00 48.24           C  
ANISOU 5171  CB  VAL C  11     5479   6319   6531   1037   -501   -817       C  
ATOM   5172  CG1 VAL C  11      45.900  87.243 -22.346  1.00 40.37           C  
ANISOU 5172  CG1 VAL C  11     4442   5358   5537    971   -472   -750       C  
ATOM   5173  CG2 VAL C  11      43.910  88.733 -22.218  1.00 51.12           C  
ANISOU 5173  CG2 VAL C  11     5956   6690   6777   1030   -521   -823       C  
ATOM   5174  N   ASP C  12      42.229  88.249 -25.227  1.00 61.94           N  
ANISOU 5174  N   ASP C  12     7377   7981   8176   1163   -542  -1004       N  
ATOM   5175  CA  ASP C  12      40.818  88.480 -25.474  1.00 62.91           C  
ANISOU 5175  CA  ASP C  12     7534   8087   8282   1218   -567  -1042       C  
ATOM   5176  C   ASP C  12      40.491  88.707 -26.943  1.00 63.46           C  
ANISOU 5176  C   ASP C  12     7651   8152   8309   1252   -571  -1115       C  
ATOM   5177  O   ASP C  12      39.312  88.867 -27.275  1.00 67.88           O  
ANISOU 5177  O   ASP C  12     8233   8705   8852   1297   -591  -1145       O  
ATOM   5178  CB  ASP C  12      40.340  89.686 -24.646  1.00 63.20           C  
ANISOU 5178  CB  ASP C  12     7656   8130   8227   1211   -573  -1007       C  
ATOM   5179  CG  ASP C  12      41.210  90.926 -24.851  1.00 69.32           C  
ANISOU 5179  CG  ASP C  12     8529   8916   8893   1169   -555  -1001       C  
ATOM   5180  OD1 ASP C  12      40.690  92.052 -24.699  1.00 72.13           O  
ANISOU 5180  OD1 ASP C  12     8976   9265   9165   1176   -553  -1000       O  
ATOM   5181  OD2 ASP C  12      42.421  90.782 -25.138  1.00 73.65           O  
ANISOU 5181  OD2 ASP C  12     9061   9477   9445   1128   -540   -993       O  
ATOM   5182  N   ASN C  13      41.493  88.724 -27.824  1.00 61.31           N  
ANISOU 5182  N   ASN C  13     7389   7888   8017   1234   -553  -1139       N  
ATOM   5183  CA  ASN C  13      41.328  89.020 -29.247  1.00 63.97           C  
ANISOU 5183  CA  ASN C  13     7769   8235   8300   1266   -554  -1205       C  
ATOM   5184  C   ASN C  13      40.728  90.406 -29.489  1.00 63.12           C  
ANISOU 5184  C   ASN C  13     7764   8140   8078   1285   -558  -1203       C  
ATOM   5185  O   ASN C  13      40.266  90.706 -30.592  1.00 66.89           O  
ANISOU 5185  O   ASN C  13     8271   8635   8508   1321   -561  -1249       O  
ATOM   5186  CB  ASN C  13      40.493  87.936 -29.939  1.00 62.53           C  
ANISOU 5186  CB  ASN C  13     7522   8044   8194   1307   -569  -1271       C  
ATOM   5187  CG  ASN C  13      40.687  87.917 -31.435  1.00 65.95           C  
ANISOU 5187  CG  ASN C  13     7972   8499   8588   1329   -564  -1342       C  
ATOM   5188  OD1 ASN C  13      41.649  88.473 -31.960  1.00 68.48           O  
ANISOU 5188  OD1 ASN C  13     8333   8837   8848   1315   -545  -1336       O  
ATOM   5189  ND2 ASN C  13      39.765  87.271 -32.135  1.00 73.84           N  
ANISOU 5189  ND2 ASN C  13     8935   9501   9619   1365   -583  -1409       N  
ATOM   5190  N   ILE C  14      40.756  91.270 -28.474  1.00 60.52           N  
ANISOU 5190  N   ILE C  14     7487   7804   7704   1259   -552  -1148       N  
ATOM   5191  CA  ILE C  14      40.340  92.658 -28.596  1.00 59.28           C  
ANISOU 5191  CA  ILE C  14     7429   7650   7445   1270   -542  -1138       C  
ATOM   5192  C   ILE C  14      41.497  93.616 -28.352  1.00 63.02           C  
ANISOU 5192  C   ILE C  14     7961   8125   7857   1219   -519  -1104       C  
ATOM   5193  O   ILE C  14      41.686  94.576 -29.108  1.00 68.79           O  
ANISOU 5193  O   ILE C  14     8756   8862   8517   1228   -502  -1111       O  
ATOM   5194  CB  ILE C  14      39.174  92.972 -27.639  1.00 57.58           C  
ANISOU 5194  CB  ILE C  14     7237   7418   7224   1288   -552  -1110       C  
ATOM   5195  CG1 ILE C  14      37.971  92.093 -27.977  1.00 63.08           C  
ANISOU 5195  CG1 ILE C  14     7876   8114   7979   1341   -577  -1139       C  
ATOM   5196  CG2 ILE C  14      38.830  94.450 -27.689  1.00 51.18           C  
ANISOU 5196  CG2 ILE C  14     6531   6602   6314   1295   -528  -1093       C  
ATOM   5197  CD1 ILE C  14      36.914  92.070 -26.899  1.00 66.28           C  
ANISOU 5197  CD1 ILE C  14     8278   8501   8406   1362   -591  -1099       C  
ATOM   5198  N   ASN C  15      42.289  93.369 -27.307  1.00 59.81           N  
ANISOU 5198  N   ASN C  15     7529   7717   7481   1164   -518  -1062       N  
ATOM   5199  CA  ASN C  15      43.445  94.189 -26.965  1.00 55.18           C  
ANISOU 5199  CA  ASN C  15     6989   7134   6841   1105   -501  -1026       C  
ATOM   5200  C   ASN C  15      44.695  93.493 -27.492  1.00 57.68           C  
ANISOU 5200  C   ASN C  15     7251   7467   7198   1080   -495  -1018       C  
ATOM   5201  O   ASN C  15      45.091  92.445 -26.975  1.00 62.33           O  
ANISOU 5201  O   ASN C  15     7757   8063   7861   1059   -498   -996       O  
ATOM   5202  CB  ASN C  15      43.529  94.387 -25.451  1.00 56.59           C  
ANISOU 5202  CB  ASN C  15     7171   7315   7018   1055   -503   -980       C  
ATOM   5203  CG  ASN C  15      42.394  95.245 -24.897  1.00 55.38           C  
ANISOU 5203  CG  ASN C  15     7087   7141   6814   1078   -500   -982       C  
ATOM   5204  OD1 ASN C  15      41.318  95.332 -25.479  1.00 48.83           O  
ANISOU 5204  OD1 ASN C  15     6276   6299   5979   1138   -502  -1009       O  
ATOM   5205  ND2 ASN C  15      42.640  95.878 -23.755  1.00 66.05           N  
ANISOU 5205  ND2 ASN C  15     8476   8493   8127   1027   -493   -952       N  
ATOM   5206  N   LEU C  16      45.321  94.078 -28.511  1.00 61.94           N  
ANISOU 5206  N   LEU C  16     7833   8013   7689   1086   -482  -1029       N  
ATOM   5207  CA  LEU C  16      46.522  93.525 -29.126  1.00 57.21           C  
ANISOU 5207  CA  LEU C  16     7192   7428   7118   1070   -473  -1017       C  
ATOM   5208  C   LEU C  16      47.767  94.218 -28.587  1.00 52.08           C  
ANISOU 5208  C   LEU C  16     6573   6784   6430   1001   -462   -956       C  
ATOM   5209  O   LEU C  16      47.757  95.425 -28.333  1.00 52.68           O  
ANISOU 5209  O   LEU C  16     6727   6852   6437    980   -457   -944       O  
ATOM   5210  CB  LEU C  16      46.468  93.673 -30.648  1.00 56.96           C  
ANISOU 5210  CB  LEU C  16     7178   7408   7058   1125   -467  -1063       C  
ATOM   5211  CG  LEU C  16      45.244  93.080 -31.346  1.00 60.81           C  
ANISOU 5211  CG  LEU C  16     7639   7899   7568   1190   -479  -1130       C  
ATOM   5212  CD1 LEU C  16      45.401  93.059 -32.872  1.00 59.75           C  
ANISOU 5212  CD1 LEU C  16     7505   7793   7405   1237   -473  -1175       C  
ATOM   5213  CD2 LEU C  16      44.984  91.685 -30.821  1.00 62.40           C  
ANISOU 5213  CD2 LEU C  16     7752   8088   7870   1186   -490  -1142       C  
ATOM   5214  N   HIS C  17      48.843  93.446 -28.432  1.00 51.47           N  
ANISOU 5214  N   HIS C  17     6433   6720   6401    964   -455   -914       N  
ATOM   5215  CA  HIS C  17      50.108  93.930 -27.890  1.00 50.42           C  
ANISOU 5215  CA  HIS C  17     6314   6603   6241    892   -447   -845       C  
ATOM   5216  C   HIS C  17      51.235  93.566 -28.848  1.00 56.87           C  
ANISOU 5216  C   HIS C  17     7106   7429   7074    897   -431   -820       C  
ATOM   5217  O   HIS C  17      51.505  92.381 -29.069  1.00 55.48           O  
ANISOU 5217  O   HIS C  17     6851   7257   6971    911   -420   -815       O  
ATOM   5218  CB  HIS C  17      50.364  93.353 -26.495  1.00 44.64           C  
ANISOU 5218  CB  HIS C  17     5520   5890   5550    832   -450   -791       C  
ATOM   5219  CG  HIS C  17      49.236  93.585 -25.544  1.00 53.92           C  
ANISOU 5219  CG  HIS C  17     6713   7060   6715    836   -465   -812       C  
ATOM   5220  ND1 HIS C  17      48.955  94.829 -25.017  1.00 56.47           N  
ANISOU 5220  ND1 HIS C  17     7122   7374   6958    809   -469   -818       N  
ATOM   5221  CD2 HIS C  17      48.315  92.739 -25.024  1.00 56.68           C  
ANISOU 5221  CD2 HIS C  17     7001   7407   7126    866   -473   -826       C  
ATOM   5222  CE1 HIS C  17      47.907  94.738 -24.217  1.00 57.81           C  
ANISOU 5222  CE1 HIS C  17     7288   7540   7136    824   -479   -834       C  
ATOM   5223  NE2 HIS C  17      47.500  93.481 -24.202  1.00 56.90           N  
ANISOU 5223  NE2 HIS C  17     7082   7431   7106    860   -484   -836       N  
ATOM   5224  N   THR C  18      51.881  94.582 -29.418  1.00 61.15           N  
ANISOU 5224  N   THR C  18     7710   7971   7551    890   -427   -803       N  
ATOM   5225  CA  THR C  18      52.960  94.351 -30.370  1.00 58.28           C  
ANISOU 5225  CA  THR C  18     7329   7619   7195    903   -412   -772       C  
ATOM   5226  C   THR C  18      54.130  93.655 -29.690  1.00 59.82           C  
ANISOU 5226  C   THR C  18     7461   7831   7435    839   -401   -689       C  
ATOM   5227  O   THR C  18      54.611  94.096 -28.641  1.00 62.46           O  
ANISOU 5227  O   THR C  18     7804   8179   7748    764   -408   -632       O  
ATOM   5228  CB  THR C  18      53.427  95.677 -30.977  1.00 57.96           C  
ANISOU 5228  CB  THR C  18     7365   7576   7080    905   -410   -756       C  
ATOM   5229  OG1 THR C  18      52.334  96.315 -31.643  1.00 62.13           O  
ANISOU 5229  OG1 THR C  18     7942   8095   7570    968   -412   -823       O  
ATOM   5230  CG2 THR C  18      54.551  95.439 -31.982  1.00 54.10           C  
ANISOU 5230  CG2 THR C  18     6856   7101   6598    926   -396   -716       C  
ATOM   5231  N   GLN C  19      54.588  92.560 -30.294  1.00 56.76           N  
ANISOU 5231  N   GLN C  19     7008   7447   7111    867   -381   -679       N  
ATOM   5232  CA  GLN C  19      55.744  91.823 -29.811  1.00 61.88           C  
ANISOU 5232  CA  GLN C  19     7588   8113   7809    815   -359   -588       C  
ATOM   5233  C   GLN C  19      56.690  91.544 -30.965  1.00 67.73           C  
ANISOU 5233  C   GLN C  19     8321   8855   8560    850   -335   -561       C  
ATOM   5234  O   GLN C  19      56.251  91.209 -32.070  1.00 71.29           O  
ANISOU 5234  O   GLN C  19     8774   9292   9019    923   -328   -631       O  
ATOM   5235  CB  GLN C  19      55.330  90.503 -29.158  1.00 61.64           C  
ANISOU 5235  CB  GLN C  19     7463   8082   7874    814   -344   -589       C  
ATOM   5236  CG  GLN C  19      54.290  90.665 -28.074  1.00 66.04           C  
ANISOU 5236  CG  GLN C  19     8021   8642   8430    796   -368   -617       C  
ATOM   5237  CD  GLN C  19      54.850  91.329 -26.845  1.00 65.00           C  
ANISOU 5237  CD  GLN C  19     7901   8544   8253    709   -379   -542       C  
ATOM   5238  OE1 GLN C  19      56.064  91.411 -26.673  1.00 64.54           O  
ANISOU 5238  OE1 GLN C  19     7826   8511   8184    655   -366   -457       O  
ATOM   5239  NE2 GLN C  19      53.967  91.817 -25.983  1.00 67.72           N  
ANISOU 5239  NE2 GLN C  19     8274   8891   8567    695   -402   -573       N  
ATOM   5240  N   VAL C  20      57.988  91.657 -30.698  1.00 69.06           N  
ANISOU 5240  N   VAL C  20     8474   9042   8722    796   -322   -456       N  
ATOM   5241  CA  VAL C  20      59.029  91.301 -31.657  1.00 73.32           C  
ANISOU 5241  CA  VAL C  20     8998   9584   9278    824   -294   -406       C  
ATOM   5242  C   VAL C  20      59.669  89.994 -31.189  1.00 64.78           C  
ANISOU 5242  C   VAL C  20     7818   8509   8287    797   -253   -334       C  
ATOM   5243  O   VAL C  20      60.175  89.905 -30.063  1.00 59.86           O  
ANISOU 5243  O   VAL C  20     7155   7913   7678    721   -249   -248       O  
ATOM   5244  CB  VAL C  20      60.059  92.432 -31.824  1.00 75.31           C  
ANISOU 5244  CB  VAL C  20     9305   9850   9459    790   -306   -329       C  
ATOM   5245  CG1 VAL C  20      60.537  92.949 -30.475  1.00 73.60           C  
ANISOU 5245  CG1 VAL C  20     9088   9657   9218    687   -322   -251       C  
ATOM   5246  CG2 VAL C  20      61.231  91.976 -32.677  1.00 77.74           C  
ANISOU 5246  CG2 VAL C  20     9585  10163   9788    816   -274   -255       C  
ATOM   5247  N   VAL C  21      59.624  88.975 -32.047  1.00 62.96           N  
ANISOU 5247  N   VAL C  21     7545   8258   8119    859   -218   -371       N  
ATOM   5248  CA  VAL C  21      60.015  87.622 -31.680  1.00 72.47           C  
ANISOU 5248  CA  VAL C  21     8650   9456   9428    847   -167   -319       C  
ATOM   5249  C   VAL C  21      61.281  87.240 -32.433  1.00 83.10           C  
ANISOU 5249  C   VAL C  21     9978  10802  10794    862   -122   -237       C  
ATOM   5250  O   VAL C  21      61.551  87.741 -33.530  1.00 86.00           O  
ANISOU 5250  O   VAL C  21    10403  11165  11108    912   -129   -261       O  
ATOM   5251  CB  VAL C  21      58.892  86.604 -31.978  1.00 65.64           C  
ANISOU 5251  CB  VAL C  21     7742   8556   8641    903   -153   -431       C  
ATOM   5252  CG1 VAL C  21      57.622  87.016 -31.293  1.00 61.62           C  
ANISOU 5252  CG1 VAL C  21     7254   8047   8110    895   -199   -504       C  
ATOM   5253  CG2 VAL C  21      58.664  86.485 -33.465  1.00 61.99           C  
ANISOU 5253  CG2 VAL C  21     7317   8073   8164    984   -147   -524       C  
ATOM   5254  N   ASP C  22      62.061  86.342 -31.829  1.00 86.86           N  
ANISOU 5254  N   ASP C  22    10367  11286  11348    822    -72   -131       N  
ATOM   5255  CA  ASP C  22      63.262  85.804 -32.455  1.00 84.86           C  
ANISOU 5255  CA  ASP C  22    10085  11029  11130    837    -16    -39       C  
ATOM   5256  C   ASP C  22      62.897  84.531 -33.206  1.00 84.90           C  
ANISOU 5256  C   ASP C  22    10040  10987  11230    905     39   -113       C  
ATOM   5257  O   ASP C  22      62.329  83.600 -32.623  1.00 85.38           O  
ANISOU 5257  O   ASP C  22    10026  11030  11384    898     66   -138       O  
ATOM   5258  CB  ASP C  22      64.339  85.517 -31.406  1.00 84.49           C  
ANISOU 5258  CB  ASP C  22     9966  11020  11117    756     17    130       C  
ATOM   5259  CG  ASP C  22      65.634  85.014 -32.019  1.00 89.93           C  
ANISOU 5259  CG  ASP C  22    10625  11705  11838    770     78    245       C  
ATOM   5260  OD1 ASP C  22      65.860  85.260 -33.223  1.00 94.17           O  
ANISOU 5260  OD1 ASP C  22    11221  12221  12340    835     80    207       O  
ATOM   5261  OD2 ASP C  22      66.424  84.368 -31.300  1.00 92.28           O  
ANISOU 5261  OD2 ASP C  22    10838  12027  12198    719    129    380       O  
ATOM   5262  N   MET C  23      63.232  84.488 -34.496  1.00 85.40           N  
ANISOU 5262  N   MET C  23    10142  11033  11273    972     58   -148       N  
ATOM   5263  CA  MET C  23      62.841  83.356 -35.329  1.00 86.61           C  
ANISOU 5263  CA  MET C  23    10261  11141  11506   1037    108   -241       C  
ATOM   5264  C   MET C  23      63.647  82.098 -35.051  1.00 90.90           C  
ANISOU 5264  C   MET C  23    10709  11660  12170   1023    198   -143       C  
ATOM   5265  O   MET C  23      63.362  81.062 -35.660  1.00 95.70           O  
ANISOU 5265  O   MET C  23    11281  12222  12860   1071    251   -219       O  
ATOM   5266  CB  MET C  23      62.941  83.724 -36.809  1.00 88.45           C  
ANISOU 5266  CB  MET C  23    10564  11373  11671   1115    101   -312       C  
ATOM   5267  CG  MET C  23      62.122  84.948 -37.189  1.00 99.25           C  
ANISOU 5267  CG  MET C  23    12016  12768  12926   1138     22   -404       C  
ATOM   5268  SD  MET C  23      61.068  84.654 -38.630  1.00108.57           S  
ANISOU 5268  SD  MET C  23    13228  13939  14085   1233     14   -592       S  
ATOM   5269  CE  MET C  23      62.242  84.779 -39.977  1.00106.14           C  
ANISOU 5269  CE  MET C  23    12950  13648  13729   1298     49   -544       C  
ATOM   5270  N   SER C  24      64.629  82.153 -34.156  1.00 93.42           N  
ANISOU 5270  N   SER C  24    10984  12010  12503    957    221     22       N  
ATOM   5271  CA  SER C  24      65.425  80.980 -33.830  1.00 96.85           C  
ANISOU 5271  CA  SER C  24    11318  12426  13054    941    315    136       C  
ATOM   5272  C   SER C  24      64.906  80.233 -32.609  1.00 99.11           C  
ANISOU 5272  C   SER C  24    11503  12714  13441    895    338    159       C  
ATOM   5273  O   SER C  24      65.189  79.038 -32.468  1.00105.16           O  
ANISOU 5273  O   SER C  24    12173  13449  14333    901    426    209       O  
ATOM   5274  CB  SER C  24      66.888  81.379 -33.603  1.00 98.45           C  
ANISOU 5274  CB  SER C  24    11516  12671  13220    897    337    326       C  
ATOM   5275  OG  SER C  24      67.017  82.261 -32.499  1.00 99.23           O  
ANISOU 5275  OG  SER C  24    11621  12831  13253    815    278    404       O  
ATOM   5276  N   MET C  25      64.162  80.896 -31.731  1.00 98.18           N  
ANISOU 5276  N   MET C  25    11398  12631  13274    853    267    127       N  
ATOM   5277  CA  MET C  25      63.559  80.260 -30.569  1.00 98.48           C  
ANISOU 5277  CA  MET C  25    11340  12677  13399    817    280    142       C  
ATOM   5278  C   MET C  25      62.095  79.930 -30.841  1.00 97.94           C  
ANISOU 5278  C   MET C  25    11283  12562  13368    868    252    -33       C  
ATOM   5279  O   MET C  25      61.457  80.494 -31.733  1.00 95.55           O  
ANISOU 5279  O   MET C  25    11073  12240  12992    914    201   -164       O  
ATOM   5280  CB  MET C  25      63.669  81.159 -29.334  1.00 97.09           C  
ANISOU 5280  CB  MET C  25    11168  12576  13146    736    223    225       C  
ATOM   5281  CG  MET C  25      65.079  81.622 -29.019  1.00 96.18           C  
ANISOU 5281  CG  MET C  25    11048  12517  12978    675    237    397       C  
ATOM   5282  SD  MET C  25      65.109  82.962 -27.808  1.00 98.87           S  
ANISOU 5282  SD  MET C  25    11429  12942  13195    581    151    449       S  
ATOM   5283  CE  MET C  25      64.339  82.183 -26.393  1.00 97.28           C  
ANISOU 5283  CE  MET C  25    11105  12774  13082    546    167    465       C  
ATOM   5284  N   THR C  26      61.563  79.004 -30.051  1.00 99.60           N  
ANISOU 5284  N   THR C  26    11388  12759  13695    858    286    -26       N  
ATOM   5285  CA  THR C  26      60.160  78.646 -30.170  1.00101.12           C  
ANISOU 5285  CA  THR C  26    11578  12910  13934    900    258   -177       C  
ATOM   5286  C   THR C  26      59.277  79.688 -29.480  1.00 98.71           C  
ANISOU 5286  C   THR C  26    11329  12645  13531    876    164   -222       C  
ATOM   5287  O   THR C  26      59.746  80.531 -28.708  1.00102.34           O  
ANISOU 5287  O   THR C  26    11810  13165  13908    819    130   -131       O  
ATOM   5288  CB  THR C  26      59.910  77.259 -29.577  1.00102.39           C  
ANISOU 5288  CB  THR C  26    11598  13037  14269    904    332   -147       C  
ATOM   5289  OG1 THR C  26      59.993  77.325 -28.146  1.00101.19           O  
ANISOU 5289  OG1 THR C  26    11367  12946  14135    846    326    -28       O  
ATOM   5290  CG2 THR C  26      60.941  76.270 -30.088  1.00103.63           C  
ANISOU 5290  CG2 THR C  26    11691  13156  14526    918    439    -72       C  
ATOM   5291  N   TYR C  27      57.972  79.622 -29.775  1.00 87.12           N  
ANISOU 5291  N   TYR C  27     9887  11143  12072    920    123   -365       N  
ATOM   5292  CA  TYR C  27      57.022  80.522 -29.128  1.00 77.45           C  
ANISOU 5292  CA  TYR C  27     8713   9948  10766    905     43   -410       C  
ATOM   5293  C   TYR C  27      56.951  80.272 -27.628  1.00 73.27           C  
ANISOU 5293  C   TYR C  27     8090   9459  10289    856     48   -311       C  
ATOM   5294  O   TYR C  27      56.749  81.214 -26.851  1.00 69.50           O  
ANISOU 5294  O   TYR C  27     7655   9031   9720    817     -7   -286       O  
ATOM   5295  CB  TYR C  27      55.632  80.385 -29.764  1.00 75.48           C  
ANISOU 5295  CB  TYR C  27     8498   9655  10526    964      6   -571       C  
ATOM   5296  CG  TYR C  27      55.517  81.084 -31.105  1.00 74.43           C  
ANISOU 5296  CG  TYR C  27     8477   9512  10290   1006    -26   -671       C  
ATOM   5297  CD1 TYR C  27      55.553  80.367 -32.292  1.00 74.88           C  
ANISOU 5297  CD1 TYR C  27     8531   9527  10392   1056     11   -752       C  
ATOM   5298  CD2 TYR C  27      55.390  82.466 -31.182  1.00 75.59           C  
ANISOU 5298  CD2 TYR C  27     8730   9696  10296    997    -89   -683       C  
ATOM   5299  CE1 TYR C  27      55.459  81.006 -33.517  1.00 73.54           C  
ANISOU 5299  CE1 TYR C  27     8455   9364  10124   1097    -18   -839       C  
ATOM   5300  CE2 TYR C  27      55.298  83.114 -32.403  1.00 72.34           C  
ANISOU 5300  CE2 TYR C  27     8409   9284   9794   1039   -114   -763       C  
ATOM   5301  CZ  TYR C  27      55.332  82.378 -33.566  1.00 70.77           C  
ANISOU 5301  CZ  TYR C  27     8199   9055   9635   1091    -80   -838       C  
ATOM   5302  OH  TYR C  27      55.244  83.013 -34.784  1.00 68.01           O  
ANISOU 5302  OH  TYR C  27     7930   8719   9191   1136   -103   -913       O  
ATOM   5303  N   GLY C  28      57.118  79.019 -27.203  1.00 77.81           N  
ANISOU 5303  N   GLY C  28     8535  10018  11011    857    118   -252       N  
ATOM   5304  CA  GLY C  28      57.106  78.722 -25.780  1.00 74.82           C  
ANISOU 5304  CA  GLY C  28     8051   9690  10687    815    130   -144       C  
ATOM   5305  C   GLY C  28      58.274  79.342 -25.038  1.00 75.38           C  
ANISOU 5305  C   GLY C  28     8116   9842  10682    741    134      5       C  
ATOM   5306  O   GLY C  28      58.136  79.770 -23.889  1.00 72.12           O  
ANISOU 5306  O   GLY C  28     7677   9496  10229    695    102     64       O  
ATOM   5307  N   GLN C  29      59.439  79.407 -25.682  1.00 82.82           N  
ANISOU 5307  N   GLN C  29     9083  10785  11600    727    172     67       N  
ATOM   5308  CA  GLN C  29      60.602  80.009 -25.047  1.00 91.30           C  
ANISOU 5308  CA  GLN C  29    10154  11937  12599    652    173    212       C  
ATOM   5309  C   GLN C  29      60.494  81.523 -24.936  1.00 94.81           C  
ANISOU 5309  C   GLN C  29    10727  12419  12877    617     84    173       C  
ATOM   5310  O   GLN C  29      61.297  82.133 -24.219  1.00 99.17           O  
ANISOU 5310  O   GLN C  29    11278  13043  13358    544     71    282       O  
ATOM   5311  CB  GLN C  29      61.862  79.651 -25.828  1.00 97.92           C  
ANISOU 5311  CB  GLN C  29    10984  12759  13461    654    239    295       C  
ATOM   5312  CG  GLN C  29      62.134  78.170 -25.945  1.00102.08           C  
ANISOU 5312  CG  GLN C  29    11384  13246  14157    683    344    349       C  
ATOM   5313  CD  GLN C  29      63.356  77.891 -26.792  1.00105.57           C  
ANISOU 5313  CD  GLN C  29    11833  13666  14612    691    410    426       C  
ATOM   5314  OE1 GLN C  29      64.216  78.755 -26.962  1.00109.80           O  
ANISOU 5314  OE1 GLN C  29    12439  14242  15038    656    383    493       O  
ATOM   5315  NE2 GLN C  29      63.424  76.696 -27.358  1.00105.75           N  
ANISOU 5315  NE2 GLN C  29    11788  13621  14772    740    499    415       N  
ATOM   5316  N   GLN C  30      59.532  82.140 -25.610  1.00 91.52           N  
ANISOU 5316  N   GLN C  30    10417  11957  12400    664     26     25       N  
ATOM   5317  CA  GLN C  30      59.397  83.591 -25.610  1.00 86.04           C  
ANISOU 5317  CA  GLN C  30     9847  11285  11557    638    -48    -16       C  
ATOM   5318  C   GLN C  30      58.097  84.067 -24.988  1.00 86.06           C  
ANISOU 5318  C   GLN C  30     9882  11291  11526    646   -106   -104       C  
ATOM   5319  O   GLN C  30      58.088  85.093 -24.302  1.00 93.90           O  
ANISOU 5319  O   GLN C  30    10931  12328  12419    595   -152    -89       O  
ATOM   5320  CB  GLN C  30      59.511  84.124 -27.047  1.00 81.19           C  
ANISOU 5320  CB  GLN C  30     9342  10624  10883    688    -63    -98       C  
ATOM   5321  CG  GLN C  30      60.772  83.658 -27.768  1.00 80.89           C  
ANISOU 5321  CG  GLN C  30     9280  10579  10877    692     -5    -14       C  
ATOM   5322  CD  GLN C  30      60.903  84.217 -29.177  1.00 83.33           C  
ANISOU 5322  CD  GLN C  30     9690  10851  11120    746    -21    -89       C  
ATOM   5323  OE1 GLN C  30      61.116  85.415 -29.368  1.00 84.76           O  
ANISOU 5323  OE1 GLN C  30     9964  11052  11191    730    -69    -91       O  
ATOM   5324  NE2 GLN C  30      60.779  83.345 -30.172  1.00 85.28           N  
ANISOU 5324  NE2 GLN C  30     9917  11048  11437    813     23   -150       N  
ATOM   5325  N   PHE C  31      56.996  83.344 -25.205  1.00 81.16           N  
ANISOU 5325  N   PHE C  31     9229  10623  10986    707   -102   -195       N  
ATOM   5326  CA  PHE C  31      55.690  83.719 -24.678  1.00 84.21           C  
ANISOU 5326  CA  PHE C  31     9643  11006  11347    725   -154   -274       C  
ATOM   5327  C   PHE C  31      55.139  82.749 -23.644  1.00 89.43           C  
ANISOU 5327  C   PHE C  31    10178  11683  12119    728   -133   -235       C  
ATOM   5328  O   PHE C  31      54.238  83.124 -22.885  1.00 90.52           O  
ANISOU 5328  O   PHE C  31    10326  11838  12228    729   -175   -262       O  
ATOM   5329  CB  PHE C  31      54.675  83.844 -25.822  1.00 80.36           C  
ANISOU 5329  CB  PHE C  31     9232  10455  10847    799   -181   -419       C  
ATOM   5330  CG  PHE C  31      55.001  84.926 -26.806  1.00 77.71           C  
ANISOU 5330  CG  PHE C  31     9020  10110  10394    807   -208   -464       C  
ATOM   5331  CD1 PHE C  31      55.691  86.055 -26.408  1.00 78.48           C  
ANISOU 5331  CD1 PHE C  31     9184  10250  10386    749   -232   -405       C  
ATOM   5332  CD2 PHE C  31      54.616  84.815 -28.130  1.00 78.20           C  
ANISOU 5332  CD2 PHE C  31     9129  10128  10455    871   -209   -564       C  
ATOM   5333  CE1 PHE C  31      55.987  87.055 -27.310  1.00 78.60           C  
ANISOU 5333  CE1 PHE C  31     9304  10255  10305    760   -254   -440       C  
ATOM   5334  CE2 PHE C  31      54.911  85.812 -29.035  1.00 77.07           C  
ANISOU 5334  CE2 PHE C  31     9090   9987  10208    884   -231   -597       C  
ATOM   5335  CZ  PHE C  31      55.594  86.933 -28.622  1.00 75.57           C  
ANISOU 5335  CZ  PHE C  31     8960   9831   9922    831   -253   -531       C  
ATOM   5336  N   GLY C  32      55.651  81.525 -23.598  1.00 86.71           N  
ANISOU 5336  N   GLY C  32     9711  11331  11903    734    -65   -166       N  
ATOM   5337  CA  GLY C  32      55.033  80.457 -22.857  1.00 80.30           C  
ANISOU 5337  CA  GLY C  32     8769  10518  11225    755    -36   -141       C  
ATOM   5338  C   GLY C  32      54.082  79.708 -23.759  1.00 74.33           C  
ANISOU 5338  C   GLY C  32     8008   9675  10560    831    -28   -263       C  
ATOM   5339  O   GLY C  32      54.214  79.735 -24.987  1.00 73.13           O  
ANISOU 5339  O   GLY C  32     7924   9471  10390    861    -22   -341       O  
ATOM   5340  N   PRO C  33      53.088  79.043 -23.174  1.00 73.64           N  
ANISOU 5340  N   PRO C  33     7839   9574  10568    863    -31   -281       N  
ATOM   5341  CA  PRO C  33      52.087  78.341 -23.996  1.00 75.79           C  
ANISOU 5341  CA  PRO C  33     8105   9764  10928    930    -31   -403       C  
ATOM   5342  C   PRO C  33      51.363  79.322 -24.907  1.00 75.45           C  
ANISOU 5342  C   PRO C  33     8213   9696  10760    957    -99   -534       C  
ATOM   5343  O   PRO C  33      50.744  80.284 -24.448  1.00 78.06           O  
ANISOU 5343  O   PRO C  33     8616  10056  10989    951   -160   -553       O  
ATOM   5344  CB  PRO C  33      51.154  77.706 -22.955  1.00 78.04           C  
ANISOU 5344  CB  PRO C  33     8280  10055  11317    951    -35   -376       C  
ATOM   5345  CG  PRO C  33      51.415  78.464 -21.679  1.00 80.01           C  
ANISOU 5345  CG  PRO C  33     8523  10396  11479    901    -63   -274       C  
ATOM   5346  CD  PRO C  33      52.847  78.884 -21.732  1.00 73.36           C  
ANISOU 5346  CD  PRO C  33     7706   9601  10567    839    -34   -188       C  
ATOM   5347  N   THR C  34      51.473  79.089 -26.213  1.00 72.32           N  
ANISOU 5347  N   THR C  34     7861   9247  10368    988    -83   -621       N  
ATOM   5348  CA  THR C  34      50.948  80.000 -27.222  1.00 72.78           C  
ANISOU 5348  CA  THR C  34     8054   9293  10306   1015   -138   -735       C  
ATOM   5349  C   THR C  34      50.045  79.250 -28.186  1.00 77.76           C  
ANISOU 5349  C   THR C  34     8675   9863  11008   1071   -137   -862       C  
ATOM   5350  O   THR C  34      50.359  78.133 -28.603  1.00 86.18           O  
ANISOU 5350  O   THR C  34     9664  10886  12195   1085    -79   -874       O  
ATOM   5351  CB  THR C  34      52.083  80.685 -28.005  1.00 73.30           C  
ANISOU 5351  CB  THR C  34     8202   9376  10271    995   -127   -717       C  
ATOM   5352  OG1 THR C  34      52.972  81.336 -27.091  1.00 72.79           O  
ANISOU 5352  OG1 THR C  34     8141   9369  10147    935   -128   -596       O  
ATOM   5353  CG2 THR C  34      51.530  81.708 -28.981  1.00 76.12           C  
ANISOU 5353  CG2 THR C  34     8688   9731  10501   1025   -182   -821       C  
ATOM   5354  N   TYR C  35      48.928  79.877 -28.544  1.00 80.31           N  
ANISOU 5354  N   TYR C  35     9074  10183  11257   1101   -200   -955       N  
ATOM   5355  CA  TYR C  35      47.954  79.307 -29.461  1.00 81.11           C  
ANISOU 5355  CA  TYR C  35     9174  10240  11405   1149   -212  -1081       C  
ATOM   5356  C   TYR C  35      47.721  80.276 -30.611  1.00 82.89           C  
ANISOU 5356  C   TYR C  35     9524  10484  11489   1171   -253  -1169       C  
ATOM   5357  O   TYR C  35      47.600  81.485 -30.398  1.00 87.11           O  
ANISOU 5357  O   TYR C  35    10144  11057  11898   1161   -294  -1147       O  
ATOM   5358  CB  TYR C  35      46.632  79.012 -28.753  1.00 82.59           C  
ANISOU 5358  CB  TYR C  35     9315  10414  11653   1171   -248  -1100       C  
ATOM   5359  CG  TYR C  35      46.749  78.053 -27.589  1.00 91.57           C  
ANISOU 5359  CG  TYR C  35    10317  11540  12937   1159   -209  -1008       C  
ATOM   5360  CD1 TYR C  35      46.563  76.687 -27.766  1.00 92.83           C  
ANISOU 5360  CD1 TYR C  35    10365  11642  13263   1179   -162  -1037       C  
ATOM   5361  CD2 TYR C  35      47.033  78.516 -26.308  1.00 98.11           C  
ANISOU 5361  CD2 TYR C  35    11123  12418  13738   1127   -216   -893       C  
ATOM   5362  CE1 TYR C  35      46.660  75.807 -26.700  1.00 95.33           C  
ANISOU 5362  CE1 TYR C  35    10546  11951  13724   1173   -120   -943       C  
ATOM   5363  CE2 TYR C  35      47.132  77.643 -25.236  1.00 99.65           C  
ANISOU 5363  CE2 TYR C  35    11183  12616  14065   1119   -178   -800       C  
ATOM   5364  CZ  TYR C  35      46.945  76.290 -25.437  1.00 98.61           C  
ANISOU 5364  CZ  TYR C  35    10936  12427  14105   1145   -129   -821       C  
ATOM   5365  OH  TYR C  35      47.044  75.420 -24.372  1.00 98.29           O  
ANISOU 5365  OH  TYR C  35    10749  12392  14204   1142    -85   -719       O  
ATOM   5366  N   LEU C  36      47.671  79.745 -31.830  1.00 84.23           N  
ANISOU 5366  N   LEU C  36     9697  10627  11678   1200   -236  -1267       N  
ATOM   5367  CA  LEU C  36      47.391  80.533 -33.030  1.00 85.56           C  
ANISOU 5367  CA  LEU C  36     9966  10823  11720   1228   -270  -1355       C  
ATOM   5368  C   LEU C  36      46.156  79.941 -33.695  1.00 97.81           C  
ANISOU 5368  C   LEU C  36    11498  12352  13312   1264   -294  -1479       C  
ATOM   5369  O   LEU C  36      46.231  78.876 -34.316  1.00102.99           O  
ANISOU 5369  O   LEU C  36    12100  12971  14061   1276   -258  -1547       O  
ATOM   5370  CB  LEU C  36      48.580  80.545 -33.987  1.00 77.36           C  
ANISOU 5370  CB  LEU C  36     8956   9792  10645   1230   -230  -1357       C  
ATOM   5371  CG  LEU C  36      48.308  81.197 -35.350  1.00 76.05           C  
ANISOU 5371  CG  LEU C  36     8874   9660  10361   1267   -258  -1452       C  
ATOM   5372  CD1 LEU C  36      47.851  82.635 -35.193  1.00 75.20           C  
ANISOU 5372  CD1 LEU C  36     8855   9600  10117   1269   -313  -1431       C  
ATOM   5373  CD2 LEU C  36      49.526  81.136 -36.257  1.00 78.30           C  
ANISOU 5373  CD2 LEU C  36     9179   9953  10617   1276   -214  -1445       C  
ATOM   5374  N   ASP C  37      45.024  80.630 -33.552  1.00101.52           N  
ANISOU 5374  N   ASP C  37    12014  12846  13714   1280   -353  -1505       N  
ATOM   5375  CA  ASP C  37      43.754  80.190 -34.128  1.00102.82           C  
ANISOU 5375  CA  ASP C  37    12164  13001  13903   1310   -385  -1612       C  
ATOM   5376  C   ASP C  37      43.373  78.803 -33.608  1.00104.71           C  
ANISOU 5376  C   ASP C  37    12288  13179  14318   1308   -362  -1625       C  
ATOM   5377  O   ASP C  37      43.006  77.905 -34.366  1.00105.79           O  
ANISOU 5377  O   ASP C  37    12384  13286  14525   1321   -351  -1725       O  
ATOM   5378  CB  ASP C  37      43.808  80.225 -35.659  1.00100.03           C  
ANISOU 5378  CB  ASP C  37    11854  12674  13480   1334   -385  -1720       C  
ATOM   5379  CG  ASP C  37      44.054  81.629 -36.206  1.00101.97           C  
ANISOU 5379  CG  ASP C  37    12203  12983  13557   1345   -409  -1703       C  
ATOM   5380  OD1 ASP C  37      43.461  82.593 -35.676  1.00103.37           O  
ANISOU 5380  OD1 ASP C  37    12429  13186  13662   1346   -446  -1658       O  
ATOM   5381  OD2 ASP C  37      44.853  81.772 -37.156  1.00101.45           O  
ANISOU 5381  OD2 ASP C  37    12167  12942  13437   1355   -386  -1730       O  
ATOM   5382  N   GLY C  38      43.493  78.626 -32.291  1.00106.36           N  
ANISOU 5382  N   GLY C  38    12440  13370  14600   1290   -351  -1522       N  
ATOM   5383  CA  GLY C  38      43.127  77.390 -31.636  1.00108.35           C  
ANISOU 5383  CA  GLY C  38    12573  13569  15027   1292   -326  -1511       C  
ATOM   5384  C   GLY C  38      44.199  76.319 -31.621  1.00110.00           C  
ANISOU 5384  C   GLY C  38    12694  13735  15365   1275   -247  -1484       C  
ATOM   5385  O   GLY C  38      44.159  75.436 -30.754  1.00111.47           O  
ANISOU 5385  O   GLY C  38    12771  13885  15698   1270   -214  -1426       O  
ATOM   5386  N   ALA C  39      45.156  76.369 -32.546  1.00108.83           N  
ANISOU 5386  N   ALA C  39    12588  13592  15169   1268   -210  -1515       N  
ATOM   5387  CA  ALA C  39      46.196  75.356 -32.640  1.00106.40           C  
ANISOU 5387  CA  ALA C  39    12204  13241  14982   1256   -126  -1489       C  
ATOM   5388  C   ALA C  39      47.347  75.685 -31.699  1.00107.26           C  
ANISOU 5388  C   ALA C  39    12294  13377  15083   1223    -90  -1336       C  
ATOM   5389  O   ALA C  39      47.794  76.833 -31.623  1.00110.61           O  
ANISOU 5389  O   ALA C  39    12806  13856  15366   1208   -121  -1286       O  
ATOM   5390  CB  ALA C  39      46.713  75.247 -34.076  1.00105.89           C  
ANISOU 5390  CB  ALA C  39    12193  13172  14867   1268   -100  -1588       C  
ATOM   5391  N   ASP C  40      47.828  74.667 -30.989  1.00106.19           N  
ANISOU 5391  N   ASP C  40    12040  13205  15103   1210    -22  -1258       N  
ATOM   5392  CA  ASP C  40      48.942  74.843 -30.065  1.00104.09           C  
ANISOU 5392  CA  ASP C  40    11736  12973  14840   1174     19  -1104       C  
ATOM   5393  C   ASP C  40      50.237  75.037 -30.851  1.00106.49           C  
ANISOU 5393  C   ASP C  40    12091  13285  15085   1162     65  -1084       C  
ATOM   5394  O   ASP C  40      50.679  74.135 -31.569  1.00109.92           O  
ANISOU 5394  O   ASP C  40    12487  13669  15609   1174    132  -1124       O  
ATOM   5395  CB  ASP C  40      49.044  73.636 -29.135  1.00102.90           C  
ANISOU 5395  CB  ASP C  40    11429  12787  14882   1169     86  -1020       C  
ATOM   5396  CG  ASP C  40      49.920  73.900 -27.923  1.00106.40           C  
ANISOU 5396  CG  ASP C  40    11819  13286  15320   1130    112   -849       C  
ATOM   5397  OD1 ASP C  40      50.768  74.814 -27.988  1.00108.26           O  
ANISOU 5397  OD1 ASP C  40    12135  13575  15424   1101     99   -796       O  
ATOM   5398  OD2 ASP C  40      49.764  73.192 -26.904  1.00106.58           O  
ANISOU 5398  OD2 ASP C  40    11716  13308  15472   1128    144   -764       O  
ATOM   5399  N   VAL C  41      50.845  76.213 -30.713  1.00102.83           N  
ANISOU 5399  N   VAL C  41    11714  12883  14474   1138     31  -1020       N  
ATOM   5400  CA  VAL C  41      52.082  76.544 -31.404  1.00 95.03           C  
ANISOU 5400  CA  VAL C  41    10779  11911  13418   1128     65   -985       C  
ATOM   5401  C   VAL C  41      53.225  76.781 -30.418  1.00 92.58           C  
ANISOU 5401  C   VAL C  41    10431  11644  13103   1079     98   -815       C  
ATOM   5402  O   VAL C  41      54.199  77.448 -30.746  1.00 93.02           O  
ANISOU 5402  O   VAL C  41    10549  11731  13064   1061    102   -762       O  
ATOM   5403  CB  VAL C  41      51.886  77.760 -32.328  1.00 91.43           C  
ANISOU 5403  CB  VAL C  41    10461  11491  12787   1145     -1  -1062       C  
ATOM   5404  CG1 VAL C  41      50.856  77.448 -33.399  1.00 89.10           C  
ANISOU 5404  CG1 VAL C  41    10194  11167  12494   1191    -25  -1224       C  
ATOM   5405  CG2 VAL C  41      51.463  78.979 -31.518  1.00 90.33           C  
ANISOU 5405  CG2 VAL C  41    10382  11404  12535   1123    -72  -1018       C  
ATOM   5406  N   THR C  42      53.115  76.225 -29.210  1.00 92.35           N  
ANISOU 5406  N   THR C  42    10293  11620  13176   1057    122   -725       N  
ATOM   5407  CA  THR C  42      54.128  76.460 -28.186  1.00 98.27           C  
ANISOU 5407  CA  THR C  42    10996  12427  13915   1004    149   -561       C  
ATOM   5408  C   THR C  42      55.488  75.923 -28.615  1.00103.92           C  
ANISOU 5408  C   THR C  42    11675  13130  14677    991    235   -478       C  
ATOM   5409  O   THR C  42      56.515  76.594 -28.457  1.00105.18           O  
ANISOU 5409  O   THR C  42    11873  13342  14750    953    236   -379       O  
ATOM   5410  CB  THR C  42      53.691  75.815 -26.868  1.00100.11           C  
ANISOU 5410  CB  THR C  42    11100  12675  14264    992    166   -482       C  
ATOM   5411  OG1 THR C  42      52.452  76.392 -26.438  1.00100.30           O  
ANISOU 5411  OG1 THR C  42    11165  12712  14234   1006     84   -547       O  
ATOM   5412  CG2 THR C  42      54.748  76.018 -25.790  1.00 98.65           C  
ANISOU 5412  CG2 THR C  42    10855  12564  14064    933    195   -307       C  
ATOM   5413  N   LYS C  43      55.514  74.709 -29.159  1.00106.85           N  
ANISOU 5413  N   LYS C  43    11975  13433  15191   1023    310   -517       N  
ATOM   5414  CA  LYS C  43      56.750  74.008 -29.473  1.00106.07           C  
ANISOU 5414  CA  LYS C  43    11822  13313  15166   1016    410   -428       C  
ATOM   5415  C   LYS C  43      57.223  74.231 -30.910  1.00106.99           C  
ANISOU 5415  C   LYS C  43    12041  13401  15211   1046    419   -511       C  
ATOM   5416  O   LYS C  43      57.962  73.395 -31.441  1.00110.58           O  
ANISOU 5416  O   LYS C  43    12453  13810  15754   1060    510   -485       O  
ATOM   5417  CB  LYS C  43      56.592  72.514 -29.175  1.00106.49           C  
ANISOU 5417  CB  LYS C  43    11727  13303  15430   1032    504   -409       C  
ATOM   5418  CG  LYS C  43      56.285  72.235 -27.705  1.00108.53           C  
ANISOU 5418  CG  LYS C  43    11864  13603  15770   1006    508   -298       C  
ATOM   5419  CD  LYS C  43      56.065  70.755 -27.425  1.00111.64           C  
ANISOU 5419  CD  LYS C  43    12101  13931  16387   1028    604   -277       C  
ATOM   5420  CE  LYS C  43      55.763  70.519 -25.949  1.00111.08           C  
ANISOU 5420  CE  LYS C  43    11900  13914  16392   1008    606   -156       C  
ATOM   5421  NZ  LYS C  43      55.534  69.079 -25.646  1.00111.09           N  
ANISOU 5421  NZ  LYS C  43    11737  13850  16623   1034    705   -126       N  
ATOM   5422  N   ILE C  44      56.802  75.318 -31.559  1.00103.24           N  
ANISOU 5422  N   ILE C  44    11696  12952  14581   1061    332   -606       N  
ATOM   5423  CA  ILE C  44      57.235  75.617 -32.919  1.00 99.46           C  
ANISOU 5423  CA  ILE C  44    11309  12459  14020   1094    334   -679       C  
ATOM   5424  C   ILE C  44      57.855  77.009 -32.953  1.00103.37           C  
ANISOU 5424  C   ILE C  44    11905  13022  14347   1072    276   -615       C  
ATOM   5425  O   ILE C  44      57.683  77.819 -32.040  1.00110.19           O  
ANISOU 5425  O   ILE C  44    12786  13937  15144   1033    219   -557       O  
ATOM   5426  CB  ILE C  44      56.086  75.517 -33.940  1.00 94.58           C  
ANISOU 5426  CB  ILE C  44    10746  11807  13385   1144    293   -873       C  
ATOM   5427  CG1 ILE C  44      55.211  76.767 -33.887  1.00 88.40           C  
ANISOU 5427  CG1 ILE C  44    10056  11074  12456   1145    184   -932       C  
ATOM   5428  CG2 ILE C  44      55.246  74.275 -33.674  1.00 95.31           C  
ANISOU 5428  CG2 ILE C  44    10736  11834  13642   1157    331   -939       C  
ATOM   5429  CD1 ILE C  44      54.199  76.829 -35.006  1.00 85.85           C  
ANISOU 5429  CD1 ILE C  44     9794  10738  12088   1193    141  -1108       C  
ATOM   5430  N   LYS C  45      58.601  77.275 -34.033  1.00 99.27           N  
ANISOU 5430  N   LYS C  45    11453  12504  13762   1099    292   -626       N  
ATOM   5431  CA  LYS C  45      59.307  78.531 -34.243  1.00 95.01           C  
ANISOU 5431  CA  LYS C  45    11005  12020  13075   1086    247   -563       C  
ATOM   5432  C   LYS C  45      58.524  79.458 -35.160  1.00 92.68           C  
ANISOU 5432  C   LYS C  45    10819  11743  12654   1127    169   -698       C  
ATOM   5433  O   LYS C  45      57.705  79.012 -35.969  1.00 92.36           O  
ANISOU 5433  O   LYS C  45    10786  11672  12633   1174    166   -839       O  
ATOM   5434  CB  LYS C  45      60.698  78.284 -34.842  1.00 95.04           C  
ANISOU 5434  CB  LYS C  45    11008  12019  13085   1095    316   -467       C  
ATOM   5435  CG  LYS C  45      61.634  77.437 -33.994  1.00 93.95           C  
ANISOU 5435  CG  LYS C  45    10761  11872  13063   1053    403   -308       C  
ATOM   5436  CD  LYS C  45      63.020  77.394 -34.623  1.00 91.02           C  
ANISOU 5436  CD  LYS C  45    10406  11503  12675   1064    463   -201       C  
ATOM   5437  CE  LYS C  45      63.976  76.517 -33.835  1.00 88.67           C  
ANISOU 5437  CE  LYS C  45     9994  11200  12496   1024    560    -30       C  
ATOM   5438  NZ  LYS C  45      65.361  76.621 -34.371  1.00 88.74           N  
ANISOU 5438  NZ  LYS C  45    10024  11220  12475   1030    612     96       N  
ATOM   5439  N   PRO C  46      58.748  80.767 -35.050  1.00 91.58           N  
ANISOU 5439  N   PRO C  46    10758  11655  12385   1109    109   -655       N  
ATOM   5440  CA  PRO C  46      58.020  81.715 -35.900  1.00 91.33           C  
ANISOU 5440  CA  PRO C  46    10821  11645  12235   1150     42   -766       C  
ATOM   5441  C   PRO C  46      58.383  81.545 -37.365  1.00 94.78           C  
ANISOU 5441  C   PRO C  46    11294  12078  12641   1212     67   -831       C  
ATOM   5442  O   PRO C  46      59.547  81.351 -37.721  1.00 90.01           O  
ANISOU 5442  O   PRO C  46    10683  11471  12045   1218    117   -747       O  
ATOM   5443  CB  PRO C  46      58.459  83.084 -35.368  1.00 90.93           C  
ANISOU 5443  CB  PRO C  46    10833  11643  12074   1110     -8   -676       C  
ATOM   5444  CG  PRO C  46      58.927  82.819 -33.980  1.00 91.49           C  
ANISOU 5444  CG  PRO C  46    10837  11721  12205   1040     12   -552       C  
ATOM   5445  CD  PRO C  46      59.545  81.457 -34.022  1.00 91.48           C  
ANISOU 5445  CD  PRO C  46    10743  11684  12332   1044     96   -505       C  
ATOM   5446  N   HIS C  47      57.366  81.621 -38.211  1.00107.53           N  
ANISOU 5446  N   HIS C  47    12944  13696  14216   1260     33   -976       N  
ATOM   5447  CA  HIS C  47      57.518  81.545 -39.655  1.00115.36           C  
ANISOU 5447  CA  HIS C  47    13972  14699  15159   1324     47  -1059       C  
ATOM   5448  C   HIS C  47      57.390  82.934 -40.271  1.00113.10           C  
ANISOU 5448  C   HIS C  47    13773  14476  14726   1352    -14  -1070       C  
ATOM   5449  O   HIS C  47      56.910  83.878 -39.639  1.00111.33           O  
ANISOU 5449  O   HIS C  47    13582  14274  14444   1326    -68  -1048       O  
ATOM   5450  CB  HIS C  47      56.464  80.605 -40.250  1.00122.54           C  
ANISOU 5450  CB  HIS C  47    14852  15582  16127   1356     55  -1218       C  
ATOM   5451  CG  HIS C  47      56.648  80.338 -41.710  1.00129.35           C  
ANISOU 5451  CG  HIS C  47    15739  16458  16949   1418     78  -1311       C  
ATOM   5452  ND1 HIS C  47      55.833  80.890 -42.675  1.00130.69           N  
ANISOU 5452  ND1 HIS C  47    15958  16682  17017   1462     27  -1428       N  
ATOM   5453  CD2 HIS C  47      57.555  79.581 -42.372  1.00131.25           C  
ANISOU 5453  CD2 HIS C  47    15960  16674  17235   1444    150  -1301       C  
ATOM   5454  CE1 HIS C  47      56.230  80.486 -43.868  1.00132.47           C  
ANISOU 5454  CE1 HIS C  47    16191  16919  17220   1512     63  -1491       C  
ATOM   5455  NE2 HIS C  47      57.274  79.690 -43.712  1.00132.45           N  
ANISOU 5455  NE2 HIS C  47    16152  16866  17308   1503    138  -1418       N  
ATOM   5456  N   ASN C  48      57.852  83.053 -41.520  1.00114.79           N  
ANISOU 5456  N   ASN C  48    14018  14717  14881   1410      0  -1101       N  
ATOM   5457  CA  ASN C  48      57.766  84.331 -42.222  1.00117.04           C  
ANISOU 5457  CA  ASN C  48    14373  15065  15033   1447    -49  -1108       C  
ATOM   5458  C   ASN C  48      56.323  84.776 -42.410  1.00112.07           C  
ANISOU 5458  C   ASN C  48    13767  14466  14350   1464   -106  -1225       C  
ATOM   5459  O   ASN C  48      56.053  85.978 -42.520  1.00110.01           O  
ANISOU 5459  O   ASN C  48    13557  14250  13994   1474   -151  -1209       O  
ATOM   5460  CB  ASN C  48      58.452  84.225 -43.584  1.00123.86           C  
ANISOU 5460  CB  ASN C  48    15252  15958  15850   1516    -19  -1127       C  
ATOM   5461  CG  ASN C  48      59.960  84.276 -43.485  1.00130.50           C  
ANISOU 5461  CG  ASN C  48    16092  16788  16705   1508     24   -978       C  
ATOM   5462  OD1 ASN C  48      60.523  85.153 -42.830  1.00133.69           O  
ANISOU 5462  OD1 ASN C  48    16519  17201  17075   1472      1   -858       O  
ATOM   5463  ND2 ASN C  48      60.626  83.327 -44.135  1.00132.10           N  
ANISOU 5463  ND2 ASN C  48    16268  16968  16957   1542     88   -984       N  
ATOM   5464  N   SER C  49      55.386  83.826 -42.444  1.00108.84           N  
ANISOU 5464  N   SER C  49    13317  14031  14006   1465   -101  -1339       N  
ATOM   5465  CA  SER C  49      53.971  84.118 -42.637  1.00104.97           C  
ANISOU 5465  CA  SER C  49    12841  13570  13473   1479   -153  -1448       C  
ATOM   5466  C   SER C  49      53.262  84.584 -41.373  1.00103.52           C  
ANISOU 5466  C   SER C  49    12661  13367  13304   1430   -191  -1409       C  
ATOM   5467  O   SER C  49      52.099  84.992 -41.459  1.00104.06           O  
ANISOU 5467  O   SER C  49    12748  13462  13328   1442   -235  -1478       O  
ATOM   5468  CB  SER C  49      53.248  82.885 -43.181  1.00102.75           C  
ANISOU 5468  CB  SER C  49    12513  13267  13259   1496   -134  -1586       C  
ATOM   5469  OG  SER C  49      53.302  81.808 -42.262  1.00100.15           O  
ANISOU 5469  OG  SER C  49    12121  12861  13069   1453    -98  -1568       O  
ATOM   5470  N   HIS C  50      53.916  84.540 -40.215  1.00101.81           N  
ANISOU 5470  N   HIS C  50    12425  13113  13145   1376   -175  -1298       N  
ATOM   5471  CA  HIS C  50      53.290  84.968 -38.971  1.00 95.70           C  
ANISOU 5471  CA  HIS C  50    11654  12326  12383   1329   -210  -1259       C  
ATOM   5472  C   HIS C  50      53.431  86.462 -38.719  1.00 90.00           C  
ANISOU 5472  C   HIS C  50    11001  11640  11553   1318   -247  -1192       C  
ATOM   5473  O   HIS C  50      52.869  86.964 -37.741  1.00 89.41           O  
ANISOU 5473  O   HIS C  50    10941  11559  11473   1283   -276  -1167       O  
ATOM   5474  CB  HIS C  50      53.865  84.181 -37.789  1.00 94.04           C  
ANISOU 5474  CB  HIS C  50    11378  12069  12283   1274   -174  -1173       C  
ATOM   5475  CG  HIS C  50      53.610  82.708 -37.863  1.00 91.37           C  
ANISOU 5475  CG  HIS C  50    10961  11683  12071   1281   -132  -1234       C  
ATOM   5476  ND1 HIS C  50      54.305  81.793 -37.102  1.00 91.10           N  
ANISOU 5476  ND1 HIS C  50    10853  11609  12152   1246    -78  -1155       N  
ATOM   5477  CD2 HIS C  50      52.727  81.991 -38.599  1.00 89.83           C  
ANISOU 5477  CD2 HIS C  50    10746  11476  11909   1318   -133  -1365       C  
ATOM   5478  CE1 HIS C  50      53.866  80.576 -37.369  1.00 89.62           C  
ANISOU 5478  CE1 HIS C  50    10602  11377  12071   1263    -43  -1236       C  
ATOM   5479  NE2 HIS C  50      52.908  80.669 -38.273  1.00 91.29           N  
ANISOU 5479  NE2 HIS C  50    10848  11604  12234   1304    -78  -1369       N  
ATOM   5480  N   GLU C  51      54.156  87.174 -39.579  1.00 90.83           N  
ANISOU 5480  N   GLU C  51    11150  11782  11580   1350   -243  -1163       N  
ATOM   5481  CA  GLU C  51      54.332  88.616 -39.469  1.00 96.47           C  
ANISOU 5481  CA  GLU C  51    11929  12526  12201   1344   -272  -1102       C  
ATOM   5482  C   GLU C  51      52.989  89.325 -39.348  1.00 97.32           C  
ANISOU 5482  C   GLU C  51    12071  12651  12257   1355   -312  -1164       C  
ATOM   5483  O   GLU C  51      52.204  89.349 -40.301  1.00102.50           O  
ANISOU 5483  O   GLU C  51    12732  13342  12871   1409   -324  -1252       O  
ATOM   5484  CB  GLU C  51      55.093  89.144 -40.687  1.00103.51           C  
ANISOU 5484  CB  GLU C  51    12849  13459  13021   1397   -261  -1084       C  
ATOM   5485  CG  GLU C  51      55.242  90.655 -40.742  1.00109.94           C  
ANISOU 5485  CG  GLU C  51    13724  14304  13745   1402   -285  -1026       C  
ATOM   5486  CD  GLU C  51      56.441  91.152 -39.971  1.00120.36           C  
ANISOU 5486  CD  GLU C  51    15058  15602  15071   1346   -278   -896       C  
ATOM   5487  OE1 GLU C  51      56.562  90.814 -38.776  1.00125.42           O  
ANISOU 5487  OE1 GLU C  51    15679  16208  15766   1278   -277   -854       O  
ATOM   5488  OE2 GLU C  51      57.270  91.873 -40.566  1.00124.17           O  
ANISOU 5488  OE2 GLU C  51    15566  16108  15503   1370   -273   -834       O  
ATOM   5489  N   GLY C  52      52.710  89.887 -38.176  1.00 90.05           N  
ANISOU 5489  N   GLY C  52    11169  11709  11335   1304   -331  -1116       N  
ATOM   5490  CA  GLY C  52      51.504  90.656 -37.968  1.00 82.66           C  
ANISOU 5490  CA  GLY C  52    10272  10784  10350   1314   -363  -1157       C  
ATOM   5491  C   GLY C  52      50.288  89.871 -37.530  1.00 77.58           C  
ANISOU 5491  C   GLY C  52     9592  10122   9763   1313   -378  -1228       C  
ATOM   5492  O   GLY C  52      49.236  90.478 -37.302  1.00 77.28           O  
ANISOU 5492  O   GLY C  52     9585  10092   9687   1322   -402  -1253       O  
ATOM   5493  N   LYS C  53      50.392  88.551 -37.387  1.00 77.72           N  
ANISOU 5493  N   LYS C  53     9543  10111   9875   1305   -360  -1255       N  
ATOM   5494  CA  LYS C  53      49.245  87.774 -36.946  1.00 81.11           C  
ANISOU 5494  CA  LYS C  53     9931  10518  10370   1305   -375  -1317       C  
ATOM   5495  C   LYS C  53      49.070  87.883 -35.431  1.00 78.76           C  
ANISOU 5495  C   LYS C  53     9623  10191  10112   1252   -385  -1251       C  
ATOM   5496  O   LYS C  53      49.950  88.349 -34.703  1.00 80.95           O  
ANISOU 5496  O   LYS C  53     9914  10464  10377   1208   -376  -1161       O  
ATOM   5497  CB  LYS C  53      49.382  86.312 -37.371  1.00 85.85           C  
ANISOU 5497  CB  LYS C  53    10457  11094  11068   1316   -347  -1375       C  
ATOM   5498  CG  LYS C  53      49.248  86.102 -38.875  1.00 93.93           C  
ANISOU 5498  CG  LYS C  53    11487  12153  12050   1371   -342  -1468       C  
ATOM   5499  CD  LYS C  53      48.997  84.640 -39.220  1.00 95.23           C  
ANISOU 5499  CD  LYS C  53    11582  12285  12317   1380   -319  -1553       C  
ATOM   5500  CE  LYS C  53      48.922  84.426 -40.726  1.00 91.67           C  
ANISOU 5500  CE  LYS C  53    11138  11877  11815   1431   -314  -1653       C  
ATOM   5501  NZ  LYS C  53      47.888  85.281 -41.367  1.00 91.20           N  
ANISOU 5501  NZ  LYS C  53    11120  11882  11649   1465   -358  -1707       N  
ATOM   5502  N   THR C  54      47.906  87.444 -34.961  1.00 69.82           N  
ANISOU 5502  N   THR C  54     8463   9042   9024   1258   -405  -1295       N  
ATOM   5503  CA  THR C  54      47.508  87.569 -33.566  1.00 56.94           C  
ANISOU 5503  CA  THR C  54     6821   7391   7423   1221   -419  -1242       C  
ATOM   5504  C   THR C  54      47.557  86.209 -32.890  1.00 63.22           C  
ANISOU 5504  C   THR C  54     7519   8152   8349   1203   -400  -1231       C  
ATOM   5505  O   THR C  54      46.935  85.252 -33.361  1.00 69.08           O  
ANISOU 5505  O   THR C  54     8211   8877   9162   1233   -398  -1304       O  
ATOM   5506  CB  THR C  54      46.103  88.167 -33.464  1.00 51.71           C  
ANISOU 5506  CB  THR C  54     6199   6736   6714   1248   -454  -1282       C  
ATOM   5507  OG1 THR C  54      46.111  89.488 -34.026  1.00 56.87           O  
ANISOU 5507  OG1 THR C  54     6936   7420   7252   1264   -461  -1276       O  
ATOM   5508  CG2 THR C  54      45.629  88.218 -32.015  1.00 47.23           C  
ANISOU 5508  CG2 THR C  54     5617   6149   6181   1217   -467  -1230       C  
ATOM   5509  N   PHE C  55      48.272  86.139 -31.769  1.00 66.13           N  
ANISOU 5509  N   PHE C  55     7857   8516   8754   1153   -384  -1139       N  
ATOM   5510  CA  PHE C  55      48.470  84.911 -31.017  1.00 65.35           C  
ANISOU 5510  CA  PHE C  55     7654   8392   8783   1134   -357  -1104       C  
ATOM   5511  C   PHE C  55      47.813  85.031 -29.648  1.00 66.38           C  
ANISOU 5511  C   PHE C  55     7760   8525   8936   1112   -379  -1057       C  
ATOM   5512  O   PHE C  55      47.874  86.087 -29.010  1.00 65.72           O  
ANISOU 5512  O   PHE C  55     7738   8465   8768   1084   -399  -1012       O  
ATOM   5513  CB  PHE C  55      49.968  84.607 -30.838  1.00 67.16           C  
ANISOU 5513  CB  PHE C  55     7847   8627   9042   1093   -312  -1017       C  
ATOM   5514  CG  PHE C  55      50.702  84.343 -32.127  1.00 68.75           C  
ANISOU 5514  CG  PHE C  55     8063   8824   9237   1119   -282  -1051       C  
ATOM   5515  CD1 PHE C  55      50.973  83.046 -32.531  1.00 75.11           C  
ANISOU 5515  CD1 PHE C  55     8789   9597  10153   1134   -236  -1075       C  
ATOM   5516  CD2 PHE C  55      51.124  85.388 -32.931  1.00 64.11           C  
ANISOU 5516  CD2 PHE C  55     7563   8263   8534   1131   -296  -1058       C  
ATOM   5517  CE1 PHE C  55      51.647  82.797 -33.716  1.00 72.35           C  
ANISOU 5517  CE1 PHE C  55     8455   9243   9793   1161   -206  -1110       C  
ATOM   5518  CE2 PHE C  55      51.802  85.144 -34.116  1.00 61.31           C  
ANISOU 5518  CE2 PHE C  55     7217   7910   8169   1161   -270  -1085       C  
ATOM   5519  CZ  PHE C  55      52.060  83.849 -34.508  1.00 63.77           C  
ANISOU 5519  CZ  PHE C  55     7456   8191   8584   1176   -225  -1113       C  
ATOM   5520  N   TYR C  56      47.172  83.950 -29.207  1.00 65.68           N  
ANISOU 5520  N   TYR C  56     7582   8411   8963   1126   -372  -1070       N  
ATOM   5521  CA  TYR C  56      46.684  83.863 -27.838  1.00 61.23           C  
ANISOU 5521  CA  TYR C  56     6972   7854   8439   1109   -385  -1009       C  
ATOM   5522  C   TYR C  56      47.801  83.404 -26.911  1.00 61.37           C  
ANISOU 5522  C   TYR C  56     6911   7891   8515   1059   -346   -901       C  
ATOM   5523  O   TYR C  56      48.627  82.562 -27.278  1.00 57.54           O  
ANISOU 5523  O   TYR C  56     6364   7393   8107   1052   -299   -882       O  
ATOM   5524  CB  TYR C  56      45.509  82.894 -27.739  1.00 55.39           C  
ANISOU 5524  CB  TYR C  56     6158   7081   7807   1151   -395  -1058       C  
ATOM   5525  CG  TYR C  56      44.156  83.532 -27.874  1.00 51.51           C  
ANISOU 5525  CG  TYR C  56     5731   6589   7252   1187   -446  -1115       C  
ATOM   5526  CD1 TYR C  56      43.388  83.812 -26.751  1.00 54.03           C  
ANISOU 5526  CD1 TYR C  56     6042   6916   7571   1190   -472  -1070       C  
ATOM   5527  CD2 TYR C  56      43.626  83.826 -29.124  1.00 59.18           C  
ANISOU 5527  CD2 TYR C  56     6765   7555   8165   1222   -464  -1208       C  
ATOM   5528  CE1 TYR C  56      42.134  84.391 -26.871  1.00 62.93           C  
ANISOU 5528  CE1 TYR C  56     7229   8041   8643   1227   -512  -1111       C  
ATOM   5529  CE2 TYR C  56      42.378  84.406 -29.255  1.00 63.58           C  
ANISOU 5529  CE2 TYR C  56     7374   8117   8665   1256   -506  -1248       C  
ATOM   5530  CZ  TYR C  56      41.635  84.686 -28.128  1.00 65.93           C  
ANISOU 5530  CZ  TYR C  56     7669   8416   8966   1258   -528  -1197       C  
ATOM   5531  OH  TYR C  56      40.389  85.257 -28.261  1.00 67.58           O  
ANISOU 5531  OH  TYR C  56     7930   8627   9119   1294   -563  -1225       O  
ATOM   5532  N   VAL C  57      47.832  83.974 -25.707  1.00 59.94           N  
ANISOU 5532  N   VAL C  57     6733   7746   8294   1023   -361   -828       N  
ATOM   5533  CA  VAL C  57      48.819  83.617 -24.700  1.00 59.37           C  
ANISOU 5533  CA  VAL C  57     6581   7711   8265    970   -328   -715       C  
ATOM   5534  C   VAL C  57      48.150  83.557 -23.332  1.00 66.10           C  
ANISOU 5534  C   VAL C  57     7379   8592   9143    964   -346   -664       C  
ATOM   5535  O   VAL C  57      47.062  84.096 -23.120  1.00 71.88           O  
ANISOU 5535  O   VAL C  57     8164   9317   9829    992   -388   -709       O  
ATOM   5536  CB  VAL C  57      50.003  84.604 -24.686  1.00 49.39           C  
ANISOU 5536  CB  VAL C  57     5388   6486   6891    912   -326   -661       C  
ATOM   5537  CG1 VAL C  57      50.783  84.511 -25.982  1.00 45.10           C  
ANISOU 5537  CG1 VAL C  57     4878   5920   6339    924   -301   -690       C  
ATOM   5538  CG2 VAL C  57      49.499  86.015 -24.477  1.00 46.37           C  
ANISOU 5538  CG2 VAL C  57     5125   6118   6375    903   -373   -691       C  
ATOM   5539  N   LEU C  58      48.814  82.885 -22.402  1.00 64.64           N  
ANISOU 5539  N   LEU C  58     7082   8445   9032    929   -311   -563       N  
ATOM   5540  CA  LEU C  58      48.357  82.851 -21.023  1.00 71.79           C  
ANISOU 5540  CA  LEU C  58     7926   9397   9955    919   -324   -499       C  
ATOM   5541  C   LEU C  58      48.837  84.099 -20.283  1.00 66.27           C  
ANISOU 5541  C   LEU C  58     7306   8759   9115    858   -349   -456       C  
ATOM   5542  O   LEU C  58      49.891  84.650 -20.606  1.00 71.96           O  
ANISOU 5542  O   LEU C  58     8078   9498   9764    808   -339   -433       O  
ATOM   5543  CB  LEU C  58      48.865  81.599 -20.317  1.00 83.46           C  
ANISOU 5543  CB  LEU C  58     9236  10901  11573    909   -272   -400       C  
ATOM   5544  CG  LEU C  58      47.960  80.365 -20.342  1.00 87.87           C  
ANISOU 5544  CG  LEU C  58     9685  11412  12291    972   -255   -422       C  
ATOM   5545  CD1 LEU C  58      47.672  79.910 -21.771  1.00 86.65           C  
ANISOU 5545  CD1 LEU C  58     9565  11173  12184   1015   -247   -531       C  
ATOM   5546  CD2 LEU C  58      48.570  79.239 -19.515  1.00 92.51           C  
ANISOU 5546  CD2 LEU C  58    10099  12035  13016    958   -194   -303       C  
ATOM   5547  N   PRO C  59      48.066  84.590 -19.314  1.00 63.55           N  
ANISOU 5547  N   PRO C  59     6977   8445   8726    860   -382   -448       N  
ATOM   5548  CA  PRO C  59      48.458  85.834 -18.634  1.00 71.79           C  
ANISOU 5548  CA  PRO C  59     8106   9540   9630    799   -405   -424       C  
ATOM   5549  C   PRO C  59      49.699  85.697 -17.762  1.00 86.81           C  
ANISOU 5549  C   PRO C  59     9932  11525  11526    721   -379   -313       C  
ATOM   5550  O   PRO C  59      49.589  85.455 -16.554  1.00 93.85           O  
ANISOU 5550  O   PRO C  59    10741  12484  12434    704   -378   -244       O  
ATOM   5551  CB  PRO C  59      47.225  86.173 -17.782  1.00 72.00           C  
ANISOU 5551  CB  PRO C  59     8149   9575   9632    833   -439   -441       C  
ATOM   5552  CG  PRO C  59      46.104  85.350 -18.347  1.00 73.88           C  
ANISOU 5552  CG  PRO C  59     8347   9750   9974    917   -444   -494       C  
ATOM   5553  CD  PRO C  59      46.758  84.100 -18.853  1.00 70.88           C  
ANISOU 5553  CD  PRO C  59     7854   9355   9723    922   -401   -466       C  
ATOM   5554  N   ASN C  60      50.883  85.859 -18.353  1.00 87.28           N  
ANISOU 5554  N   ASN C  60    10014  11589  11558    675   -357   -288       N  
ATOM   5555  CA  ASN C  60      52.146  85.934 -17.617  1.00 85.77           C  
ANISOU 5555  CA  ASN C  60     9771  11482  11336    590   -336   -180       C  
ATOM   5556  C   ASN C  60      52.603  87.378 -17.443  1.00 82.82           C  
ANISOU 5556  C   ASN C  60     9524  11134  10809    523   -369   -196       C  
ATOM   5557  O   ASN C  60      53.795  87.683 -17.522  1.00 82.52           O  
ANISOU 5557  O   ASN C  60     9496  11132  10727    457   -357   -139       O  
ATOM   5558  CB  ASN C  60      53.219  85.099 -18.316  1.00 95.75           C  
ANISOU 5558  CB  ASN C  60    10965  12737  12680    581   -286   -122       C  
ATOM   5559  CG  ASN C  60      53.528  85.584 -19.734  1.00104.32           C  
ANISOU 5559  CG  ASN C  60    12163  13752  13723    600   -290   -195       C  
ATOM   5560  OD1 ASN C  60      53.008  86.605 -20.192  1.00107.63           O  
ANISOU 5560  OD1 ASN C  60    12710  14135  14048    614   -330   -282       O  
ATOM   5561  ND2 ASN C  60      54.370  84.835 -20.439  1.00105.12           N  
ANISOU 5561  ND2 ASN C  60    12211  13835  13894    604   -244   -154       N  
ATOM   5562  N   ASP C  61      51.668  88.287 -17.194  1.00 83.91           N  
ANISOU 5562  N   ASP C  61     9761  11253  10868    539   -407   -270       N  
ATOM   5563  CA  ASP C  61      51.979  89.707 -17.123  1.00 84.67           C  
ANISOU 5563  CA  ASP C  61     9988  11355  10827    482   -433   -302       C  
ATOM   5564  C   ASP C  61      50.871  90.398 -16.346  1.00 77.84           C  
ANISOU 5564  C   ASP C  61     9182  10491   9901    497   -462   -353       C  
ATOM   5565  O   ASP C  61      49.765  89.870 -16.215  1.00 73.71           O  
ANISOU 5565  O   ASP C  61     8625   9944   9438    568   -467   -379       O  
ATOM   5566  CB  ASP C  61      52.130  90.282 -18.539  1.00 95.81           C  
ANISOU 5566  CB  ASP C  61    11507  12688  12206    508   -435   -371       C  
ATOM   5567  CG  ASP C  61      52.319  91.774 -18.553  1.00105.58           C  
ANISOU 5567  CG  ASP C  61    12881  13917  13318    461   -457   -410       C  
ATOM   5568  OD1 ASP C  61      53.452  92.235 -18.305  1.00110.86           O  
ANISOU 5568  OD1 ASP C  61    13559  14628  13934    380   -455   -357       O  
ATOM   5569  OD2 ASP C  61      51.332  92.485 -18.826  1.00109.59           O  
ANISOU 5569  OD2 ASP C  61    13482  14374  13784    505   -473   -491       O  
ATOM   5570  N   ASP C  62      51.176  91.591 -15.832  1.00 87.64           N  
ANISOU 5570  N   ASP C  62    11813  11860   9627  -2197   -850    688       N  
ATOM   5571  CA  ASP C  62      50.174  92.348 -15.082  1.00 89.73           C  
ANISOU 5571  CA  ASP C  62    12296  11988   9808  -2240   -848    559       C  
ATOM   5572  C   ASP C  62      49.075  92.893 -15.988  1.00 82.52           C  
ANISOU 5572  C   ASP C  62    11447  10988   8919  -2128   -767    418       C  
ATOM   5573  O   ASP C  62      47.898  92.891 -15.609  1.00 77.46           O  
ANISOU 5573  O   ASP C  62    10917  10241   8275  -2064   -698    287       O  
ATOM   5574  CB  ASP C  62      50.845  93.485 -14.315  1.00102.87           C  
ANISOU 5574  CB  ASP C  62    14102  13625  11358  -2446   -975    631       C  
ATOM   5575  CG  ASP C  62      51.703  92.987 -13.172  1.00112.72           C  
ANISOU 5575  CG  ASP C  62    15330  14934  12565  -2577  -1065    758       C  
ATOM   5576  OD1 ASP C  62      51.259  92.063 -12.455  1.00117.58           O  
ANISOU 5576  OD1 ASP C  62    15939  15541  13193  -2528  -1017    720       O  
ATOM   5577  OD2 ASP C  62      52.829  93.505 -13.005  1.00114.53           O  
ANISOU 5577  OD2 ASP C  62    15542  15220  12754  -2733  -1189    906       O  
ATOM   5578  N   THR C  63      49.432  93.364 -17.186  1.00 80.65           N  
ANISOU 5578  N   THR C  63    11137  10795   8712  -2103   -773    452       N  
ATOM   5579  CA  THR C  63      48.405  93.877 -18.091  1.00 76.06           C  
ANISOU 5579  CA  THR C  63    10606  10136   8158  -2005   -707    334       C  
ATOM   5580  C   THR C  63      47.532  92.752 -18.631  1.00 70.33           C  
ANISOU 5580  C   THR C  63     9793   9410   7521  -1827   -599    246       C  
ATOM   5581  O   THR C  63      46.309  92.903 -18.734  1.00 64.60           O  
ANISOU 5581  O   THR C  63     9147   8581   6817  -1749   -537    126       O  
ATOM   5582  CB  THR C  63      49.049  94.660 -19.240  1.00 72.66           C  
ANISOU 5582  CB  THR C  63    10117   9761   7728  -2033   -748    404       C  
ATOM   5583  OG1 THR C  63      49.571  95.900 -18.745  1.00 75.41           O  
ANISOU 5583  OG1 THR C  63    10584  10071   7995  -2198   -851    459       O  
ATOM   5584  CG2 THR C  63      48.031  94.956 -20.325  1.00 71.84           C  
ANISOU 5584  CG2 THR C  63    10028   9600   7667  -1918   -678    298       C  
ATOM   5585  N   LEU C  64      48.135  91.600 -18.934  1.00 72.94           N  
ANISOU 5585  N   LEU C  64     9960   9846   7908  -1764   -575    309       N  
ATOM   5586  CA  LEU C  64      47.361  90.478 -19.455  1.00 68.53           C  
ANISOU 5586  CA  LEU C  64     9324   9282   7433  -1602   -480    228       C  
ATOM   5587  C   LEU C  64      46.401  89.925 -18.409  1.00 66.37           C  
ANISOU 5587  C   LEU C  64     9121   8924   7171  -1567   -442    144       C  
ATOM   5588  O   LEU C  64      45.265  89.567 -18.738  1.00 67.30           O  
ANISOU 5588  O   LEU C  64     9256   8974   7342  -1454   -374     39       O  
ATOM   5589  CB  LEU C  64      48.301  89.381 -19.949  1.00 64.08           C  
ANISOU 5589  CB  LEU C  64     8580   8841   6928  -1547   -458    319       C  
ATOM   5590  CG  LEU C  64      49.131  89.772 -21.171  1.00 61.52           C  
ANISOU 5590  CG  LEU C  64     8170   8603   6602  -1546   -464    394       C  
ATOM   5591  CD1 LEU C  64      50.029  88.613 -21.609  1.00 62.42           C  
ANISOU 5591  CD1 LEU C  64     8108   8826   6782  -1476   -416    482       C  
ATOM   5592  CD2 LEU C  64      48.230  90.256 -22.309  1.00 60.05           C  
ANISOU 5592  CD2 LEU C  64     8034   8364   6418  -1470   -424    290       C  
ATOM   5593  N   ARG C  65      46.831  89.869 -17.143  1.00 73.17           N  
ANISOU 5593  N   ARG C  65    10029   9790   7984  -1668   -488    196       N  
ATOM   5594  CA  ARG C  65      45.956  89.390 -16.076  1.00 67.87           C  
ANISOU 5594  CA  ARG C  65     9434   9042   7312  -1643   -449    125       C  
ATOM   5595  C   ARG C  65      44.739  90.287 -15.928  1.00 66.36           C  
ANISOU 5595  C   ARG C  65     9408   8714   7093  -1627   -409      7       C  
ATOM   5596  O   ARG C  65      43.624  89.807 -15.697  1.00 73.00           O  
ANISOU 5596  O   ARG C  65    10274   9481   7982  -1531   -335    -80       O  
ATOM   5597  CB  ARG C  65      46.708  89.343 -14.750  1.00 67.17           C  
ANISOU 5597  CB  ARG C  65     9386   8983   7152  -1780   -519    211       C  
ATOM   5598  CG  ARG C  65      47.670  88.188 -14.587  1.00 70.99           C  
ANISOU 5598  CG  ARG C  65     9699   9584   7689  -1778   -541    329       C  
ATOM   5599  CD  ARG C  65      48.313  88.251 -13.206  1.00 75.17           C  
ANISOU 5599  CD  ARG C  65    10288  10134   8139  -1933   -624    419       C  
ATOM   5600  NE  ARG C  65      49.653  87.678 -13.211  1.00 74.65           N  
ANISOU 5600  NE  ARG C  65    10060  10193   8111  -1990   -687    587       N  
ATOM   5601  CZ  ARG C  65      50.756  88.417 -13.150  1.00 76.27           C  
ANISOU 5601  CZ  ARG C  65    10264  10453   8261  -2136   -791    714       C  
ATOM   5602  NH1 ARG C  65      50.657  89.738 -13.055  1.00 72.80           N  
ANISOU 5602  NH1 ARG C  65     9991   9950   7720  -2240   -846    679       N  
ATOM   5603  NH2 ARG C  65      51.951  87.843 -13.171  1.00 84.70           N  
ANISOU 5603  NH2 ARG C  65    11164  11634   9383  -2177   -841    883       N  
ATOM   5604  N   VAL C  66      44.940  91.598 -16.022  1.00 61.52           N  
ANISOU 5604  N   VAL C  66     8907   8059   6410  -1723   -456     11       N  
ATOM   5605  CA  VAL C  66      43.822  92.527 -15.926  1.00 60.78           C  
ANISOU 5605  CA  VAL C  66     8968   7825   6301  -1706   -410    -93       C  
ATOM   5606  C   VAL C  66      42.890  92.359 -17.117  1.00 58.52           C  
ANISOU 5606  C   VAL C  66     8614   7508   6113  -1562   -344   -160       C  
ATOM   5607  O   VAL C  66      41.663  92.315 -16.971  1.00 55.64           O  
ANISOU 5607  O   VAL C  66     8305   7041   5796  -1479   -270   -245       O  
ATOM   5608  CB  VAL C  66      44.337  93.969 -15.817  1.00 62.09           C  
ANISOU 5608  CB  VAL C  66     9265   7952   6377  -1845   -482    -65       C  
ATOM   5609  CG1 VAL C  66      43.173  94.933 -15.835  1.00 61.27           C  
ANISOU 5609  CG1 VAL C  66     9309   7695   6277  -1811   -421   -169       C  
ATOM   5610  CG2 VAL C  66      45.165  94.119 -14.564  1.00 63.77           C  
ANISOU 5610  CG2 VAL C  66     9565   8182   6483  -1999   -557     -2       C  
ATOM   5611  N   GLU C  67      43.460  92.292 -18.319  1.00 62.93           N  
ANISOU 5611  N   GLU C  67     9056   8153   6703  -1538   -371   -114       N  
ATOM   5612  CA  GLU C  67      42.646  92.124 -19.513  1.00 61.31           C  
ANISOU 5612  CA  GLU C  67     8792   7925   6576  -1418   -323   -170       C  
ATOM   5613  C   GLU C  67      41.954  90.768 -19.513  1.00 61.05           C  
ANISOU 5613  C   GLU C  67     8676   7893   6625  -1293   -260   -215       C  
ATOM   5614  O   GLU C  67      40.806  90.653 -19.960  1.00 63.75           O  
ANISOU 5614  O   GLU C  67     9027   8161   7035  -1201   -212   -284       O  
ATOM   5615  CB  GLU C  67      43.508  92.307 -20.766  1.00 59.25           C  
ANISOU 5615  CB  GLU C  67     8434   7767   6312  -1428   -363   -105       C  
ATOM   5616  CG  GLU C  67      43.964  93.744 -20.984  1.00 64.11           C  
ANISOU 5616  CG  GLU C  67     9129   8366   6866  -1538   -425    -65       C  
ATOM   5617  CD  GLU C  67      44.911  93.908 -22.163  1.00 73.12           C  
ANISOU 5617  CD  GLU C  67    10164   9620   7997  -1553   -463     16       C  
ATOM   5618  OE1 GLU C  67      45.300  92.887 -22.767  1.00 78.15           O  
ANISOU 5618  OE1 GLU C  67    10674  10352   8669  -1479   -434     41       O  
ATOM   5619  OE2 GLU C  67      45.265  95.063 -22.485  1.00 75.01           O  
ANISOU 5619  OE2 GLU C  67    10453   9850   8197  -1636   -517     55       O  
ATOM   5620  N   ALA C  68      42.631  89.731 -19.007  1.00 56.95           N  
ANISOU 5620  N   ALA C  68     8073   7455   6110  -1293   -265   -168       N  
ATOM   5621  CA  ALA C  68      42.001  88.416 -18.946  1.00 56.58           C  
ANISOU 5621  CA  ALA C  68     7949   7403   6145  -1180   -210   -208       C  
ATOM   5622  C   ALA C  68      40.832  88.408 -17.974  1.00 62.87           C  
ANISOU 5622  C   ALA C  68     8840   8087   6962  -1152   -162   -274       C  
ATOM   5623  O   ALA C  68      39.801  87.781 -18.239  1.00 65.56           O  
ANISOU 5623  O   ALA C  68     9150   8374   7386  -1045   -112   -330       O  
ATOM   5624  CB  ALA C  68      43.024  87.355 -18.554  1.00 48.72           C  
ANISOU 5624  CB  ALA C  68     6841   6512   5157  -1190   -225   -132       C  
ATOM   5625  N   PHE C  69      40.953  89.131 -16.864  1.00 68.18           N  
ANISOU 5625  N   PHE C  69     9635   8716   7556  -1249   -175   -266       N  
ATOM   5626  CA  PHE C  69      39.859  89.173 -15.903  1.00 68.70           C  
ANISOU 5626  CA  PHE C  69     9802   8670   7631  -1221   -113   -327       C  
ATOM   5627  C   PHE C  69      38.677  89.965 -16.444  1.00 69.57           C  
ANISOU 5627  C   PHE C  69     9981   8662   7789  -1160    -62   -395       C  
ATOM   5628  O   PHE C  69      37.520  89.589 -16.232  1.00 74.42           O  
ANISOU 5628  O   PHE C  69    10601   9196   8479  -1069      7   -441       O  
ATOM   5629  CB  PHE C  69      40.338  89.766 -14.583  1.00 68.55           C  
ANISOU 5629  CB  PHE C  69     9917   8631   7497  -1349   -136   -305       C  
ATOM   5630  CG  PHE C  69      39.234  90.028 -13.619  1.00 67.95           C  
ANISOU 5630  CG  PHE C  69     9975   8431   7411  -1325    -56   -371       C  
ATOM   5631  CD1 PHE C  69      38.619  88.979 -12.962  1.00 65.04           C  
ANISOU 5631  CD1 PHE C  69     9566   8054   7094  -1252      0   -384       C  
ATOM   5632  CD2 PHE C  69      38.800  91.318 -13.376  1.00 69.62           C  
ANISOU 5632  CD2 PHE C  69    10352   8530   7569  -1370    -29   -416       C  
ATOM   5633  CE1 PHE C  69      37.591  89.209 -12.076  1.00 71.61           C  
ANISOU 5633  CE1 PHE C  69    10517   8773   7919  -1223     87   -437       C  
ATOM   5634  CE2 PHE C  69      37.773  91.559 -12.488  1.00 76.17           C  
ANISOU 5634  CE2 PHE C  69    11309   9238   8392  -1337     65   -475       C  
ATOM   5635  CZ  PHE C  69      37.166  90.503 -11.836  1.00 79.23           C  
ANISOU 5635  CZ  PHE C  69    11652   9625   8828  -1262    127   -484       C  
ATOM   5636  N   GLU C  70      38.948  91.060 -17.151  1.00 68.02           N  
ANISOU 5636  N   GLU C  70     9828   8454   7561  -1210    -98   -389       N  
ATOM   5637  CA  GLU C  70      37.875  91.885 -17.692  1.00 60.19           C  
ANISOU 5637  CA  GLU C  70     8895   7349   6624  -1160    -56   -437       C  
ATOM   5638  C   GLU C  70      37.077  91.169 -18.772  1.00 54.82           C  
ANISOU 5638  C   GLU C  70     8099   6671   6060  -1039    -36   -456       C  
ATOM   5639  O   GLU C  70      35.924  91.539 -19.017  1.00 53.45           O  
ANISOU 5639  O   GLU C  70     7955   6391   5961   -977     10   -488       O  
ATOM   5640  CB  GLU C  70      38.461  93.191 -18.228  1.00 63.82           C  
ANISOU 5640  CB  GLU C  70     9418   7806   7024  -1250   -111   -414       C  
ATOM   5641  CG  GLU C  70      39.053  94.078 -17.139  1.00 74.82           C  
ANISOU 5641  CG  GLU C  70    10961   9162   8304  -1378   -135   -404       C  
ATOM   5642  CD  GLU C  70      39.560  95.415 -17.660  1.00 92.32           C  
ANISOU 5642  CD  GLU C  70    13246  11360  10472  -1469   -193   -380       C  
ATOM   5643  OE1 GLU C  70      39.328  95.730 -18.849  1.00 97.50           O  
ANISOU 5643  OE1 GLU C  70    13836  12022  11187  -1425   -204   -373       O  
ATOM   5644  OE2 GLU C  70      40.173  96.164 -16.867  1.00 99.58           O  
ANISOU 5644  OE2 GLU C  70    14290  12254  11291  -1591   -232   -365       O  
ATOM   5645  N   TYR C  71      37.653  90.154 -19.413  1.00 58.12           N  
ANISOU 5645  N   TYR C  71     8390   7199   6496  -1006    -69   -431       N  
ATOM   5646  CA  TYR C  71      36.977  89.427 -20.481  1.00 59.01           C  
ANISOU 5646  CA  TYR C  71     8407   7314   6702   -904    -62   -452       C  
ATOM   5647  C   TYR C  71      36.316  88.141 -19.998  1.00 61.94           C  
ANISOU 5647  C   TYR C  71     8719   7666   7150   -818    -21   -473       C  
ATOM   5648  O   TYR C  71      35.186  87.850 -20.402  1.00 68.16           O  
ANISOU 5648  O   TYR C  71     9483   8382   8031   -738      3   -500       O  
ATOM   5649  CB  TYR C  71      37.960  89.107 -21.614  1.00 60.71           C  
ANISOU 5649  CB  TYR C  71     8532   7648   6888   -913   -112   -420       C  
ATOM   5650  CG  TYR C  71      37.284  88.715 -22.911  1.00 63.83           C  
ANISOU 5650  CG  TYR C  71     8868   8034   7349   -834   -116   -445       C  
ATOM   5651  CD1 TYR C  71      36.375  89.571 -23.519  1.00 71.20           C  
ANISOU 5651  CD1 TYR C  71     9847   8885   8321   -825   -121   -459       C  
ATOM   5652  CD2 TYR C  71      37.564  87.505 -23.535  1.00 56.65           C  
ANISOU 5652  CD2 TYR C  71     7865   7194   6464   -774   -119   -450       C  
ATOM   5653  CE1 TYR C  71      35.754  89.233 -24.700  1.00 73.32           C  
ANISOU 5653  CE1 TYR C  71    10070   9146   8643   -769   -141   -473       C  
ATOM   5654  CE2 TYR C  71      36.950  87.158 -24.724  1.00 57.75           C  
ANISOU 5654  CE2 TYR C  71     7973   7320   6647   -716   -131   -477       C  
ATOM   5655  CZ  TYR C  71      36.042  88.027 -25.299  1.00 72.82           C  
ANISOU 5655  CZ  TYR C  71     9929   9152   8587   -719   -149   -485       C  
ATOM   5656  OH  TYR C  71      35.411  87.710 -26.481  1.00 81.23           O  
ANISOU 5656  OH  TYR C  71    10970  10205   9691   -676   -176   -502       O  
ATOM   5657  N   TYR C  72      36.981  87.375 -19.125  1.00 56.59           N  
ANISOU 5657  N   TYR C  72     8012   7048   6441   -838    -19   -452       N  
ATOM   5658  CA  TYR C  72      36.465  86.094 -18.656  1.00 55.41           C  
ANISOU 5658  CA  TYR C  72     7796   6891   6367   -761     14   -462       C  
ATOM   5659  C   TYR C  72      35.847  86.147 -17.260  1.00 61.91           C  
ANISOU 5659  C   TYR C  72     8694   7640   7190   -766     67   -471       C  
ATOM   5660  O   TYR C  72      35.198  85.174 -16.859  1.00 63.84           O  
ANISOU 5660  O   TYR C  72     8887   7861   7510   -696    100   -478       O  
ATOM   5661  CB  TYR C  72      37.579  85.032 -18.658  1.00 51.90           C  
ANISOU 5661  CB  TYR C  72     7249   6562   5908   -766    -14   -423       C  
ATOM   5662  CG  TYR C  72      38.195  84.769 -20.014  1.00 57.10           C  
ANISOU 5662  CG  TYR C  72     7829   7295   6570   -743    -45   -416       C  
ATOM   5663  CD1 TYR C  72      39.426  85.308 -20.354  1.00 64.56           C  
ANISOU 5663  CD1 TYR C  72     8766   8327   7435   -817    -80   -366       C  
ATOM   5664  CD2 TYR C  72      37.548  83.970 -20.952  1.00 61.40           C  
ANISOU 5664  CD2 TYR C  72     8315   7821   7195   -650    -38   -453       C  
ATOM   5665  CE1 TYR C  72      39.995  85.067 -21.594  1.00 74.90           C  
ANISOU 5665  CE1 TYR C  72    10008   9707   8743   -790    -93   -356       C  
ATOM   5666  CE2 TYR C  72      38.105  83.723 -22.194  1.00 65.13           C  
ANISOU 5666  CE2 TYR C  72     8737   8357   7654   -630    -56   -454       C  
ATOM   5667  CZ  TYR C  72      39.331  84.274 -22.511  1.00 75.16           C  
ANISOU 5667  CZ  TYR C  72     9998   9717   8843   -695    -76   -406       C  
ATOM   5668  OH  TYR C  72      39.900  84.036 -23.745  1.00 79.39           O  
ANISOU 5668  OH  TYR C  72    10487  10318   9360   -670    -79   -403       O  
ATOM   5669  N   HIS C  73      36.030  87.244 -16.515  1.00 62.35           N  
ANISOU 5669  N   HIS C  73     8876   7657   7159   -849     78   -471       N  
ATOM   5670  CA  HIS C  73      35.510  87.380 -15.146  1.00 63.58           C  
ANISOU 5670  CA  HIS C  73     9130   7741   7289   -864    140   -484       C  
ATOM   5671  C   HIS C  73      36.054  86.290 -14.221  1.00 59.13           C  
ANISOU 5671  C   HIS C  73     8514   7250   6703   -881    131   -449       C  
ATOM   5672  O   HIS C  73      35.331  85.750 -13.384  1.00 56.02           O  
ANISOU 5672  O   HIS C  73     8131   6810   6346   -836    189   -457       O  
ATOM   5673  CB  HIS C  73      33.978  87.396 -15.113  1.00 62.91           C  
ANISOU 5673  CB  HIS C  73     9061   7532   7310   -762    222   -518       C  
ATOM   5674  CG  HIS C  73      33.371  88.699 -15.539  1.00 64.40           C  
ANISOU 5674  CG  HIS C  73     9340   7620   7508   -764    251   -542       C  
ATOM   5675  ND1 HIS C  73      34.106  89.711 -16.118  1.00 66.16           N  
ANISOU 5675  ND1 HIS C  73     9613   7866   7660   -844    197   -539       N  
ATOM   5676  CD2 HIS C  73      32.094  89.149 -15.478  1.00 63.54           C  
ANISOU 5676  CD2 HIS C  73     9273   7384   7485   -695    330   -558       C  
ATOM   5677  CE1 HIS C  73      33.309  90.730 -16.394  1.00 62.78           C  
ANISOU 5677  CE1 HIS C  73     9256   7326   7271   -824    240   -557       C  
ATOM   5678  NE2 HIS C  73      32.084  90.414 -16.016  1.00 62.30           N  
ANISOU 5678  NE2 HIS C  73     9190   7173   7309   -732    324   -567       N  
ATOM   5679  N   THR C  74      37.341  85.974 -14.358  1.00 59.70           N  
ANISOU 5679  N   THR C  74     8525   7437   6722   -947     61   -399       N  
ATOM   5680  CA  THR C  74      37.991  85.003 -13.488  1.00 61.86           C  
ANISOU 5680  CA  THR C  74     8741   7786   6978   -978     42   -347       C  
ATOM   5681  C   THR C  74      39.479  85.320 -13.427  1.00 63.91           C  
ANISOU 5681  C   THR C  74     8993   8147   7144  -1098    -38   -277       C  
ATOM   5682  O   THR C  74      40.046  85.880 -14.369  1.00 67.14           O  
ANISOU 5682  O   THR C  74     9382   8591   7537  -1121    -77   -265       O  
ATOM   5683  CB  THR C  74      37.764  83.558 -13.976  1.00 66.74           C  
ANISOU 5683  CB  THR C  74     9200   8441   7717   -869     50   -340       C  
ATOM   5684  OG1 THR C  74      38.408  82.629 -13.094  1.00 63.81           O  
ANISOU 5684  OG1 THR C  74     8768   8140   7339   -900     31   -280       O  
ATOM   5685  CG2 THR C  74      38.322  83.367 -15.376  1.00 70.44           C  
ANISOU 5685  CG2 THR C  74     9572   8971   8222   -836     12   -335       C  
ATOM   5686  N   THR C  75      40.106  84.976 -12.300  1.00 66.92           N  
ANISOU 5686  N   THR C  75     9388   8575   7465  -1180    -65   -219       N  
ATOM   5687  CA  THR C  75      41.539  85.170 -12.122  1.00 68.53           C  
ANISOU 5687  CA  THR C  75     9569   8879   7592  -1303   -151   -127       C  
ATOM   5688  C   THR C  75      42.297  83.855 -12.054  1.00 70.66           C  
ANISOU 5688  C   THR C  75     9670   9251   7927  -1283   -178    -43       C  
ATOM   5689  O   THR C  75      43.496  83.857 -11.757  1.00 75.84           O  
ANISOU 5689  O   THR C  75    10285   9993   8537  -1385   -249     58       O  
ATOM   5690  CB  THR C  75      41.825  85.985 -10.857  1.00 71.01           C  
ANISOU 5690  CB  THR C  75    10049   9166   7767  -1449   -184   -106       C  
ATOM   5691  OG1 THR C  75      41.292  85.299  -9.720  1.00 80.32           O  
ANISOU 5691  OG1 THR C  75    11257  10320   8941  -1438   -144   -111       O  
ATOM   5692  CG2 THR C  75      41.192  87.366 -10.943  1.00 71.48           C  
ANISOU 5692  CG2 THR C  75    10283   9114   7761  -1475   -154   -186       C  
ATOM   5693  N   ASP C  76      41.630  82.739 -12.310  1.00 72.32           N  
ANISOU 5693  N   ASP C  76     9779   9448   8251  -1156   -125    -74       N  
ATOM   5694  CA  ASP C  76      42.296  81.446 -12.366  1.00 74.78           C  
ANISOU 5694  CA  ASP C  76     9925   9844   8645  -1118   -139     -1       C  
ATOM   5695  C   ASP C  76      43.360  81.479 -13.458  1.00 74.34           C  
ANISOU 5695  C   ASP C  76     9769   9870   8609  -1119   -171     51       C  
ATOM   5696  O   ASP C  76      43.024  81.691 -14.636  1.00 73.67           O  
ANISOU 5696  O   ASP C  76     9672   9761   8556  -1043   -144    -11       O  
ATOM   5697  CB  ASP C  76      41.270  80.343 -12.630  1.00 79.16           C  
ANISOU 5697  CB  ASP C  76    10405  10350   9324   -974    -78    -60       C  
ATOM   5698  CG  ASP C  76      41.822  78.947 -12.392  1.00 82.54           C  
ANISOU 5698  CG  ASP C  76    10679  10843   9841   -938    -85     14       C  
ATOM   5699  OD1 ASP C  76      43.058  78.770 -12.445  1.00 83.90           O  
ANISOU 5699  OD1 ASP C  76    10768  11105  10004   -995   -127    109       O  
ATOM   5700  OD2 ASP C  76      41.012  78.023 -12.147  1.00 79.15           O  
ANISOU 5700  OD2 ASP C  76    10204  10371   9498   -852    -47    -15       O  
ATOM   5701  N   PRO C  77      44.637  81.299 -13.124  1.00 74.34           N  
ANISOU 5701  N   PRO C  77     9693   9963   8588  -1205   -227    173       N  
ATOM   5702  CA  PRO C  77      45.674  81.310 -14.170  1.00 75.18           C  
ANISOU 5702  CA  PRO C  77     9694  10150   8722  -1197   -241    236       C  
ATOM   5703  C   PRO C  77      45.530  80.174 -15.168  1.00 79.52           C  
ANISOU 5703  C   PRO C  77    10112  10709   9394  -1047   -177    205       C  
ATOM   5704  O   PRO C  77      45.887  80.339 -16.343  1.00 80.83           O  
ANISOU 5704  O   PRO C  77    10236  10902   9573  -1002   -156    197       O  
ATOM   5705  CB  PRO C  77      46.976  81.202 -13.369  1.00 72.60           C  
ANISOU 5705  CB  PRO C  77     9301   9914   8368  -1321   -314    393       C  
ATOM   5706  CG  PRO C  77      46.569  80.574 -12.063  1.00 71.27           C  
ANISOU 5706  CG  PRO C  77     9155   9725   8201  -1349   -321    406       C  
ATOM   5707  CD  PRO C  77      45.200  81.105 -11.776  1.00 70.28           C  
ANISOU 5707  CD  PRO C  77     9188   9490   8026  -1320   -280    269       C  
ATOM   5708  N   SER C  78      45.030  79.022 -14.728  1.00 78.72           N  
ANISOU 5708  N   SER C  78     9950  10583   9378   -973   -143    190       N  
ATOM   5709  CA  SER C  78      44.836  77.844 -15.567  1.00 76.06           C  
ANISOU 5709  CA  SER C  78     9502  10239   9160   -833    -84    155       C  
ATOM   5710  C   SER C  78      43.577  77.910 -16.425  1.00 79.32           C  
ANISOU 5710  C   SER C  78     9982  10563   9595   -733    -43     17       C  
ATOM   5711  O   SER C  78      43.258  76.925 -17.100  1.00 86.95           O  
ANISOU 5711  O   SER C  78    10880  11505  10652   -623     -1    -27       O  
ATOM   5712  CB  SER C  78      44.779  76.591 -14.689  1.00 68.23           C  
ANISOU 5712  CB  SER C  78     8419   9249   8256   -802    -76    202       C  
ATOM   5713  OG  SER C  78      43.565  76.548 -13.955  1.00 57.70           O  
ANISOU 5713  OG  SER C  78     7169   7837   6919   -789    -69    131       O  
ATOM   5714  N   PHE C  79      42.863  79.036 -16.431  1.00 75.34           N  
ANISOU 5714  N   PHE C  79     9609  10003   9016   -773    -56    -48       N  
ATOM   5715  CA  PHE C  79      41.571  79.087 -17.103  1.00 66.25           C  
ANISOU 5715  CA  PHE C  79     8513   8760   7899   -686    -25   -160       C  
ATOM   5716  C   PHE C  79      41.716  78.961 -18.615  1.00 67.84           C  
ANISOU 5716  C   PHE C  79     8678   8975   8122   -617     -7   -199       C  
ATOM   5717  O   PHE C  79      41.101  78.084 -19.233  1.00 73.66           O  
ANISOU 5717  O   PHE C  79     9380   9670   8938   -518     21   -256       O  
ATOM   5718  CB  PHE C  79      40.830  80.373 -16.739  1.00 62.89           C  
ANISOU 5718  CB  PHE C  79     8230   8269   7398   -745    -35   -204       C  
ATOM   5719  CG  PHE C  79      39.464  80.465 -17.353  1.00 60.30           C  
ANISOU 5719  CG  PHE C  79     7948   7842   7120   -662     -7   -297       C  
ATOM   5720  CD1 PHE C  79      38.389  79.804 -16.779  1.00 57.76           C  
ANISOU 5720  CD1 PHE C  79     7624   7449   6874   -601     22   -328       C  
ATOM   5721  CD2 PHE C  79      39.258  81.189 -18.515  1.00 56.14           C  
ANISOU 5721  CD2 PHE C  79     7458   7298   6573   -649    -13   -339       C  
ATOM   5722  CE1 PHE C  79      37.134  79.873 -17.348  1.00 54.89           C  
ANISOU 5722  CE1 PHE C  79     7290   6996   6571   -529     41   -392       C  
ATOM   5723  CE2 PHE C  79      37.999  81.262 -19.090  1.00 53.05           C  
ANISOU 5723  CE2 PHE C  79     7102   6817   6238   -582      2   -407       C  
ATOM   5724  CZ  PHE C  79      36.937  80.608 -18.506  1.00 51.84           C  
ANISOU 5724  CZ  PHE C  79     6940   6590   6165   -523     27   -430       C  
ATOM   5725  N   LEU C  80      42.522  79.829 -19.235  1.00 68.63           N  
ANISOU 5725  N   LEU C  80     8795   9132   8151   -672    -24   -168       N  
ATOM   5726  CA  LEU C  80      42.679  79.757 -20.686  1.00 74.52           C  
ANISOU 5726  CA  LEU C  80     9517   9895   8901   -611     -1   -203       C  
ATOM   5727  C   LEU C  80      43.229  78.405 -21.116  1.00 70.50           C  
ANISOU 5727  C   LEU C  80     8895   9424   8469   -525     44   -185       C  
ATOM   5728  O   LEU C  80      42.797  77.846 -22.132  1.00 61.86           O  
ANISOU 5728  O   LEU C  80     7799   8297   7409   -438     75   -255       O  
ATOM   5729  CB  LEU C  80      43.591  80.876 -21.189  1.00 82.54           C  
ANISOU 5729  CB  LEU C  80    10554  10979   9828   -689    -25   -150       C  
ATOM   5730  CG  LEU C  80      42.960  82.240 -21.455  1.00 92.90           C  
ANISOU 5730  CG  LEU C  80    11984  12241  11072   -742    -58   -196       C  
ATOM   5731  CD1 LEU C  80      42.723  82.976 -20.147  1.00 99.65           C  
ANISOU 5731  CD1 LEU C  80    12921  13058  11885   -833    -92   -178       C  
ATOM   5732  CD2 LEU C  80      43.830  83.061 -22.394  1.00 97.69           C  
ANISOU 5732  CD2 LEU C  80    12586  12918  11613   -785    -72   -152       C  
ATOM   5733  N   GLY C  81      44.155  77.846 -20.334  1.00 75.42           N  
ANISOU 5733  N   GLY C  81     9427  10107   9123   -551     47    -89       N  
ATOM   5734  CA  GLY C  81      44.680  76.528 -20.656  1.00 77.10           C  
ANISOU 5734  CA  GLY C  81     9526  10344   9426   -464    100    -64       C  
ATOM   5735  C   GLY C  81      43.596  75.471 -20.712  1.00 70.01           C  
ANISOU 5735  C   GLY C  81     8630   9357   8614   -367    122   -153       C  
ATOM   5736  O   GLY C  81      43.542  74.663 -21.643  1.00 62.69           O  
ANISOU 5736  O   GLY C  81     7677   8408   7735   -274    168   -204       O  
ATOM   5737  N   ARG C  82      42.705  75.475 -19.720  1.00 69.24           N  
ANISOU 5737  N   ARG C  82     8571   9204   8535   -389     89   -172       N  
ATOM   5738  CA  ARG C  82      41.617  74.504 -19.701  1.00 67.72           C  
ANISOU 5738  CA  ARG C  82     8374   8924   8432   -305    101   -243       C  
ATOM   5739  C   ARG C  82      40.575  74.808 -20.772  1.00 65.40           C  
ANISOU 5739  C   ARG C  82     8166   8557   8126   -259     96   -349       C  
ATOM   5740  O   ARG C  82      39.943  73.883 -21.295  1.00 68.54           O  
ANISOU 5740  O   ARG C  82     8552   8893   8596   -178    107   -408       O  
ATOM   5741  CB  ARG C  82      40.988  74.475 -18.309  1.00 57.95           C  
ANISOU 5741  CB  ARG C  82     7149   7654   7214   -344     75   -218       C  
ATOM   5742  CG  ARG C  82      41.946  73.972 -17.236  1.00 56.15           C  
ANISOU 5742  CG  ARG C  82     6829   7495   7009   -390     69   -106       C  
ATOM   5743  CD  ARG C  82      41.295  73.941 -15.864  1.00 64.99           C  
ANISOU 5743  CD  ARG C  82     7976   8585   8133   -433     47    -84       C  
ATOM   5744  NE  ARG C  82      41.100  75.275 -15.296  1.00 66.54           N  
ANISOU 5744  NE  ARG C  82     8289   8778   8212   -531     21    -86       N  
ATOM   5745  CZ  ARG C  82      39.954  75.949 -15.334  1.00 68.65           C  
ANISOU 5745  CZ  ARG C  82     8662   8967   8453   -521     28   -164       C  
ATOM   5746  NH1 ARG C  82      38.885  75.420 -15.920  1.00 76.43           N  
ANISOU 5746  NH1 ARG C  82     9644   9875   9521   -425     48   -237       N  
ATOM   5747  NH2 ARG C  82      39.873  77.151 -14.784  1.00 57.68           N  
ANISOU 5747  NH2 ARG C  82     7384   7570   6960   -609     14   -163       N  
ATOM   5748  N   TYR C  83      40.399  76.086 -21.125  1.00 54.98           N  
ANISOU 5748  N   TYR C  83     6932   7241   6717   -315     73   -368       N  
ATOM   5749  CA  TYR C  83      39.438  76.449 -22.162  1.00 58.40           C  
ANISOU 5749  CA  TYR C  83     7440   7609   7139   -284     59   -452       C  
ATOM   5750  C   TYR C  83      39.921  76.032 -23.549  1.00 62.74           C  
ANISOU 5750  C   TYR C  83     7980   8184   7673   -232     84   -487       C  
ATOM   5751  O   TYR C  83      39.120  75.603 -24.390  1.00 53.58           O  
ANISOU 5751  O   TYR C  83     6857   6959   6540   -179     75   -559       O  
ATOM   5752  CB  TYR C  83      39.166  77.952 -22.114  1.00 62.24           C  
ANISOU 5752  CB  TYR C  83     8015   8089   7543   -360     30   -451       C  
ATOM   5753  CG  TYR C  83      38.543  78.502 -23.378  1.00 60.81           C  
ANISOU 5753  CG  TYR C  83     7899   7871   7334   -345     12   -511       C  
ATOM   5754  CD1 TYR C  83      37.302  78.069 -23.812  1.00 68.63           C  
ANISOU 5754  CD1 TYR C  83     8915   8771   8391   -291     -6   -570       C  
ATOM   5755  CD2 TYR C  83      39.197  79.462 -24.130  1.00 61.87           C  
ANISOU 5755  CD2 TYR C  83     8067   8062   7380   -393      5   -497       C  
ATOM   5756  CE1 TYR C  83      36.733  78.570 -24.968  1.00 72.76           C  
ANISOU 5756  CE1 TYR C  83     9496   9262   8889   -290    -35   -612       C  
ATOM   5757  CE2 TYR C  83      38.639  79.970 -25.280  1.00 67.51           C  
ANISOU 5757  CE2 TYR C  83     8839   8747   8066   -387    -17   -543       C  
ATOM   5758  CZ  TYR C  83      37.410  79.519 -25.697  1.00 73.58           C  
ANISOU 5758  CZ  TYR C  83     9633   9426   8897   -338    -39   -599       C  
ATOM   5759  OH  TYR C  83      36.860  80.032 -26.845  1.00 76.13           O  
ANISOU 5759  OH  TYR C  83    10012   9722   9190   -344    -73   -632       O  
ATOM   5760  N   MET C  84      41.224  76.167 -23.813  1.00 67.98           N  
ANISOU 5760  N   MET C  84     8599   8940   8290   -252    116   -431       N  
ATOM   5761  CA  MET C  84      41.768  75.751 -25.102  1.00 68.91           C  
ANISOU 5761  CA  MET C  84     8711   9086   8387   -196    162   -459       C  
ATOM   5762  C   MET C  84      41.767  74.232 -25.239  1.00 69.63           C  
ANISOU 5762  C   MET C  84     8749   9139   8569   -102    207   -489       C  
ATOM   5763  O   MET C  84      41.539  73.701 -26.333  1.00 72.13           O  
ANISOU 5763  O   MET C  84     9108   9420   8881    -42    232   -562       O  
ATOM   5764  CB  MET C  84      43.184  76.306 -25.270  1.00 70.60           C  
ANISOU 5764  CB  MET C  84     8878   9409   8539   -238    194   -372       C  
ATOM   5765  CG  MET C  84      43.273  77.829 -25.310  1.00 71.16           C  
ANISOU 5765  CG  MET C  84     9008   9515   8514   -333    147   -343       C  
ATOM   5766  SD  MET C  84      43.030  78.557 -26.937  1.00 73.79           S  
ANISOU 5766  SD  MET C  84     9427   9851   8758   -328    147   -406       S  
ATOM   5767  CE  MET C  84      41.251  78.661 -27.019  1.00 72.45           C  
ANISOU 5767  CE  MET C  84     9352   9558   8618   -316     87   -506       C  
ATOM   5768  N   SER C  85      42.022  73.515 -24.140  1.00 67.89           N  
ANISOU 5768  N   SER C  85     8443   8922   8431    -93    215   -433       N  
ATOM   5769  CA  SER C  85      41.953  72.057 -24.173  1.00 68.21           C  
ANISOU 5769  CA  SER C  85     8429   8913   8574     -4    254   -457       C  
ATOM   5770  C   SER C  85      40.537  71.580 -24.456  1.00 71.51           C  
ANISOU 5770  C   SER C  85     8914   9220   9037     35    211   -554       C  
ATOM   5771  O   SER C  85      40.332  70.648 -25.243  1.00 68.41           O  
ANISOU 5771  O   SER C  85     8540   8771   8681    107    235   -619       O  
ATOM   5772  CB  SER C  85      42.451  71.478 -22.857  1.00 68.22           C  
ANISOU 5772  CB  SER C  85     8320   8943   8657    -16    259   -363       C  
ATOM   5773  OG  SER C  85      43.800  71.835 -22.650  1.00 78.86           O  
ANISOU 5773  OG  SER C  85     9595  10392   9976    -56    290   -257       O  
ATOM   5774  N   ALA C  86      39.546  72.201 -23.814  1.00 71.69           N  
ANISOU 5774  N   ALA C  86     8976   9203   9059    -12    150   -559       N  
ATOM   5775  CA  ALA C  86      38.165  71.825 -24.078  1.00 69.51           C  
ANISOU 5775  CA  ALA C  86     8752   8822   8836     20    103   -629       C  
ATOM   5776  C   ALA C  86      37.779  72.162 -25.511  1.00 65.28           C  
ANISOU 5776  C   ALA C  86     8311   8257   8235     27     85   -705       C  
ATOM   5777  O   ALA C  86      37.093  71.376 -26.175  1.00 52.70           O  
ANISOU 5777  O   ALA C  86     6755   6586   6684     73     63   -769       O  
ATOM   5778  CB  ALA C  86      37.232  72.521 -23.086  1.00 68.91           C  
ANISOU 5778  CB  ALA C  86     8693   8712   8775    -28     59   -604       C  
ATOM   5779  N   LEU C  87      38.219  73.326 -26.006  1.00 70.69           N  
ANISOU 5779  N   LEU C  87     9041   9004   8814    -26     87   -694       N  
ATOM   5780  CA  LEU C  87      37.894  73.733 -27.371  1.00 71.91           C  
ANISOU 5780  CA  LEU C  87     9287   9141   8895    -31     66   -756       C  
ATOM   5781  C   LEU C  87      38.464  72.761 -28.394  1.00 68.11           C  
ANISOU 5781  C   LEU C  87     8822   8660   8397     33    118   -807       C  
ATOM   5782  O   LEU C  87      37.927  72.637 -29.501  1.00 59.19           O  
ANISOU 5782  O   LEU C  87     7781   7483   7226     41     91   -877       O  
ATOM   5783  CB  LEU C  87      38.417  75.147 -27.638  1.00 69.25           C  
ANISOU 5783  CB  LEU C  87     8981   8880   8451   -100     64   -720       C  
ATOM   5784  CG  LEU C  87      38.015  75.800 -28.966  1.00 62.55           C  
ANISOU 5784  CG  LEU C  87     8225   8020   7519   -123     31   -767       C  
ATOM   5785  CD1 LEU C  87      36.508  75.861 -29.099  1.00 62.58           C  
ANISOU 5785  CD1 LEU C  87     8282   7922   7575   -131    -48   -803       C  
ATOM   5786  CD2 LEU C  87      38.606  77.189 -29.094  1.00 62.75           C  
ANISOU 5786  CD2 LEU C  87     8265   8123   7452   -193     30   -718       C  
ATOM   5787  N   ASN C  88      39.540  72.058 -28.038  1.00 72.91           N  
ANISOU 5787  N   ASN C  88     9350   9315   9036     76    194   -770       N  
ATOM   5788  CA  ASN C  88      40.128  71.083 -28.946  1.00 77.04           C  
ANISOU 5788  CA  ASN C  88     9889   9828   9553    149    267   -818       C  
ATOM   5789  C   ASN C  88      39.194  69.907 -29.203  1.00 77.75           C  
ANISOU 5789  C   ASN C  88    10023   9801   9719    201    236   -898       C  
ATOM   5790  O   ASN C  88      39.282  69.267 -30.256  1.00 81.74           O  
ANISOU 5790  O   ASN C  88    10602  10266  10189    247    270   -972       O  
ATOM   5791  CB  ASN C  88      41.459  70.598 -28.375  1.00 79.06           C  
ANISOU 5791  CB  ASN C  88    10029  10154   9854    185    358   -739       C  
ATOM   5792  CG  ASN C  88      42.336  69.966 -29.414  1.00 87.22           C  
ANISOU 5792  CG  ASN C  88    11080  11202  10856    257    463   -769       C  
ATOM   5793  OD1 ASN C  88      42.251  68.766 -29.668  1.00 93.17           O  
ANISOU 5793  OD1 ASN C  88    11843  11883  11673    333    505   -822       O  
ATOM   5794  ND2 ASN C  88      43.182  70.774 -30.041  1.00 95.67           N  
ANISOU 5794  ND2 ASN C  88    12161  12361  11827    235    512   -735       N  
ATOM   5795  N   HIS C  89      38.303  69.601 -28.263  1.00 74.50           N  
ANISOU 5795  N   HIS C  89     9572   9329   9407    194    172   -882       N  
ATOM   5796  CA  HIS C  89      37.313  68.547 -28.439  1.00 71.65           C  
ANISOU 5796  CA  HIS C  89     9245   8850   9127    233    124   -944       C  
ATOM   5797  C   HIS C  89      35.962  69.073 -28.906  1.00 76.41           C  
ANISOU 5797  C   HIS C  89     9936   9386   9712    184     18   -981       C  
ATOM   5798  O   HIS C  89      35.339  68.467 -29.784  1.00 82.47           O  
ANISOU 5798  O   HIS C  89    10787  10070  10477    197    -26  -1051       O  
ATOM   5799  CB  HIS C  89      37.128  67.763 -27.135  1.00 71.33           C  
ANISOU 5799  CB  HIS C  89     9096   8780   9224    259    119   -891       C  
ATOM   5800  CG  HIS C  89      38.283  66.874 -26.788  1.00 76.40           C  
ANISOU 5800  CG  HIS C  89     9649   9456   9922    319    211   -857       C  
ATOM   5801  ND1 HIS C  89      39.461  67.353 -26.254  1.00 77.15           N  
ANISOU 5801  ND1 HIS C  89     9662   9660   9990    303    274   -773       N  
ATOM   5802  CD2 HIS C  89      38.436  65.532 -26.888  1.00 77.90           C  
ANISOU 5802  CD2 HIS C  89     9816   9581  10203    393    248   -885       C  
ATOM   5803  CE1 HIS C  89      40.291  66.347 -26.046  1.00 75.98           C  
ANISOU 5803  CE1 HIS C  89     9433   9515   9920    367    349   -742       C  
ATOM   5804  NE2 HIS C  89      39.693  65.230 -26.421  1.00 77.47           N  
ANISOU 5804  NE2 HIS C  89     9657   9596  10181    426    340   -814       N  
ATOM   5805  N   THR C  90      35.489  70.184 -28.330  1.00 74.59           N  
ANISOU 5805  N   THR C  90     9689   9182   9470    125    -26   -929       N  
ATOM   5806  CA  THR C  90      34.158  70.684 -28.665  1.00 72.20           C  
ANISOU 5806  CA  THR C  90     9446   8808   9177     83   -122   -941       C  
ATOM   5807  C   THR C  90      34.076  71.130 -30.118  1.00 80.92           C  
ANISOU 5807  C   THR C  90    10664   9912  10170     53   -152   -996       C  
ATOM   5808  O   THR C  90      32.998  71.068 -30.723  1.00 86.09           O  
ANISOU 5808  O   THR C  90    11382  10487  10840     28   -241  -1021       O  
ATOM   5809  CB  THR C  90      33.754  71.830 -27.726  1.00 64.15           C  
ANISOU 5809  CB  THR C  90     8389   7815   8172     35   -140   -872       C  
ATOM   5810  OG1 THR C  90      34.652  72.934 -27.877  1.00 65.15           O  
ANISOU 5810  OG1 THR C  90     8528   8036   8188     -6    -98   -850       O  
ATOM   5811  CG2 THR C  90      33.769  71.368 -26.274  1.00 61.72           C  
ANISOU 5811  CG2 THR C  90     7984   7506   7962     58   -112   -818       C  
ATOM   5812  N   LYS C  91      35.194  71.569 -30.701  1.00 80.74           N  
ANISOU 5812  N   LYS C  91    10666   9978  10035     49    -84  -1006       N  
ATOM   5813  CA  LYS C  91      35.182  71.950 -32.107  1.00 74.36           C  
ANISOU 5813  CA  LYS C  91     9969   9176   9107     20   -104  -1058       C  
ATOM   5814  C   LYS C  91      35.007  70.746 -33.016  1.00 69.28           C  
ANISOU 5814  C   LYS C  91     9411   8457   8453     59   -110  -1144       C  
ATOM   5815  O   LYS C  91      34.685  70.917 -34.195  1.00 74.46           O  
ANISOU 5815  O   LYS C  91    10183   9092   9016     24   -154  -1193       O  
ATOM   5816  CB  LYS C  91      36.472  72.685 -32.472  1.00 76.84           C  
ANISOU 5816  CB  LYS C  91    10280   9608   9307     11    -19  -1037       C  
ATOM   5817  CG  LYS C  91      37.700  71.780 -32.496  1.00 81.28           C  
ANISOU 5817  CG  LYS C  91    10806  10211   9867     84     98  -1050       C  
ATOM   5818  CD  LYS C  91      38.986  72.561 -32.753  1.00 80.71           C  
ANISOU 5818  CD  LYS C  91    10707  10261   9700     73    182  -1003       C  
ATOM   5819  CE  LYS C  91      40.180  71.630 -32.901  1.00 83.19           C  
ANISOU 5819  CE  LYS C  91    10981  10607  10020    154    308  -1006       C  
ATOM   5820  NZ  LYS C  91      41.449  72.384 -33.085  1.00 87.96           N  
ANISOU 5820  NZ  LYS C  91    11540  11333  10550    144    390   -936       N  
ATOM   5821  N   LYS C  92      35.198  69.537 -32.494  1.00 70.16           N  
ANISOU 5821  N   LYS C  92     9476   8523   8657    125    -70  -1161       N  
ATOM   5822  CA  LYS C  92      34.995  68.306 -33.242  1.00 74.56           C  
ANISOU 5822  CA  LYS C  92    10121   8990   9220    164    -76  -1247       C  
ATOM   5823  C   LYS C  92      33.598  67.722 -33.053  1.00 75.52           C  
ANISOU 5823  C   LYS C  92    10260   8990   9446    144   -201  -1255       C  
ATOM   5824  O   LYS C  92      33.272  66.712 -33.688  1.00 79.83           O  
ANISOU 5824  O   LYS C  92    10891   9441   9998    162   -231  -1327       O  
ATOM   5825  CB  LYS C  92      36.054  67.279 -32.831  1.00 77.90           C  
ANISOU 5825  CB  LYS C  92    10480   9423   9694    253     45  -1256       C  
ATOM   5826  CG  LYS C  92      37.477  67.722 -33.144  1.00 85.27           C  
ANISOU 5826  CG  LYS C  92    11395  10470  10534    279    175  -1239       C  
ATOM   5827  CD  LYS C  92      38.502  66.742 -32.586  1.00 95.71           C  
ANISOU 5827  CD  LYS C  92    12625  11803  11940    367    294  -1219       C  
ATOM   5828  CE  LYS C  92      39.925  67.252 -32.771  1.00 98.53           C  
ANISOU 5828  CE  LYS C  92    12933  12278  12225    390    421  -1169       C  
ATOM   5829  NZ  LYS C  92      40.917  66.381 -32.081  1.00 99.41           N  
ANISOU 5829  NZ  LYS C  92    12924  12405  12442    470    531  -1117       N  
ATOM   5830  N   TRP C  93      32.773  68.331 -32.206  1.00 69.77           N  
ANISOU 5830  N   TRP C  93     9454   8255   8800    108   -270  -1180       N  
ATOM   5831  CA  TRP C  93      31.419  67.861 -31.953  1.00 67.99           C  
ANISOU 5831  CA  TRP C  93     9223   7919   8690     89   -386  -1162       C  
ATOM   5832  C   TRP C  93      30.462  68.320 -33.051  1.00 70.02           C  
ANISOU 5832  C   TRP C  93     9592   8124   8889     14   -504  -1179       C  
ATOM   5833  O   TRP C  93      30.781  69.172 -33.886  1.00 69.13           O  
ANISOU 5833  O   TRP C  93     9552   8069   8647    -29   -499  -1195       O  
ATOM   5834  CB  TRP C  93      30.933  68.356 -30.594  1.00 68.67           C  
ANISOU 5834  CB  TRP C  93     9183   8020   8889     86   -395  -1068       C  
ATOM   5835  CG  TRP C  93      31.598  67.676 -29.445  1.00 73.26           C  
ANISOU 5835  CG  TRP C  93     9655   8628   9551    148   -313  -1041       C  
ATOM   5836  CD1 TRP C  93      32.403  66.576 -29.496  1.00 74.45           C  
ANISOU 5836  CD1 TRP C  93     9797   8771   9719    209   -247  -1085       C  
ATOM   5837  CD2 TRP C  93      31.522  68.054 -28.066  1.00 72.35           C  
ANISOU 5837  CD2 TRP C  93     9428   8550   9514    152   -287   -959       C  
ATOM   5838  NE1 TRP C  93      32.832  66.242 -28.233  1.00 72.81           N  
ANISOU 5838  NE1 TRP C  93     9465   8598   9600    246   -191  -1025       N  
ATOM   5839  CE2 TRP C  93      32.303  67.134 -27.336  1.00 70.70           C  
ANISOU 5839  CE2 TRP C  93     9139   8360   9362    208   -216   -950       C  
ATOM   5840  CE3 TRP C  93      30.866  69.077 -27.375  1.00 69.56           C  
ANISOU 5840  CE3 TRP C  93     9038   8208   9183    113   -310   -891       C  
ATOM   5841  CZ2 TRP C  93      32.447  67.209 -25.955  1.00 65.34           C  
ANISOU 5841  CZ2 TRP C  93     8352   7720   8752    216   -181   -875       C  
ATOM   5842  CZ3 TRP C  93      31.013  69.149 -26.000  1.00 67.09           C  
ANISOU 5842  CZ3 TRP C  93     8630   7929   8933    127   -263   -827       C  
ATOM   5843  CH2 TRP C  93      31.797  68.223 -25.307  1.00 65.74           C  
ANISOU 5843  CH2 TRP C  93     8387   7785   8807    173   -205   -818       C  
ATOM   5844  N   LYS C  94      29.268  67.733 -33.040  1.00 78.44           N  
ANISOU 5844  N   LYS C  94    10666   9080  10057     -7   -619  -1162       N  
ATOM   5845  CA  LYS C  94      28.189  68.094 -33.952  1.00 83.35           C  
ANISOU 5845  CA  LYS C  94    11374   9639  10656    -88   -756  -1150       C  
ATOM   5846  C   LYS C  94      27.085  68.792 -33.171  1.00 79.57           C  
ANISOU 5846  C   LYS C  94    10794   9135  10305   -117   -824  -1036       C  
ATOM   5847  O   LYS C  94      26.708  68.338 -32.085  1.00 78.68           O  
ANISOU 5847  O   LYS C  94    10575   8989  10331    -75   -815   -985       O  
ATOM   5848  CB  LYS C  94      27.633  66.861 -34.669  1.00 86.53           C  
ANISOU 5848  CB  LYS C  94    11878   9923  11076   -103   -850  -1210       C  
ATOM   5849  CG  LYS C  94      28.599  66.220 -35.647  1.00 93.54           C  
ANISOU 5849  CG  LYS C  94    12903  10816  11822    -81   -783  -1331       C  
ATOM   5850  CD  LYS C  94      28.866  67.139 -36.825  1.00103.09           C  
ANISOU 5850  CD  LYS C  94    14231  12086  12853   -145   -792  -1361       C  
ATOM   5851  CE  LYS C  94      29.958  66.584 -37.721  1.00113.19           C  
ANISOU 5851  CE  LYS C  94    15641  13385  13981   -109   -689  -1478       C  
ATOM   5852  NZ  LYS C  94      31.275  66.562 -37.026  1.00114.64           N  
ANISOU 5852  NZ  LYS C  94    15729  13662  14168    -14   -512  -1483       N  
ATOM   5853  N   TYR C  95      26.575  69.898 -33.719  1.00 77.27           N  
ANISOU 5853  N   TYR C  95    10533   8859   9969   -185   -886   -990       N  
ATOM   5854  CA  TYR C  95      25.560  70.722 -33.060  1.00 71.65           C  
ANISOU 5854  CA  TYR C  95     9728   8121   9374   -208   -932   -876       C  
ATOM   5855  C   TYR C  95      24.338  70.809 -33.968  1.00 71.79           C  
ANISOU 5855  C   TYR C  95     9800   8052   9424   -289  -1091   -827       C  
ATOM   5856  O   TYR C  95      24.125  71.825 -34.646  1.00 69.08           O  
ANISOU 5856  O   TYR C  95     9495   7733   9018   -351  -1134   -793       O  
ATOM   5857  CB  TYR C  95      26.113  72.106 -32.724  1.00 71.85           C  
ANISOU 5857  CB  TYR C  95     9720   8244   9338   -213   -846   -845       C  
ATOM   5858  CG  TYR C  95      27.354  72.022 -31.869  1.00 73.28           C  
ANISOU 5858  CG  TYR C  95     9851   8511   9480   -150   -706   -882       C  
ATOM   5859  CD1 TYR C  95      27.263  71.918 -30.487  1.00 78.02           C  
ANISOU 5859  CD1 TYR C  95    10344   9111  10189   -102   -648   -832       C  
ATOM   5860  CD2 TYR C  95      28.615  72.006 -32.445  1.00 72.18           C  
ANISOU 5860  CD2 TYR C  95     9772   8455   9199   -140   -633   -957       C  
ATOM   5861  CE1 TYR C  95      28.396  71.821 -29.705  1.00 79.97           C  
ANISOU 5861  CE1 TYR C  95    10546   9438  10401    -58   -535   -854       C  
ATOM   5862  CE2 TYR C  95      29.751  71.908 -31.672  1.00 74.68           C  
ANISOU 5862  CE2 TYR C  95    10031   8850   9493    -89   -515   -971       C  
ATOM   5863  CZ  TYR C  95      29.638  71.816 -30.306  1.00 77.16           C  
ANISOU 5863  CZ  TYR C  95    10241   9163   9915    -53   -473   -918       C  
ATOM   5864  OH  TYR C  95      30.774  71.718 -29.540  1.00 77.31           O  
ANISOU 5864  OH  TYR C  95    10204   9261   9910    -16   -370   -919       O  
ATOM   5865  N   PRO C  96      23.504  69.768 -33.991  1.00 76.01           N  
ANISOU 5865  N   PRO C  96    10334   8483  10065   -296  -1191   -809       N  
ATOM   5866  CA  PRO C  96      22.332  69.780 -34.870  1.00 75.70           C  
ANISOU 5866  CA  PRO C  96    10345   8356  10062   -386  -1361   -749       C  
ATOM   5867  C   PRO C  96      21.248  70.706 -34.352  1.00 78.34           C  
ANISOU 5867  C   PRO C  96    10565   8662  10539   -407  -1404   -600       C  
ATOM   5868  O   PRO C  96      21.061  70.872 -33.145  1.00 74.29           O  
ANISOU 5868  O   PRO C  96     9929   8153  10147   -342  -1325   -539       O  
ATOM   5869  CB  PRO C  96      21.856  68.325 -34.840  1.00 74.88           C  
ANISOU 5869  CB  PRO C  96    10259   8147  10044   -379  -1443   -769       C  
ATOM   5870  CG  PRO C  96      22.272  67.841 -33.506  1.00 71.75           C  
ANISOU 5870  CG  PRO C  96     9745   7772   9745   -278  -1323   -770       C  
ATOM   5871  CD  PRO C  96      23.587  68.521 -33.211  1.00 75.28           C  
ANISOU 5871  CD  PRO C  96    10189   8344  10070   -229  -1161   -834       C  
ATOM   5872  N   GLN C  97      20.515  71.297 -35.292  1.00 88.37           N  
ANISOU 5872  N   GLN C  97    11881   9899  11794   -499  -1529   -535       N  
ATOM   5873  CA  GLN C  97      19.366  72.137 -34.968  1.00 87.89           C  
ANISOU 5873  CA  GLN C  97    11714   9793  11887   -524  -1583   -377       C  
ATOM   5874  C   GLN C  97      18.158  71.229 -34.771  1.00 86.79           C  
ANISOU 5874  C   GLN C  97    11515   9535  11925   -541  -1710   -282       C  
ATOM   5875  O   GLN C  97      17.486  70.845 -35.730  1.00 92.22           O  
ANISOU 5875  O   GLN C  97    12271  10154  12614   -633  -1877   -248       O  
ATOM   5876  CB  GLN C  97      19.118  73.161 -36.068  1.00 92.16           C  
ANISOU 5876  CB  GLN C  97    12317  10352  12347   -620  -1668   -332       C  
ATOM   5877  CG  GLN C  97      20.193  74.228 -36.191  1.00 94.92           C  
ANISOU 5877  CG  GLN C  97    12703  10817  12547   -606  -1547   -395       C  
ATOM   5878  CD  GLN C  97      20.204  75.195 -35.024  1.00100.18           C  
ANISOU 5878  CD  GLN C  97    13246  11511  13307   -538  -1418   -331       C  
ATOM   5879  OE1 GLN C  97      21.262  75.506 -34.473  1.00105.15           O  
ANISOU 5879  OE1 GLN C  97    13875  12224  13851   -482  -1278   -407       O  
ATOM   5880  NE2 GLN C  97      19.026  75.684 -34.646  1.00 98.19           N  
ANISOU 5880  NE2 GLN C  97    12894  11185  13230   -546  -1462   -186       N  
ATOM   5881  N   VAL C  98      17.888  70.874 -33.524  1.00 83.58           N  
ANISOU 5881  N   VAL C  98    10984