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***  TRANSCRIPTION 02-MAY-14 4D1M  ***

elNémo ID: 21041520510080514

Job options:

ID        	=	 21041520510080514
JOBID     	=	 TRANSCRIPTION 02-MAY-14 4D1M
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 3
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER    TRANSCRIPTION                           02-MAY-14   4D1M              
TITLE     TETRAMERIZATION DOMAIN OF ZEBRAFISH P53 (CRYSTAL FORM II)             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;                                
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 FRAGMENT: TETRAMERIZATION DOMAIN, RESIDUES 302-346;                  
COMPND   5 SYNONYM: P53;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DANIO RERIO;                                    
SOURCE   3 ORGANISM_COMMON: ZEBRAFISH;                                          
SOURCE   4 ORGANISM_TAXID: 7955;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSCRIPTION, P53 FAMILY, TUMOR SUPPRESSOR, TRANSCRIPTION FACTOR,    
KEYWDS   2 TETRAMER, PROTEIN EVOLUTION                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.JOERGER                                                           
REVDAT   5   22-MAY-19 4D1M    1       REMARK                                   
REVDAT   4   08-MAY-19 4D1M    1       REMARK                                   
REVDAT   3   17-SEP-14 4D1M    1       JRNL                                     
REVDAT   2   03-SEP-14 4D1M    1       TITLE                                    
REVDAT   1   27-AUG-14 4D1M    0                                                
JRNL        AUTH   A.C.JOERGER,R.WILCKEN,A.ANDREEVA                             
JRNL        TITL   TRACING THE EVOLUTION OF THE P53 TETRAMERIZATION DOMAIN      
JRNL        REF    STRUCTURE                     V.  22  1301 2014              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   25185827                                                     
JRNL        DOI    10.1016/J.STR.2014.07.010                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 33164                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1744                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2398                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2820                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 129                          
REMARK   3   BIN FREE R VALUE                    : 0.3220                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3964                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 59                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.20000                                              
REMARK   3    B22 (A**2) : -0.14000                                             
REMARK   3    B33 (A**2) : -1.13000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.29000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.246         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.219         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.181         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.086        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4002 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  3970 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5356 ; 1.336 ; 1.999       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9135 ; 0.777 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   464 ; 4.824 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   219 ;32.097 ;23.881       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   815 ;17.220 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    48 ;19.387 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   596 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4394 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   878 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1893 ; 1.626 ; 2.848       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1892 ; 1.625 ; 2.847       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2346 ; 2.369 ; 4.251       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2109 ; 2.057 ; 3.167       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 36                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   303        A   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.3590  44.7800 -12.3350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3145 T22:   0.1876                                     
REMARK   3      T33:   0.2695 T12:   0.0131                                     
REMARK   3      T13:  -0.0307 T23:  -0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8904 L22:   3.3103                                     
REMARK   3      L33:  30.2075 L12:   1.0746                                     
REMARK   3      L13:  -8.5699 L23:   0.7983                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0475 S12:  -0.7133 S13:  -0.0090                       
REMARK   3      S21:   0.2988 S22:  -0.2382 S23:  -0.1372                       
REMARK   3      S31:  -0.5372 S32:   0.8915 S33:   0.1907                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   312        A   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8560  36.3030 -16.9470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2815 T22:   0.1982                                     
REMARK   3      T33:   0.1982 T12:   0.2281                                     
REMARK   3      T13:  -0.1210 T23:  -0.0551                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.8252 L22:  15.4930                                     
REMARK   3      L33:  27.9017 L12:  11.8748                                     
REMARK   3      L13: -18.1248 L23: -18.8088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2597 S12:   0.3088 S13:  -0.1044                       
REMARK   3      S21:  -0.5817 S22:  -0.2622 S23:   0.6362                       
REMARK   3      S31:  -0.2959 S32:  -0.4183 S33:   0.0025                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   332        A   340                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3260  21.5950  -8.0070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0540 T22:   0.1677                                     
REMARK   3      T33:   0.3293 T12:  -0.0086                                     
REMARK   3      T13:  -0.0020 T23:   0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.5631 L22:  17.4960                                     
REMARK   3      L33:  20.0311 L12:   6.4624                                     
REMARK   3      L13:   7.1890 L23:   0.8577                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1152 S12:   0.0629 S13:  -0.8491                       
REMARK   3      S21:   0.0254 S22:   0.0561 S23:   0.5847                       
REMARK   3      S31:   0.8598 S32:  -0.3633 S33:  -0.1713                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   303        B   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8170  45.1320 -15.5290              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3604 T22:   0.2315                                     
REMARK   3      T33:   0.1370 T12:   0.0605                                     
REMARK   3      T13:  -0.0253 T23:  -0.1391                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5663 L22:  22.7648                                     
REMARK   3      L33:  22.9445 L12:   0.8575                                     
REMARK   3      L13:   0.5003 L23: -22.6495                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5499 S12:  -0.2625 S13:   0.2298                       
REMARK   3      S21:   0.1355 S22:   0.5398 S23:   0.0722                       
REMARK   3      S31:  -0.3100 S32:  -0.6622 S33:   0.0101                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   312        B   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.2970  36.7440 -14.0030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1280 T22:   0.0814                                     
REMARK   3      T33:   0.0725 T12:  -0.0544                                     
REMARK   3      T13:  -0.0248 T23:  -0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.1527 L22:   3.9353                                     
REMARK   3      L33:  13.9542 L12:   0.6721                                     
REMARK   3      L13: -12.1830 L23:   0.3194                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2168 S12:  -0.4657 S13:   0.0710                       
REMARK   3      S21:   0.1528 S22:  -0.0560 S23:   0.0224                       
REMARK   3      S31:  -0.1909 S32:   0.4822 S33:  -0.1608                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   332        B   342                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8220  28.7400 -25.6420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4425 T22:   0.3528                                     
REMARK   3      T33:   0.2506 T12:  -0.0162                                     
REMARK   3      T13:   0.1408 T23:  -0.0923                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2122 L22:  24.1305                                     
REMARK   3      L33:  16.3456 L12:   4.5320                                     
REMARK   3      L13:  -1.0087 L23:  -3.8613                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4674 S12:   0.0171 S13:  -0.8608                       
REMARK   3      S21:  -1.6948 S22:  -0.5749 S23:  -1.2845                       
REMARK   3      S31:   1.0901 S32:   1.3310 S33:   0.1075                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   302        C   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.2940  17.3150 -18.0100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2224 T22:   0.2268                                     
REMARK   3      T33:   0.4391 T12:  -0.1348                                     
REMARK   3      T13:   0.0195 T23:   0.1103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  20.4226 L22:   4.7968                                     
REMARK   3      L33:   9.5316 L12:  -7.1773                                     
REMARK   3      L13:  11.1847 L23:  -1.2471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2989 S12:  -0.4276 S13:  -1.1996                       
REMARK   3      S21:   0.1849 S22:   0.0836 S23:   0.4555                       
REMARK   3      S31:   0.4079 S32:  -0.1381 S33:  -0.3825                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   312        C   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6250  27.6790 -22.8720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1419 T22:   0.1609                                     
REMARK   3      T33:   0.1003 T12:   0.0500                                     
REMARK   3      T13:  -0.0275 T23:  -0.0369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  25.2453 L22:   2.9246                                     
REMARK   3      L33:   6.3009 L12:   6.1887                                     
REMARK   3      L13:   9.3702 L23:   3.8578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1772 S12:   0.7601 S13:  -0.7885                       
REMARK   3      S21:  -0.2150 S22:  -0.0353 S23:  -0.0663                       
REMARK   3      S31:  -0.0829 S32:   0.3457 S33:  -0.1419                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   332        C   341                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.9750  40.0030 -18.4010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2685 T22:   0.2329                                     
REMARK   3      T33:   0.2614 T12:  -0.1397                                     
REMARK   3      T13:   0.0817 T23:  -0.1043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.7451 L22:  11.6489                                     
REMARK   3      L33:  26.0309 L12:  -4.8493                                     
REMARK   3      L13:  11.1938 L23: -13.9267                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0644 S12:   0.2019 S13:   0.9208                       
REMARK   3      S21:   0.3674 S22:  -0.2162 S23:  -0.4501                       
REMARK   3      S31:  -1.4821 S32:   0.6394 S33:   0.2806                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   303        D   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0110  18.4290 -22.9930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1586 T22:   0.1887                                     
REMARK   3      T33:   0.4890 T12:  -0.0235                                     
REMARK   3      T13:   0.0158 T23:  -0.1587                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  30.4148 L22:   4.3684                                     
REMARK   3      L33:  22.1480 L12:   4.9865                                     
REMARK   3      L13:  23.0149 L23:  -0.2743                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0152 S12:   0.2001 S13:  -0.7601                       
REMARK   3      S21:  -0.3140 S22:  -0.1020 S23:  -0.5138                       
REMARK   3      S31:   0.3634 S32:   0.1918 S33:   0.0869                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   312        D   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.5910  24.5620 -13.6410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1028 T22:   0.1376                                     
REMARK   3      T33:   0.1541 T12:  -0.0470                                     
REMARK   3      T13:  -0.0218 T23:   0.0695                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  25.2841 L22:   5.5874                                     
REMARK   3      L33:   2.5454 L12:   0.0732                                     
REMARK   3      L13:  -3.5768 L23:   0.7858                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2049 S12:  -1.0037 S13:  -0.9691                       
REMARK   3      S21:   0.2983 S22:  -0.1022 S23:  -0.1534                       
REMARK   3      S31:   0.0898 S32:   0.0767 S33:   0.3071                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   332        D   341                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.6110  33.7510 -11.0180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1486 T22:   0.3384                                     
REMARK   3      T33:   0.6324 T12:   0.1275                                     
REMARK   3      T13:   0.0350 T23:   0.0768                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.6238 L22:  19.9814                                     
REMARK   3      L33:  27.0134 L12:   2.0679                                     
REMARK   3      L13:   7.2035 L23:   5.4012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6704 S12:  -0.1371 S13:   0.8811                       
REMARK   3      S21:  -0.5497 S22:   0.8377 S23:   1.7903                       
REMARK   3      S31:  -1.4566 S32:  -0.5700 S33:  -0.1673                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   303        E   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6660  21.0480   6.5800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4087 T22:   0.4190                                     
REMARK   3      T33:   0.3418 T12:  -0.1436                                     
REMARK   3      T13:  -0.0007 T23:  -0.0553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.8263 L22:   2.6449                                     
REMARK   3      L33:  25.8760 L12:  -1.2480                                     
REMARK   3      L13: -21.1463 L23:  -1.1870                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0313 S12:   0.4601 S13:   0.1251                       
REMARK   3      S21:  -0.2206 S22:  -0.4629 S23:  -0.4967                       
REMARK   3      S31:  -0.3342 S32:  -0.0007 S33:   0.4316                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   312        E   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.2360  10.0910  10.4500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0591 T22:   0.5344                                     
REMARK   3      T33:   0.1446 T12:  -0.1472                                     
REMARK   3      T13:  -0.0231 T23:  -0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0755 L22:  27.1658                                     
REMARK   3      L33:  20.4129 L12: -10.4949                                     
REMARK   3      L13:  -7.2034 L23:  18.9779                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2189 S12:  -0.1271 S13:   0.0983                       
REMARK   3      S21:   0.6099 S22:   0.1417 S23:  -0.1905                       
REMARK   3      S31:   0.1522 S32:   0.9077 S33:   0.0772                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   332        E   344                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.1070  -9.5480   4.4280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3696 T22:   0.4090                                     
REMARK   3      T33:   0.4465 T12:  -0.1009                                     
REMARK   3      T13:  -0.1170 T23:   0.0962                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1149 L22:  19.2225                                     
REMARK   3      L33:  30.2763 L12:  -2.1715                                     
REMARK   3      L13: -11.9111 L23:  -2.4412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8539 S12:  -0.2716 S13:  -1.2099                       
REMARK   3      S21:   0.7936 S22:  -0.0015 S23:   0.5350                       
REMARK   3      S31:   2.3440 S32:  -1.2299 S33:   0.8554                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   303        F   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8350  18.7510  10.3480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0754 T22:   0.4399                                     
REMARK   3      T33:   0.3426 T12:  -0.1336                                     
REMARK   3      T13:  -0.0714 T23:  -0.0510                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8710 L22:  16.6329                                     
REMARK   3      L33:  31.0779 L12:  -3.2786                                     
REMARK   3      L13:  -8.3020 L23:  12.9517                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0885 S12:  -0.4679 S13:   0.2369                       
REMARK   3      S21:   0.1219 S22:   0.5009 S23:  -0.8929                       
REMARK   3      S31:   0.1758 S32:   0.5606 S33:  -0.4124                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   312        F   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2960  19.4520   4.4770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2644 T22:   0.1525                                     
REMARK   3      T33:   0.1224 T12:  -0.1486                                     
REMARK   3      T13:   0.0601 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.9225 L22:  12.9655                                     
REMARK   3      L33:  12.0043 L12: -12.6002                                     
REMARK   3      L13: -11.3809 L23:   8.3441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6064 S12:   0.3911 S13:   0.5832                       
REMARK   3      S21:  -0.9260 S22:  -0.1719 S23:  -0.5985                       
REMARK   3      S31:  -0.7970 S32:   0.0492 S33:  -0.4345                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   332        F   343                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2800  26.6350   7.3150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1834 T22:   0.2234                                     
REMARK   3      T33:   0.2756 T12:   0.0650                                     
REMARK   3      T13:   0.0715 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5203 L22:  13.2652                                     
REMARK   3      L33:  27.1319 L12:   1.0678                                     
REMARK   3      L13:   1.4135 L23:   3.0583                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4385 S12:   0.7377 S13:   0.1485                       
REMARK   3      S21:  -0.4088 S22:  -0.4015 S23:   0.9213                       
REMARK   3      S31:  -0.0709 S32:  -0.9188 S33:  -0.0370                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   302        G   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0670   3.7190   5.0760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4878 T22:   0.2531                                     
REMARK   3      T33:   0.7546 T12:  -0.0264                                     
REMARK   3      T13:  -0.3181 T23:  -0.1333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.7977 L22:  11.7620                                     
REMARK   3      L33:  13.0259 L12:  -4.4311                                     
REMARK   3      L13:   3.0668 L23:   6.7867                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6715 S12:   0.3389 S13:  -0.2622                       
REMARK   3      S21:  -0.8370 S22:  -1.2627 S23:   2.0867                       
REMARK   3      S31:   1.2491 S32:  -1.0608 S33:   0.5912                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   312        G   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2350  13.4230  10.7920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0729 T22:   0.2704                                     
REMARK   3      T33:   0.1633 T12:  -0.0322                                     
REMARK   3      T13:   0.0075 T23:  -0.0964                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5621 L22:  25.0512                                     
REMARK   3      L33:  11.3562 L12:  -8.3195                                     
REMARK   3      L13:   3.9968 L23: -15.9326                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0428 S12:  -0.3345 S13:  -0.2276                       
REMARK   3      S21:   0.8515 S22:   0.1987 S23:   0.5428                       
REMARK   3      S31:  -0.7180 S32:  -0.1853 S33:  -0.1559                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   332        G   341                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.6780  32.1590   3.6770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2131 T22:   0.2194                                     
REMARK   3      T33:   0.3360 T12:  -0.0626                                     
REMARK   3      T13:   0.0154 T23:   0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2076 L22:  13.7425                                     
REMARK   3      L33:  20.4095 L12:   0.9027                                     
REMARK   3      L13:  -1.6242 L23:   1.4363                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1286 S12:  -0.0701 S13:   0.0110                       
REMARK   3      S21:   0.4857 S22:  -0.1064 S23:  -0.1836                       
REMARK   3      S31:  -1.1944 S32:   0.7257 S33:  -0.0222                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   303        H   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.4600   4.7590   9.9800              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1018 T22:   0.2426                                     
REMARK   3      T33:   0.3728 T12:  -0.0617                                     
REMARK   3      T13:   0.0072 T23:  -0.0455                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0821 L22:  22.5535                                     
REMARK   3      L33:  35.6645 L12:  -8.0846                                     
REMARK   3      L13:  10.6380 L23: -20.9880                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0833 S12:  -0.5499 S13:  -0.1410                       
REMARK   3      S21:   0.8190 S22:  -0.0589 S23:   1.2582                       
REMARK   3      S31:  -0.8804 S32:  -0.5934 S33:  -0.0243                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   312        H   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9800   4.6120   3.7650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1540 T22:   0.1870                                     
REMARK   3      T33:   0.1461 T12:   0.0007                                     
REMARK   3      T13:  -0.0936 T23:  -0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  24.9973 L22:  19.6576                                     
REMARK   3      L33:   8.1057 L12: -18.8922                                     
REMARK   3      L13:   7.5815 L23:  -8.5088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5347 S12:   0.2687 S13:  -0.7261                       
REMARK   3      S21:  -0.9434 S22:  -0.4390 S23:   0.7256                       
REMARK   3      S31:  -0.1450 S32:   0.3499 S33:  -0.0957                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   332        H   342                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.0730  -2.4800   6.5450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0503 T22:   0.3211                                     
REMARK   3      T33:   0.2195 T12:   0.0598                                     
REMARK   3      T13:  -0.0691 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2025 L22:  14.0682                                     
REMARK   3      L33:  31.2941 L12:   1.8501                                     
REMARK   3      L13:  -6.8358 L23:  -5.6347                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0453 S12:   0.4204 S13:   0.1085                       
REMARK   3      S21:  -0.1839 S22:   0.0405 S23:  -0.2685                       
REMARK   3      S31:   0.0796 S32:   1.5057 S33:   0.0049                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   303        I   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7650   7.2860 -20.2520              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3908 T22:   0.1248                                     
REMARK   3      T33:   0.2816 T12:  -0.0346                                     
REMARK   3      T13:  -0.1048 T23:   0.0563                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  21.5967 L22:   7.3014                                     
REMARK   3      L33:  12.7354 L12:  -4.3704                                     
REMARK   3      L13: -12.2151 L23:   5.0964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2570 S12:   0.1741 S13:   1.6454                       
REMARK   3      S21:   0.1224 S22:  -0.1571 S23:  -0.1907                       
REMARK   3      S31:  -0.9292 S32:  -0.1952 S33:  -0.0999                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   312        I   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.5700  -3.1630 -24.4380              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3022 T22:   0.1010                                     
REMARK   3      T33:   0.1001 T12:   0.0338                                     
REMARK   3      T13:   0.0196 T23:   0.0312                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  24.4890 L22:   5.1930                                     
REMARK   3      L33:   5.0999 L12:  10.2642                                     
REMARK   3      L13:  -8.4229 L23:  -3.1627                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3606 S12:   0.2179 S13:   0.6369                       
REMARK   3      S21:  -0.2884 S22:   0.3194 S23:   0.2405                       
REMARK   3      S31:   0.1690 S32:   0.0015 S33:   0.0412                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   332        I   341                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.2800 -16.5560 -19.9370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2304 T22:   0.2241                                     
REMARK   3      T33:   0.1704 T12:  -0.0426                                     
REMARK   3      T13:   0.0296 T23:   0.0620                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.5150 L22:  25.2345                                     
REMARK   3      L33:   8.8748 L12:  -5.4775                                     
REMARK   3      L13:  -3.9935 L23:   6.4749                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0076 S12:   0.4702 S13:  -0.8490                       
REMARK   3      S21:  -0.2246 S22:   0.1252 S23:   0.3970                       
REMARK   3      S31:   0.5147 S32:  -0.2964 S33:  -0.1175                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J   303        J   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4590   6.1480 -24.1350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2661 T22:   0.0535                                     
REMARK   3      T33:   0.2821 T12:   0.0049                                     
REMARK   3      T13:  -0.0789 T23:   0.0397                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  29.2027 L22:   6.1711                                     
REMARK   3      L33:  22.1261 L12:   6.6847                                     
REMARK   3      L13: -22.2569 L23:  -5.4304                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1987 S12:   0.3428 S13:   0.6852                       
REMARK   3      S21:  -0.0254 S22:   0.0722 S23:   0.1362                       
REMARK   3      S31:   0.1091 S32:  -0.1644 S33:   0.1264                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J   312        J   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.6740   0.0450 -15.1580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3184 T22:   0.0865                                     
REMARK   3      T33:   0.1000 T12:  -0.0242                                     
REMARK   3      T13:  -0.0209 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  24.3896 L22:   3.9945                                     
REMARK   3      L33:   4.6149 L12:  -1.3967                                     
REMARK   3      L13:  -1.0776 L23:   0.5121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0354 S12:  -0.6247 S13:   0.2411                       
REMARK   3      S21:   0.1998 S22:  -0.0830 S23:   0.1831                       
REMARK   3      S31:  -0.3297 S32:   0.3061 S33:   0.1183                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J   332        J   340                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7530  -8.6470 -13.0230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2494 T22:   0.4136                                     
REMARK   3      T33:   0.4408 T12:   0.1754                                     
REMARK   3      T13:   0.1117 T23:   0.0144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0628 L22:  21.6689                                     
REMARK   3      L33:  16.7841 L12:   1.4047                                     
REMARK   3      L13:   0.1739 L23:  -7.1847                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2722 S12:   0.2904 S13:  -1.2603                       
REMARK   3      S21:  -0.5334 S22:   0.2177 S23:  -0.9228                       
REMARK   3      S31:   1.0763 S32:   0.4556 S33:   0.0545                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   302        K   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.4120 -20.4480 -13.9110              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2644 T22:   0.2733                                     
REMARK   3      T33:   0.2499 T12:  -0.0194                                     
REMARK   3      T13:   0.0373 T23:   0.0073                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5317 L22:   5.3865                                     
REMARK   3      L33:  27.3327 L12:  -1.2627                                     
REMARK   3      L13:   6.9947 L23:   0.2340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1076 S12:  -0.4398 S13:  -0.0111                       
REMARK   3      S21:   0.2741 S22:  -0.0842 S23:   0.0794                       
REMARK   3      S31:   0.3647 S32:  -0.5383 S33:  -0.0234                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   312        K   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6640 -11.5010 -18.7870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5135 T22:   0.2000                                     
REMARK   3      T33:   0.0892 T12:   0.2118                                     
REMARK   3      T13:   0.1396 T23:   0.0439                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.9977 L22:  10.0649                                     
REMARK   3      L33:  19.9931 L12:  10.1501                                     
REMARK   3      L13:  16.3288 L23:  13.8695                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0861 S12:   0.5459 S13:  -0.4306                       
REMARK   3      S21:  -0.1837 S22:   0.7426 S23:  -0.5412                       
REMARK   3      S31:  -0.0326 S32:   1.0520 S33:  -0.6565                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   332        K   341                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9520   3.7830  -9.8320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2416 T22:   0.2148                                     
REMARK   3      T33:   0.6555 T12:   0.0031                                     
REMARK   3      T13:  -0.1179 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9112 L22:  12.7147                                     
REMARK   3      L33:  15.9635 L12:   5.3447                                     
REMARK   3      L13:  -9.6333 L23:  -5.0536                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0967 S12:  -0.1178 S13:   0.7678                       
REMARK   3      S21:  -0.5469 S22:   0.0264 S23:  -1.1136                       
REMARK   3      S31:  -1.1021 S32:   0.1846 S33:  -0.1231                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   303        L   311                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.2650 -20.3950 -17.6710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2106 T22:   0.1617                                     
REMARK   3      T33:   0.2094 T12:   0.0522                                     
REMARK   3      T13:   0.0540 T23:   0.0809                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9603 L22:  13.7207                                     
REMARK   3      L33:  42.8295 L12:   6.2792                                     
REMARK   3      L13:  11.1795 L23:  19.1507                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0207 S12:   0.0299 S13:  -0.4054                       
REMARK   3      S21:   0.0297 S22:  -0.0981 S23:  -0.3576                       
REMARK   3      S31:   0.0583 S32:   0.8057 S33:   0.1189                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   312        L   331                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2530 -12.7160 -15.9100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3220 T22:   0.0487                                     
REMARK   3      T33:   0.0774 T12:   0.0216                                     
REMARK   3      T13:   0.0734 T23:   0.0371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  18.3908 L22:   2.3136                                     
REMARK   3      L33:  18.2894 L12:   0.9824                                     
REMARK   3      L13:  14.5045 L23:   0.0558                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1769 S12:  -0.5698 S13:  -0.1323                       
REMARK   3      S21:   0.3609 S22:  -0.0848 S23:   0.0567                       
REMARK   3      S31:   0.5791 S32:  -0.5284 S33:  -0.0921                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   332        L   341                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.3450  -5.4510 -27.5940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6678 T22:   0.3667                                     
REMARK   3      T33:   0.3360 T12:   0.1189                                     
REMARK   3      T13:  -0.1581 T23:   0.1345                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  22.5735 L22:   8.4199                                     
REMARK   3      L33:  24.6283 L12:  -6.2420                                     
REMARK   3      L13:  -9.9290 L23:   5.6095                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4220 S12:   1.1173 S13:   1.2612                       
REMARK   3      S21:  -1.5611 S22:  -0.6451 S23:   0.6739                       
REMARK   3      S31:  -2.0118 S32:  -1.5751 S33:   0.2231                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4D1M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290060336.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34925                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP VAPOR DIFFUSION AT 20       
REMARK 280  DEGREE C; PROTEIN SOLUTION: 12 MG/ML IN 20 MM TRIS PH 7.5, 50 MM    
REMARK 280  NACL, 5 MM DTT; CRYSTALLIZATION BUFFER: 160 MM ZINC ACETATE, 80     
REMARK 280  MM SODIUM CACODYLATE, PH 6.5, 12% (W/V) POLYETHYLENE GLYCOL 8,      
REMARK 280  000 AND 19% (W/V) GLYCEROL, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 293K                                                    
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       37.25350            
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                                                 
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.7 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.3 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A   299                                                      
REMARK 465     GLY A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     GLU A   302                                                      
REMARK 465     GLN A   341                                                      
REMARK 465     LYS A   342                                                      
REMARK 465     PHE A   343                                                      
REMARK 465     MET A   344                                                      
REMARK 465     THR A   345                                                      
REMARK 465     LYS A   346                                                      
REMARK 465     GLY B   299                                                      
REMARK 465     GLY B   300                                                      
REMARK 465     SER B   301                                                      
REMARK 465     GLU B   302                                                      
REMARK 465     PHE B   343                                                      
REMARK 465     MET B   344                                                      
REMARK 465     THR B   345                                                      
REMARK 465     LYS B   346                                                      
REMARK 465     GLY C   299                                                      
REMARK 465     GLY C   300                                                      
REMARK 465     SER C   301                                                      
REMARK 465     LYS C   342                                                      
REMARK 465     PHE C   343                                                      
REMARK 465     MET C   344                                                      
REMARK 465     THR C   345                                                      
REMARK 465     LYS C   346                                                      
REMARK 465     GLY D   299                                                      
REMARK 465     GLY D   300                                                      
REMARK 465     SER D   301                                                      
REMARK 465     GLU D   302                                                      
REMARK 465     LYS D   342                                                      
REMARK 465     PHE D   343                                                      
REMARK 465     MET D   344                                                      
REMARK 465     THR D   345                                                      
REMARK 465     LYS D   346                                                      
REMARK 465     GLY E   299                                                      
REMARK 465     GLY E   300                                                      
REMARK 465     SER E   301                                                      
REMARK 465     GLU E   302                                                      
REMARK 465     THR E   345                                                      
REMARK 465     LYS E   346                                                      
REMARK 465     GLY F   299                                                      
REMARK 465     GLY F   300                                                      
REMARK 465     SER F   301                                                      
REMARK 465     GLU F   302                                                      
REMARK 465     MET F   344                                                      
REMARK 465     THR F   345                                                      
REMARK 465     LYS F   346                                                      
REMARK 465     GLY G   299                                                      
REMARK 465     GLY G   300                                                      
REMARK 465     SER G   301                                                      
REMARK 465     LYS G   342                                                      
REMARK 465     PHE G   343                                                      
REMARK 465     MET G   344                                                      
REMARK 465     THR G   345                                                      
REMARK 465     LYS G   346                                                      
REMARK 465     GLY H   299                                                      
REMARK 465     GLY H   300                                                      
REMARK 465     SER H   301                                                      
REMARK 465     GLU H   302                                                      
REMARK 465     PHE H   343                                                      
REMARK 465     MET H   344                                                      
REMARK 465     THR H   345                                                      
REMARK 465     LYS H   346                                                      
REMARK 465     GLY I   299                                                      
REMARK 465     GLY I   300                                                      
REMARK 465     SER I   301                                                      
REMARK 465     GLU I   302                                                      
REMARK 465     LYS I   342                                                      
REMARK 465     PHE I   343                                                      
REMARK 465     MET I   344                                                      
REMARK 465     THR I   345                                                      
REMARK 465     LYS I   346                                                      
REMARK 465     GLY J   299                                                      
REMARK 465     GLY J   300                                                      
REMARK 465     SER J   301                                                      
REMARK 465     GLU J   302                                                      
REMARK 465     LYS J   342                                                      
REMARK 465     PHE J   343                                                      
REMARK 465     MET J   344                                                      
REMARK 465     THR J   345                                                      
REMARK 465     LYS J   346                                                      
REMARK 465     GLY K   299                                                      
REMARK 465     GLY K   300                                                      
REMARK 465     SER K   301                                                      
REMARK 465     LYS K   342                                                      
REMARK 465     PHE K   343                                                      
REMARK 465     MET K   344                                                      
REMARK 465     THR K   345                                                      
REMARK 465     LYS K   346                                                      
REMARK 465     GLY L   299                                                      
REMARK 465     GLY L   300                                                      
REMARK 465     SER L   301                                                      
REMARK 465     GLU L   302                                                      
REMARK 465     LYS L   342                                                      
REMARK 465     PHE L   343                                                      
REMARK 465     MET L   344                                                      
REMARK 465     THR L   345                                                      
REMARK 465     LYS L   346                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN G 341    CA   C    O    CB   CG   CD   OE1                   
REMARK 470     GLN G 341    NE2                                                 
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    ARG L 340        9.92    -63.86                                   
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 B1343  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU L 303   OE2                                                    
REMARK 620 2 GLU B 303   OE2 130.3                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 1344                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1343                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4D1L   RELATED DB: PDB                                   
REMARK 900 P53 A CRYSTAL FORM I                                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 ADDITIONAL GGS SEQUENCE AT THE N TERMINUS AS A RESULT OF             
REMARK 999 CLONING STRATEGY                                                     
DBREF  4D1M A  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
DBREF  4D1M B  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
DBREF  4D1M C  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
DBREF  4D1M D  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
DBREF  4D1M E  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
DBREF  4D1M F  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
DBREF  4D1M G  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
DBREF  4D1M H  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
DBREF  4D1M I  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
DBREF  4D1M J  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
DBREF  4D1M K  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
DBREF  4D1M L  302   346  UNP    G1K2L5   G1K2L5_DANRE   302    346             
SEQADV 4D1M GLY A  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY A  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER A  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY B  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY B  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER B  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY C  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY C  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER C  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY D  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY D  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER D  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY E  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY E  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER E  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY F  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY F  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER F  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY G  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY G  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER G  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY H  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY H  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER H  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY I  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY I  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER I  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY J  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY J  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER J  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY K  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY K  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER K  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY L  299  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M GLY L  300  UNP  G1K2L5              EXPRESSION TAG                 
SEQADV 4D1M SER L  301  UNP  G1K2L5              EXPRESSION TAG                 
SEQRES   1 A   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 A   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 A   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 A   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
SEQRES   1 B   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 B   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 B   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 B   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
SEQRES   1 C   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 C   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 C   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 C   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
SEQRES   1 D   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 D   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 D   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 D   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
SEQRES   1 E   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 E   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 E   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 E   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
SEQRES   1 F   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 F   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 F   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 F   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
SEQRES   1 G   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 G   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 G   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 G   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
SEQRES   1 H   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 H   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 H   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 H   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
SEQRES   1 I   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 I   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 I   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 I   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
SEQRES   1 J   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 J   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 J   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 J   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
SEQRES   1 K   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 K   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 K   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 K   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
SEQRES   1 L   48  GLY GLY SER GLU GLU ILE PHE THR LEU GLN VAL ARG GLY          
SEQRES   2 L   48  ARG GLU ARG TYR GLU ILE LEU LYS LYS LEU ASN ASP SER          
SEQRES   3 L   48  LEU GLU LEU SER ASP VAL VAL PRO ALA SER ASP ALA GLU          
SEQRES   4 L   48  LYS TYR ARG GLN LYS PHE MET THR LYS                          
HET     ZN  B1343       1                                                       
HET     ZN  F1344       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  13   ZN    2(ZN 2+)                                                     
FORMUL  15  HOH   *59(H2 O)                                                     
HELIX    1   1 GLY A  311  VAL A  331  1                                  21    
HELIX    2   2 PRO A  332  ARG A  340  1                                   9    
HELIX    3   3 GLY B  311  VAL B  331  1                                  21    
HELIX    4   4 PRO B  332  LYS B  342  1                                  11    
HELIX    5   5 GLY C  311  VAL C  331  1                                  21    
HELIX    6   6 PRO C  332  GLN C  341  1                                  10    
HELIX    7   7 GLY D  311  VAL D  331  1                                  21    
HELIX    8   8 PRO D  332  GLN D  341  1                                  10    
HELIX    9   9 GLY E  311  VAL E  331  1                                  21    
HELIX   10  10 PRO E  332  PHE E  343  1                                  12    
HELIX   11  11 GLY F  311  ASP F  329  1                                  19    
HELIX   12  12 PRO F  332  PHE F  343  1                                  12    
HELIX   13  13 GLY G  311  VAL G  331  1                                  21    
HELIX   14  14 PRO G  332  ARG G  340  1                                   9    
HELIX   15  15 GLY H  311  ASP H  329  1                                  19    
HELIX   16  16 PRO H  332  LYS H  342  1                                  11    
HELIX   17  17 GLY I  311  ASP I  329  1                                  19    
HELIX   18  18 PRO I  332  ARG I  340  1                                   9    
HELIX   19  19 GLY J  311  VAL J  331  1                                  21    
HELIX   20  20 PRO J  332  GLN J  341  1                                  10    
HELIX   21  21 GLY K  311  VAL K  331  1                                  21    
HELIX   22  22 PRO K  332  GLN K  341  1                                  10    
HELIX   23  23 GLY L  311  VAL L  331  1                                  21    
HELIX   24  24 PRO L  332  ARG L  340  1                                   9    
SHEET    1  AA 2 ILE A 304  ARG A 310  0                                        
SHEET    2  AA 2 ILE B 304  ARG B 310 -1  O  PHE B 305   N  VAL A 309           
SHEET    1  CA 2 ILE C 304  ARG C 310  0                                        
SHEET    2  CA 2 ILE D 304  ARG D 310 -1  O  PHE D 305   N  VAL C 309           
SHEET    1  EA 2 ILE E 304  ARG E 310  0                                        
SHEET    2  EA 2 ILE F 304  ARG F 310 -1  O  PHE F 305   N  VAL E 309           
SHEET    1  GA 2 ILE G 304  ARG G 310  0                                        
SHEET    2  GA 2 ILE H 304  ARG H 310 -1  O  PHE H 305   N  VAL G 309           
SHEET    1  IA 2 ILE I 304  ARG I 310  0                                        
SHEET    2  IA 2 ILE J 304  ARG J 310 -1  O  PHE J 305   N  VAL I 309           
SHEET    1  KA 2 ILE K 304  ARG K 310  0                                        
SHEET    2  KA 2 ILE L 304  ARG L 310 -1  O  PHE L 305   N  VAL K 309           
LINK        ZN    ZN B1343                 OE2 GLU L 303     1555   1565  2.19  
LINK        ZN    ZN B1343                 OE2 GLU B 303     1555   1555  2.22  
LINK        ZN    ZN F1344                 OD1 ASP F 335     1555   1555  2.47  
SITE     1 AC1  1 ASP F 335                                                     
SITE     1 AC2  2 GLU B 303  GLU L 303                                          
CRYST1   70.861   74.507   74.945  90.00 117.79  90.00 P 1 21 1     24          
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      0.014112  0.000000  0.007437        0.00000                         
SCALE2      0.000000  0.013422  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015083        0.00000                         
ATOM      1  N   GLU A 303      16.048  43.217  -0.692  1.00 67.06           N  
ANISOU    1  N   GLU A 303     9986   8487   7004   -669    551   -724       N  
ATOM      2  CA  GLU A 303      17.367  43.811  -1.104  1.00 67.98           C  
ANISOU    2  CA  GLU A 303    10084   8518   7227   -520    274   -562       C  
ATOM      3  C   GLU A 303      17.531  43.770  -2.637  1.00 64.15           C  
ANISOU    3  C   GLU A 303     9400   7947   7025   -357    216   -526       C  
ATOM      4  O   GLU A 303      17.612  42.700  -3.229  1.00 60.42           O  
ANISOU    4  O   GLU A 303     8954   7389   6611   -345    285   -397       O  
ATOM      5  CB  GLU A 303      18.550  43.088  -0.426  1.00 71.89           C  
ANISOU    5  CB  GLU A 303    10691   9134   7486   -484    130   -254       C  
ATOM      6  CG  GLU A 303      19.237  43.865   0.699  1.00 77.44           C  
ANISOU    6  CG  GLU A 303    11403  10159   7860   -691    -33   -274       C  
ATOM      7  CD  GLU A 303      20.678  43.402   0.960  1.00 83.37           C  
ANISOU    7  CD  GLU A 303    11936  11468   8271   -528   -282     57       C  
ATOM      8  OE1 GLU A 303      20.880  42.351   1.621  1.00 85.62           O  
ANISOU    8  OE1 GLU A 303    12380  11887   8264   -182   -243    363       O  
ATOM      9  OE2 GLU A 303      21.618  44.091   0.492  1.00 84.63           O  
ANISOU    9  OE2 GLU A 303    11780  12024   8350   -711   -477     23       O  
ATOM     10  N   ILE A 304      17.592  44.945  -3.254  1.00 61.72           N  
ANISOU   10  N   ILE A 304     9063   7575   6813   -242    160   -642       N  
ATOM     11  CA  ILE A 304      17.592  45.069  -4.700  1.00 60.12           C  
ANISOU   11  CA  ILE A 304     8707   7302   6831    -58    124   -630       C  
ATOM     12  C   ILE A 304      19.023  45.316  -5.198  1.00 57.84           C  
ANISOU   12  C   ILE A 304     8446   6934   6595   -155    -61   -494       C  
ATOM     13  O   ILE A 304      19.688  46.263  -4.765  1.00 55.83           O  
ANISOU   13  O   ILE A 304     8398   6669   6145   -392    -97   -571       O  
ATOM     14  CB  ILE A 304      16.624  46.182  -5.146  1.00 63.23           C  
ANISOU   14  CB  ILE A 304     9151   7709   7164    299    265   -802       C  
ATOM     15  CG1 ILE A 304      15.202  45.805  -4.705  1.00 66.67           C  
ANISOU   15  CG1 ILE A 304     9287   8609   7433    409    443   -941       C  
ATOM     16  CG2 ILE A 304      16.692  46.404  -6.655  1.00 62.28           C  
ANISOU   16  CG2 ILE A 304     8925   7543   7193    548    213   -755       C  
ATOM     17  CD1 ILE A 304      14.214  46.951  -4.729  1.00 72.12           C  
ANISOU   17  CD1 ILE A 304    10012   9520   7868   1033    640  -1051       C  
ATOM     18  N   PHE A 305      19.490  44.426  -6.085  1.00 52.49           N  
ANISOU   18  N   PHE A 305     7592   6269   6082    -64   -118   -325       N  
ATOM     19  CA  PHE A 305      20.772  44.583  -6.727  1.00 51.56           C  
ANISOU   19  CA  PHE A 305     7355   6254   5979    -94   -265   -201       C  
ATOM     20  C   PHE A 305      20.523  44.949  -8.164  1.00 50.38           C  
ANISOU   20  C   PHE A 305     7203   5877   6059      3   -235   -270       C  
ATOM     21  O   PHE A 305      19.451  44.670  -8.722  1.00 49.74           O  
ANISOU   21  O   PHE A 305     7092   5711   6095    152   -133   -342       O  
ATOM     22  CB  PHE A 305      21.581  43.295  -6.634  1.00 53.06           C  
ANISOU   22  CB  PHE A 305     7425   6655   6079    147   -288    104       C  
ATOM     23  CG  PHE A 305      21.783  42.824  -5.224  1.00 55.89           C  
ANISOU   23  CG  PHE A 305     7845   7280   6111    217   -299    247       C  
ATOM     24  CD1 PHE A 305      20.811  42.059  -4.588  1.00 55.11           C  
ANISOU   24  CD1 PHE A 305     8086   6884   5968    249    -88    244       C  
ATOM     25  CD2 PHE A 305      22.931  43.174  -4.524  1.00 59.04           C  
ANISOU   25  CD2 PHE A 305     7941   8354   6136    160   -504    356       C  
ATOM     26  CE1 PHE A 305      20.983  41.649  -3.282  1.00 58.68           C  
ANISOU   26  CE1 PHE A 305     8696   7526   6074    339    -74    393       C  
ATOM     27  CE2 PHE A 305      23.111  42.761  -3.216  1.00 62.10           C  
ANISOU   27  CE2 PHE A 305     8353   9109   6134    283   -540    515       C  
ATOM     28  CZ  PHE A 305      22.137  41.996  -2.599  1.00 62.53           C  
ANISOU   28  CZ  PHE A 305     8869   8677   6212    433   -322    557       C  
ATOM     29  N   THR A 306      21.506  45.583  -8.775  1.00 51.37           N  
ANISOU   29  N   THR A 306     7323   6039   6154   -152   -312   -271       N  
ATOM     30  CA  THR A 306      21.364  45.993 -10.165  1.00 51.15           C  
ANISOU   30  CA  THR A 306     7384   5756   6293    -51   -271   -316       C  
ATOM     31  C   THR A 306      22.541  45.513 -11.012  1.00 50.37           C  
ANISOU   31  C   THR A 306     7033   5848   6257   -109   -351   -175       C  
ATOM     32  O   THR A 306      23.681  45.516 -10.570  1.00 53.47           O  
ANISOU   32  O   THR A 306     7193   6697   6424   -324   -439   -112       O  
ATOM     33  CB  THR A 306      21.135  47.512 -10.297  1.00 53.22           C  
ANISOU   33  CB  THR A 306     8184   5671   6364   -138   -129   -504       C  
ATOM     34  OG1 THR A 306      22.112  48.214  -9.547  1.00 57.06           O  
ANISOU   34  OG1 THR A 306     8901   6258   6521   -718   -102   -620       O  
ATOM     35  CG2 THR A 306      19.765  47.880  -9.773  1.00 54.84           C  
ANISOU   35  CG2 THR A 306     8598   5749   6487    258     14   -583       C  
ATOM     36  N   LEU A 307      22.233  45.082 -12.229  1.00 48.36           N  
ANISOU   36  N   LEU A 307     6754   5397   6222     92   -307   -131       N  
ATOM     37  CA  LEU A 307      23.213  44.498 -13.140  1.00 49.35           C  
ANISOU   37  CA  LEU A 307     6688   5648   6414    146   -315     12       C  
ATOM     38  C   LEU A 307      23.219  45.315 -14.440  1.00 46.61           C  
ANISOU   38  C   LEU A 307     6509   5052   6148     39   -291    -97       C  
ATOM     39  O   LEU A 307      22.146  45.659 -14.952  1.00 44.42           O  
ANISOU   39  O   LEU A 307     6429   4513   5933    200   -248   -180       O  
ATOM     40  CB  LEU A 307      22.789  43.048 -13.434  1.00 50.62           C  
ANISOU   40  CB  LEU A 307     6898   5657   6677    428   -172    155       C  
ATOM     41  CG  LEU A 307      23.815  41.920 -13.455  1.00 56.89           C  
ANISOU   41  CG  LEU A 307     7667   6601   7345    785    -54    438       C  
ATOM     42  CD1 LEU A 307      24.602  41.860 -12.163  1.00 60.48           C  
ANISOU   42  CD1 LEU A 307     7893   7591   7496    982   -154    612       C  
ATOM     43  CD2 LEU A 307      23.141  40.566 -13.668  1.00 57.72           C  
ANISOU   43  CD2 LEU A 307     8272   6242   7415    927    273    510       C  
ATOM     44  N   GLN A 308      24.405  45.611 -14.969  1.00 46.71           N  
ANISOU   44  N   GLN A 308     6405   5277   6063   -194   -301    -86       N  
ATOM     45  CA  GLN A 308      24.540  46.234 -16.306  1.00 48.50           C  
ANISOU   45  CA  GLN A 308     6870   5223   6332   -315   -230   -163       C  
ATOM     46  C   GLN A 308      24.756  45.151 -17.372  1.00 44.63           C  
ANISOU   46  C   GLN A 308     6154   4754   6049    -46   -199    -14       C  
ATOM     47  O   GLN A 308      25.718  44.403 -17.287  1.00 46.27           O  
ANISOU   47  O   GLN A 308     6022   5362   6194     67   -179    134       O  
ATOM     48  CB  GLN A 308      25.717  47.214 -16.337  1.00 54.73           C  
ANISOU   48  CB  GLN A 308     7748   6259   6787   -946   -168   -312       C  
ATOM     49  CG  GLN A 308      25.651  48.291 -15.259  1.00 62.92           C  
ANISOU   49  CG  GLN A 308     9219   7217   7470  -1425    -82   -518       C  
ATOM     50  CD  GLN A 308      24.673  49.384 -15.613  1.00 67.45           C  
ANISOU   50  CD  GLN A 308    10732   6936   7958  -1279    142   -627       C  
ATOM     51  OE1 GLN A 308      23.452  49.214 -15.489  1.00 66.58           O  
ANISOU   51  OE1 GLN A 308    10708   6561   8029   -626    115   -535       O  
ATOM     52  NE2 GLN A 308      25.203  50.520 -16.066  1.00 73.84           N  
ANISOU   52  NE2 GLN A 308    12303   7379   8370  -1857    428   -819       N  
ATOM     53  N   VAL A 309      23.872  45.085 -18.364  1.00 41.53           N  
ANISOU   53  N   VAL A 309     5966   4019   5795    106   -159    -45       N  
ATOM     54  CA  VAL A 309      23.892  44.039 -19.388  1.00 41.36           C  
ANISOU   54  CA  VAL A 309     5887   3928   5898    232    -61     37       C  
ATOM     55  C   VAL A 309      24.106  44.663 -20.762  1.00 42.10           C  
ANISOU   55  C   VAL A 309     6140   3859   5994    130    -41    -15       C  
ATOM     56  O   VAL A 309      23.369  45.579 -21.145  1.00 43.88           O  
ANISOU   56  O   VAL A 309     6625   3919   6126    184    -83    -92       O  
ATOM     57  CB  VAL A 309      22.549  43.255 -19.397  1.00 40.34           C  
ANISOU   57  CB  VAL A 309     5819   3734   5771    281      0    -16       C  
ATOM     58  CG1 VAL A 309      22.573  42.105 -20.398  1.00 40.17           C  
ANISOU   58  CG1 VAL A 309     5954   3563   5745    201    215      4       C  
ATOM     59  CG2 VAL A 309      22.234  42.738 -18.009  1.00 40.41           C  
ANISOU   59  CG2 VAL A 309     5803   3826   5724    313     26      8       C  
ATOM     60  N   ARG A 310      25.131  44.200 -21.481  1.00 43.96           N  
ANISOU   60  N   ARG A 310     6269   4174   6259     90     59     57       N  
ATOM     61  CA  ARG A 310      25.433  44.676 -22.857  1.00 44.59           C  
ANISOU   61  CA  ARG A 310     6525   4090   6324    -56    116      7       C  
ATOM     62  C   ARG A 310      24.632  43.935 -23.922  1.00 43.38           C  
ANISOU   62  C   ARG A 310     6505   3744   6234     44    184      7       C  
ATOM     63  O   ARG A 310      24.768  42.718 -24.065  1.00 44.70           O  
ANISOU   63  O   ARG A 310     6674   3873   6436    117    362     69       O  
ATOM     64  CB  ARG A 310      26.897  44.468 -23.169  1.00 47.41           C  
ANISOU   64  CB  ARG A 310     6612   4789   6610   -168    229     62       C  
ATOM     65  CG  ARG A 310      27.782  45.319 -22.300  1.00 54.84           C  
ANISOU   65  CG  ARG A 310     7327   6209   7299   -550    177    -23       C  
ATOM     66  CD  ARG A 310      29.240  44.917 -22.371  1.00 60.13           C  
ANISOU   66  CD  ARG A 310     7395   7708   7741   -584    265     47       C  
ATOM     67  NE  ARG A 310      30.001  45.844 -21.544  1.00 67.93           N  
ANISOU   67  NE  ARG A 310     8107   9380   8322  -1233    215   -128       N  
ATOM     68  CZ  ARG A 310      30.397  47.061 -21.922  1.00 70.49           C  
ANISOU   68  CZ  ARG A 310     8762   9677   8342  -2105    332   -411       C  
ATOM     69  NH1 ARG A 310      30.141  47.528 -23.145  1.00 69.24           N  
ANISOU   69  NH1 ARG A 310     9207   8825   8274  -2266    477   -490       N  
ATOM     70  NH2 ARG A 310      31.068  47.812 -21.068  1.00 75.70           N  
ANISOU   70  NH2 ARG A 310     9244  11018   8499  -2895    357   -633       N  
ATOM     71  N   GLY A 311      23.813  44.664 -24.675  1.00 42.54           N  
ANISOU   71  N   GLY A 311     6596   3549   6017     64    101    -57       N  
ATOM     72  CA  GLY A 311      23.082  44.084 -25.809  1.00 39.80           C  
ANISOU   72  CA  GLY A 311     6272   3270   5579     27    135    -96       C  
ATOM     73  C   GLY A 311      21.676  43.709 -25.416  1.00 40.18           C  
ANISOU   73  C   GLY A 311     6109   3711   5445     42     56   -180       C  
ATOM     74  O   GLY A 311      21.457  43.119 -24.360  1.00 40.29           O  
ANISOU   74  O   GLY A 311     6017   3780   5511    -32    101   -207       O  
ATOM     75  N   ARG A 312      20.726  44.034 -26.278  1.00 47.18           N  
ANISOU   75  N   ARG A 312     9249   4965   3710   3507   -627     52       N  
ATOM     76  CA  ARG A 312      19.303  43.809 -26.037  1.00 48.51           C  
ANISOU   76  CA  ARG A 312     9089   5289   4052   3685   -793    179       C  
ATOM     77  C   ARG A 312      18.985  42.302 -25.862  1.00 49.46           C  
ANISOU   77  C   ARG A 312     8967   5628   4196   3400  -1141      4       C  
ATOM     78  O   ARG A 312      18.287  41.919 -24.948  1.00 50.97           O  
ANISOU   78  O   ARG A 312     8859   5906   4599   3343  -1190      0       O  
ATOM     79  CB  ARG A 312      18.481  44.406 -27.191  1.00 52.24           C  
ANISOU   79  CB  ARG A 312     9419   6020   4408   4037   -923    644       C  
ATOM     80  CG  ARG A 312      16.994  44.323 -26.941  1.00 56.25           C  
ANISOU   80  CG  ARG A 312     9276   6981   5114   4246  -1064   1228       C  
ATOM     81  CD  ARG A 312      16.225  45.061 -27.962  1.00 63.62           C  
ANISOU   81  CD  ARG A 312     9762   8450   5959   4637  -1130   2159       C  
ATOM     82  NE  ARG A 312      16.483  46.499 -27.939  1.00 67.00           N  
ANISOU   82  NE  ARG A 312    10532   8269   6656   5376   -227   2500       N  
ATOM     83  CZ  ARG A 312      15.906  47.372 -27.119  1.00 71.47           C  
ANISOU   83  CZ  ARG A 312    11151   8299   7703   6060    795   3000       C  
ATOM     84  NH1 ARG A 312      15.055  46.969 -26.190  1.00 73.54           N  
ANISOU   84  NH1 ARG A 312    11005   8633   8303   6170    944   3235       N  
ATOM     85  NH2 ARG A 312      16.208  48.659 -27.212  1.00 75.23           N  
ANISOU   85  NH2 ARG A 312    12283   8000   8300   6616   1883   3240       N  
ATOM     86  N   GLU A 313      19.492  41.447 -26.736  1.00 50.03           N  
ANISOU   86  N   GLU A 313     9347   5640   4019   3196  -1181   -150       N  
ATOM     87  CA  GLU A 313      19.095  40.061 -26.651  1.00 51.80           C  
ANISOU   87  CA  GLU A 313     9688   5836   4157   2831  -1200   -353       C  
ATOM     88  C   GLU A 313      19.557  39.432 -25.367  1.00 46.55           C  
ANISOU   88  C   GLU A 313     8759   5018   3908   2941   -915   -347       C  
ATOM     89  O   GLU A 313      18.822  38.677 -24.744  1.00 44.69           O  
ANISOU   89  O   GLU A 313     8362   4848   3770   2754  -1006   -452       O  
ATOM     90  CB  GLU A 313      19.592  39.200 -27.814  1.00 55.17           C  
ANISOU   90  CB  GLU A 313    10942   5883   4136   2487   -839   -574       C  
ATOM     91  CG  GLU A 313      19.249  37.759 -27.490  1.00 58.02           C  
ANISOU   91  CG  GLU A 313    11701   5936   4406   2057   -489   -831       C  
ATOM     92  CD  GLU A 313      19.603  36.780 -28.550  1.00 64.28           C  
ANISOU   92  CD  GLU A 313    13765   6031   4625   1526    285  -1144       C  
ATOM     93  OE1 GLU A 313      20.187  37.180 -29.567  1.00 70.51           O  
ANISOU   93  OE1 GLU A 313    15089   6597   5105   1526    516  -1152       O  
ATOM     94  OE2 GLU A 313      19.289  35.602 -28.324  1.00 68.56           O  
ANISOU   94  OE2 GLU A 313    14920   6132   4998   1068    816  -1405       O  
ATOM     95  N   ARG A 314      20.802  39.714 -25.002  1.00 45.41           N  
ANISOU   95  N   ARG A 314     8491   4821   3942   3147   -601    -76       N  
ATOM     96  CA  ARG A 314      21.353  39.233 -23.777  1.00 43.39           C  
ANISOU   96  CA  ARG A 314     7759   4754   3972   3123   -424    265       C  
ATOM     97  C   ARG A 314      20.538  39.700 -22.579  1.00 41.61           C  
ANISOU   97  C   ARG A 314     7249   4767   3793   2850   -757    107       C  
ATOM     98  O   ARG A 314      20.390  38.960 -21.607  1.00 42.07           O  
ANISOU   98  O   ARG A 314     6988   4960   4037   2739   -730    218       O  
ATOM     99  CB  ARG A 314      22.814  39.653 -23.625  1.00 45.74           C  
ANISOU   99  CB  ARG A 314     7728   5377   4272   3123   -203    914       C  
ATOM    100  CG  ARG A 314      23.446  39.114 -22.352  1.00 48.13           C  
ANISOU  100  CG  ARG A 314     7271   6266   4749   2924   -118   1659       C  
ATOM    101  CD  ARG A 314      24.915  39.453 -22.224  1.00 54.84           C  
ANISOU  101  CD  ARG A 314     7490   7848   5497   2730      1   2712       C  
ATOM    102  NE  ARG A 314      25.688  38.992 -23.373  1.00 59.98           N  
ANISOU  102  NE  ARG A 314     8238   8124   6425   3475    685   3194       N  
ATOM    103  CZ  ARG A 314      26.957  39.314 -23.617  1.00 65.28           C  
ANISOU  103  CZ  ARG A 314     8349   9369   7084   3509    907   4229       C  
ATOM    104  NH1 ARG A 314      27.621  40.108 -22.787  1.00 67.72           N  
ANISOU  104  NH1 ARG A 314     7937  10841   6953   2567    338   4893       N  
ATOM    105  NH2 ARG A 314      27.559  38.819 -24.687  1.00 69.86           N  
ANISOU  105  NH2 ARG A 314     9176   9373   7994   4337   1785   4653       N  
ATOM    106  N   TYR A 315      20.047  40.923 -22.637  1.00 40.73           N  
ANISOU  106  N   TYR A 315     7344   4599   3532   2803   -860    -68       N  
ATOM    107  CA  TYR A 315      19.200  41.467 -21.598  1.00 41.25           C  
ANISOU  107  CA  TYR A 315     7424   4597   3653   2652   -782   -180       C  
ATOM    108  C   TYR A 315      17.840  40.743 -21.551  1.00 42.08           C  
ANISOU  108  C   TYR A 315     7233   4736   4019   2893   -980   -239       C  
ATOM    109  O   TYR A 315      17.379  40.395 -20.475  1.00 41.65           O  
ANISOU  109  O   TYR A 315     7005   4695   4124   2750   -931   -285       O  
ATOM    110  CB  TYR A 315      18.991  42.968 -21.825  1.00 42.57           C  
ANISOU  110  CB  TYR A 315     8096   4415   3662   2746   -382   -190       C  
ATOM    111  CG  TYR A 315      17.889  43.602 -21.017  1.00 44.81           C  
ANISOU  111  CG  TYR A 315     8613   4304   4105   2895    155   -163       C  
ATOM    112  CD1 TYR A 315      18.022  43.800 -19.662  1.00 46.39           C  
ANISOU  112  CD1 TYR A 315     9242   4288   4094   2245    559   -364       C  
ATOM    113  CD2 TYR A 315      16.736  44.058 -21.642  1.00 49.70           C  
ANISOU  113  CD2 TYR A 315     9029   4813   5040   3657    392    258       C  
ATOM    114  CE1 TYR A 315      17.010  44.394 -18.918  1.00 51.38           C  
ANISOU  114  CE1 TYR A 315    10332   4305   4885   2442   1393   -326       C  
ATOM    115  CE2 TYR A 315      15.730  44.656 -20.930  1.00 54.95           C  
ANISOU  115  CE2 TYR A 315     9848   5029   5999   4051   1207    580       C  
ATOM    116  CZ  TYR A 315      15.868  44.819 -19.570  1.00 56.06           C  
ANISOU  116  CZ  TYR A 315    10657   4658   5984   3494   1812    198       C  
ATOM    117  OH  TYR A 315      14.849  45.416 -18.896  1.00 63.89           O  
ANISOU  117  OH  TYR A 315    12002   4978   7294   3973   2928    548       O  
ATOM    118  N   GLU A 316      17.189  40.560 -22.695  1.00 43.60           N  
ANISOU  118  N   GLU A 316     7356   5072   4138   3075  -1241   -158       N  
ATOM    119  CA  GLU A 316      15.923  39.820 -22.717  1.00 46.95           C  
ANISOU  119  CA  GLU A 316     7407   5825   4605   2958  -1560    -50       C  
ATOM    120  C   GLU A 316      16.108  38.389 -22.134  1.00 44.39           C  
ANISOU  120  C   GLU A 316     7138   5400   4325   2616  -1560   -374       C  
ATOM    121  O   GLU A 316      15.272  37.913 -21.366  1.00 44.89           O  
ANISOU  121  O   GLU A 316     6889   5598   4568   2515  -1652   -362       O  
ATOM    122  CB  GLU A 316      15.342  39.780 -24.123  1.00 52.25           C  
ANISOU  122  CB  GLU A 316     8021   6967   4864   2735  -1969    221       C  
ATOM    123  CG  GLU A 316      14.949  41.162 -24.674  1.00 57.33           C  
ANISOU  123  CG  GLU A 316     8373   7839   5568   3252  -1886    876       C  
ATOM    124  CD  GLU A 316      14.526  41.122 -26.133  1.00 65.13           C  
ANISOU  124  CD  GLU A 316     9209   9553   5985   2840  -2418   1325       C  
ATOM    125  OE1 GLU A 316      14.898  40.156 -26.829  1.00 68.26           O  
ANISOU  125  OE1 GLU A 316    10173   9960   5802   2041  -2677    827       O  
ATOM    126  OE2 GLU A 316      13.822  42.057 -26.612  1.00 73.59           O  
ANISOU  126  OE2 GLU A 316     9664  11178   7119   3260  -2444   2291       O  
ATOM    127  N   ILE A 317      17.236  37.756 -22.425  1.00 42.65           N  
ANISOU  127  N   ILE A 317     7294   4882   4027   2570  -1266   -513       N  
ATOM    128  CA  ILE A 317      17.518  36.407 -21.908  1.00 43.43           C  
ANISOU  128  CA  ILE A 317     7504   4727   4270   2474   -897   -581       C  
ATOM    129  C   ILE A 317      17.725  36.420 -20.389  1.00 40.98           C  
ANISOU  129  C   ILE A 317     6657   4588   4322   2586   -863   -364       C  
ATOM    130  O   ILE A 317      17.190  35.561 -19.669  1.00 40.75           O  
ANISOU  130  O   ILE A 317     6488   4533   4462   2486   -807   -427       O  
ATOM    131  CB  ILE A 317      18.699  35.746 -22.655  1.00 45.09           C  
ANISOU  131  CB  ILE A 317     8256   4454   4422   2646   -189   -451       C  
ATOM    132  CG1 ILE A 317      18.284  35.481 -24.082  1.00 49.83           C  
ANISOU  132  CG1 ILE A 317     9712   4785   4435   2169   -127   -834       C  
ATOM    133  CG2 ILE A 317      19.100  34.422 -22.009  1.00 48.54           C  
ANISOU  133  CG2 ILE A 317     8762   4503   5175   2842    583   -196       C  
ATOM    134  CD1 ILE A 317      19.383  34.950 -24.977  1.00 54.68           C  
ANISOU  134  CD1 ILE A 317    11178   4667   4931   2351    856   -755       C  
ATOM    135  N   LEU A 318      18.495  37.386 -19.891  1.00 40.16           N  
ANISOU  135  N   LEU A 318     6352   4707   4200   2581   -890   -110       N  
ATOM    136  CA  LEU A 318      18.781  37.434 -18.481  1.00 39.97           C  
ANISOU  136  CA  LEU A 318     5963   5003   4219   2279   -894    144       C  
ATOM    137  C   LEU A 318      17.514  37.877 -17.728  1.00 39.48           C  
ANISOU  137  C   LEU A 318     5981   4818   4200   2139  -1005   -214       C  
ATOM    138  O   LEU A 318      17.271  37.408 -16.593  1.00 38.19           O  
ANISOU  138  O   LEU A 318     5606   4780   4125   1903   -987   -170       O  
ATOM    139  CB  LEU A 318      20.009  38.297 -18.158  1.00 41.50           C  
ANISOU  139  CB  LEU A 318     6054   5638   4074   1835   -894    587       C  
ATOM    140  CG  LEU A 318      21.377  37.736 -18.589  1.00 45.01           C  
ANISOU  140  CG  LEU A 318     6045   6452   4602   2049   -668   1414       C  
ATOM    141  CD1 LEU A 318      22.554  38.637 -18.205  1.00 49.21           C  
ANISOU  141  CD1 LEU A 318     6276   7780   4641   1300   -841   2064       C  
ATOM    142  CD2 LEU A 318      21.615  36.366 -18.013  1.00 48.01           C  
ANISOU  142  CD2 LEU A 318     5856   7009   5374   2372   -327   2079       C  
ATOM    143  N   LYS A 319      16.713  38.735 -18.348  1.00 39.33           N  
ANISOU  143  N   LYS A 319     6196   4578   4169   2373  -1000   -383       N  
ATOM    144  CA  LYS A 319      15.414  39.120 -17.785  1.00 43.32           C  
ANISOU  144  CA  LYS A 319     6651   4928   4879   2532   -835   -389       C  
ATOM    145  C   LYS A 319      14.509  37.890 -17.639  1.00 44.75           C  
ANISOU  145  C   LYS A 319     6388   5319   5295   2554  -1131   -408       C  
ATOM    146  O   LYS A 319      13.903  37.696 -16.588  1.00 43.36           O  
ANISOU  146  O   LYS A 319     6075   5087   5312   2500   -986   -418       O  
ATOM    147  CB  LYS A 319      14.712  40.182 -18.628  1.00 48.40           C  
ANISOU  147  CB  LYS A 319     7355   5447   5588   3016   -621   -103       C  
ATOM    148  CG  LYS A 319      13.591  40.866 -17.869  1.00 55.44           C  
ANISOU  148  CG  LYS A 319     8255   6015   6793   3389     37    224       C  
ATOM    149  CD  LYS A 319      12.606  41.604 -18.771  1.00 64.27           C  
ANISOU  149  CD  LYS A 319     8950   7289   8181   4143    289   1043       C  
ATOM    150  CE  LYS A 319      13.134  42.959 -19.203  1.00 68.21           C  
ANISOU  150  CE  LYS A 319    10126   7221   8567   4459   1040   1171       C  
ATOM    151  NZ  LYS A 319      12.128  43.809 -19.917  1.00 77.63           N  
ANISOU  151  NZ  LYS A 319    10820   8521  10152   5429   1616   2327       N  
ATOM    152  N   LYS A 320      14.423  37.083 -18.706  1.00 45.98           N  
ANISOU  152  N   LYS A 320     6501   5654   5312   2470  -1447   -454       N  
ATOM    153  CA  LYS A 320      13.685  35.815 -18.698  1.00 46.92           C  
ANISOU  153  CA  LYS A 320     6501   5914   5410   2141  -1631   -572       C  
ATOM    154  C   LYS A 320      14.213  34.865 -17.609  1.00 44.15           C  
ANISOU  154  C   LYS A 320     6179   5319   5277   2098  -1338   -716       C  
ATOM    155  O   LYS A 320      13.451  34.282 -16.846  1.00 44.09           O  
ANISOU  155  O   LYS A 320     5946   5366   5439   1975  -1370   -764       O  
ATOM    156  CB  LYS A 320      13.749  35.149 -20.081  1.00 50.42           C  
ANISOU  156  CB  LYS A 320     7398   6399   5359   1677  -1755   -726       C  
ATOM    157  CG  LYS A 320      12.643  34.146 -20.327  1.00 56.65           C  
ANISOU  157  CG  LYS A 320     8229   7505   5787    896  -2013   -805       C  
ATOM    158  CD  LYS A 320      12.653  33.573 -21.748  1.00 64.27           C  
ANISOU  158  CD  LYS A 320    10003   8507   5907    -41  -2048  -1030       C  
ATOM    159  CE  LYS A 320      11.854  32.278 -21.828  1.00 71.32           C  
ANISOU  159  CE  LYS A 320    11420   9468   6208  -1225  -2017  -1323       C  
ATOM    160  NZ  LYS A 320      12.122  31.509 -23.078  1.00 80.39           N  
ANISOU  160  NZ  LYS A 320    13993  10218   6331  -2425  -1595  -1794       N  
ATOM    161  N   LEU A 321      15.519  34.719 -17.486  1.00 41.71           N  
ANISOU  161  N   LEU A 321     5995   4862   4989   2232  -1027   -576       N  
ATOM    162  CA  LEU A 321      15.997  33.842 -16.453  1.00 40.78           C  
ANISOU  162  CA  LEU A 321     5648   4745   5101   2262   -726   -328       C  
ATOM    163  C   LEU A 321      15.670  34.362 -15.053  1.00 39.34           C  
ANISOU  163  C   LEU A 321     5126   4842   4980   2044   -912   -270       C  
ATOM    164  O   LEU A 321      15.386  33.596 -14.164  1.00 39.95           O  
ANISOU  164  O   LEU A 321     4985   4960   5233   1975   -824   -202       O  
ATOM    165  CB  LEU A 321      17.480  33.562 -16.597  1.00 42.82           C  
ANISOU  165  CB  LEU A 321     5797   5054   5416   2520   -280    287       C  
ATOM    166  CG  LEU A 321      17.873  32.765 -17.826  1.00 45.60           C  
ANISOU  166  CG  LEU A 321     6752   4812   5760   2806    378    283       C  
ATOM    167  CD1 LEU A 321      19.394  32.789 -17.929  1.00 48.18           C  
ANISOU  167  CD1 LEU A 321     6733   5310   6263   3264    913   1225       C  
ATOM    168  CD2 LEU A 321      17.309  31.350 -17.763  1.00 49.77           C  
ANISOU  168  CD2 LEU A 321     7771   4750   6387   2766   1015     77       C  
ATOM    169  N   ASN A 322      15.716  35.664 -14.870  1.00 38.43           N  
ANISOU  169  N   ASN A 322     5159   4794   4649   1862   -999   -323       N  
ATOM    170  CA  ASN A 322      15.386  36.257 -13.622  1.00 38.19           C  
ANISOU  170  CA  ASN A 322     5248   4771   4489   1457   -876   -382       C  
ATOM    171  C   ASN A 322      13.915  36.010 -13.285  1.00 40.11           C  
ANISOU  171  C   ASN A 322     5409   4753   5077   1723   -799   -594       C  
ATOM    172  O   ASN A 322      13.588  35.649 -12.148  1.00 42.18           O  
ANISOU  172  O   ASN A 322     5612   5019   5393   1480   -685   -618       O  
ATOM    173  CB  ASN A 322      15.658  37.769 -13.676  1.00 39.56           C  
ANISOU  173  CB  ASN A 322     6032   4734   4264   1146   -598   -481       C  
ATOM    174  CG  ASN A 322      15.408  38.452 -12.362  1.00 41.98           C  
ANISOU  174  CG  ASN A 322     6949   4797   4203    441   -123   -638       C  
ATOM    175  OD1 ASN A 322      15.866  38.020 -11.309  1.00 43.96           O  
ANISOU  175  OD1 ASN A 322     7103   5482   4118   -317   -259   -489       O  
ATOM    176  ND2 ASN A 322      14.674  39.514 -12.414  1.00 45.73           N  
ANISOU  176  ND2 ASN A 322     8122   4552   4701    662    588   -824       N  
ATOM    177  N   ASP A 323      13.032  36.252 -14.239  1.00 41.08           N  
ANISOU  177  N   ASP A 323     5430   4797   5379   2142   -873   -576       N  
ATOM    178  CA  ASP A 323      11.615  36.062 -14.014  1.00 45.52           C  
ANISOU  178  CA  ASP A 323     5633   5401   6260   2370   -842   -419       C  
ATOM    179  C   ASP A 323      11.331  34.620 -13.662  1.00 44.71           C  
ANISOU  179  C   ASP A 323     5258   5477   6253   2115  -1115   -579       C  
ATOM    180  O   ASP A 323      10.537  34.329 -12.783  1.00 45.19           O  
ANISOU  180  O   ASP A 323     5104   5519   6547   2113   -996   -537       O  
ATOM    181  CB  ASP A 323      10.831  36.436 -15.260  1.00 51.84           C  
ANISOU  181  CB  ASP A 323     6066   6536   7093   2665  -1065      5       C  
ATOM    182  CG  ASP A 323      10.980  37.912 -15.614  1.00 58.34           C  
ANISOU  182  CG  ASP A 323     7158   7072   7935   3121   -561    322       C  
ATOM    183  OD1 ASP A 323      11.235  38.725 -14.684  1.00 62.00           O  
ANISOU  183  OD1 ASP A 323     8227   6913   8415   3166    194    195       O  
ATOM    184  OD2 ASP A 323      10.844  38.256 -16.817  1.00 63.74           O  
ANISOU  184  OD2 ASP A 323     7592   8112   8513   3301   -821    698       O  
ATOM    185  N   SER A 324      12.021  33.720 -14.332  1.00 42.07           N  
ANISOU  185  N   SER A 324     5076   5168   5739   1929  -1269   -742       N  
ATOM    186  CA  SER A 324      11.793  32.324 -14.131  1.00 44.52           C  
ANISOU  186  CA  SER A 324     5419   5408   6089   1682  -1209   -899       C  
ATOM    187  C   SER A 324      12.322  31.916 -12.738  1.00 42.55           C  
ANISOU  187  C   SER A 324     5030   5072   6063   1753   -936   -794       C  
ATOM    188  O   SER A 324      11.621  31.202 -12.014  1.00 41.66           O  
ANISOU  188  O   SER A 324     4767   4931   6128   1647   -886   -867       O  
ATOM    189  CB  SER A 324      12.387  31.525 -15.299  1.00 46.25           C  
ANISOU  189  CB  SER A 324     6195   5374   6003   1477  -1001  -1058       C  
ATOM    190  OG  SER A 324      12.317  30.155 -15.047  1.00 53.31           O  
ANISOU  190  OG  SER A 324     7444   5899   6912   1254   -536  -1211       O  
ATOM    191  N   LEU A 325      13.501  32.415 -12.336  1.00 39.63           N  
ANISOU  191  N   LEU A 325     4629   4833   5592   1778   -831   -505       N  
ATOM    192  CA  LEU A 325      14.037  32.122 -11.011  1.00 39.34           C  
ANISOU  192  CA  LEU A 325     4310   5079   5557   1560   -721   -138       C  
ATOM    193  C   LEU A 325      13.147  32.698  -9.909  1.00 39.64           C  
ANISOU  193  C   LEU A 325     4443   5071   5547   1239   -749   -390       C  
ATOM    194  O   LEU A 325      12.967  32.091  -8.876  1.00 39.73           O  
ANISOU  194  O   LEU A 325     4270   5197   5628   1053   -681   -280       O  
ATOM    195  CB  LEU A 325      15.480  32.630 -10.855  1.00 40.38           C  
ANISOU  195  CB  LEU A 325     4245   5736   5359   1295   -748    482       C  
ATOM    196  CG  LEU A 325      16.526  31.880 -11.660  1.00 42.65           C  
ANISOU  196  CG  LEU A 325     4283   6083   5838   1791   -412   1112       C  
ATOM    197  CD1 LEU A 325      17.835  32.658 -11.648  1.00 46.27           C  
ANISOU  197  CD1 LEU A 325     4388   7269   5919   1447   -571   1860       C  
ATOM    198  CD2 LEU A 325      16.743  30.462 -11.121  1.00 45.72           C  
ANISOU  198  CD2 LEU A 325     4282   6469   6620   2183    130   1762       C  
ATOM    199  N   GLU A 326      12.569  33.859 -10.158  1.00 41.43           N  
ANISOU  199  N   GLU A 326     5020   5029   5690   1265   -656   -637       N  
ATOM    200  CA  GLU A 326      11.602  34.451  -9.262  1.00 45.86           C  
ANISOU  200  CA  GLU A 326     5864   5247   6311   1184   -260   -779       C  
ATOM    201  C   GLU A 326      10.416  33.473  -9.075  1.00 45.83           C  
ANISOU  201  C   GLU A 326     5385   5238   6788   1510   -347   -791       C  
ATOM    202  O   GLU A 326      10.032  33.145  -7.942  1.00 42.49           O  
ANISOU  202  O   GLU A 326     4985   4726   6431   1310   -142   -834       O  
ATOM    203  CB  GLU A 326      11.180  35.805  -9.812  1.00 51.02           C  
ANISOU  203  CB  GLU A 326     6961   5464   6959   1486    205   -765       C  
ATOM    204  CG  GLU A 326      10.152  36.555  -8.989  1.00 61.63           C  
ANISOU  204  CG  GLU A 326     8776   6165   8475   1662   1119   -702       C  
ATOM    205  CD  GLU A 326       9.810  37.928  -9.558  1.00 69.12           C  
ANISOU  205  CD  GLU A 326    10238   6513   9511   2183   1981   -431       C  
ATOM    206  OE1 GLU A 326       9.432  38.009 -10.745  1.00 72.68           O  
ANISOU  206  OE1 GLU A 326    10022   7291  10301   2859   1666      1       O  
ATOM    207  OE2 GLU A 326       9.887  38.930  -8.811  1.00 82.02           O  
ANISOU  207  OE2 GLU A 326    13052   7306  10805   1840   3118   -587       O  
ATOM    208  N   LEU A 327       9.898  32.941 -10.170  1.00 44.98           N  
ANISOU  208  N   LEU A 327     4911   5311   6869   1779   -681   -744       N  
ATOM    209  CA  LEU A 327       8.738  32.063 -10.072  1.00 47.64           C  
ANISOU  209  CA  LEU A 327     4831   5805   7464   1766   -821   -695       C  
ATOM    210  C   LEU A 327       9.065  30.846  -9.210  1.00 45.09           C  
ANISOU  210  C   LEU A 327     4546   5401   7184   1524   -763   -894       C  
ATOM    211  O   LEU A 327       8.243  30.430  -8.393  1.00 47.30           O  
ANISOU  211  O   LEU A 327     4626   5658   7687   1482   -663   -892       O  
ATOM    212  CB  LEU A 327       8.213  31.628 -11.451  1.00 48.24           C  
ANISOU  212  CB  LEU A 327     4673   6285   7368   1561  -1263   -591       C  
ATOM    213  CG  LEU A 327       6.907  30.821 -11.433  1.00 50.81           C  
ANISOU  213  CG  LEU A 327     4527   7047   7732   1166  -1513   -395       C  
ATOM    214  CD1 LEU A 327       5.783  31.639 -10.809  1.00 53.79           C  
ANISOU  214  CD1 LEU A 327     4226   7643   8567   1662  -1289    287       C  
ATOM    215  CD2 LEU A 327       6.558  30.381 -12.839  1.00 56.49           C  
ANISOU  215  CD2 LEU A 327     5244   8334   7885    413  -2013   -302       C  
ATOM    216  N   SER A 328      10.272  30.321  -9.365  1.00 44.25           N  
ANISOU  216  N   SER A 328     4624   5263   6924   1476   -698   -880       N  
ATOM    217  CA  SER A 328      10.715  29.118  -8.660  1.00 44.37           C  
ANISOU  217  CA  SER A 328     4579   5218   7062   1456   -422   -735       C  
ATOM    218  C   SER A 328      10.775  29.297  -7.146  1.00 41.67           C  
ANISOU  218  C   SER A 328     4033   5075   6723   1265   -375   -536       C  
ATOM    219  O   SER A 328      10.559  28.343  -6.381  1.00 39.50           O  
ANISOU  219  O   SER A 328     3594   4778   6635   1258   -191   -429       O  
ATOM    220  CB  SER A 328      12.105  28.668  -9.138  1.00 46.98           C  
ANISOU  220  CB  SER A 328     4972   5540   7338   1686    -93   -303       C  
ATOM    221  OG  SER A 328      12.017  27.914 -10.324  1.00 51.08           O  
ANISOU  221  OG  SER A 328     6000   5584   7822   1746    258   -545       O  
ATOM    222  N   ASP A 329      11.135  30.501  -6.738  1.00 40.03           N  
ANISOU  222  N   ASP A 329     3998   5024   6186    961   -443   -489       N  
ATOM    223  CA  ASP A 329      11.209  30.834  -5.336  1.00 42.27           C  
ANISOU  223  CA  ASP A 329     4425   5477   6156    372   -326   -386       C  
ATOM    224  C   ASP A 329       9.839  31.133  -4.675  1.00 41.40           C  
ANISOU  224  C   ASP A 329     4603   4862   6263    423     11   -769       C  
ATOM    225  O   ASP A 329       9.744  31.056  -3.453  1.00 42.73           O  
ANISOU  225  O   ASP A 329     4970   5054   6209    -71    211   -752       O  
ATOM    226  CB  ASP A 329      12.228  31.967  -5.131  1.00 48.59           C  
ANISOU  226  CB  ASP A 329     5616   6610   6232   -387   -361   -202       C  
ATOM    227  CG  ASP A 329      13.679  31.456  -5.111  1.00 53.45           C  
ANISOU  227  CG  ASP A 329     5592   8150   6564   -677   -680    675       C  
ATOM    228  OD1 ASP A 329      13.878  30.223  -5.272  1.00 53.62           O  
ANISOU  228  OD1 ASP A 329     4974   8314   7083    -39   -614   1158       O  
ATOM    229  OD2 ASP A 329      14.615  32.278  -4.913  1.00 64.84           O  
ANISOU  229  OD2 ASP A 329     7184  10187   7263  -1577   -855   1028       O  
ATOM    230  N   VAL A 330       8.785  31.409  -5.456  1.00 39.42           N  
ANISOU  230  N   VAL A 330     4266   4282   6427    991    108   -912       N  
ATOM    231  CA  VAL A 330       7.456  31.732  -4.875  1.00 42.70           C  
ANISOU  231  CA  VAL A 330     4728   4307   7187   1248    609   -893       C  
ATOM    232  C   VAL A 330       6.447  30.577  -4.958  1.00 41.60           C  
ANISOU  232  C   VAL A 330     3908   4388   7508   1480    336   -810       C  
ATOM    233  O   VAL A 330       5.448  30.601  -4.279  1.00 46.06           O  
ANISOU  233  O   VAL A 330     4350   4769   8382   1649    719   -661       O  
ATOM    234  CB  VAL A 330       6.807  32.996  -5.473  1.00 46.24           C  
ANISOU  234  CB  VAL A 330     5353   4385   7830   1772   1163   -623       C  
ATOM    235  CG1 VAL A 330       7.571  34.241  -5.050  1.00 50.14           C  
ANISOU  235  CG1 VAL A 330     6946   4331   7775   1347   1856   -821       C  
ATOM    236  CG2 VAL A 330       6.667  32.902  -6.986  1.00 45.41           C  
ANISOU  236  CG2 VAL A 330     4614   4759   7880   2136    579   -356       C  
ATOM    237  N   VAL A 331       6.734  29.579  -5.778  1.00 38.96           N  
ANISOU  237  N   VAL A 331     3295   4366   7140   1382   -164   -896       N  
ATOM    238  CA  VAL A 331       5.902  28.402  -5.920  1.00 40.58           C  
ANISOU  238  CA  VAL A 331     3164   4736   7516   1218   -348   -934       C  
ATOM    239  C   VAL A 331       6.378  27.304  -4.950  1.00 40.65           C  
ANISOU  239  C   VAL A 331     3327   4562   7555   1067   -148  -1093       C  
ATOM    240  O   VAL A 331       7.554  26.923  -4.959  1.00 39.55           O  
ANISOU  240  O   VAL A 331     3375   4387   7263   1085    -44  -1018       O  
ATOM    241  CB  VAL A 331       5.915  27.922  -7.386  1.00 41.68           C  
ANISOU  241  CB  VAL A 331     3332   5127   7377    906   -712  -1004       C  
ATOM    242  CG1 VAL A 331       5.080  26.664  -7.572  1.00 45.52           C  
ANISOU  242  CG1 VAL A 331     3797   5759   7736    280   -807  -1138       C  
ATOM    243  CG2 VAL A 331       5.409  29.035  -8.312  1.00 44.41           C  
ANISOU  243  CG2 VAL A 331     3313   5880   7678   1058   -974   -589       C  
ATOM    244  N   PRO A 332       5.481  26.827  -4.064  1.00 38.42           N  
ANISOU  244  N   PRO A 332     4360   4885   5351    167    218    382       N  
ATOM    245  CA  PRO A 332       5.831  25.775  -3.133  1.00 40.02           C  
ANISOU  245  CA  PRO A 332     4640   5191   5374    -31    323    563       C  
ATOM    246  C   PRO A 332       6.325  24.565  -3.908  1.00 39.98           C  
ANISOU  246  C   PRO A 332     4372   5179   5639    -45    163    733       C  
ATOM    247  O   PRO A 332       5.752  24.258  -4.972  1.00 39.34           O  
ANISOU  247  O   PRO A 332     4028   5096   5822     40    199    634       O  
ATOM    248  CB  PRO A 332       4.511  25.445  -2.472  1.00 43.92           C  
ANISOU  248  CB  PRO A 332     5029   5832   5825    -48    778    433       C  
ATOM    249  CG  PRO A 332       3.712  26.701  -2.571  1.00 46.35           C  
ANISOU  249  CG  PRO A 332     5260   6120   6230    298    938     46       C  
ATOM    250  CD  PRO A 332       4.096  27.304  -3.868  1.00 42.92           C  
ANISOU  250  CD  PRO A 332     4775   5450   6083    456    487     91       C  
ATOM    251  N   ALA A 333       7.382  23.916  -3.417  1.00 40.02           N  
ANISOU  251  N   ALA A 333     4469   5140   5594   -105    -86    942       N  
ATOM    252  CA  ALA A 333       7.850  22.669  -4.050  1.00 42.67           C  
ANISOU  252  CA  ALA A 333     4593   5348   6270     59   -252    978       C  
ATOM    253  C   ALA A 333       6.686  21.697  -4.344  1.00 43.28           C  
ANISOU  253  C   ALA A 333     4704   5221   6517    -11   -104    955       C  
ATOM    254  O   ALA A 333       6.605  21.149  -5.428  1.00 44.65           O  
ANISOU  254  O   ALA A 333     4724   5301   6939    121   -131    768       O  
ATOM    255  CB  ALA A 333       8.929  21.978  -3.205  1.00 43.59           C  
ANISOU  255  CB  ALA A 333     4818   5318   6427    115   -671   1239       C  
ATOM    256  N   SER A 334       5.799  21.503  -3.379  1.00 47.34           N  
ANISOU  256  N   SER A 334     5436   5726   6824   -323     69   1126       N  
ATOM    257  CA  SER A 334       4.568  20.688  -3.572  1.00 51.05           C  
ANISOU  257  CA  SER A 334     5841   6129   7426   -612    231   1166       C  
ATOM    258  C   SER A 334       3.732  21.060  -4.792  1.00 49.75           C  
ANISOU  258  C   SER A 334     5247   6124   7531   -508    346    886       C  
ATOM    259  O   SER A 334       3.273  20.163  -5.511  1.00 49.57           O  
ANISOU  259  O   SER A 334     5194   5904   7737   -660    196    869       O  
ATOM    260  CB  SER A 334       3.669  20.776  -2.355  1.00 54.10           C  
ANISOU  260  CB  SER A 334     6339   6784   7433  -1067    612   1327       C  
ATOM    261  OG  SER A 334       4.067  19.802  -1.411  1.00 62.37           O  
ANISOU  261  OG  SER A 334     7943   7540   8215  -1455    354   1755       O  
ATOM    262  N   ASP A 335       3.528  22.365  -5.019  1.00 47.22           N  
ANISOU  262  N   ASP A 335     4702   6065   7175   -282    484    691       N  
ATOM    263  CA  ASP A 335       2.707  22.808  -6.153  1.00 47.79           C  
ANISOU  263  CA  ASP A 335     4420   6232   7504   -177    404    515       C  
ATOM    264  C   ASP A 335       3.487  22.639  -7.456  1.00 45.41           C  
ANISOU  264  C   ASP A 335     4253   5789   7211    -92    102    432       C  
ATOM    265  O   ASP A 335       2.896  22.295  -8.474  1.00 45.07           O  
ANISOU  265  O   ASP A 335     4114   5719   7290   -200    -81    351       O  
ATOM    266  CB  ASP A 335       2.293  24.275  -6.033  1.00 49.50           C  
ANISOU  266  CB  ASP A 335     4486   6583   7738    119    470    349       C  
ATOM    267  CG  ASP A 335       1.346  24.552  -4.869  1.00 55.64           C  
ANISOU  267  CG  ASP A 335     5008   7633   8498    144    927    218       C  
ATOM    268  OD1 ASP A 335       0.854  23.609  -4.223  1.00 59.90           O  
ANISOU  268  OD1 ASP A 335     5422   8376   8960   -240   1225    343       O  
ATOM    269  OD2 ASP A 335       1.081  25.757  -4.610  1.00 61.72           O  
ANISOU  269  OD2 ASP A 335     5743   8405   9301    533   1000    -45       O  
ATOM    270  N   ALA A 336       4.798  22.929  -7.416  1.00 39.75           N  
ANISOU  270  N   ALA A 336     3720   5072   6309     35     68    430       N  
ATOM    271  CA  ALA A 336       5.660  22.758  -8.561  1.00 41.52           C  
ANISOU  271  CA  ALA A 336     3973   5358   6446     76    -23    275       C  
ATOM    272  C   ALA A 336       5.660  21.312  -9.053  1.00 45.45           C  
ANISOU  272  C   ALA A 336     4554   5620   7094    110    -69     95       C  
ATOM    273  O   ALA A 336       5.611  21.095 -10.252  1.00 48.13           O  
ANISOU  273  O   ALA A 336     4965   6001   7319     54   -111   -148       O  
ATOM    274  CB  ALA A 336       7.114  23.206  -8.256  1.00 40.43           C  
ANISOU  274  CB  ALA A 336     3793   5411   6158    150      6    308       C  
ATOM    275  N   GLU A 337       5.770  20.348  -8.133  1.00 50.16           N  
ANISOU  275  N   GLU A 337     5277   5902   7878    164   -127    214       N  
ATOM    276  CA  GLU A 337       5.696  18.908  -8.455  1.00 55.49           C  
ANISOU  276  CA  GLU A 337     6221   6097   8765    198   -317     64       C  
ATOM    277  C   GLU A 337       4.363  18.554  -9.153  1.00 56.90           C  
ANISOU  277  C   GLU A 337     6480   6172   8967   -204   -421     16       C  
ATOM    278  O   GLU A 337       4.337  17.742 -10.070  1.00 59.70           O  
ANISOU  278  O   GLU A 337     7110   6227   9344   -215   -590   -295       O  
ATOM    279  CB  GLU A 337       5.922  18.037  -7.187  1.00 61.17           C  
ANISOU  279  CB  GLU A 337     7223   6366   9651    191   -540    383       C  
ATOM    280  CG  GLU A 337       7.389  18.040  -6.666  1.00 67.13           C  
ANISOU  280  CG  GLU A 337     7890   7101  10513    669   -692    396       C  
ATOM    281  CD  GLU A 337       7.584  17.447  -5.260  1.00 73.82           C  
ANISOU  281  CD  GLU A 337     9108   7536  11401    560  -1074    879       C  
ATOM    282  OE1 GLU A 337       6.902  16.447  -4.947  1.00 81.25           O  
ANISOU  282  OE1 GLU A 337    10535   7926  12407    242  -1321   1103       O  
ATOM    283  OE2 GLU A 337       8.426  17.962  -4.461  1.00 74.95           O  
ANISOU  283  OE2 GLU A 337     9138   7883  11453    679  -1214   1090       O  
ATOM    284  N   LYS A 338       3.265  19.181  -8.743  1.00 54.95           N  
ANISOU  284  N   LYS A 338     5951   6201   8725   -517   -338    265       N  
ATOM    285  CA  LYS A 338       1.972  18.963  -9.398  1.00 58.72           C  
ANISOU  285  CA  LYS A 338     6271   6723   9317   -919   -520    262       C  
ATOM    286  C   LYS A 338       1.957  19.470 -10.852  1.00 58.28           C  
ANISOU  286  C   LYS A 338     6240   6810   9092   -863   -731      4       C  
ATOM    287  O   LYS A 338       1.599  18.739 -11.768  1.00 60.12           O  
ANISOU  287  O   LYS A 338     6736   6829   9276  -1129  -1027   -180       O  
ATOM    288  CB  LYS A 338       0.856  19.641  -8.606  1.00 60.96           C  
ANISOU  288  CB  LYS A 338     6001   7422   9735  -1114   -316    498       C  
ATOM    289  CG  LYS A 338       0.544  18.977  -7.273  1.00 67.04           C  
ANISOU  289  CG  LYS A 338     6806   8173  10493  -1491    -73    786       C  
ATOM    290  CD  LYS A 338      -0.796  19.440  -6.689  1.00 73.55           C  
ANISOU  290  CD  LYS A 338     6914   9586  11444  -1792    260    882       C  
ATOM    291  CE  LYS A 338      -1.961  19.183  -7.650  1.00 79.06           C  
ANISOU  291  CE  LYS A 338     7099  10448  12490  -2138    -61    851       C  
ATOM    292  NZ  LYS A 338      -3.314  19.111  -7.013  1.00 87.67           N  
ANISOU  292  NZ  LYS A 338     7345  12166  13797  -2651    261    989       N  
ATOM    293  N   TYR A 339       2.377  20.716 -11.067  1.00 55.66           N  
ANISOU  293  N   TYR A 339     5776   6788   8583   -617   -644     14       N  
ATOM    294  CA  TYR A 339       2.360  21.296 -12.429  1.00 56.06           C  
ANISOU  294  CA  TYR A 339     5987   6984   8326   -723   -915    -98       C  
ATOM    295  C   TYR A 339       3.194  20.513 -13.474  1.00 58.99           C  
ANISOU  295  C   TYR A 339     6836   7279   8296   -785   -862   -499       C  
ATOM    296  O   TYR A 339       2.773  20.402 -14.623  1.00 60.33           O  
ANISOU  296  O   TYR A 339     7297   7471   8153  -1101  -1166   -638       O  
ATOM    297  CB  TYR A 339       2.849  22.731 -12.413  1.00 50.74           C  
ANISOU  297  CB  TYR A 339     5278   6531   7468   -562   -884     53       C  
ATOM    298  CG  TYR A 339       1.927  23.736 -11.770  1.00 50.48           C  
ANISOU  298  CG  TYR A 339     4889   6510   7781   -389  -1039    277       C  
ATOM    299  CD1 TYR A 339       0.679  24.003 -12.313  1.00 53.92           C  
ANISOU  299  CD1 TYR A 339     5056   6949   8482   -451  -1514    370       C  
ATOM    300  CD2 TYR A 339       2.338  24.473 -10.651  1.00 46.69           C  
ANISOU  300  CD2 TYR A 339     4338   6033   7366   -116   -763    336       C  
ATOM    301  CE1 TYR A 339      -0.158  24.950 -11.750  1.00 57.68           C  
ANISOU  301  CE1 TYR A 339     5082   7439   9392    -96  -1641    447       C  
ATOM    302  CE2 TYR A 339       1.511  25.421 -10.080  1.00 49.78           C  
ANISOU  302  CE2 TYR A 339     4458   6393   8061    169   -843    366       C  
ATOM    303  CZ  TYR A 339       0.263  25.659 -10.639  1.00 54.91           C  
ANISOU  303  CZ  TYR A 339     4729   7054   9079    253  -1252    389       C  
ATOM    304  OH  TYR A 339      -0.567  26.603 -10.101  1.00 60.75           O  
ANISOU  304  OH  TYR A 339     5075   7761  10246    725  -1327    300       O  
ATOM    305  N   ARG A 340       4.366  20.002 -13.082  1.00 55.69           N  
ANISOU  305  N   ARG A 340     6480   6801   7879   -455   -503   -727       N  
ATOM    306  CA  ARG A 340       5.236  19.272 -14.004  1.00 62.41           C  
ANISOU  306  CA  ARG A 340     7646   7648   8418   -323   -310  -1280       C  
ATOM    307  C   ARG A 340       4.693  17.903 -14.463  1.00 66.37           C  
ANISOU  307  C   ARG A 340     8627   7588   9002   -420   -571  -1642       C  
ATOM    308  O   ARG A 340       3.861  17.283 -13.803  1.00 65.71           O  
ANISOU  308  O   ARG A 340     8588   7056   9322   -599   -878  -1389       O  
ATOM    309  CB  ARG A 340       6.634  19.085 -13.392  1.00 66.17           C  
ANISOU  309  CB  ARG A 340     7849   8227   9063    202     70  -1461       C  
ATOM    310  CG  ARG A 340       7.493  20.351 -13.337  1.00 65.72           C  
ANISOU  310  CG  ARG A 340     7417   8809   8742    146    345  -1268       C  
ATOM    311  CD  ARG A 340       8.963  19.973 -13.407  1.00 74.51           C  
ANISOU  311  CD  ARG A 340     8167  10252   9889    573    756  -1692       C  
ATOM    312  NE  ARG A 340       9.866  21.117 -13.271  1.00 73.99           N  
ANISOU  312  NE  ARG A 340     7662  10849   9600    363    986  -1455       N  
ATOM    313  CZ  ARG A 340      10.182  21.688 -12.119  1.00 67.62           C  
ANISOU  313  CZ  ARG A 340     6585  10025   9082    403    815  -1019       C  
ATOM    314  NH1 ARG A 340       9.659  21.247 -10.976  1.00 66.85           N  
ANISOU  314  NH1 ARG A 340     6615   9358   9426    643    492   -763       N  
ATOM    315  NH2 ARG A 340      11.004  22.715 -12.113  1.00 67.42           N  
ANISOU  315  NH2 ARG A 340     6244  10565   8806     68    950   -819       N  
TER     316      ARG A 340                                                      
ATOM    317  N   GLU B 303      24.180  49.331 -26.998  1.00 67.64           N  
ANISOU  317  N   GLU B 303    10800   7629   7271    870   1622    908       N  
ATOM    318  CA  GLU B 303      23.061  49.491 -26.018  1.00 61.89           C  
ANISOU  318  CA  GLU B 303     9880   6951   6682    304    748    227       C  
ATOM    319  C   GLU B 303      23.383  48.712 -24.731  1.00 59.65           C  
ANISOU  319  C   GLU B 303     9318   6721   6622    505    851    203       C  
ATOM    320  O   GLU B 303      23.797  47.545 -24.766  1.00 61.69           O  
ANISOU  320  O   GLU B 303    10077   6780   6579    933   1568    326       O  
ATOM    321  CB  GLU B 303      21.723  48.999 -26.600  1.00 63.78           C  
ANISOU  321  CB  GLU B 303    11046   6933   6253   -162    480   -282       C  
ATOM    322  CG  GLU B 303      21.434  49.414 -28.048  1.00 69.52           C  
ANISOU  322  CG  GLU B 303    12408   7504   6501   -437    437   -177       C  
ATOM    323  CD  GLU B 303      20.202  48.745 -28.643  1.00 74.04           C  
ANISOU  323  CD  GLU B 303    14063   7765   6303  -1165    -35   -407       C  
ATOM    324  OE1 GLU B 303      19.799  47.653 -28.168  1.00 78.02           O  
ANISOU  324  OE1 GLU B 303    15167   8022   6455  -1343    -86   -609       O  
ATOM    325  OE2 GLU B 303      19.641  49.307 -29.613  1.00 79.72           O  
ANISOU  325  OE2 GLU B 303    15051   8480   6760  -1684   -472   -254       O  
ATOM    326  N   ILE B 304      23.189  49.382 -23.608  1.00 54.78           N  
ANISOU  326  N   ILE B 304     8093   6277   6442    237    175     65       N  
ATOM    327  CA  ILE B 304      23.522  48.855 -22.305  1.00 54.97           C  
ANISOU  327  CA  ILE B 304     7841   6373   6670    308    100     96       C  
ATOM    328  C   ILE B 304      22.254  48.987 -21.472  1.00 50.56           C  
ANISOU  328  C   ILE B 304     7479   5768   5963     89   -367   -547       C  
ATOM    329  O   ILE B 304      21.617  50.024 -21.497  1.00 50.00           O  
ANISOU  329  O   ILE B 304     7405   5655   5937    -58   -772   -711       O  
ATOM    330  CB  ILE B 304      24.723  49.611 -21.704  1.00 57.32           C  
ANISOU  330  CB  ILE B 304     7410   6846   7523    153   -309    840       C  
ATOM    331  CG1 ILE B 304      25.883  49.570 -22.708  1.00 63.37           C  
ANISOU  331  CG1 ILE B 304     7723   7808   8544    494    294   1842       C  
ATOM    332  CG2 ILE B 304      25.109  49.026 -20.359  1.00 57.96           C  
ANISOU  332  CG2 ILE B 304     7275   6997   7747     89   -500    992       C  
ATOM    333  CD1 ILE B 304      27.273  49.734 -22.126  1.00 70.26           C  
ANISOU  333  CD1 ILE B 304     7596   9025  10072    392     83   3148       C  
ATOM    334  N   PHE B 305      21.860  47.917 -20.793  1.00 48.23           N  
ANISOU  334  N   PHE B 305     7362   5475   5487    178   -188   -775       N  
ATOM    335  CA  PHE B 305      20.607  47.906 -20.050  1.00 46.19           C  
ANISOU  335  CA  PHE B 305     7169   5274   5105    107   -450  -1120       C  
ATOM    336  C   PHE B 305      20.885  47.558 -18.583  1.00 46.41           C  
ANISOU  336  C   PHE B 305     7093   5340   5200    241   -514  -1182       C  
ATOM    337  O   PHE B 305      21.898  46.938 -18.259  1.00 51.00           O  
ANISOU  337  O   PHE B 305     7529   5940   5906    291   -356   -939       O  
ATOM    338  CB  PHE B 305      19.609  46.912 -20.663  1.00 47.75           C  
ANISOU  338  CB  PHE B 305     7722   5465   4953   -109   -355  -1178       C  
ATOM    339  CG  PHE B 305      19.341  47.120 -22.132  1.00 48.59           C  
ANISOU  339  CG  PHE B 305     8213   5444   4804   -417   -416  -1071       C  
ATOM    340  CD1 PHE B 305      20.235  46.659 -23.091  1.00 50.91           C  
ANISOU  340  CD1 PHE B 305     9117   5435   4789   -312     28  -1014       C  
ATOM    341  CD2 PHE B 305      18.164  47.719 -22.556  1.00 49.58           C  
ANISOU  341  CD2 PHE B 305     8152   5742   4943   -752   -839   -875       C  
ATOM    342  CE1 PHE B 305      19.986  46.838 -24.437  1.00 54.94           C  
ANISOU  342  CE1 PHE B 305    10253   5738   4881   -607    -20   -938       C  
ATOM    343  CE2 PHE B 305      17.902  47.906 -23.907  1.00 52.49           C  
ANISOU  343  CE2 PHE B 305     8930   5995   5019  -1188  -1037   -700       C  
ATOM    344  CZ  PHE B 305      18.812  47.465 -24.850  1.00 56.00           C  
ANISOU  344  CZ  PHE B 305    10202   6055   5017  -1160   -667   -821       C  
ATOM    345  N   THR B 306      19.980  47.978 -17.707  1.00 46.85           N  
ANISOU  345  N   THR B 306     7242   5408   5151    378   -668  -1364       N  
ATOM    346  CA  THR B 306      20.035  47.775 -16.278  1.00 47.95           C  
ANISOU  346  CA  THR B 306     7540   5510   5166    535   -725  -1462       C  
ATOM    347  C   THR B 306      18.928  46.784 -15.943  1.00 47.85           C  
ANISOU  347  C   THR B 306     7377   5760   5043    700   -438  -1450       C  
ATOM    348  O   THR B 306      17.754  46.984 -16.317  1.00 46.78           O  
ANISOU  348  O   THR B 306     7071   5796   4904    803   -350  -1248       O  
ATOM    349  CB  THR B 306      19.805  49.086 -15.531  1.00 53.93           C  
ANISOU  349  CB  THR B 306     8886   5916   5689    735   -956  -1590       C  
ATOM    350  OG1 THR B 306      20.767  50.050 -15.981  1.00 62.15           O  
ANISOU  350  OG1 THR B 306    10093   6673   6845    368  -1429  -1473       O  
ATOM    351  CG2 THR B 306      19.946  48.910 -14.020  1.00 57.34           C  
ANISOU  351  CG2 THR B 306     9874   6154   5756    854  -1049  -1710       C  
ATOM    352  N   LEU B 307      19.325  45.700 -15.280  1.00 46.32           N  
ANISOU  352  N   LEU B 307     7128   5643   4827    661   -346  -1457       N  
ATOM    353  CA  LEU B 307      18.416  44.686 -14.786  1.00 47.43           C  
ANISOU  353  CA  LEU B 307     7121   6019   4881    722   -183  -1348       C  
ATOM    354  C   LEU B 307      18.449  44.714 -13.248  1.00 49.05           C  
ANISOU  354  C   LEU B 307     7468   6253   4916   1042   -130  -1409       C  
ATOM    355  O   LEU B 307      19.525  44.644 -12.629  1.00 50.19           O  
ANISOU  355  O   LEU B 307     7780   6249   5039    920   -308  -1491       O  
ATOM    356  CB  LEU B 307      18.888  43.331 -15.292  1.00 48.84           C  
ANISOU  356  CB  LEU B 307     7383   6113   5061    445    -74  -1318       C  
ATOM    357  CG  LEU B 307      18.072  42.111 -14.919  1.00 51.78           C  
ANISOU  357  CG  LEU B 307     7737   6611   5323    282    -75  -1142       C  
ATOM    358  CD1 LEU B 307      16.655  42.255 -15.467  1.00 55.54           C  
ANISOU  358  CD1 LEU B 307     8017   7316   5769    -24   -353   -727       C  
ATOM    359  CD2 LEU B 307      18.754  40.871 -15.487  1.00 53.42           C  
ANISOU  359  CD2 LEU B 307     8486   6431   5379    104    118  -1188       C  
ATOM    360  N   GLN B 308      17.283  44.786 -12.629  1.00 50.41           N  
ANISOU  360  N   GLN B 308     7564   6637   4950   1446    122  -1184       N  
ATOM    361  CA  GLN B 308      17.212  44.716 -11.177  1.00 55.50           C  
ANISOU  361  CA  GLN B 308     8554   7263   5268   1854    313  -1212       C  
ATOM    362  C   GLN B 308      16.847  43.325 -10.683  1.00 54.51           C  
ANISOU  362  C   GLN B 308     7957   7512   5241   1759    419   -950       C  
ATOM    363  O   GLN B 308      15.955  42.666 -11.197  1.00 54.73           O  
ANISOU  363  O   GLN B 308     7426   7876   5491   1596    445   -495       O  
ATOM    364  CB  GLN B 308      16.324  45.832 -10.571  1.00 62.61           C  
ANISOU  364  CB  GLN B 308     9987   8013   5789   2680    786  -1046       C  
ATOM    365  CG  GLN B 308      14.890  45.920 -11.070  1.00 68.30           C  
ANISOU  365  CG  GLN B 308     9967   9198   6785   3135   1255   -278       C  
ATOM    366  CD  GLN B 308      14.384  47.363 -11.284  1.00 74.92           C  
ANISOU  366  CD  GLN B 308    11271   9730   7465   3867   1691    -93       C  
ATOM    367  OE1 GLN B 308      14.795  48.319 -10.601  1.00 77.41           O  
ANISOU  367  OE1 GLN B 308    12873   9353   7185   4353   1877   -536       O  
ATOM    368  NE2 GLN B 308      13.461  47.510 -12.231  1.00 76.73           N  
ANISOU  368  NE2 GLN B 308    10586  10401   8166   3890   1798    667       N  
ATOM    369  N   VAL B 309      17.596  42.874  -9.690  1.00 56.23           N  
ANISOU  369  N   VAL B 309     8442   7637   5284   1711    331  -1137       N  
ATOM    370  CA  VAL B 309      17.486  41.519  -9.188  1.00 55.55           C  
ANISOU  370  CA  VAL B 309     7968   7828   5308   1572    385   -931       C  
ATOM    371  C   VAL B 309      17.268  41.635  -7.704  1.00 59.86           C  
ANISOU  371  C   VAL B 309     8901   8426   5416   2029    600   -879       C  
ATOM    372  O   VAL B 309      17.886  42.469  -7.031  1.00 65.25           O  
ANISOU  372  O   VAL B 309    10422   8720   5648   2113    443  -1166       O  
ATOM    373  CB  VAL B 309      18.752  40.685  -9.473  1.00 52.90           C  
ANISOU  373  CB  VAL B 309     7551   7328   5221   1116    165  -1050       C  
ATOM    374  CG1 VAL B 309      18.565  39.243  -9.002  1.00 53.34           C  
ANISOU  374  CG1 VAL B 309     7336   7559   5369   1019    268   -823       C  
ATOM    375  CG2 VAL B 309      19.097  40.738 -10.952  1.00 51.58           C  
ANISOU  375  CG2 VAL B 309     7362   6953   5281    864    141  -1113       C  
ATOM    376  N   ARG B 310      16.365  40.792  -7.217  1.00 60.66           N  
ANISOU  376  N   ARG B 310     8523   8952   5572   2244    890   -419       N  
ATOM    377  CA  ARG B 310      15.890  40.802  -5.857  1.00 62.84           C  
ANISOU  377  CA  ARG B 310     9117   9369   5390   2861   1311   -191       C  
ATOM    378  C   ARG B 310      16.592  39.636  -5.160  1.00 58.28           C  
ANISOU  378  C   ARG B 310     8392   8879   4872   2432   1028   -257       C  
ATOM    379  O   ARG B 310      16.513  38.490  -5.600  1.00 54.32           O  
ANISOU  379  O   ARG B 310     7207   8602   4829   2001    866    -25       O  
ATOM    380  CB  ARG B 310      14.365  40.647  -5.882  1.00 70.97           C  
ANISOU  380  CB  ARG B 310     9394  10968   6602   3421   1869    726       C  
ATOM    381  CG  ARG B 310      13.703  41.558  -6.938  1.00 75.71           C  
ANISOU  381  CG  ARG B 310     9726  11601   7436   3617   2011   1045       C  
ATOM    382  CD  ARG B 310      12.174  41.437  -7.053  1.00 85.64           C  
ANISOU  382  CD  ARG B 310     9911  13574   9054   4084   2480   2423       C  
ATOM    383  NE  ARG B 310      11.579  42.460  -7.937  1.00 90.35           N  
ANISOU  383  NE  ARG B 310    10262  14206   9861   4390   2687   2878       N  
ATOM    384  CZ  ARG B 310      11.615  42.457  -9.277  1.00 86.17           C  
ANISOU  384  CZ  ARG B 310     9325  13670   9744   3508   1996   2869       C  
ATOM    385  NH1 ARG B 310      12.216  41.479  -9.954  1.00 80.23           N  
ANISOU  385  NH1 ARG B 310     8571  12763   9146   2342   1145   2393       N  
ATOM    386  NH2 ARG B 310      11.039  43.448  -9.948  1.00 89.03           N  
ANISOU  386  NH2 ARG B 310     9435  14106  10285   3877   2243   3392       N  
ATOM    387  N   GLY B 311      17.369  39.943  -4.133  1.00 58.88           N  
ANISOU  387  N   GLY B 311     9274   8661   4435   2435    862   -541       N  
ATOM    388  CA  GLY B 311      18.060  38.912  -3.372  1.00 57.37           C  
ANISOU  388  CA  GLY B 311     8893   8595   4310   2044    582   -449       C  
ATOM    389  C   GLY B 311      19.458  38.601  -3.880  1.00 54.51           C  
ANISOU  389  C   GLY B 311     8264   8050   4395   1338     24   -519       C  
ATOM    390  O   GLY B 311      19.698  38.483  -5.093  1.00 47.55           O  
ANISOU  390  O   GLY B 311     6945   7107   4012   1158     25   -553       O  
ATOM    391  N   ARG B 312      20.366  38.432  -2.926  1.00 44.95           N  
ANISOU  391  N   ARG B 312     6502   6044   4531  -1505   1144   -754       N  
ATOM    392  CA  ARG B 312      21.767  38.229  -3.187  1.00 48.85           C  
ANISOU  392  CA  ARG B 312     6851   6976   4731  -1544    863   -724       C  
ATOM    393  C   ARG B 312      21.991  36.942  -3.972  1.00 46.78           C  
ANISOU  393  C   ARG B 312     6529   6632   4611  -1148    588   -257       C  
ATOM    394  O   ARG B 312      22.820  36.921  -4.876  1.00 44.70           O  
ANISOU  394  O   ARG B 312     6190   6369   4424  -1081    412   -219       O  
ATOM    395  CB  ARG B 312      22.560  38.214  -1.868  1.00 57.31           C  
ANISOU  395  CB  ARG B 312     7752   8929   5094  -1811    821   -864       C  
ATOM    396  CG  ARG B 312      24.071  38.203  -2.065  1.00 64.53           C  
ANISOU  396  CG  ARG B 312     8371  10531   5614  -1903    552   -903       C  
ATOM    397  CD  ARG B 312      24.825  38.500  -0.773  1.00 75.99           C  
ANISOU  397  CD  ARG B 312     9502  13142   6228  -2307    535  -1205       C  
ATOM    398  NE  ARG B 312      25.227  39.910  -0.641  1.00 82.00           N  
ANISOU  398  NE  ARG B 312    10245  14022   6887  -3062    852  -2057       N  
ATOM    399  CZ  ARG B 312      24.635  40.833   0.126  1.00 86.88           C  
ANISOU  399  CZ  ARG B 312    11043  14524   7443  -3599   1327  -2660       C  
ATOM    400  NH1 ARG B 312      23.570  40.554   0.880  1.00 87.54           N  
ANISOU  400  NH1 ARG B 312    11304  14443   7514  -3457   1466  -2501       N  
ATOM    401  NH2 ARG B 312      25.122  42.069   0.139  1.00 91.95           N  
ANISOU  401  NH2 ARG B 312    11713  15155   8069  -4335   1780  -3483       N  
ATOM    402  N   GLU B 313      21.239  35.894  -3.668  1.00 47.81           N  
ANISOU  402  N   GLU B 313     6725   6614   4824   -935    662     45       N  
ATOM    403  CA  GLU B 313      21.458  34.584  -4.308  1.00 51.31           C  
ANISOU  403  CA  GLU B 313     7183   6872   5440   -635    624    417       C  
ATOM    404  C   GLU B 313      21.160  34.606  -5.822  1.00 45.13           C  
ANISOU  404  C   GLU B 313     6390   5656   5100   -643    555    281       C  
ATOM    405  O   GLU B 313      21.936  34.133  -6.638  1.00 44.98           O  
ANISOU  405  O   GLU B 313     6339   5602   5147   -527    451    389       O  
ATOM    406  CB  GLU B 313      20.640  33.506  -3.592  1.00 56.03           C  
ANISOU  406  CB  GLU B 313     7919   7288   6081   -500    928    693       C  
ATOM    407  CG  GLU B 313      21.184  33.159  -2.198  1.00 66.26           C  
ANISOU  407  CG  GLU B 313     9191   9165   6817   -317   1001   1053       C  
ATOM    408  CD  GLU B 313      20.506  33.894  -1.036  1.00 69.89           C  
ANISOU  408  CD  GLU B 313     9666   9904   6983   -576   1095    814       C  
ATOM    409  OE1 GLU B 313      19.994  35.039  -1.197  1.00 70.88           O  
ANISOU  409  OE1 GLU B 313     9792   9873   7265   -912   1080    318       O  
ATOM    410  OE2 GLU B 313      20.487  33.305   0.064  1.00 78.53           O  
ANISOU  410  OE2 GLU B 313    10788  11365   7681   -396   1272   1174       O  
ATOM    411  N   ARG B 314      20.023  35.171  -6.176  1.00 43.15           N  
ANISOU  411  N   ARG B 314     6114   5184   5095   -752    632     71       N  
ATOM    412  CA  ARG B 314      19.682  35.394  -7.543  1.00 42.20           C  
ANISOU  412  CA  ARG B 314     5871   4937   5224   -730    540    -23       C  
ATOM    413  C   ARG B 314      20.707  36.315  -8.215  1.00 39.88           C  
ANISOU  413  C   ARG B 314     5570   4701   4879   -697    383    -64       C  
ATOM    414  O   ARG B 314      21.094  36.095  -9.358  1.00 40.29           O  
ANISOU  414  O   ARG B 314     5556   4741   5009   -635    251    -37       O  
ATOM    415  CB  ARG B 314      18.282  35.993  -7.635  1.00 42.99           C  
ANISOU  415  CB  ARG B 314     5830   5015   5489   -732    673   -124       C  
ATOM    416  CG  ARG B 314      17.629  35.718  -8.962  1.00 44.28           C  
ANISOU  416  CG  ARG B 314     5715   5333   5776   -704    584   -168       C  
ATOM    417  CD  ARG B 314      16.145  36.008  -8.918  1.00 46.31           C  
ANISOU  417  CD  ARG B 314     5683   5797   6115   -670    720   -209       C  
ATOM    418  NE  ARG B 314      15.496  35.180  -7.940  1.00 45.63           N  
ANISOU  418  NE  ARG B 314     5658   5603   6074   -885    934   -320       N  
ATOM    419  CZ  ARG B 314      14.625  35.578  -7.012  1.00 46.17           C  
ANISOU  419  CZ  ARG B 314     5706   5647   6190   -868   1150   -324       C  
ATOM    420  NH1 ARG B 314      14.250  36.830  -6.906  1.00 47.08           N  
ANISOU  420  NH1 ARG B 314     5747   5786   6355   -622   1243   -226       N  
ATOM    421  NH2 ARG B 314      14.122  34.682  -6.176  1.00 45.53           N  
ANISOU  421  NH2 ARG B 314     5716   5444   6139  -1085   1385   -410       N  
ATOM    422  N   TYR B 315      21.112  37.357  -7.518  1.00 37.89           N  
ANISOU  422  N   TYR B 315     5395   4505   4495   -809    481   -197       N  
ATOM    423  CA  TYR B 315      22.014  38.334  -8.086  1.00 40.08           C  
ANISOU  423  CA  TYR B 315     5700   4752   4774   -877    500   -321       C  
ATOM    424  C   TYR B 315      23.366  37.672  -8.433  1.00 40.73           C  
ANISOU  424  C   TYR B 315     5702   5092   4681   -878    241   -250       C  
ATOM    425  O   TYR B 315      23.907  37.888  -9.532  1.00 38.93           O  
ANISOU  425  O   TYR B 315     5455   4770   4565   -820    172   -235       O  
ATOM    426  CB  TYR B 315      22.198  39.519  -7.139  1.00 41.70           C  
ANISOU  426  CB  TYR B 315     6024   4947   4873  -1170    828   -640       C  
ATOM    427  CG  TYR B 315      23.367  40.417  -7.499  1.00 45.77           C  
ANISOU  427  CG  TYR B 315     6578   5465   5345  -1416    966   -899       C  
ATOM    428  CD1 TYR B 315      23.274  41.322  -8.540  1.00 45.65           C  
ANISOU  428  CD1 TYR B 315     6695   4986   5661  -1283   1257   -852       C  
ATOM    429  CD2 TYR B 315      24.563  40.373  -6.780  1.00 47.93           C  
ANISOU  429  CD2 TYR B 315     6710   6297   5203  -1779    862  -1174       C  
ATOM    430  CE1 TYR B 315      24.330  42.163  -8.858  1.00 49.11           C  
ANISOU  430  CE1 TYR B 315     7219   5325   6113  -1566   1523  -1125       C  
ATOM    431  CE2 TYR B 315      25.630  41.196  -7.116  1.00 50.75           C  
ANISOU  431  CE2 TYR B 315     7047   6715   5519  -2121   1045  -1519       C  
ATOM    432  CZ  TYR B 315      25.501  42.090  -8.156  1.00 51.23           C  
ANISOU  432  CZ  TYR B 315     7338   6119   6008  -2044   1416  -1520       C  
ATOM    433  OH  TYR B 315      26.546  42.924  -8.499  1.00 60.27           O  
ANISOU  433  OH  TYR B 315     8516   7215   7167  -2432   1733  -1890       O  
ATOM    434  N   GLU B 316      23.883  36.847  -7.513  1.00 43.31           N  
ANISOU  434  N   GLU B 316     5957   5781   4716   -865    142   -129       N  
ATOM    435  CA  GLU B 316      25.135  36.135  -7.733  1.00 44.24           C  
ANISOU  435  CA  GLU B 316     5932   6220   4657   -727    -36     64       C  
ATOM    436  C   GLU B 316      25.064  35.149  -8.893  1.00 41.59           C  
ANISOU  436  C   GLU B 316     5650   5526   4625   -492    -55    267       C  
ATOM    437  O   GLU B 316      26.029  35.020  -9.624  1.00 42.86           O  
ANISOU  437  O   GLU B 316     5733   5759   4794   -422   -147    309       O  
ATOM    438  CB  GLU B 316      25.633  35.453  -6.452  1.00 51.35           C  
ANISOU  438  CB  GLU B 316     6681   7716   5113   -598    -64    323       C  
ATOM    439  CG  GLU B 316      26.204  36.459  -5.458  1.00 58.51           C  
ANISOU  439  CG  GLU B 316     7387   9311   5530   -972    -94    -20       C  
ATOM    440  CD  GLU B 316      26.738  35.835  -4.182  1.00 69.35           C  
ANISOU  440  CD  GLU B 316     8476  11605   6268   -810   -176    285       C  
ATOM    441  OE1 GLU B 316      26.308  34.705  -3.831  1.00 72.50           O  
ANISOU  441  OE1 GLU B 316     8970  11884   6691   -361    -82    824       O  
ATOM    442  OE2 GLU B 316      27.586  36.498  -3.520  1.00 77.29           O  
ANISOU  442  OE2 GLU B 316     9136  13521   6709  -1156   -270    -26       O  
ATOM    443  N   ILE B 317      23.928  34.491  -9.101  1.00 41.08           N  
ANISOU  443  N   ILE B 317     5695   5115   4798   -453     83    303       N  
ATOM    444  CA  ILE B 317      23.797  33.600 -10.244  1.00 40.65           C  
ANISOU  444  CA  ILE B 317     5673   4780   4992   -412    163    304       C  
ATOM    445  C   ILE B 317      23.849  34.392 -11.567  1.00 36.80           C  
ANISOU  445  C   ILE B 317     5104   4301   4575   -499      0    111       C  
ATOM    446  O   ILE B 317      24.598  34.060 -12.472  1.00 34.53           O  
ANISOU  446  O   ILE B 317     4802   3990   4325   -465    -31    111       O  
ATOM    447  CB  ILE B 317      22.492  32.773 -10.184  1.00 45.82           C  
ANISOU  447  CB  ILE B 317     6392   5173   5841   -527    425    218       C  
ATOM    448  CG1 ILE B 317      22.543  31.794  -9.022  1.00 50.81           C  
ANISOU  448  CG1 ILE B 317     7180   5674   6448   -365    737    516       C  
ATOM    449  CG2 ILE B 317      22.301  31.967 -11.471  1.00 48.64           C  
ANISOU  449  CG2 ILE B 317     6734   5350   6398   -687    576      3       C  
ATOM    450  CD1 ILE B 317      21.178  31.311  -8.583  1.00 54.35           C  
ANISOU  450  CD1 ILE B 317     7702   5893   7055   -553   1042    387       C  
ATOM    451  N   LEU B 318      23.030  35.428 -11.673  1.00 35.49           N  
ANISOU  451  N   LEU B 318     4889   4172   4423   -547    -29     11       N  
ATOM    452  CA  LEU B 318      22.954  36.233 -12.885  1.00 34.64           C  
ANISOU  452  CA  LEU B 318     4696   4124   4338   -489    -92     -9       C  
ATOM    453  C   LEU B 318      24.232  37.048 -13.156  1.00 35.57           C  
ANISOU  453  C   LEU B 318     4893   4209   4412   -481   -108      0       C  
ATOM    454  O   LEU B 318      24.663  37.178 -14.315  1.00 37.41           O  
ANISOU  454  O   LEU B 318     5094   4472   4645   -423   -154     29       O  
ATOM    455  CB  LEU B 318      21.714  37.136 -12.851  1.00 36.25           C  
ANISOU  455  CB  LEU B 318     4806   4383   4584   -378     12     44       C  
ATOM    456  CG  LEU B 318      20.347  36.427 -12.667  1.00 36.88           C  
ANISOU  456  CG  LEU B 318     4692   4638   4681   -439     37    -23       C  
ATOM    457  CD1 LEU B 318      19.201  37.400 -12.418  1.00 38.69           C  
ANISOU  457  CD1 LEU B 318     4775   4971   4951   -235    184    107       C  
ATOM    458  CD2 LEU B 318      20.021  35.558 -13.867  1.00 40.59           C  
ANISOU  458  CD2 LEU B 318     4919   5440   5063   -569    -59   -168       C  
ATOM    459  N   LYS B 319      24.833  37.625 -12.123  1.00 35.89           N  
ANISOU  459  N   LYS B 319     5001   4261   4371   -606    -31    -86       N  
ATOM    460  CA  LYS B 319      26.144  38.288 -12.280  1.00 37.44           C  
ANISOU  460  CA  LYS B 319     5200   4531   4492   -748      7   -210       C  
ATOM    461  C   LYS B 319      27.192  37.314 -12.834  1.00 36.60           C  
ANISOU  461  C   LYS B 319     4978   4605   4323   -669   -188   -116       C  
ATOM    462  O   LYS B 319      27.975  37.657 -13.738  1.00 39.19           O  
ANISOU  462  O   LYS B 319     5294   4910   4684   -691   -174   -153       O  
ATOM    463  CB  LYS B 319      26.628  38.880 -10.932  1.00 41.94           C  
ANISOU  463  CB  LYS B 319     5744   5337   4854  -1051    128   -464       C  
ATOM    464  CG  LYS B 319      27.810  39.838 -11.034  1.00 45.61           C  
ANISOU  464  CG  LYS B 319     6171   5918   5239  -1387    311   -780       C  
ATOM    465  CD  LYS B 319      28.413  40.080  -9.657  1.00 50.47           C  
ANISOU  465  CD  LYS B 319     6590   7120   5464  -1799    347  -1130       C  
ATOM    466  CE  LYS B 319      29.511  41.131  -9.646  1.00 55.13           C  
ANISOU  466  CE  LYS B 319     7090   7914   5942  -2346    646  -1651       C  
ATOM    467  NZ  LYS B 319      30.750  40.681 -10.350  1.00 55.90           N  
ANISOU  467  NZ  LYS B 319     6912   8391   5935  -2291    400  -1569       N  
ATOM    468  N   LYS B 320      27.194  36.087 -12.341  1.00 36.27           N  
ANISOU  468  N   LYS B 320     4878   4673   4227   -532   -266     48       N  
ATOM    469  CA  LYS B 320      28.117  35.088 -12.876  1.00 37.86           C  
ANISOU  469  CA  LYS B 320     5006   4928   4450   -360   -289    207       C  
ATOM    470  C   LYS B 320      27.849  34.755 -14.347  1.00 36.89           C  
ANISOU  470  C   LYS B 320     4968   4526   4521   -357   -245    136       C  
ATOM    471  O   LYS B 320      28.775  34.543 -15.123  1.00 38.39           O  
ANISOU  471  O   LYS B 320     5117   4732   4734   -312   -235    144       O  
ATOM    472  CB  LYS B 320      28.102  33.857 -11.990  1.00 45.07           C  
ANISOU  472  CB  LYS B 320     5906   5896   5321   -116   -176    503       C  
ATOM    473  CG  LYS B 320      28.937  32.689 -12.483  1.00 53.16           C  
ANISOU  473  CG  LYS B 320     6913   6820   6463    179      7    765       C  
ATOM    474  CD  LYS B 320      29.504  31.849 -11.334  1.00 59.92           C  
ANISOU  474  CD  LYS B 320     7641   7987   7138    602    161   1265       C  
ATOM    475  CE  LYS B 320      28.496  31.567 -10.228  1.00 62.59           C  
ANISOU  475  CE  LYS B 320     8107   8264   7408    635    287   1402       C  
ATOM    476  NZ  LYS B 320      29.080  31.616  -8.844  1.00 68.21           N  
ANISOU  476  NZ  LYS B 320     8536   9753   7627    906    188   1785       N  
ATOM    477  N   LEU B 321      26.583  34.724 -14.758  1.00 34.97           N  
ANISOU  477  N   LEU B 321     4779   4154   4353   -432   -215     37       N  
ATOM    478  CA  LEU B 321      26.275  34.463 -16.167  1.00 33.97           C  
ANISOU  478  CA  LEU B 321     4620   4041   4244   -504   -200    -95       C  
ATOM    479  C   LEU B 321      26.685  35.683 -16.993  1.00 32.32           C  
ANISOU  479  C   LEU B 321     4386   3950   3942   -453   -286    -53       C  
ATOM    480  O   LEU B 321      27.322  35.554 -18.032  1.00 32.50           O  
ANISOU  480  O   LEU B 321     4399   4024   3925   -462   -279    -89       O  
ATOM    481  CB  LEU B 321      24.792  34.128 -16.353  1.00 35.02           C  
ANISOU  481  CB  LEU B 321     4660   4287   4358   -640   -160   -244       C  
ATOM    482  CG  LEU B 321      24.297  32.887 -15.602  1.00 35.85           C  
ANISOU  482  CG  LEU B 321     4847   4157   4614   -764     89   -336       C  
ATOM    483  CD1 LEU B 321      22.816  32.688 -15.849  1.00 37.80           C  
ANISOU  483  CD1 LEU B 321     4908   4646   4807  -1014    140   -595       C  
ATOM    484  CD2 LEU B 321      25.073  31.660 -16.041  1.00 37.98           C  
ANISOU  484  CD2 LEU B 321     5257   4131   5040   -814    404   -412       C  
ATOM    485  N   ASN B 322      26.376  36.871 -16.501  1.00 31.84           N  
ANISOU  485  N   ASN B 322     4362   3859   3877   -398   -252     29       N  
ATOM    486  CA  ASN B 322      26.673  38.071 -17.245  1.00 34.25           C  
ANISOU  486  CA  ASN B 322     4724   4121   4167   -305   -125    133       C  
ATOM    487  C   ASN B 322      28.179  38.273 -17.418  1.00 34.59           C  
ANISOU  487  C   ASN B 322     4820   4091   4232   -429    -70     39       C  
ATOM    488  O   ASN B 322      28.653  38.566 -18.520  1.00 37.24           O  
ANISOU  488  O   ASN B 322     5183   4431   4535   -374      0    101       O  
ATOM    489  CB  ASN B 322      26.023  39.292 -16.572  1.00 36.92           C  
ANISOU  489  CB  ASN B 322     5166   4263   4596   -222    129    225       C  
ATOM    490  CG  ASN B 322      25.957  40.493 -17.484  1.00 39.45           C  
ANISOU  490  CG  ASN B 322     5589   4444   4953     28    455    489       C  
ATOM    491  OD1 ASN B 322      25.413  40.442 -18.605  1.00 42.54           O  
ANISOU  491  OD1 ASN B 322     5837   5144   5180    319    390    767       O  
ATOM    492  ND2 ASN B 322      26.507  41.592 -17.015  1.00 42.13           N  
ANISOU  492  ND2 ASN B 322     6163   4370   5472    -93    891    403       N  
ATOM    493  N   ASP B 323      28.932  38.141 -16.339  1.00 38.35           N  
ANISOU  493  N   ASP B 323     5249   4620   4699   -595    -94    -99       N  
ATOM    494  CA  ASP B 323      30.376  38.333 -16.411  1.00 38.80           C  
ANISOU  494  CA  ASP B 323     5212   4814   4713   -750    -55   -226       C  
ATOM    495  C   ASP B 323      31.013  37.304 -17.323  1.00 37.66           C  
ANISOU  495  C   ASP B 323     4987   4743   4578   -611   -165   -138       C  
ATOM    496  O   ASP B 323      31.868  37.669 -18.115  1.00 38.57           O  
ANISOU  496  O   ASP B 323     5091   4859   4705   -670    -71   -189       O  
ATOM    497  CB  ASP B 323      31.018  38.277 -15.029  1.00 43.04           C  
ANISOU  497  CB  ASP B 323     5546   5726   5080   -938   -114   -375       C  
ATOM    498  CG  ASP B 323      30.746  39.527 -14.192  1.00 48.33           C  
ANISOU  498  CG  ASP B 323     6303   6339   5721  -1273    146   -663       C  
ATOM    499  OD1 ASP B 323      30.652  40.684 -14.692  1.00 58.20           O  
ANISOU  499  OD1 ASP B 323     7775   7192   7145  -1418    530   -792       O  
ATOM    500  OD2 ASP B 323      30.679  39.355 -12.982  1.00 52.58           O  
ANISOU  500  OD2 ASP B 323     6698   7228   6050  -1398     63   -763       O  
ATOM    501  N   SER B 324      30.570  36.044 -17.295  1.00 37.43           N  
ANISOU  501  N   SER B 324     4944   4693   4581   -458   -244    -39       N  
ATOM    502  CA  SER B 324      31.191  35.036 -18.182  1.00 37.48           C  
ANISOU  502  CA  SER B 324     4932   4649   4656   -365   -169    -19       C  
ATOM    503  C   SER B 324      30.861  35.262 -19.657  1.00 38.00           C  
ANISOU  503  C   SER B 324     5090   4667   4679   -440   -128   -123       C  
ATOM    504  O   SER B 324      31.698  35.006 -20.509  1.00 40.20           O  
ANISOU  504  O   SER B 324     5357   4947   4968   -443    -34   -169       O  
ATOM    505  CB  SER B 324      30.893  33.612 -17.770  1.00 40.05           C  
ANISOU  505  CB  SER B 324     5292   4821   5101   -222    -25     74       C  
ATOM    506  OG  SER B 324      29.590  33.233 -18.203  1.00 46.47           O  
ANISOU  506  OG  SER B 324     6226   5484   5945   -375     37    -96       O  
ATOM    507  N   LEU B 325      29.677  35.765 -19.978  1.00 37.13           N  
ANISOU  507  N   LEU B 325     5015   4629   4462   -461   -183   -120       N  
ATOM    508  CA  LEU B 325      29.358  36.077 -21.381  1.00 38.24           C  
ANISOU  508  CA  LEU B 325     5136   4992   4400   -455   -168   -118       C  
ATOM    509  C   LEU B 325      30.197  37.239 -21.925  1.00 39.43           C  
ANISOU  509  C   LEU B 325     5369   5081   4529   -371    -45     35       C  
ATOM    510  O   LEU B 325      30.655  37.193 -23.071  1.00 43.66           O  
ANISOU  510  O   LEU B 325     5909   5750   4929   -372     22     30       O  
ATOM    511  CB  LEU B 325      27.874  36.382 -21.568  1.00 38.17           C  
ANISOU  511  CB  LEU B 325     5006   5306   4189   -386   -254    -36       C  
ATOM    512  CG  LEU B 325      26.904  35.226 -21.387  1.00 39.24           C  
ANISOU  512  CG  LEU B 325     5009   5615   4283   -601   -292   -307       C  
ATOM    513  CD1 LEU B 325      25.478  35.754 -21.234  1.00 38.65           C  
ANISOU  513  CD1 LEU B 325     4718   5939   4025   -491   -398   -178       C  
ATOM    514  CD2 LEU B 325      26.997  34.260 -22.568  1.00 40.81           C  
ANISOU  514  CD2 LEU B 325     5121   6092   4293   -885   -195   -655       C  
ATOM    515  N   GLU B 326      30.419  38.253 -21.096  1.00 39.49           N  
ANISOU  515  N   GLU B 326     5463   4866   4674   -364     73    109       N  
ATOM    516  CA  GLU B 326      31.289  39.384 -21.443  1.00 42.71           C  
ANISOU  516  CA  GLU B 326     6000   5078   5150   -406    375    153       C  
ATOM    517  C   GLU B 326      32.741  38.965 -21.639  1.00 43.85           C  
ANISOU  517  C   GLU B 326     6050   5265   5344   -593    381    -47       C  
ATOM    518  O   GLU B 326      33.455  39.495 -22.501  1.00 45.27           O  
ANISOU  518  O   GLU B 326     6307   5373   5520   -627    612    -25       O  
ATOM    519  CB  GLU B 326      31.237  40.468 -20.365  1.00 41.88           C  
ANISOU  519  CB  GLU B 326     6011   4688   5211   -537    648     84       C  
ATOM    520  CG  GLU B 326      29.889  41.160 -20.271  1.00 44.78           C  
ANISOU  520  CG  GLU B 326     6502   4912   5597   -259    822    369       C  
ATOM    521  CD  GLU B 326      29.895  42.359 -19.333  1.00 51.47           C  
ANISOU  521  CD  GLU B 326     7560   5319   6675   -430   1321    245       C  
ATOM    522  OE1 GLU B 326      30.929  42.609 -18.673  1.00 53.68           O  
ANISOU  522  OE1 GLU B 326     7829   5538   7026   -886   1468   -172       O  
ATOM    523  OE2 GLU B 326      28.864  43.060 -19.265  1.00 52.82           O  
ANISOU  523  OE2 GLU B 326     7870   5265   6935   -128   1627    539       O  
ATOM    524  N   LEU B 327      33.199  38.027 -20.824  1.00 41.51           N  
ANISOU  524  N   LEU B 327     5567   5117   5088   -655    185   -177       N  
ATOM    525  CA  LEU B 327      34.548  37.533 -21.003  1.00 40.56           C  
ANISOU  525  CA  LEU B 327     5260   5152   4998   -706    208   -269       C  
ATOM    526  C   LEU B 327      34.630  36.802 -22.359  1.00 39.99           C  
ANISOU  526  C   LEU B 327     5266   5027   4901   -598    261   -238       C  
ATOM    527  O   LEU B 327      35.622  36.936 -23.081  1.00 40.62           O  
ANISOU  527  O   LEU B 327     5306   5133   4995   -651    412   -291       O  
ATOM    528  CB  LEU B 327      34.970  36.644 -19.827  1.00 40.36           C  
ANISOU  528  CB  LEU B 327     4964   5402   4967   -616     54   -235       C  
ATOM    529  CG  LEU B 327      36.371  36.053 -19.886  1.00 42.03           C  
ANISOU  529  CG  LEU B 327     4860   5927   5183   -515    101   -199       C  
ATOM    530  CD1 LEU B 327      37.419  37.151 -19.925  1.00 43.74           C  
ANISOU  530  CD1 LEU B 327     4873   6422   5324   -849    209   -446       C  
ATOM    531  CD2 LEU B 327      36.619  35.107 -18.720  1.00 43.52           C  
ANISOU  531  CD2 LEU B 327     4756   6477   5303   -218      4     49       C  
ATOM    532  N   SER B 328      33.600  36.028 -22.698  1.00 37.66           N  
ANISOU  532  N   SER B 328     5054   4711   4544   -527    186   -231       N  
ATOM    533  CA  SER B 328      33.602  35.288 -23.968  1.00 42.55           C  
ANISOU  533  CA  SER B 328     5721   5381   5063   -569    301   -355       C  
ATOM    534  C   SER B 328      33.628  36.227 -25.189  1.00 42.64           C  
ANISOU  534  C   SER B 328     5809   5563   4828   -579    372   -277       C  
ATOM    535  O   SER B 328      34.081  35.836 -26.239  1.00 46.92           O  
ANISOU  535  O   SER B 328     6366   6207   5253   -648    505   -393       O  
ATOM    536  CB  SER B 328      32.388  34.373 -24.066  1.00 43.89           C  
ANISOU  536  CB  SER B 328     5910   5619   5148   -664    280   -516       C  
ATOM    537  OG  SER B 328      32.622  33.182 -23.376  1.00 49.28           O  
ANISOU  537  OG  SER B 328     6610   6015   6099   -636    457   -587       O  
ATOM    538  N   ASP B 329      33.097  37.438 -25.030  1.00 44.15           N  
ANISOU  538  N   ASP B 329     6069   5761   4942   -468    372    -38       N  
ATOM    539  CA  ASP B 329      33.167  38.495 -26.036  1.00 46.50           C  
ANISOU  539  CA  ASP B 329     6484   6133   5048   -333    591    218       C  
ATOM    540  C   ASP B 329      34.570  39.002 -26.315  1.00 46.35           C  
ANISOU  540  C   ASP B 329     6550   5862   5199   -453    880    160       C  
ATOM    541  O   ASP B 329      34.856  39.392 -27.423  1.00 48.54           O  
ANISOU  541  O   ASP B 329     6923   6224   5293   -379   1095    308       O  
ATOM    542  CB  ASP B 329      32.394  39.723 -25.559  1.00 49.81           C  
ANISOU  542  CB  ASP B 329     7022   6398   5506   -112    746    552       C  
ATOM    543  CG  ASP B 329      30.891  39.520 -25.518  1.00 51.11           C  
ANISOU  543  CG  ASP B 329     7041   6952   5423    101    520    732       C  
ATOM    544  OD1 ASP B 329      30.364  38.754 -26.353  1.00 55.04           O  
ANISOU  544  OD1 ASP B 329     7340   8022   5549     83    313    658       O  
ATOM    545  OD2 ASP B 329      30.249  40.191 -24.673  1.00 54.30           O  
ANISOU  545  OD2 ASP B 329     7505   7139   5985    244    612    903       O  
ATOM    546  N   VAL B 330      35.422  39.062 -25.297  1.00 43.95           N  
ANISOU  546  N   VAL B 330     6159   5358   5183   -651    908    -49       N  
ATOM    547  CA  VAL B 330      36.712  39.747 -25.420  1.00 46.50           C  
ANISOU  547  CA  VAL B 330     6473   5541   5651   -867   1234   -182       C  
ATOM    548  C   VAL B 330      37.908  38.825 -25.508  1.00 46.18           C  
ANISOU  548  C   VAL B 330     6163   5701   5680   -964   1157   -397       C  
ATOM    549  O   VAL B 330      39.030  39.288 -25.750  1.00 49.20           O  
ANISOU  549  O   VAL B 330     6453   6092   6146  -1166   1421   -541       O  
ATOM    550  CB  VAL B 330      36.943  40.764 -24.254  1.00 48.02           C  
ANISOU  550  CB  VAL B 330     6660   5549   6035  -1146   1458   -361       C  
ATOM    551  CG1 VAL B 330      35.921  41.882 -24.342  1.00 49.52           C  
ANISOU  551  CG1 VAL B 330     7200   5358   6255   -989   1803    -86       C  
ATOM    552  CG2 VAL B 330      36.896  40.089 -22.878  1.00 44.65           C  
ANISOU  552  CG2 VAL B 330     5938   5407   5619  -1230   1089   -543       C  
ATOM    553  N   VAL B 331      37.694  37.535 -25.289  1.00 44.66           N  
ANISOU  553  N   VAL B 331     5838   5642   5488   -813    902   -410       N  
ATOM    554  CA  VAL B 331      38.782  36.575 -25.403  1.00 46.78           C  
ANISOU  554  CA  VAL B 331     5867   6036   5872   -752    962   -492       C  
ATOM    555  C   VAL B 331      38.716  36.095 -26.853  1.00 49.57           C  
ANISOU  555  C   VAL B 331     6417   6302   6115   -733   1138   -538       C  
ATOM    556  O   VAL B 331      37.705  35.545 -27.248  1.00 50.64           O  
ANISOU  556  O   VAL B 331     6706   6428   6105   -711   1069   -568       O  
ATOM    557  CB  VAL B 331      38.622  35.370 -24.447  1.00 43.73           C  
ANISOU  557  CB  VAL B 331     5305   5711   5599   -518    820   -404       C  
ATOM    558  CG1 VAL B 331      39.720  34.343 -24.695  1.00 44.94           C  
ANISOU  558  CG1 VAL B 331     5240   5921   5913   -295   1049   -351       C  
ATOM    559  CG2 VAL B 331      38.632  35.836 -22.988  1.00 44.48           C  
ANISOU  559  CG2 VAL B 331     5160   6077   5664   -547    612   -355       C  
ATOM    560  N   PRO B 332      39.774  36.306 -27.642  1.00 56.02           N  
ANISOU  560  N   PRO B 332     9326   6532   5426  -1067   1220   -920       N  
ATOM    561  CA  PRO B 332      39.674  35.850 -29.036  1.00 61.50           C  
ANISOU  561  CA  PRO B 332    10637   7046   5683   -890    984   -849       C  
ATOM    562  C   PRO B 332      39.559  34.333 -29.109  1.00 62.90           C  
ANISOU  562  C   PRO B 332    10732   7333   5832   -781    782   -993       C  
ATOM    563  O   PRO B 332      40.234  33.629 -28.350  1.00 63.56           O  
ANISOU  563  O   PRO B 332    10366   7683   6098   -810   1080  -1077       O  
ATOM    564  CB  PRO B 332      40.984  36.335 -29.661  1.00 62.85           C  
ANISOU  564  CB  PRO B 332    11198   7260   5421  -1065   1619   -774       C  
ATOM    565  CG  PRO B 332      41.433  37.464 -28.777  1.00 61.71           C  
ANISOU  565  CG  PRO B 332    10731   7172   5544  -1381   1926   -729       C  
ATOM    566  CD  PRO B 332      41.009  37.062 -27.394  1.00 56.57           C  
ANISOU  566  CD  PRO B 332     9401   6731   5359  -1404   1742   -883       C  
ATOM    567  N   ALA B 333      38.683  33.847 -29.987  1.00 66.78           N  
ANISOU  567  N   ALA B 333    11708   7559   6104   -696    178   -983       N  
ATOM    568  CA  ALA B 333      38.429  32.418 -30.142  1.00 67.07           C  
ANISOU  568  CA  ALA B 333    11888   7531   6063   -690   -101  -1147       C  
ATOM    569  C   ALA B 333      39.735  31.642 -30.230  1.00 67.68           C  
ANISOU  569  C   ALA B 333    12157   7678   5878   -559    611  -1302       C  
ATOM    570  O   ALA B 333      39.810  30.488 -29.805  1.00 66.73           O  
ANISOU  570  O   ALA B 333    11891   7530   5933   -486    609  -1423       O  
ATOM    571  CB  ALA B 333      37.576  32.157 -31.380  1.00 72.13           C  
ANISOU  571  CB  ALA B 333    13360   7805   6239   -765   -879  -1114       C  
ATOM    572  N   SER B 334      40.755  32.284 -30.790  1.00 70.56           N  
ANISOU  572  N   SER B 334    12819   8092   5898   -512   1263  -1255       N  
ATOM    573  CA  SER B 334      42.098  31.722 -30.845  1.00 73.32           C  
ANISOU  573  CA  SER B 334    13058   8571   6228   -308   2108  -1328       C  
ATOM    574  C   SER B 334      42.555  31.390 -29.435  1.00 68.72           C  
ANISOU  574  C   SER B 334    11395   8360   6354   -282   2162  -1248       C  
ATOM    575  O   SER B 334      42.648  30.213 -29.081  1.00 67.04           O  
ANISOU  575  O   SER B 334    11055   8067   6347    -54   2115  -1319       O  
ATOM    576  CB  SER B 334      43.087  32.700 -31.525  1.00 78.34           C  
ANISOU  576  CB  SER B 334    13922   9293   6550   -401   2881  -1204       C  
ATOM    577  OG  SER B 334      42.423  33.614 -32.394  1.00 80.27           O  
ANISOU  577  OG  SER B 334    15025   9249   6224   -604   2552  -1101       O  
ATOM    578  N   ASP B 335      42.785  32.433 -28.623  1.00 65.75           N  
ANISOU  578  N   ASP B 335    10405   8300   6274   -568   2180  -1086       N  
ATOM    579  CA  ASP B 335      43.323  32.281 -27.265  1.00 60.52           C  
ANISOU  579  CA  ASP B 335     8881   8003   6109   -691   2140   -966       C  
ATOM    580  C   ASP B 335      42.428  31.387 -26.417  1.00 55.51           C  
ANISOU  580  C   ASP B 335     8136   7290   5665   -664   1614  -1017       C  
ATOM    581  O   ASP B 335      42.910  30.667 -25.545  1.00 54.47           O  
ANISOU  581  O   ASP B 335     7574   7318   5804   -619   1544   -897       O  
ATOM    582  CB  ASP B 335      43.450  33.632 -26.558  1.00 61.01           C  
ANISOU  582  CB  ASP B 335     8654   8263   6262  -1156   2124   -871       C  
ATOM    583  CG  ASP B 335      44.208  34.664 -27.365  1.00 64.24           C  
ANISOU  583  CG  ASP B 335     9254   8676   6478  -1351   2622   -779       C  
ATOM    584  OD1 ASP B 335      44.922  34.312 -28.311  1.00 72.16           O  
ANISOU  584  OD1 ASP B 335    10396   9675   7343  -1140   3141   -746       O  
ATOM    585  OD2 ASP B 335      44.072  35.852 -27.055  1.00 65.38           O  
ANISOU  585  OD2 ASP B 335     9504   8754   6584  -1737   2583   -747       O  
ATOM    586  N   ALA B 336      41.124  31.458 -26.660  1.00 52.12           N  
ANISOU  586  N   ALA B 336     8056   6609   5136   -727   1216  -1128       N  
ATOM    587  CA  ALA B 336      40.153  30.631 -25.947  1.00 50.01           C  
ANISOU  587  CA  ALA B 336     7656   6251   5093   -811    808  -1155       C  
ATOM    588  C   ALA B 336      40.505  29.157 -26.067  1.00 52.88           C  
ANISOU  588  C   ALA B 336     8221   6417   5453   -587    781  -1177       C  
ATOM    589  O   ALA B 336      40.546  28.462 -25.064  1.00 51.92           O  
ANISOU  589  O   ALA B 336     7831   6343   5552   -655    675  -1063       O  
ATOM    590  CB  ALA B 336      38.754  30.876 -26.486  1.00 50.41           C  
ANISOU  590  CB  ALA B 336     7911   6069   5174   -890    367  -1213       C  
ATOM    591  N   GLU B 337      40.761  28.702 -27.296  1.00 56.95           N  
ANISOU  591  N   GLU B 337     9365   6626   5648   -326    916  -1321       N  
ATOM    592  CA  GLU B 337      41.197  27.328 -27.570  1.00 64.99           C  
ANISOU  592  CA  GLU B 337    10787   7276   6630     -3   1057  -1411       C  
ATOM    593  C   GLU B 337      42.456  26.961 -26.767  1.00 66.15           C  
ANISOU  593  C   GLU B 337    10304   7644   7186    325   1439  -1185       C  
ATOM    594  O   GLU B 337      42.516  25.884 -26.171  1.00 67.56           O  
ANISOU  594  O   GLU B 337    10475   7590   7601    485   1280  -1084       O  
ATOM    595  CB  GLU B 337      41.433  27.118 -29.098  1.00 72.30           C  
ANISOU  595  CB  GLU B 337    12693   7793   6982    227   1375  -1670       C  
ATOM    596  CG  GLU B 337      41.658  25.674 -29.553  1.00 79.97           C  
ANISOU  596  CG  GLU B 337    14437   8147   7799    560   1565  -1890       C  
ATOM    597  CD  GLU B 337      41.870  25.515 -31.072  1.00 89.65           C  
ANISOU  597  CD  GLU B 337    16920   8893   8250    718   1997  -2226       C  
ATOM    598  OE1 GLU B 337      41.571  26.456 -31.849  1.00 89.72           O  
ANISOU  598  OE1 GLU B 337    17332   9015   7740    450   1892  -2248       O  
ATOM    599  OE2 GLU B 337      42.330  24.426 -31.507  1.00 97.77           O  
ANISOU  599  OE2 GLU B 337    18696   9334   9116   1120   2474  -2472       O  
ATOM    600  N   LYS B 338      43.452  27.852 -26.750  1.00 66.64           N  
ANISOU  600  N   LYS B 338     9822   8125   7371    381   1860  -1044       N  
ATOM    601  CA  LYS B 338      44.700  27.610 -26.004  1.00 70.52           C  
ANISOU  601  CA  LYS B 338     9494   8920   8379    633   2057   -728       C  
ATOM    602  C   LYS B 338      44.439  27.377 -24.519  1.00 66.95           C  
ANISOU  602  C   LYS B 338     8637   8653   8147    333   1425   -465       C  
ATOM    603  O   LYS B 338      45.105  26.549 -23.907  1.00 71.86           O  
ANISOU  603  O   LYS B 338     8914   9248   9139    637   1286   -170       O  
ATOM    604  CB  LYS B 338      45.687  28.783 -26.139  1.00 73.11           C  
ANISOU  604  CB  LYS B 338     9191   9739   8848    470   2472   -579       C  
ATOM    605  CG  LYS B 338      46.366  28.921 -27.493  1.00 81.22           C  
ANISOU  605  CG  LYS B 338    10483  10642   9732    805   3352   -714       C  
ATOM    606  CD  LYS B 338      47.288  30.139 -27.520  1.00 84.33           C  
ANISOU  606  CD  LYS B 338    10188  11533  10319    450   3750   -503       C  
ATOM    607  CE  LYS B 338      47.907  30.345 -28.897  1.00 92.21           C  
ANISOU  607  CE  LYS B 338    11560  12395  11078    682   4798   -620       C  
ATOM    608  NZ  LYS B 338      48.615  31.651 -29.004  1.00 94.69           N  
ANISOU  608  NZ  LYS B 338    11374  13117  11485    138   5181   -410       N  
ATOM    609  N   TYR B 339      43.506  28.138 -23.939  1.00 59.68           N  
ANISOU  609  N   TYR B 339     7799   7884   6993   -232   1096   -539       N  
ATOM    610  CA  TYR B 339      43.123  27.968 -22.518  1.00 58.40           C  
ANISOU  610  CA  TYR B 339     7502   7845   6842   -620    650   -345       C  
ATOM    611  C   TYR B 339      42.387  26.659 -22.239  1.00 59.85           C  
ANISOU  611  C   TYR B 339     8106   7598   7035   -546    399   -313       C  
ATOM    612  O   TYR B 339      42.625  26.029 -21.199  1.00 63.48           O  
ANISOU  612  O   TYR B 339     8513   8051   7555   -629     98      0       O  
ATOM    613  CB  TYR B 339      42.255  29.138 -22.017  1.00 52.88           C  
ANISOU  613  CB  TYR B 339     6875   7313   5903  -1172    627   -504       C  
ATOM    614  CG  TYR B 339      43.004  30.438 -21.824  1.00 51.69           C  
ANISOU  614  CG  TYR B 339     6438   7510   5692  -1461    756   -476       C  
ATOM    615  CD1 TYR B 339      44.008  30.553 -20.871  1.00 54.54           C  
ANISOU  615  CD1 TYR B 339     6428   8199   6093  -1740    491   -188       C  
ATOM    616  CD2 TYR B 339      42.680  31.551 -22.562  1.00 49.42           C  
ANISOU  616  CD2 TYR B 339     6315   7167   5295  -1534   1033   -690       C  
ATOM    617  CE1 TYR B 339      44.678  31.740 -20.672  1.00 55.50           C  
ANISOU  617  CE1 TYR B 339     6345   8593   6148  -2182    521   -169       C  
ATOM    618  CE2 TYR B 339      43.350  32.744 -22.381  1.00 52.22           C  
ANISOU  618  CE2 TYR B 339     6537   7722   5580  -1897   1163   -664       C  
ATOM    619  CZ  TYR B 339      44.338  32.828 -21.433  1.00 53.86           C  
ANISOU  619  CZ  TYR B 339     6375   8260   5829  -2270    917   -432       C  
ATOM    620  OH  TYR B 339      44.985  34.009 -21.284  1.00 56.07           O  
ANISOU  620  OH  TYR B 339     6579   8690   6034  -2778    977   -419       O  
ATOM    621  N   ARG B 340      41.485  26.263 -23.144  1.00 60.59           N  
ANISOU  621  N   ARG B 340     8691   7300   7027   -488    437   -594       N  
ATOM    622  CA  ARG B 340      40.729  25.006 -22.981  1.00 63.80           C  
ANISOU  622  CA  ARG B 340     9567   7215   7459   -568    181   -584       C  
ATOM    623  C   ARG B 340      41.601  23.749 -23.082  1.00 69.80           C  
ANISOU  623  C   ARG B 340    10598   7532   8390    -18    217   -423       C  
ATOM    624  O   ARG B 340      41.208  22.710 -22.564  1.00 74.34           O  
ANISOU  624  O   ARG B 340    11553   7680   9010   -128    -31   -274       O  
ATOM    625  CB  ARG B 340      39.546  24.913 -23.959  1.00 63.93           C  
ANISOU  625  CB  ARG B 340    10023   6919   7347   -781     35   -898       C  
ATOM    626  CG  ARG B 340      38.456  25.963 -23.739  1.00 60.74           C  
ANISOU  626  CG  ARG B 340     9240   6836   7001  -1233    -65   -960       C  
ATOM    627  CD  ARG B 340      37.342  25.848 -24.773  1.00 62.56           C  
ANISOU  627  CD  ARG B 340     9753   6791   7226  -1426   -434  -1151       C  
ATOM    628  NE  ARG B 340      36.558  27.087 -24.931  1.00 63.28           N  
ANISOU  628  NE  ARG B 340     9394   7169   7477  -1565   -509  -1169       N  
ATOM    629  CZ  ARG B 340      35.514  27.455 -24.173  1.00 62.43           C  
ANISOU  629  CZ  ARG B 340     8702   7233   7785  -1886   -505  -1077       C  
ATOM    630  NH1 ARG B 340      35.093  26.711 -23.153  1.00 65.27           N  
ANISOU  630  NH1 ARG B 340     8894   7562   8340  -2238   -390   -960       N  
ATOM    631  NH2 ARG B 340      34.869  28.579 -24.446  1.00 61.17           N  
ANISOU  631  NH2 ARG B 340     8148   7221   7871  -1826   -540  -1077       N  
ATOM    632  N   GLN B 341      42.768  23.832 -23.729  1.00 74.59           N  
ANISOU  632  N   GLN B 341    11007   8181   9150    585    603   -423       N  
ATOM    633  CA  GLN B 341      43.725  22.701 -23.740  1.00 82.97           C  
ANISOU  633  CA  GLN B 341    12139   8808  10577   1302    760   -210       C  
ATOM    634  C   GLN B 341      44.415  22.530 -22.376  1.00 84.97           C  
ANISOU  634  C   GLN B 341    11756   9346  11182   1335    329    378       C  
ATOM    635  O   GLN B 341      44.354  21.454 -21.772  1.00 89.10           O  
ANISOU  635  O   GLN B 341    12631   9388  11833   1483      5    668       O  
ATOM    636  CB  GLN B 341      44.787  22.854 -24.843  1.00 88.44           C  
ANISOU  636  CB  GLN B 341    12677   9478  11448   1996   1502   -366       C  
ATOM    637  CG  GLN B 341      44.360  22.368 -26.225  1.00 92.22           C  
ANISOU  637  CG  GLN B 341    14253   9291  11494   2198   1950   -893       C  
ATOM    638  CD  GLN B 341      45.443  21.563 -26.939  1.00103.64           C  
ANISOU  638  CD  GLN B 341    15924  10210  13243   3163   2780   -968       C  
ATOM    639  OE1 GLN B 341      46.092  22.054 -27.867  1.00108.03           O  
ANISOU  639  OE1 GLN B 341    16445  10893  13709   3477   3588  -1167       O  
ATOM    640  NE2 GLN B 341      45.642  20.318 -26.507  1.00109.26           N  
ANISOU  640  NE2 GLN B 341    16917  10261  14333   3666   2683   -791       N  
ATOM    641  N   LYS B 342      45.073  23.592 -21.913  1.00 83.41           N  
ANISOU  641  N   LYS B 342    10736   9872  11085   1128    250    581       N  
ATOM    642  CA  LYS B 342      45.693  23.636 -20.582  1.00 87.14           C  
ANISOU  642  CA  LYS B 342    10680  10706  11722    933   -369   1152       C  
ATOM    643  C   LYS B 342      44.753  24.278 -19.555  1.00 81.53           C  
ANISOU  643  C   LYS B 342    10293  10268  10416     -3   -741   1119       C  
ATOM    644  O   LYS B 342      43.943  23.606 -18.911  1.00 81.61           O  
ANISOU  644  O   LYS B 342    10916   9941  10150   -302   -974   1207       O  
ATOM    645  CB  LYS B 342      46.996  24.431 -20.658  1.00 91.91           C  
ANISOU  645  CB  LYS B 342    10226  11919  12777   1099   -302   1394       C  
ATOM    646  CG  LYS B 342      47.583  24.841 -19.316  1.00 96.76           C  
ANISOU  646  CG  LYS B 342    10316  13048  13401    591  -1135   1938       C  
ATOM    647  CD  LYS B 342      49.032  25.286 -19.472  1.00104.67           C  
ANISOU  647  CD  LYS B 342    10064  14567  15136    856  -1176   2314       C  
ATOM    648  CE  LYS B 342      49.498  26.121 -18.290  1.00107.39           C  
ANISOU  648  CE  LYS B 342     9999  15523  15280    -15  -2076   2705       C  
ATOM    649  NZ  LYS B 342      50.980  26.255 -18.274  1.00118.57           N  
ANISOU  649  NZ  LYS B 342     9993  17428  17628    235  -2399   3280       N  
TER     650      LYS B 342                                                      
ATOM    651  N   GLU C 302      37.127  15.729 -13.629  1.00 86.71           N  
ANISOU  651  N   GLU C 302     9763  11603  11578     23   -827    100       N  
ATOM    652  CA  GLU C 302      36.037  16.145 -12.691  1.00 84.04           C  
ANISOU  652  CA  GLU C 302     9749  10912  11270    -86   -776    281       C  
ATOM    653  C   GLU C 302      34.717  15.439 -13.033  1.00 78.47           C  
ANISOU  653  C   GLU C 302     9253   9962  10597   -137   -665    459       C  
ATOM    654  O   GLU C 302      34.567  14.899 -14.135  1.00 75.73           O  
ANISOU  654  O   GLU C 302     8818   9632  10322   -115   -676    360       O  
ATOM    655  CB  GLU C 302      35.870  17.669 -12.730  1.00 83.64           C  
ANISOU  655  CB  GLU C 302     9550  10861  11368   -350   -780    343       C  
ATOM    656  CG  GLU C 302      35.443  18.282 -11.402  1.00 87.07           C  
ANISOU  656  CG  GLU C 302    10183  11156  11740   -181   -945    234       C  
ATOM    657  CD  GLU C 302      35.736  19.777 -11.292  1.00 90.03           C  
ANISOU  657  CD  GLU C 302    10369  11377  12461   -311  -1285     89       C  
ATOM    658  OE1 GLU C 302      36.323  20.369 -12.227  1.00 91.69           O  
ANISOU  658  OE1 GLU C 302    10244  11565  13029   -672  -1358    280       O  
ATOM    659  OE2 GLU C 302      35.380  20.366 -10.252  1.00 90.09           O  
ANISOU  659  OE2 GLU C 302    10504  11323  12402     -9  -1560   -194       O  
ATOM    660  N   GLU C 303      33.785  15.439 -12.072  1.00 76.05           N  
ANISOU  660  N   GLU C 303     9147   9532  10216   -143   -605    711       N  
ATOM    661  CA  GLU C 303      32.451  14.832 -12.241  1.00 73.75           C  
ANISOU  661  CA  GLU C 303     8950   9037  10033   -273   -519   1031       C  
ATOM    662  C   GLU C 303      31.738  15.404 -13.488  1.00 70.62           C  
ANISOU  662  C   GLU C 303     8466   8614   9751   -486   -376    929       C  
ATOM    663  O   GLU C 303      31.496  16.615 -13.581  1.00 66.76           O  
ANISOU  663  O   GLU C 303     7922   8266   9177   -595   -258    874       O  
ATOM    664  CB  GLU C 303      31.555  15.031 -10.984  1.00 74.57           C  
ANISOU  664  CB  GLU C 303     9098   9359   9875   -218   -387   1418       C  
ATOM    665  CG  GLU C 303      31.935  14.217  -9.737  1.00 77.65           C  
ANISOU  665  CG  GLU C 303     9531   9889  10080     10   -503   1766       C  
ATOM    666  CD  GLU C 303      30.796  14.000  -8.710  1.00 80.67           C  
ANISOU  666  CD  GLU C 303     9793  10703  10153     54   -326   2447       C  
ATOM    667  OE1 GLU C 303      29.610  14.334  -8.964  1.00 73.94           O  
ANISOU  667  OE1 GLU C 303     8813  10001   9279   -110   -120   2644       O  
ATOM    668  OE2 GLU C 303      31.106  13.461  -7.614  1.00 83.04           O  
ANISOU  668  OE2 GLU C 303    10062  11316  10174    288   -390   2855       O  
ATOM    669  N   ILE C 304      31.435  14.521 -14.440  1.00 68.21           N  
ANISOU  669  N   ILE C 304     8141   8096   9677   -481   -501    858       N  
ATOM    670  CA  ILE C 304      30.668  14.857 -15.641  1.00 66.20           C  
ANISOU  670  CA  ILE C 304     7801   7864   9487   -587   -411    752       C  
ATOM    671  C   ILE C 304      29.184  14.531 -15.438  1.00 65.48           C  
ANISOU  671  C   ILE C 304     7780   7480   9619   -773   -387   1058       C  
ATOM    672  O   ILE C 304      28.833  13.502 -14.837  1.00 65.83           O  
ANISOU  672  O   ILE C 304     7860   7204   9947   -810   -591   1367       O  
ATOM    673  CB  ILE C 304      31.227  14.108 -16.866  1.00 67.49           C  
ANISOU  673  CB  ILE C 304     7822   8123   9697   -296   -656    339       C  
ATOM    674  CG1 ILE C 304      32.595  14.696 -17.233  1.00 72.23           C  
ANISOU  674  CG1 ILE C 304     8165   9317   9960   -154   -556    172       C  
ATOM    675  CG2 ILE C 304      30.283  14.210 -18.053  1.00 67.72           C  
ANISOU  675  CG2 ILE C 304     7771   8188   9771   -288   -647    202       C  
ATOM    676  CD1 ILE C 304      33.626  13.672 -17.664  1.00 75.86           C  
ANISOU  676  CD1 ILE C 304     8471  10012  10341    325   -877   -269       C  
ATOM    677  N   PHE C 305      28.328  15.421 -15.932  1.00 60.90           N  
ANISOU  677  N   PHE C 305     7160   7021   8955   -915   -179   1057       N  
ATOM    678  CA  PHE C 305      26.880  15.287 -15.817  1.00 60.31           C  
ANISOU  678  CA  PHE C 305     7060   6809   9046  -1089   -117   1328       C  
ATOM    679  C   PHE C 305      26.210  15.541 -17.161  1.00 59.01           C  
ANISOU  679  C   PHE C 305     6841   6595   8983  -1109   -132   1072       C  
ATOM    680  O   PHE C 305      26.781  16.158 -18.066  1.00 57.78           O  
ANISOU  680  O   PHE C 305     6647   6680   8628  -1005    -87    803       O  
ATOM    681  CB  PHE C 305      26.302  16.294 -14.825  1.00 60.67           C  
ANISOU  681  CB  PHE C 305     7089   7199   8763  -1114    137   1524       C  
ATOM    682  CG  PHE C 305      26.967  16.317 -13.459  1.00 64.80           C  
ANISOU  682  CG  PHE C 305     7633   7987   9000   -940    155   1675       C  
ATOM    683  CD1 PHE C 305      28.196  16.941 -13.269  1.00 63.66           C  
ANISOU  683  CD1 PHE C 305     7564   7913   8710   -790     71   1356       C  
ATOM    684  CD2 PHE C 305      26.315  15.777 -12.335  1.00 70.54           C  
ANISOU  684  CD2 PHE C 305     8221   9008   9571   -906    243   2204       C  
ATOM    685  CE1 PHE C 305      28.781  16.992 -12.011  1.00 67.23           C  
ANISOU  685  CE1 PHE C 305     8032   8629   8883   -543     21   1391       C  
ATOM    686  CE2 PHE C 305      26.898  15.827 -11.069  1.00 72.60           C  
ANISOU  686  CE2 PHE C 305     8465   9691   9426   -625    259   2336       C  
ATOM    687  CZ  PHE C 305      28.131  16.436 -10.907  1.00 71.73           C  
ANISOU  687  CZ  PHE C 305     8510   9561   9184   -408    123   1843       C  
ATOM    688  N   THR C 306      24.969  15.090 -17.279  1.00 61.77           N  
ANISOU  688  N   THR C 306     7117   6717   9632  -1250   -201   1244       N  
ATOM    689  CA  THR C 306      24.171  15.295 -18.493  1.00 61.97           C  
ANISOU  689  CA  THR C 306     7087   6696   9762  -1224   -258    972       C  
ATOM    690  C   THR C 306      22.833  15.986 -18.145  1.00 60.21           C  
ANISOU  690  C   THR C 306     6786   6601   9489  -1419    -25   1221       C  
ATOM    691  O   THR C 306      22.236  15.685 -17.119  1.00 62.51           O  
ANISOU  691  O   THR C 306     6945   6952   9853  -1574     55   1671       O  
ATOM    692  CB  THR C 306      23.932  13.938 -19.187  1.00 67.38           C  
ANISOU  692  CB  THR C 306     7695   6895  11010  -1108   -776    754       C  
ATOM    693  OG1 THR C 306      23.479  14.143 -20.529  1.00 70.92           O  
ANISOU  693  OG1 THR C 306     8087   7438  11420   -887   -896    291       O  
ATOM    694  CG2 THR C 306      22.907  13.098 -18.432  1.00 69.93           C  
ANISOU  694  CG2 THR C 306     7868   6766  11936  -1444   -980   1303       C  
ATOM    695  N   LEU C 307      22.373  16.920 -18.980  1.00 57.24           N  
ANISOU  695  N   LEU C 307     6431   6382   8933  -1366     73    977       N  
ATOM    696  CA  LEU C 307      21.062  17.570 -18.781  1.00 55.71           C  
ANISOU  696  CA  LEU C 307     6148   6325   8692  -1455    215   1078       C  
ATOM    697  C   LEU C 307      20.114  17.365 -19.936  1.00 54.65           C  
ANISOU  697  C   LEU C 307     5933   6027   8803  -1441     64    860       C  
ATOM    698  O   LEU C 307      20.499  17.533 -21.088  1.00 51.63           O  
ANISOU  698  O   LEU C 307     5622   5666   8328  -1256    -43    532       O  
ATOM    699  CB  LEU C 307      21.200  19.084 -18.670  1.00 54.91           C  
ANISOU  699  CB  LEU C 307     6163   6475   8225  -1357    333    936       C  
ATOM    700  CG  LEU C 307      21.463  19.761 -17.345  1.00 55.38           C  
ANISOU  700  CG  LEU C 307     6239   6791   8011  -1244    393    994       C  
ATOM    701  CD1 LEU C 307      21.334  21.258 -17.569  1.00 55.54           C  
ANISOU  701  CD1 LEU C 307     6356   6808   7935  -1117    236    722       C  
ATOM    702  CD2 LEU C 307      20.494  19.274 -16.294  1.00 58.77           C  
ANISOU  702  CD2 LEU C 307     6424   7585   8317  -1207    541   1282       C  
ATOM    703  N   GLN C 308      18.849  17.112 -19.609  1.00 56.46           N  
ANISOU  703  N   GLN C 308     5942   6243   9265  -1595     71   1075       N  
ATOM    704  CA  GLN C 308      17.800  17.034 -20.611  1.00 59.66           C  
ANISOU  704  CA  GLN C 308     6236   6501   9929  -1574   -100    836       C  
ATOM    705  C   GLN C 308      17.126  18.390 -20.840  1.00 54.64           C  
ANISOU  705  C   GLN C 308     5658   6198   8902  -1457     94    658       C  
ATOM    706  O   GLN C 308      16.515  18.939 -19.938  1.00 53.97           O  
ANISOU  706  O   GLN C 308     5444   6451   8611  -1474    283    838       O  
ATOM    707  CB  GLN C 308      16.777  15.988 -20.192  1.00 67.65           C  
ANISOU  707  CB  GLN C 308     6875   7277  11552  -1864   -289   1240       C  
ATOM    708  CG  GLN C 308      17.312  14.578 -20.334  1.00 74.47           C  
ANISOU  708  CG  GLN C 308     7693   7521  13078  -1946   -781   1302       C  
ATOM    709  CD  GLN C 308      17.542  14.231 -21.788  1.00 76.63           C  
ANISOU  709  CD  GLN C 308     8100   7457  13556  -1578  -1249    541       C  
ATOM    710  OE1 GLN C 308      16.593  13.975 -22.528  1.00 80.64           O  
ANISOU  710  OE1 GLN C 308     8439   7722  14478  -1540  -1581    284       O  
ATOM    711  NE2 GLN C 308      18.803  14.251 -22.213  1.00 75.04           N  
ANISOU  711  NE2 GLN C 308     8141   7379  12992  -1230  -1287    149       N  
ATOM    712  N   VAL C 309      17.243  18.916 -22.054  1.00 50.98           N  
ANISOU  712  N   VAL C 309     5348   5718   8302  -1262     -6    306       N  
ATOM    713  CA  VAL C 309      16.785  20.260 -22.337  1.00 49.90           C  
ANISOU  713  CA  VAL C 309     5313   5771   7873  -1152     56    191       C  
ATOM    714  C   VAL C 309      15.749  20.226 -23.442  1.00 51.44           C  
ANISOU  714  C   VAL C 309     5430   5930   8184  -1022   -105    -81       C  
ATOM    715  O   VAL C 309      15.975  19.568 -24.444  1.00 52.49           O  
ANISOU  715  O   VAL C 309     5544   5996   8402   -862   -293   -302       O  
ATOM    716  CB  VAL C 309      17.941  21.165 -22.763  1.00 48.23           C  
ANISOU  716  CB  VAL C 309     5306   5635   7385  -1085     49    245       C  
ATOM    717  CG1 VAL C 309      17.464  22.610 -22.873  1.00 49.49           C  
ANISOU  717  CG1 VAL C 309     5567   5795   7438  -1024    -62    223       C  
ATOM    718  CG2 VAL C 309      19.091  21.040 -21.775  1.00 48.16           C  
ANISOU  718  CG2 VAL C 309     5348   5619   7330  -1189    136    439       C  
ATOM    719  N   ARG C 310      14.633  20.945 -23.257  1.00 50.78           N  
ANISOU  719  N   ARG C 310     5275   5963   8056   -986    -87   -156       N  
ATOM    720  CA  ARG C 310      13.512  20.943 -24.210  1.00 51.48           C  
ANISOU  720  CA  ARG C 310     5259   6029   8270   -849   -258   -442       C  
ATOM    721  C   ARG C 310      13.518  22.220 -25.031  1.00 50.98           C  
ANISOU  721  C   ARG C 310     5429   6054   7887   -625   -351   -566       C  
ATOM    722  O   ARG C 310      13.557  23.328 -24.458  1.00 50.55           O  
ANISOU  722  O   ARG C 310     5501   6022   7682   -604   -367   -498       O  
ATOM    723  CB  ARG C 310      12.178  20.840 -23.471  1.00 55.50           C  
ANISOU  723  CB  ARG C 310     5427   6703   8955   -945   -201   -394       C  
ATOM    724  CG  ARG C 310      12.125  19.698 -22.460  1.00 59.48           C  
ANISOU  724  CG  ARG C 310     5584   7222   9793  -1262   -101     42       C  
ATOM    725  CD  ARG C 310      11.034  19.889 -21.414  1.00 65.04           C  
ANISOU  725  CD  ARG C 310     5831   8491  10389  -1317    102    324       C  
ATOM    726  NE  ARG C 310       9.700  19.701 -21.973  1.00 68.31           N  
ANISOU  726  NE  ARG C 310     5888   8940  11125  -1350    -48    208       N  
ATOM    727  CZ  ARG C 310       9.156  18.516 -22.240  1.00 73.55           C  
ANISOU  727  CZ  ARG C 310     6156   9272  12515  -1682   -288    467       C  
ATOM    728  NH1 ARG C 310       9.815  17.380 -21.987  1.00 75.62           N  
ANISOU  728  NH1 ARG C 310     6350   9095  13287  -1997   -452    867       N  
ATOM    729  NH2 ARG C 310       7.937  18.465 -22.755  1.00 76.66           N  
ANISOU  729  NH2 ARG C 310     6198   9701  13225  -1692   -472    313       N  
ATOM    730  N   GLY C 311      13.497  22.080 -26.362  1.00 49.55           N  
ANISOU  730  N   GLY C 311     5273   5934   7617   -402   -507   -743       N  
ATOM    731  CA  GLY C 311      13.483  23.241 -27.250  1.00 49.65           C  
ANISOU  731  CA  GLY C 311     5442   6097   7326   -211   -620   -666       C  
ATOM    732  C   GLY C 311      14.892  23.626 -27.652  1.00 52.79           C  
ANISOU  732  C   GLY C 311     5915   6706   7435   -240   -558   -226       C  
ATOM    733  O   GLY C 311      15.857  23.503 -26.863  1.00 48.12           O  
ANISOU  733  O   GLY C 311     5349   6037   6897   -462   -426      3       O  
ATOM    734  N   ARG C 312      14.998  24.103 -28.889  1.00 46.28           N  
ANISOU  734  N   ARG C 312     5239   6596   5748   1062   -934  -2192       N  
ATOM    735  CA  ARG C 312      16.273  24.277 -29.567  1.00 49.21           C  
ANISOU  735  CA  ARG C 312     5538   7311   5845   1046   -879  -2248       C  
ATOM    736  C   ARG C 312      16.964  25.567 -29.136  1.00 46.15           C  
ANISOU  736  C   ARG C 312     5405   6911   5219    956   -859  -1722       C  
ATOM    737  O   ARG C 312      18.185  25.571 -28.946  1.00 42.58           O  
ANISOU  737  O   ARG C 312     4953   6505   4719    905   -771  -1674       O  
ATOM    738  CB  ARG C 312      16.084  24.291 -31.096  1.00 52.54           C  
ANISOU  738  CB  ARG C 312     5685   8481   5795   1015   -918  -2548       C  
ATOM    739  CG  ARG C 312      17.326  24.627 -31.928  1.00 58.18           C  
ANISOU  739  CG  ARG C 312     6184   9961   5958    842   -850  -2590       C  
ATOM    740  CD  ARG C 312      18.247  23.431 -32.148  1.00 62.17           C  
ANISOU  740  CD  ARG C 312     6248  10654   6717    954   -764  -3426       C  
ATOM    741  NE  ARG C 312      19.653  23.767 -31.883  1.00 64.58           N  
ANISOU  741  NE  ARG C 312     6544  11120   6872    861   -661  -3316       N  
ATOM    742  CZ  ARG C 312      20.683  22.926 -32.029  1.00 70.30           C  
ANISOU  742  CZ  ARG C 312     6821  12034   7854    970   -633  -4078       C  
ATOM    743  NH1 ARG C 312      20.508  21.679 -32.464  1.00 77.48           N  
ANISOU  743  NH1 ARG C 312     7199  12933   9306   1199   -761  -5082       N  
ATOM    744  NH2 ARG C 312      21.912  23.335 -31.757  1.00 70.43           N  
ANISOU  744  NH2 ARG C 312     6843  12226   7690    871   -534  -3934       N  
ATOM    745  N   GLU C 313      16.229  26.673 -29.105  1.00 44.92           N  
ANISOU  745  N   GLU C 313     5387   6681   4996    949  -1013  -1399       N  
ATOM    746  CA  GLU C 313      16.869  27.932 -28.754  1.00 48.20           C  
ANISOU  746  CA  GLU C 313     5960   6950   5401    870  -1128   -956       C  
ATOM    747  C   GLU C 313      17.225  27.858 -27.220  1.00 43.43           C  
ANISOU  747  C   GLU C 313     5447   5953   5098    920   -966  -1024       C  
ATOM    748  O   GLU C 313      18.246  28.404 -26.814  1.00 43.47           O  
ANISOU  748  O   GLU C 313     5537   5886   5090    853   -937   -815       O  
ATOM    749  CB  GLU C 313      16.106  29.221 -29.275  1.00 52.05           C  
ANISOU  749  CB  GLU C 313     6455   7337   5983    844  -1554   -584       C  
ATOM    750  CG  GLU C 313      16.356  29.642 -30.808  1.00 58.00           C  
ANISOU  750  CG  GLU C 313     7090   8706   6239    537  -1826    -89       C  
ATOM    751  CD  GLU C 313      17.560  30.620 -31.125  1.00 61.08           C  
ANISOU  751  CD  GLU C 313     7502   9282   6422    173  -2040    604       C  
ATOM    752  OE1 GLU C 313      18.258  31.027 -30.162  1.00 70.25           O  
ANISOU  752  OE1 GLU C 313     8811   9966   7915    245  -1970    631       O  
ATOM    753  OE2 GLU C 313      17.846  31.000 -32.306  1.00 57.45           O  
ANISOU  753  OE2 GLU C 313     6863   9545   5419   -262  -2296   1169       O  
ATOM    754  N   ARG C 314      16.483  27.078 -26.419  1.00 40.21           N  
ANISOU  754  N   ARG C 314     4963   5440   4874    943   -866  -1269       N  
ATOM    755  CA  ARG C 314      16.836  26.888 -25.009  1.00 40.26           C  
ANISOU  755  CA  ARG C 314     4947   5367   4981    827   -742  -1227       C  
ATOM    756  C   ARG C 314      18.135  26.087 -24.797  1.00 39.76           C  
ANISOU  756  C   ARG C 314     4919   5222   4963    740   -660  -1076       C  
ATOM    757  O   ARG C 314      18.958  26.430 -23.941  1.00 35.39           O  
ANISOU  757  O   ARG C 314     4408   4651   4387    654   -599   -905       O  
ATOM    758  CB  ARG C 314      15.719  26.232 -24.218  1.00 40.04           C  
ANISOU  758  CB  ARG C 314     4727   5472   5013    685   -717  -1364       C  
ATOM    759  CG  ARG C 314      16.072  26.123 -22.746  1.00 39.20           C  
ANISOU  759  CG  ARG C 314     4488   5589   4818    405   -626  -1212       C  
ATOM    760  CD  ARG C 314      14.996  25.401 -21.976  1.00 42.23           C  
ANISOU  760  CD  ARG C 314     4580   6359   5105     67   -630  -1204       C  
ATOM    761  NE  ARG C 314      13.759  26.157 -21.916  1.00 43.70           N  
ANISOU  761  NE  ARG C 314     4530   6892   5179    163   -607  -1707       N  
ATOM    762  CZ  ARG C 314      12.575  25.635 -21.594  1.00 44.74           C  
ANISOU  762  CZ  ARG C 314     4362   7456   5179    -88   -601  -1841       C  
ATOM    763  NH1 ARG C 314      12.433  24.340 -21.335  1.00 46.10           N  
ANISOU  763  NH1 ARG C 314     4467   7686   5362   -507   -674  -1367       N  
ATOM    764  NH2 ARG C 314      11.528  26.410 -21.562  1.00 45.24           N  
ANISOU  764  NH2 ARG C 314     4139   7845   5204     66   -602  -2453       N  
ATOM    765  N   TYR C 315      18.265  24.992 -25.538  1.00 38.52           N  
ANISOU  765  N   TYR C 315     4661   5009   4966    782   -712  -1247       N  
ATOM    766  CA  TYR C 315      19.479  24.236 -25.562  1.00 40.53           C  
ANISOU  766  CA  TYR C 315     4823   5126   5451    792   -749  -1310       C  
ATOM    767  C   TYR C 315      20.667  25.101 -26.039  1.00 39.48           C  
ANISOU  767  C   TYR C 315     4763   5260   4978    829   -628  -1286       C  
ATOM    768  O   TYR C 315      21.749  25.014 -25.485  1.00 37.16           O  
ANISOU  768  O   TYR C 315     4468   4863   4787    798   -607  -1195       O  
ATOM    769  CB  TYR C 315      19.317  23.016 -26.484  1.00 43.54           C  
ANISOU  769  CB  TYR C 315     4914   5427   6200    911   -904  -1801       C  
ATOM    770  CG  TYR C 315      20.612  22.392 -26.851  1.00 45.22           C  
ANISOU  770  CG  TYR C 315     4867   5603   6711   1026   -989  -2190       C  
ATOM    771  CD1 TYR C 315      21.289  21.621 -25.945  1.00 48.13           C  
ANISOU  771  CD1 TYR C 315     5140   5430   7717    981  -1239  -2030       C  
ATOM    772  CD2 TYR C 315      21.177  22.583 -28.107  1.00 49.18           C  
ANISOU  772  CD2 TYR C 315     5121   6730   6834   1127   -868  -2733       C  
ATOM    773  CE1 TYR C 315      22.506  21.036 -26.266  1.00 53.13           C  
ANISOU  773  CE1 TYR C 315     5438   5962   8784   1151  -1397  -2529       C  
ATOM    774  CE2 TYR C 315      22.400  22.013 -28.439  1.00 53.34           C  
ANISOU  774  CE2 TYR C 315     5255   7390   7620   1242   -934  -3316       C  
ATOM    775  CZ  TYR C 315      23.060  21.238 -27.510  1.00 55.00           C  
ANISOU  775  CZ  TYR C 315     5379   6875   8642   1312  -1211  -3274       C  
ATOM    776  OH  TYR C 315      24.269  20.639 -27.806  1.00 62.88           O  
ANISOU  776  OH  TYR C 315     5899   7909  10082   1492  -1366  -3980       O  
ATOM    777  N   GLU C 316      20.469  25.891 -27.086  1.00 39.71           N  
ANISOU  777  N   GLU C 316     4807   5676   4602    826   -607  -1293       N  
ATOM    778  CA  GLU C 316      21.545  26.726 -27.623  1.00 41.76           C  
ANISOU  778  CA  GLU C 316     5071   6319   4475    701   -562  -1112       C  
ATOM    779  C   GLU C 316      21.966  27.802 -26.571  1.00 39.41           C  
ANISOU  779  C   GLU C 316     5017   5695   4261    639   -569   -686       C  
ATOM    780  O   GLU C 316      23.146  28.057 -26.370  1.00 37.64           O  
ANISOU  780  O   GLU C 316     4796   5555   3947    556   -496   -584       O  
ATOM    781  CB  GLU C 316      21.156  27.345 -28.964  1.00 43.65           C  
ANISOU  781  CB  GLU C 316     5207   7145   4230    539   -668   -977       C  
ATOM    782  CG  GLU C 316      21.212  26.390 -30.185  1.00 49.66           C  
ANISOU  782  CG  GLU C 316     5545   8637   4685    519   -605  -1568       C  
ATOM    783  CD  GLU C 316      21.048  27.126 -31.535  1.00 53.56           C  
ANISOU  783  CD  GLU C 316     5842  10069   4437    165   -727  -1265       C  
ATOM    784  OE1 GLU C 316      21.156  28.373 -31.457  1.00 51.73           O  
ANISOU  784  OE1 GLU C 316     5839   9736   4081    -79   -931   -472       O  
ATOM    785  OE2 GLU C 316      20.866  26.512 -32.679  1.00 62.27           O  
ANISOU  785  OE2 GLU C 316     6490  12077   5092     65   -689  -1779       O  
ATOM    786  N   ILE C 317      21.005  28.345 -25.842  1.00 37.52           N  
ANISOU  786  N   ILE C 317     4883   5138   4235    696   -656   -596       N  
ATOM    787  CA  ILE C 317      21.300  29.289 -24.742  1.00 37.27           C  
ANISOU  787  CA  ILE C 317     4919   4868   4374    678   -683   -472       C  
ATOM    788  C   ILE C 317      22.101  28.658 -23.590  1.00 37.04           C  
ANISOU  788  C   ILE C 317     4868   4827   4379    626   -503   -505       C  
ATOM    789  O   ILE C 317      23.158  29.185 -23.186  1.00 35.12           O  
ANISOU  789  O   ILE C 317     4664   4571   4108    568   -461   -381       O  
ATOM    790  CB  ILE C 317      20.011  29.968 -24.257  1.00 39.37           C  
ANISOU  790  CB  ILE C 317     5099   4959   4901    780   -848   -663       C  
ATOM    791  CG1 ILE C 317      19.535  30.956 -25.325  1.00 43.68           C  
ANISOU  791  CG1 ILE C 317     5654   5345   5595    803  -1216   -448       C  
ATOM    792  CG2 ILE C 317      20.221  30.675 -22.916  1.00 41.13           C  
ANISOU  792  CG2 ILE C 317     5189   5123   5314    781   -834   -873       C  
ATOM    793  CD1 ILE C 317      18.062  31.337 -25.262  1.00 46.49           C  
ANISOU  793  CD1 ILE C 317     5849   5519   6293    976  -1462   -751       C  
ATOM    794  N   LEU C 318      21.645  27.505 -23.104  1.00 36.01           N  
ANISOU  794  N   LEU C 318     4645   4697   4339    588   -468   -579       N  
ATOM    795  CA  LEU C 318      22.358  26.772 -22.047  1.00 37.02           C  
ANISOU  795  CA  LEU C 318     4698   4805   4560    435   -455   -409       C  
ATOM    796  C   LEU C 318      23.734  26.239 -22.476  1.00 36.59           C  
ANISOU  796  C   LEU C 318     4635   4625   4642    501   -478   -409       C  
ATOM    797  O   LEU C 318      24.640  26.133 -21.642  1.00 34.80           O  
ANISOU  797  O   LEU C 318     4378   4366   4477    405   -495   -226       O  
ATOM    798  CB  LEU C 318      21.534  25.597 -21.478  1.00 37.77           C  
ANISOU  798  CB  LEU C 318     4632   4886   4832    241   -588   -271       C  
ATOM    799  CG  LEU C 318      20.170  25.962 -20.930  1.00 40.76           C  
ANISOU  799  CG  LEU C 318     4881   5608   4995     98   -539   -363       C  
ATOM    800  CD1 LEU C 318      19.377  24.710 -20.559  1.00 45.23           C  
ANISOU  800  CD1 LEU C 318     5258   6218   5707   -209   -717   -101       C  
ATOM    801  CD2 LEU C 318      20.289  26.918 -19.753  1.00 42.89           C  
ANISOU  801  CD2 LEU C 318     4993   6339   4962    -54   -419   -447       C  
ATOM    802  N   LYS C 319      23.876  25.887 -23.744  1.00 36.02           N  
ANISOU  802  N   LYS C 319     4492   4602   4588    643   -493   -698       N  
ATOM    803  CA  LYS C 319      25.162  25.476 -24.269  1.00 38.66           C  
ANISOU  803  CA  LYS C 319     4654   5032   5001    718   -496   -957       C  
ATOM    804  C   LYS C 319      26.152  26.656 -24.340  1.00 37.68           C  
ANISOU  804  C   LYS C 319     4638   5205   4471    623   -334   -789       C  
ATOM    805  O   LYS C 319      27.297  26.511 -23.989  1.00 38.65           O  
ANISOU  805  O   LYS C 319     4676   5332   4677    621   -318   -832       O  
ATOM    806  CB  LYS C 319      25.024  24.842 -25.641  1.00 41.12           C  
ANISOU  806  CB  LYS C 319     4679   5632   5313    841   -528  -1517       C  
ATOM    807  CG  LYS C 319      26.339  24.283 -26.127  1.00 46.56           C  
ANISOU  807  CG  LYS C 319     4984   6563   6143    937   -554  -2067       C  
ATOM    808  CD  LYS C 319      26.178  23.314 -27.264  1.00 55.74           C  
ANISOU  808  CD  LYS C 319     5639   8023   7515   1101   -660  -2927       C  
ATOM    809  CE  LYS C 319      27.468  22.525 -27.494  1.00 63.39           C  
ANISOU  809  CE  LYS C 319     6044   9101   8939   1284   -801  -3741       C  
ATOM    810  NZ  LYS C 319      28.688  23.366 -27.320  1.00 63.68           N  
ANISOU  810  NZ  LYS C 319     6137   9590   8466   1132   -577  -3543       N  
ATOM    811  N   LYS C 320      25.684  27.805 -24.791  1.00 38.13           N  
ANISOU  811  N   LYS C 320     4845   5440   4199    523   -303   -559       N  
ATOM    812  CA  LYS C 320      26.449  29.038 -24.735  1.00 39.81           C  
ANISOU  812  CA  LYS C 320     5155   5761   4207    360   -290   -247       C  
ATOM    813  C   LYS C 320      26.838  29.376 -23.270  1.00 37.43           C  
ANISOU  813  C   LYS C 320     4952   5139   4130    378   -257   -142       C  
ATOM    814  O   LYS C 320      27.999  29.664 -22.969  1.00 36.33           O  
ANISOU  814  O   LYS C 320     4793   5073   3934    304   -194    -76       O  
ATOM    815  CB  LYS C 320      25.632  30.132 -25.436  1.00 42.66           C  
ANISOU  815  CB  LYS C 320     5601   6143   4464    234   -487     72       C  
ATOM    816  CG  LYS C 320      26.153  31.547 -25.395  1.00 48.67           C  
ANISOU  816  CG  LYS C 320     6428   6781   5283     17   -691    523       C  
ATOM    817  CD  LYS C 320      27.437  31.754 -26.185  1.00 54.90           C  
ANISOU  817  CD  LYS C 320     7082   8157   5620   -322   -644    774       C  
ATOM    818  CE  LYS C 320      28.122  33.041 -25.733  1.00 56.43           C  
ANISOU  818  CE  LYS C 320     7345   8034   6061   -535   -864   1222       C  
ATOM    819  NZ  LYS C 320      29.356  33.346 -26.490  1.00 60.99           N  
ANISOU  819  NZ  LYS C 320     7747   9288   6137   -992   -848   1578       N  
ATOM    820  N   LEU C 321      25.891  29.300 -22.349  1.00 35.99           N  
ANISOU  820  N   LEU C 321     4789   4763   4120    430   -287   -181       N  
ATOM    821  CA  LEU C 321      26.213  29.528 -20.971  1.00 34.92           C  
ANISOU  821  CA  LEU C 321     4600   4635   4032    361   -242   -163       C  
ATOM    822  C   LEU C 321      27.259  28.547 -20.485  1.00 36.16           C  
ANISOU  822  C   LEU C 321     4690   4819   4228    308   -219    -57       C  
ATOM    823  O   LEU C 321      28.226  28.937 -19.845  1.00 35.24           O  
ANISOU  823  O   LEU C 321     4551   4776   4062    242   -172     10       O  
ATOM    824  CB  LEU C 321      24.995  29.497 -20.094  1.00 36.12           C  
ANISOU  824  CB  LEU C 321     4614   4915   4192    312   -260   -305       C  
ATOM    825  CG  LEU C 321      24.058  30.681 -20.262  1.00 39.75           C  
ANISOU  825  CG  LEU C 321     5007   5287   4807    423   -374   -590       C  
ATOM    826  CD1 LEU C 321      22.818  30.435 -19.412  1.00 40.62           C  
ANISOU  826  CD1 LEU C 321     4840   5755   4838    353   -347   -908       C  
ATOM    827  CD2 LEU C 321      24.732  32.008 -19.895  1.00 41.38           C  
ANISOU  827  CD2 LEU C 321     5141   5346   5234    447   -477   -723       C  
ATOM    828  N   ASN C 322      27.084  27.275 -20.802  1.00 38.27           N  
ANISOU  828  N   ASN C 322     4875   4956   4708    350   -334    -72       N  
ATOM    829  CA  ASN C 322      28.039  26.290 -20.361  1.00 38.13           C  
ANISOU  829  CA  ASN C 322     4709   4777   5001    330   -503     21       C  
ATOM    830  C   ASN C 322      29.431  26.585 -20.882  1.00 38.75           C  
ANISOU  830  C   ASN C 322     4738   4946   5036    438   -414   -199       C  
ATOM    831  O   ASN C 322      30.393  26.477 -20.136  1.00 38.07           O  
ANISOU  831  O   ASN C 322     4579   4826   5057    389   -479    -70       O  
ATOM    832  CB  ASN C 322      27.639  24.911 -20.827  1.00 41.00           C  
ANISOU  832  CB  ASN C 322     4894   4802   5882    413   -790    -91       C  
ATOM    833  CG  ASN C 322      28.561  23.839 -20.297  1.00 43.95           C  
ANISOU  833  CG  ASN C 322     5022   4789   6884    401  -1184     38       C  
ATOM    834  OD1 ASN C 322      28.811  23.742 -19.110  1.00 45.83           O  
ANISOU  834  OD1 ASN C 322     5240   5031   7141    138  -1351    578       O  
ATOM    835  ND2 ASN C 322      29.040  23.027 -21.170  1.00 47.87           N  
ANISOU  835  ND2 ASN C 322     5243   5007   7936    665  -1397   -499       N  
ATOM    836  N   ASP C 323      29.537  26.882 -22.171  1.00 38.02           N  
ANISOU  836  N   ASP C 323     4611   5095   4738    522   -291   -516       N  
ATOM    837  CA  ASP C 323      30.822  27.172 -22.774  1.00 42.29           C  
ANISOU  837  CA  ASP C 323     4991   5991   5083    509   -183   -756       C  
ATOM    838  C   ASP C 323      31.454  28.413 -22.126  1.00 39.83           C  
ANISOU  838  C   ASP C 323     4867   5758   4508    337    -56   -405       C  
ATOM    839  O   ASP C 323      32.643  28.400 -21.841  1.00 38.50           O  
ANISOU  839  O   ASP C 323     4577   5695   4354    321    -25   -485       O  
ATOM    840  CB  ASP C 323      30.722  27.336 -24.307  1.00 46.00           C  
ANISOU  840  CB  ASP C 323     5276   7049   5153    447    -81  -1074       C  
ATOM    841  CG  ASP C 323      30.262  26.040 -25.023  1.00 52.71           C  
ANISOU  841  CG  ASP C 323     5784   7914   6327    661   -214  -1693       C  
ATOM    842  OD1 ASP C 323      30.224  24.978 -24.359  1.00 53.31           O  
ANISOU  842  OD1 ASP C 323     5752   7395   7106    862   -471  -1838       O  
ATOM    843  OD2 ASP C 323      29.909  26.087 -26.248  1.00 58.81           O  
ANISOU  843  OD2 ASP C 323     6341   9307   6695    581   -134  -2003       O  
ATOM    844  N   SER C 324      30.658  29.453 -21.865  1.00 38.07           N  
ANISOU  844  N   SER C 324     4866   5429   4168    239    -44   -117       N  
ATOM    845  CA  SER C 324      31.171  30.661 -21.196  1.00 41.36           C  
ANISOU  845  CA  SER C 324     5366   5797   4552    110    -25     76       C  
ATOM    846  C   SER C 324      31.652  30.421 -19.772  1.00 37.71           C  
ANISOU  846  C   SER C 324     4847   5278   4199    126      0     64       C  
ATOM    847  O   SER C 324      32.710  30.861 -19.403  1.00 37.65           O  
ANISOU  847  O   SER C 324     4797   5357   4150     55     49     83       O  
ATOM    848  CB  SER C 324      30.133  31.780 -21.192  1.00 43.30           C  
ANISOU  848  CB  SER C 324     5710   5814   4928     75   -167    188       C  
ATOM    849  OG  SER C 324      30.109  32.359 -22.462  1.00 51.05           O  
ANISOU  849  OG  SER C 324     6713   6897   5786    -92   -298    445       O  
ATOM    850  N   LEU C 325      30.887  29.683 -18.981  1.00 36.98           N  
ANISOU  850  N   LEU C 325     4707   5150   4192    140    -63     96       N  
ATOM    851  CA  LEU C 325      31.345  29.354 -17.622  1.00 35.89           C  
ANISOU  851  CA  LEU C 325     4428   5180   4029      6   -106    242       C  
ATOM    852  C   LEU C 325      32.633  28.541 -17.646  1.00 37.73           C  
ANISOU  852  C   LEU C 325     4569   5313   4453     50   -216    321       C  
ATOM    853  O   LEU C 325      33.529  28.767 -16.814  1.00 33.89           O  
ANISOU  853  O   LEU C 325     3992   4985   3897    -46   -218    416       O  
ATOM    854  CB  LEU C 325      30.249  28.644 -16.863  1.00 38.11           C  
ANISOU  854  CB  LEU C 325     4588   5626   4266   -160   -224    428       C  
ATOM    855  CG  LEU C 325      29.012  29.506 -16.601  1.00 38.52           C  
ANISOU  855  CG  LEU C 325     4572   5938   4124   -199   -117    150       C  
ATOM    856  CD1 LEU C 325      27.780  28.602 -16.385  1.00 40.87           C  
ANISOU  856  CD1 LEU C 325     4758   6410   4361   -368   -220    319       C  
ATOM    857  CD2 LEU C 325      29.270  30.430 -15.408  1.00 39.17           C  
ANISOU  857  CD2 LEU C 325     4387   6528   3966   -353    -27   -108       C  
ATOM    858  N   GLU C 326      32.763  27.638 -18.634  1.00 37.59           N  
ANISOU  858  N   GLU C 326     4488   5068   4725    223   -333    148       N  
ATOM    859  CA  GLU C 326      34.006  26.898 -18.806  1.00 41.45           C  
ANISOU  859  CA  GLU C 326     4745   5444   5558    350   -500    -45       C  
ATOM    860  C   GLU C 326      35.199  27.852 -18.979  1.00 40.82           C  
ANISOU  860  C   GLU C 326     4659   5688   5161    317   -256   -213       C  
ATOM    861  O   GLU C 326      36.240  27.668 -18.368  1.00 38.79           O  
ANISOU  861  O   GLU C 326     4257   5431   5050    321   -354   -198       O  
ATOM    862  CB  GLU C 326      33.958  26.001 -20.029  1.00 47.17           C  
ANISOU  862  CB  GLU C 326     5238   6045   6636    581   -626   -559       C  
ATOM    863  CG  GLU C 326      33.528  24.583 -19.742  1.00 57.51           C  
ANISOU  863  CG  GLU C 326     6338   6789   8724    673  -1123   -494       C  
ATOM    864  CD  GLU C 326      33.639  23.683 -20.959  1.00 64.73           C  
ANISOU  864  CD  GLU C 326     6852   7580  10160    976  -1304  -1303       C  
ATOM    865  OE1 GLU C 326      34.619  23.857 -21.736  1.00 68.53           O  
ANISOU  865  OE1 GLU C 326     7036   8498  10503   1117  -1139  -1986       O  
ATOM    866  OE2 GLU C 326      32.754  22.805 -21.117  1.00 68.35           O  
ANISOU  866  OE2 GLU C 326     7211   7606  11152   1037  -1621  -1321       O  
ATOM    867  N   LEU C 327      35.024  28.839 -19.852  1.00 38.19           N  
ANISOU  867  N   LEU C 327     4447   5624   4439    235    -13   -297       N  
ATOM    868  CA  LEU C 327      36.074  29.770 -20.177  1.00 39.76           C  
ANISOU  868  CA  LEU C 327     4603   6161   4342     80    152   -334       C  
ATOM    869  C   LEU C 327      36.472  30.558 -18.936  1.00 38.29           C  
ANISOU  869  C   LEU C 327     4520   5874   4152    -19    174    -99       C  
ATOM    870  O   LEU C 327      37.657  30.728 -18.647  1.00 41.23           O  
ANISOU  870  O   LEU C 327     4766   6407   4490    -67    217   -170       O  
ATOM    871  CB  LEU C 327      35.613  30.710 -21.320  1.00 38.80           C  
ANISOU  871  CB  LEU C 327     4567   6309   3864   -141    235   -190       C  
ATOM    872  CG  LEU C 327      36.634  31.724 -21.830  1.00 39.66           C  
ANISOU  872  CG  LEU C 327     4579   6846   3642   -482    309    -24       C  
ATOM    873  CD1 LEU C 327      37.843  30.983 -22.388  1.00 44.21           C  
ANISOU  873  CD1 LEU C 327     4743   8047   4006   -486    430   -513       C  
ATOM    874  CD2 LEU C 327      36.048  32.628 -22.891  1.00 41.29           C  
ANISOU  874  CD2 LEU C 327     4840   7268   3579   -834    203    401       C  
ATOM    875  N   SER C 328      35.498  31.019 -18.187  1.00 36.89           N  
ANISOU  875  N   SER C 328     4479   5534   4003    -51    144     54       N  
ATOM    876  CA  SER C 328      35.795  31.708 -16.933  1.00 38.22           C  
ANISOU  876  CA  SER C 328     4587   5790   4144   -147    162     64       C  
ATOM    877  C   SER C 328      36.581  30.884 -15.905  1.00 41.39           C  
ANISOU  877  C   SER C 328     4819   6362   4546   -171     81    165       C  
ATOM    878  O   SER C 328      37.268  31.452 -15.034  1.00 41.32           O  
ANISOU  878  O   SER C 328     4693   6577   4427   -277    124    125       O  
ATOM    879  CB  SER C 328      34.509  32.191 -16.287  1.00 37.96           C  
ANISOU  879  CB  SER C 328     4531   5773   4118   -172    130    -32       C  
ATOM    880  OG  SER C 328      33.983  33.264 -17.037  1.00 42.33           O  
ANISOU  880  OG  SER C 328     5172   6048   4861   -156     69   -122       O  
ATOM    881  N   ASP C 329      36.457  29.561 -15.989  1.00 42.29           N  
ANISOU  881  N   ASP C 329     4867   6328   4872    -94   -122    316       N  
ATOM    882  CA  ASP C 329      37.207  28.625 -15.134  1.00 42.93           C  
ANISOU  882  CA  ASP C 329     4737   6405   5168   -147   -413    574       C  
ATOM    883  C   ASP C 329      38.652  28.383 -15.586  1.00 41.89           C  
ANISOU  883  C   ASP C 329     4449   6178   5289     25   -466    302       C  
ATOM    884  O   ASP C 329      39.447  27.805 -14.838  1.00 40.97           O  
ANISOU  884  O   ASP C 329     4125   6017   5423      0   -758    493       O  
ATOM    885  CB  ASP C 329      36.510  27.258 -15.103  1.00 47.60           C  
ANISOU  885  CB  ASP C 329     5235   6667   6181   -155   -816    892       C  
ATOM    886  CG  ASP C 329      35.578  27.108 -13.951  1.00 54.93           C  
ANISOU  886  CG  ASP C 329     6095   7949   6825   -535   -950   1425       C  
ATOM    887  OD1 ASP C 329      35.062  28.122 -13.439  1.00 61.71           O  
ANISOU  887  OD1 ASP C 329     6972   9339   7133   -693   -634   1279       O  
ATOM    888  OD2 ASP C 329      35.343  25.956 -13.538  1.00 68.09           O  
ANISOU  888  OD2 ASP C 329     7594   9412   8864   -725  -1440   1973       O  
ATOM    889  N   VAL C 330      38.982  28.718 -16.823  1.00 39.17           N  
ANISOU  889  N   VAL C 330     4112   5889   4879    155   -250   -130       N  
ATOM    890  CA  VAL C 330      40.326  28.440 -17.293  1.00 44.39           C  
ANISOU  890  CA  VAL C 330     4479   6682   5702    281   -277   -548       C  
ATOM    891  C   VAL C 330      41.143  29.705 -17.612  1.00 44.42           C  
ANISOU  891  C   VAL C 330     4517   7137   5223     87     71   -663       C  
ATOM    892  O   VAL C 330      42.341  29.598 -17.863  1.00 46.84           O  
ANISOU  892  O   VAL C 330     4531   7715   5548    118     93  -1013       O  
ATOM    893  CB  VAL C 330      40.340  27.436 -18.497  1.00 47.60           C  
ANISOU  893  CB  VAL C 330     4565   7044   6477    531   -419  -1146       C  
ATOM    894  CG1 VAL C 330      39.779  26.072 -18.087  1.00 49.62           C  
ANISOU  894  CG1 VAL C 330     4683   6649   7520    722   -952  -1026       C  
ATOM    895  CG2 VAL C 330      39.586  27.975 -19.710  1.00 46.16           C  
ANISOU  895  CG2 VAL C 330     4497   7225   5817    422   -112  -1299       C  
ATOM    896  N   VAL C 331      40.514  30.880 -17.659  1.00 40.72           N  
ANISOU  896  N   VAL C 331     4325   6717   4430   -126    264   -401       N  
ATOM    897  CA  VAL C 331      41.270  32.126 -17.905  1.00 41.17           C  
ANISOU  897  CA  VAL C 331     4380   7043   4218   -394    434   -356       C  
ATOM    898  C   VAL C 331      41.699  32.713 -16.545  1.00 40.26           C  
ANISOU  898  C   VAL C 331     4281   6840   4174   -438    417   -266       C  
ATOM    899  O   VAL C 331      40.861  32.905 -15.675  1.00 38.22           O  
ANISOU  899  O   VAL C 331     4116   6425   3979   -415    358   -169       O  
ATOM    900  CB  VAL C 331      40.440  33.135 -18.713  1.00 40.28           C  
ANISOU  900  CB  VAL C 331     4455   6883   3966   -633    451    -82       C  
ATOM    901  CG1 VAL C 331      41.206  34.428 -18.938  1.00 42.65           C  
ANISOU  901  CG1 VAL C 331     4710   7322   4172  -1013    448    146       C  
ATOM    902  CG2 VAL C 331      40.063  32.542 -20.061  1.00 41.59           C  
ANISOU  902  CG2 VAL C 331     4521   7370   3908   -661    482   -182       C  
ATOM    903  N   PRO C 332      43.010  32.936 -16.335  1.00 42.60           N  
ANISOU  903  N   PRO C 332     5299   5639   5247   -876   -239  -1247       N  
ATOM    904  CA  PRO C 332      43.433  33.578 -15.081  1.00 42.24           C  
ANISOU  904  CA  PRO C 332     4874   5886   5286  -1172    -17  -1213       C  
ATOM    905  C   PRO C 332      42.860  34.981 -14.900  1.00 41.86           C  
ANISOU  905  C   PRO C 332     4785   5875   5244  -1356    265  -1240       C  
ATOM    906  O   PRO C 332      42.614  35.681 -15.895  1.00 41.38           O  
ANISOU  906  O   PRO C 332     4821   5708   5193  -1272    422  -1255       O  
ATOM    907  CB  PRO C 332      44.968  33.667 -15.206  1.00 44.45           C  
ANISOU  907  CB  PRO C 332     4913   6463   5510   -990    150  -1203       C  
ATOM    908  CG  PRO C 332      45.349  32.582 -16.165  1.00 48.82           C  
ANISOU  908  CG  PRO C 332     5733   6956   5858   -328     33  -1259       C  
ATOM    909  CD  PRO C 332      44.151  32.378 -17.089  1.00 48.54           C  
ANISOU  909  CD  PRO C 332     6226   6459   5758   -265   -199  -1382       C  
ATOM    910  N   ALA C 333      42.738  35.395 -13.637  1.00 41.01           N  
ANISOU  910  N   ALA C 333     4651   5886   5042  -1495    291  -1267       N  
ATOM    911  CA  ALA C 333      42.181  36.667 -13.266  1.00 42.16           C  
ANISOU  911  CA  ALA C 333     5048   5953   5018  -1399    466  -1392       C  
ATOM    912  C   ALA C 333      42.788  37.838 -14.015  1.00 44.24           C  
ANISOU  912  C   ALA C 333     5558   5880   5367  -1533    478  -1498       C  
ATOM    913  O   ALA C 333      42.068  38.701 -14.512  1.00 47.79           O  
ANISOU  913  O   ALA C 333     6268   6108   5783  -1333    592  -1533       O  
ATOM    914  CB  ALA C 333      42.330  36.889 -11.760  1.00 45.95           C  
ANISOU  914  CB  ALA C 333     5704   6566   5186  -1383    397  -1516       C  
ATOM    915  N   SER C 334      44.108  37.888 -14.076  1.00 47.28           N  
ANISOU  915  N   SER C 334     5794   6306   5863  -1896    314  -1397       N  
ATOM    916  CA  SER C 334      44.810  39.009 -14.713  1.00 49.58           C  
ANISOU  916  CA  SER C 334     6178   6396   6261  -2261    173  -1203       C  
ATOM    917  C   SER C 334      44.615  39.061 -16.218  1.00 49.37           C  
ANISOU  917  C   SER C 334     5939   6490   6328  -2079    433   -998       C  
ATOM    918  O   SER C 334      44.428  40.159 -16.779  1.00 51.53           O  
ANISOU  918  O   SER C 334     6474   6444   6658  -2243    360   -884       O  
ATOM    919  CB  SER C 334      46.289  38.928 -14.419  1.00 53.27           C  
ANISOU  919  CB  SER C 334     6236   7186   6816  -2771    -97   -816       C  
ATOM    920  OG  SER C 334      46.735  37.608 -14.583  1.00 51.88           O  
ANISOU  920  OG  SER C 334     5504   7571   6636  -2426    133   -697       O  
ATOM    921  N   ASP C 335      44.672  37.894 -16.879  1.00 48.51           N  
ANISOU  921  N   ASP C 335     5507   6758   6165  -1698    642   -959       N  
ATOM    922  CA  ASP C 335      44.425  37.820 -18.332  1.00 48.31           C  
ANISOU  922  CA  ASP C 335     5452   6857   6045  -1377    846   -843       C  
ATOM    923  C   ASP C 335      43.016  38.306 -18.612  1.00 48.04           C  
ANISOU  923  C   ASP C 335     5777   6415   6058  -1309    847  -1002       C  
ATOM    924  O   ASP C 335      42.797  39.117 -19.512  1.00 49.22           O  
ANISOU  924  O   ASP C 335     6003   6479   6218  -1333    926   -842       O  
ATOM    925  CB  ASP C 335      44.580  36.384 -18.869  1.00 51.45           C  
ANISOU  925  CB  ASP C 335     5856   7485   6205   -795    875   -945       C  
ATOM    926  CG  ASP C 335      45.987  35.844 -18.704  1.00 56.11           C  
ANISOU  926  CG  ASP C 335     6020   8651   6648   -544    975   -706       C  
ATOM    927  OD1 ASP C 335      46.813  36.557 -18.103  1.00 60.61           O  
ANISOU  927  OD1 ASP C 335     6149   9499   7381  -1045    956   -352       O  
ATOM    928  OD2 ASP C 335      46.275  34.719 -19.177  1.00 58.83           O  
ANISOU  928  OD2 ASP C 335     6530   9152   6670    191    989   -819       O  
ATOM    929  N   ALA C 336      42.054  37.817 -17.831  1.00 45.51           N  
ANISOU  929  N   ALA C 336     5569   5972   5747  -1214    759  -1166       N  
ATOM    930  CA  ALA C 336      40.694  38.328 -17.922  1.00 46.69           C  
ANISOU  930  CA  ALA C 336     5847   5993   5900  -1059    809  -1109       C  
ATOM    931  C   ALA C 336      40.657  39.852 -17.771  1.00 51.85           C  
ANISOU  931  C   ALA C 336     6822   6325   6553  -1033    882  -1167       C  
ATOM    932  O   ALA C 336      40.016  40.527 -18.578  1.00 53.10           O  
ANISOU  932  O   ALA C 336     7099   6336   6741   -879    947  -1039       O  
ATOM    933  CB  ALA C 336      39.786  37.671 -16.895  1.00 46.43           C  
ANISOU  933  CB  ALA C 336     5652   6186   5802   -961    746  -1004       C  
ATOM    934  N   GLU C 337      41.333  40.392 -16.756  1.00 56.35           N  
ANISOU  934  N   GLU C 337     7670   6680   7060  -1191    738  -1347       N  
ATOM    935  CA  GLU C 337      41.443  41.867 -16.613  1.00 64.10           C  
ANISOU  935  CA  GLU C 337     9312   7046   7995  -1234    506  -1437       C  
ATOM    936  C   GLU C 337      42.035  42.559 -17.857  1.00 62.70           C  
ANISOU  936  C   GLU C 337     9092   6679   8051  -1673    365  -1080       C  
ATOM    937  O   GLU C 337      41.493  43.563 -18.311  1.00 61.96           O  
ANISOU  937  O   GLU C 337     9452   6116   7974  -1522    263  -1033       O  
ATOM    938  CB  GLU C 337      42.274  42.261 -15.400  1.00 72.01           C  
ANISOU  938  CB  GLU C 337    10797   7710   8851  -1533     91  -1648       C  
ATOM    939  CG  GLU C 337      41.540  42.176 -14.088  1.00 79.59           C  
ANISOU  939  CG  GLU C 337    12166   8708   9364   -891    181  -2029       C  
ATOM    940  CD  GLU C 337      42.485  42.305 -12.907  1.00 89.53           C  
ANISOU  940  CD  GLU C 337    13893   9710  10414  -1266   -303  -2243       C  
ATOM    941  OE1 GLU C 337      43.368  43.213 -12.932  1.00 94.58           O  
ANISOU  941  OE1 GLU C 337    15126   9667  11143  -1897   -966  -2194       O  
ATOM    942  OE2 GLU C 337      42.337  41.495 -11.956  1.00 90.52           O  
ANISOU  942  OE2 GLU C 337    13784  10326  10284  -1027   -126  -2349       O  
ATOM    943  N   LYS C 338      43.127  42.018 -18.399  1.00 60.79           N  
ANISOU  943  N   LYS C 338     8268   6906   7920  -2103    383   -737       N  
ATOM    944  CA  LYS C 338      43.701  42.524 -19.660  1.00 65.31           C  
ANISOU  944  CA  LYS C 338     8551   7674   8589  -2429    375   -181       C  
ATOM    945  C   LYS C 338      42.670  42.552 -20.804  1.00 61.53           C  
ANISOU  945  C   LYS C 338     8105   7219   8053  -1990    660   -182       C  
ATOM    946  O   LYS C 338      42.508  43.577 -21.480  1.00 65.41           O  
ANISOU  946  O   LYS C 338     8818   7400   8632  -2168    513    118       O  
ATOM    947  CB  LYS C 338      44.881  41.658 -20.127  1.00 69.73           C  
ANISOU  947  CB  LYS C 338     8312   9127   9054  -2510    588    243       C  
ATOM    948  CG  LYS C 338      46.160  41.741 -19.315  1.00 77.51           C  
ANISOU  948  CG  LYS C 338     8957  10361  10130  -3106    262    632       C  
ATOM    949  CD  LYS C 338      47.178  40.712 -19.818  1.00 81.08           C  
ANISOU  949  CD  LYS C 338     8513  11927  10364  -2769    654   1079       C  
ATOM    950  CE  LYS C 338      48.225  40.328 -18.770  1.00 84.56           C  
ANISOU  950  CE  LYS C 338     8530  12728  10871  -3106    418   1333       C  
ATOM    951  NZ  LYS C 338      49.503  41.076 -18.909  1.00 93.05           N  
ANISOU  951  NZ  LYS C 338     8858  14434  12061  -3944     70   2484       N  
ATOM    952  N   TYR C 339      42.001  41.425 -21.040  1.00 53.06           N  
ANISOU  952  N   TYR C 339     6860   6462   6838  -1518    923   -429       N  
ATOM    953  CA  TYR C 339      41.024  41.335 -22.125  1.00 52.20           C  
ANISOU  953  CA  TYR C 339     6798   6394   6641  -1215   1030   -359       C  
ATOM    954  C   TYR C 339      39.846  42.283 -21.944  1.00 53.03           C  
ANISOU  954  C   TYR C 339     7234   6048   6867  -1031    974   -373       C  
ATOM    955  O   TYR C 339      39.315  42.820 -22.913  1.00 54.94           O  
ANISOU  955  O   TYR C 339     7536   6222   7114   -951    981   -126       O  
ATOM    956  CB  TYR C 339      40.470  39.913 -22.284  1.00 49.19           C  
ANISOU  956  CB  TYR C 339     6360   6241   6088   -919   1005   -550       C  
ATOM    957  CG  TYR C 339      41.455  38.881 -22.786  1.00 48.84           C  
ANISOU  957  CG  TYR C 339     6240   6574   5743   -712   1040   -600       C  
ATOM    958  CD1 TYR C 339      42.014  38.970 -24.053  1.00 53.43           C  
ANISOU  958  CD1 TYR C 339     6786   7541   5973   -459   1207   -374       C  
ATOM    959  CD2 TYR C 339      41.783  37.789 -21.999  1.00 48.69           C  
ANISOU  959  CD2 TYR C 339     6227   6583   5687   -605    917   -838       C  
ATOM    960  CE1 TYR C 339      42.901  38.013 -24.505  1.00 57.52           C  
ANISOU  960  CE1 TYR C 339     7314   8526   6013     96   1320   -428       C  
ATOM    961  CE2 TYR C 339      42.659  36.831 -22.434  1.00 52.31           C  
ANISOU  961  CE2 TYR C 339     6754   7339   5782   -148    938   -917       C  
ATOM    962  CZ  TYR C 339      43.221  36.947 -23.681  1.00 57.28           C  
ANISOU  962  CZ  TYR C 339     7386   8408   5966    303   1173   -737       C  
ATOM    963  OH  TYR C 339      44.078  35.963 -24.082  1.00 62.92           O  
ANISOU  963  OH  TYR C 339     8252   9517   6136   1098   1259   -836       O  
ATOM    964  N   ARG C 340      39.419  42.485 -20.712  1.00 54.67           N  
ANISOU  964  N   ARG C 340     7666   6029   7077   -815    946   -626       N  
ATOM    965  CA  ARG C 340      38.342  43.417 -20.466  1.00 59.69           C  
ANISOU  965  CA  ARG C 340     8666   6352   7661   -295    972   -627       C  
ATOM    966  C   ARG C 340      38.726  44.859 -20.805  1.00 65.05           C  
ANISOU  966  C   ARG C 340     9988   6297   8430   -427    681   -554       C  
ATOM    967  O   ARG C 340      37.842  45.702 -20.909  1.00 66.96           O  
ANISOU  967  O   ARG C 340    10638   6194   8608    136    670   -517       O  
ATOM    968  CB  ARG C 340      37.835  43.303 -19.028  1.00 63.08           C  
ANISOU  968  CB  ARG C 340     9244   6874   7848    231   1079   -887       C  
ATOM    969  CG  ARG C 340      36.926  42.103 -18.817  1.00 61.43           C  
ANISOU  969  CG  ARG C 340     8326   7442   7571    410   1284   -619       C  
ATOM    970  CD  ARG C 340      36.463  42.006 -17.377  1.00 65.29           C  
ANISOU  970  CD  ARG C 340     8809   8284   7714    979   1470   -692       C  
ATOM    971  NE  ARG C 340      35.868  40.692 -17.121  1.00 65.21           N  
ANISOU  971  NE  ARG C 340     8003   9052   7719    792   1493   -230       N  
ATOM    972  CZ  ARG C 340      34.571  40.393 -17.274  1.00 66.94           C  
ANISOU  972  CZ  ARG C 340     7562   9994   7877   1062   1586    482       C  
ATOM    973  NH1 ARG C 340      33.696  41.331 -17.689  1.00 71.08           N  
ANISOU  973  NH1 ARG C 340     8071  10656   8280   1740   1813    758       N  
ATOM    974  NH2 ARG C 340      34.152  39.154 -17.008  1.00 61.41           N  
ANISOU  974  NH2 ARG C 340     6192   9893   7248    609   1358   1051       N  
ATOM    975  N   GLN C 341      40.029  45.116 -20.981  1.00 67.59           N  
ANISOU  975  N   GLN C 341    10354   6435   8891  -1171    383   -397       N  
ATOM    976  CA  GLN C 341      40.577  46.401 -21.467  1.00 75.80           C  
ANISOU  976  CA  GLN C 341    11896   6807  10098  -1670   -117    -29       C  
ATOM    977  C   GLN C 341      40.557  47.444 -20.372  1.00 82.51           C  
ANISOU  977  C   GLN C 341    13901   6591  10857  -1532   -708   -378       C  
ATOM    978  O   GLN C 341      41.185  47.261 -19.325  1.00 83.26           O  
ANISOU  978  O   GLN C 341    14251   6535  10849  -1769   -977   -647       O  
ATOM    979  CB  GLN C 341      39.828  46.905 -22.707  1.00 78.99           C  
ANISOU  979  CB  GLN C 341    12258   7190  10565  -1454     -7    323       C  
ATOM    980  CG  GLN C 341      39.721  45.852 -23.815  1.00 74.36           C  
ANISOU  980  CG  GLN C 341    10813   7555   9884  -1441    461    556       C  
ATOM    981  CD  GLN C 341      38.418  45.882 -24.593  1.00 74.57           C  
ANISOU  981  CD  GLN C 341    10789   7686   9856   -919    641    651       C  
ATOM    982  OE1 GLN C 341      37.524  46.689 -24.328  1.00 80.68           O  
ANISOU  982  OE1 GLN C 341    12005   7972  10678   -426    552    613       O  
ATOM    983  NE2 GLN C 341      38.310  44.996 -25.574  1.00 72.01           N  
ANISOU  983  NE2 GLN C 341     9994   8011   9353   -941    836    807       N  
TER     984      GLN C 341                                                      
ATOM    985  N   GLU D 303      11.315  16.775 -28.678  1.00 73.04           N  
ANISOU  985  N   GLU D 303     8244   9597   9912  -1997   -902  -1174       N  
ATOM    986  CA  GLU D 303      12.346  17.736 -29.183  1.00 70.89           C  
ANISOU  986  CA  GLU D 303     8223   8895   9816  -1596   -715  -1565       C  
ATOM    987  C   GLU D 303      13.301  18.064 -28.039  1.00 67.44           C  
ANISOU  987  C   GLU D 303     7616   8520   9485  -1273   -553  -1688       C  
ATOM    988  O   GLU D 303      13.552  19.221 -27.733  1.00 67.78           O  
ANISOU  988  O   GLU D 303     7518   8595   9638   -900   -636  -1921       O  
ATOM    989  CB  GLU D 303      11.667  18.988 -29.765  1.00 71.52           C  
ANISOU  989  CB  GLU D 303     8178   9057   9937  -1432   -959  -1659       C  
ATOM    990  CG  GLU D 303      10.296  19.301 -29.162  1.00 74.35           C  
ANISOU  990  CG  GLU D 303     7936  10138  10173  -1216  -1165  -1746       C  
ATOM    991  CD  GLU D 303       9.632  20.489 -29.823  1.00 78.48           C  
ANISOU  991  CD  GLU D 303     8373  10472  10973   -924  -1692  -1953       C  
ATOM    992  OE1 GLU D 303      10.299  21.549 -29.931  1.00 77.00           O  
ANISOU  992  OE1 GLU D 303     8373   9678  11202   -650  -2107  -2118       O  
ATOM    993  OE2 GLU D 303       8.445  20.358 -30.229  1.00 80.96           O  
ANISOU  993  OE2 GLU D 303     8428  11174  11157  -1041  -1867  -1858       O  
ATOM    994  N   ILE D 304      13.813  16.999 -27.426  1.00 65.82           N  
ANISOU  994  N   ILE D 304     7468   8198   9340  -1455   -531  -1503       N  
ATOM    995  CA  ILE D 304      14.568  17.027 -26.190  1.00 63.77           C  
ANISOU  995  CA  ILE D 304     6990   8118   9119  -1320   -438  -1454       C  
ATOM    996  C   ILE D 304      16.060  16.868 -26.500  1.00 59.60           C  
ANISOU  996  C   ILE D 304     6804   6947   8895  -1107   -309  -1671       C  
ATOM    997  O   ILE D 304      16.455  15.841 -27.044  1.00 60.24           O  
ANISOU  997  O   ILE D 304     7158   6540   9190  -1162   -482  -1772       O  
ATOM    998  CB  ILE D 304      14.120  15.857 -25.289  1.00 69.73           C  
ANISOU  998  CB  ILE D 304     7504   9227   9762  -1891   -755   -842       C  
ATOM    999  CG1 ILE D 304      12.834  16.191 -24.518  1.00 75.94           C  
ANISOU  999  CG1 ILE D 304     7508  11438   9906  -2120   -759   -600       C  
ATOM   1000  CG2 ILE D 304      15.183  15.522 -24.255  1.00 71.08           C  
ANISOU 1000  CG2 ILE D 304     7624   9283  10098  -1918   -807   -657       C  
ATOM   1001  CD1 ILE D 304      11.709  16.787 -25.332  1.00 77.05           C  
ANISOU 1001  CD1 ILE D 304     7499  11902   9872  -1936   -728   -873       C  
ATOM   1002  N   PHE D 305      16.881  17.864 -26.148  1.00 55.09           N  
ANISOU 1002  N   PHE D 305     6148   6431   8353   -816   -143  -1824       N  
ATOM   1003  CA  PHE D 305      18.333  17.827 -26.406  1.00 52.95           C  
ANISOU 1003  CA  PHE D 305     5992   5902   8223   -678      6  -1946       C  
ATOM   1004  C   PHE D 305      19.092  17.360 -25.175  1.00 54.80           C  
ANISOU 1004  C   PHE D 305     6107   6058   8656   -601     -9  -1822       C  
ATOM   1005  O   PHE D 305      18.558  17.420 -24.069  1.00 58.29           O  
ANISOU 1005  O   PHE D 305     6322   6842   8984   -710    -98  -1607       O  
ATOM   1006  CB  PHE D 305      18.839  19.195 -26.886  1.00 51.62           C  
ANISOU 1006  CB  PHE D 305     5805   5833   7974   -682    -30  -1900       C  
ATOM   1007  CG  PHE D 305      18.213  19.621 -28.166  1.00 53.37           C  
ANISOU 1007  CG  PHE D 305     6119   6155   8001   -947   -174  -1823       C  
ATOM   1008  CD1 PHE D 305      16.938  20.192 -28.169  1.00 53.77           C  
ANISOU 1008  CD1 PHE D 305     6182   6106   8139   -923   -498  -1809       C  
ATOM   1009  CD2 PHE D 305      18.834  19.353 -29.390  1.00 56.47           C  
ANISOU 1009  CD2 PHE D 305     6459   6973   8021  -1198    -10  -1843       C  
ATOM   1010  CE1 PHE D 305      16.327  20.545 -29.360  1.00 56.04           C  
ANISOU 1010  CE1 PHE D 305     6568   6420   8303  -1240   -736  -1637       C  
ATOM   1011  CE2 PHE D 305      18.230  19.703 -30.589  1.00 57.70           C  
ANISOU 1011  CE2 PHE D 305     6644   7417   7860  -1599   -177  -1667       C  
ATOM   1012  CZ  PHE D 305      16.971  20.296 -30.573  1.00 58.41           C  
ANISOU 1012  CZ  PHE D 305     6889   7109   8195  -1667   -575  -1479       C  
ATOM   1013  N   THR D 306      20.315  16.859 -25.390  1.00 54.11           N  
ANISOU 1013  N   THR D 306     6048   5741   8770   -419     40  -1996       N  
ATOM   1014  CA  THR D 306      21.193  16.403 -24.336  1.00 54.83           C  
ANISOU 1014  CA  THR D 306     6034   5645   9152   -342    -77  -1849       C  
ATOM   1015  C   THR D 306      22.427  17.310 -24.242  1.00 53.59           C  
ANISOU 1015  C   THR D 306     5707   5735   8917   -179    175  -1882       C  
ATOM   1016  O   THR D 306      23.189  17.416 -25.197  1.00 55.03           O  
ANISOU 1016  O   THR D 306     5748   6214   8946    -49    345  -2133       O  
ATOM   1017  CB  THR D 306      21.703  14.983 -24.616  1.00 61.26           C  
ANISOU 1017  CB  THR D 306     6946   5874  10455   -123   -504  -2133       C  
ATOM   1018  OG1 THR D 306      20.591  14.096 -24.763  1.00 66.02           O  
ANISOU 1018  OG1 THR D 306     7782   6065  11236   -428  -1026  -1957       O  
ATOM   1019  CG2 THR D 306      22.591  14.496 -23.477  1.00 62.82           C  
ANISOU 1019  CG2 THR D 306     7034   5744  11089   -102   -831  -1859       C  
ATOM   1020  N   LEU D 307      22.634  17.929 -23.083  1.00 50.36           N  
ANISOU 1020  N   LEU D 307     5213   5410   8510   -250    134  -1618       N  
ATOM   1021  CA  LEU D 307      23.719  18.875 -22.907  1.00 51.01           C  
ANISOU 1021  CA  LEU D 307     5193   5614   8574   -225    169  -1516       C  
ATOM   1022  C   LEU D 307      24.707  18.269 -21.945  1.00 51.86           C  
ANISOU 1022  C   LEU D 307     5153   5620   8931   -155    131  -1371       C  
ATOM   1023  O   LEU D 307      24.351  17.967 -20.813  1.00 50.97           O  
ANISOU 1023  O   LEU D 307     5012   5507   8845   -282    -26  -1173       O  
ATOM   1024  CB  LEU D 307      23.190  20.202 -22.336  1.00 48.69           C  
ANISOU 1024  CB  LEU D 307     4968   5338   8193   -242   -117  -1515       C  
ATOM   1025  CG  LEU D 307      24.249  21.201 -21.850  1.00 49.92           C  
ANISOU 1025  CG  LEU D 307     5115   5380   8469   -302   -423  -1328       C  
ATOM   1026  CD1 LEU D 307      25.062  21.723 -23.028  1.00 52.21           C  
ANISOU 1026  CD1 LEU D 307     5361   5777   8697   -678   -534   -922       C  
ATOM   1027  CD2 LEU D 307      23.638  22.361 -21.051  1.00 52.06           C  
ANISOU 1027  CD2 LEU D 307     5473   5491   8814    -55  -1017  -1687       C  
ATOM   1028  N   GLN D 308      25.945  18.095 -22.391  1.00 56.53           N  
ANISOU 1028  N   GLN D 308     5519   6353   9604     -5    235  -1437       N  
ATOM   1029  CA  GLN D 308      26.997  17.592 -21.512  1.00 57.94           C  
ANISOU 1029  CA  GLN D 308     5507   6400  10107    115    110  -1304       C  
ATOM   1030  C   GLN D 308      27.686  18.725 -20.780  1.00 54.33           C  
ANISOU 1030  C   GLN D 308     4990   6134   9518   -124     77   -916       C  
ATOM   1031  O   GLN D 308      28.112  19.708 -21.394  1.00 53.94           O  
ANISOU 1031  O   GLN D 308     4853   6421   9221   -329     80   -748       O  
ATOM   1032  CB  GLN D 308      28.038  16.763 -22.272  1.00 65.05           C  
ANISOU 1032  CB  GLN D 308     6012   7519  11183    594    136  -1783       C  
ATOM   1033  CG  GLN D 308      27.861  15.257 -22.111  1.00 72.69           C  
ANISOU 1033  CG  GLN D 308     7083   7716  12820    986   -406  -2154       C  
ATOM   1034  CD  GLN D 308      29.160  14.498 -22.306  1.00 81.33           C  
ANISOU 1034  CD  GLN D 308     7684   8883  14335   1702   -677  -2778       C  
ATOM   1035  OE1 GLN D 308      30.066  14.560 -21.470  1.00 84.45           O  
ANISOU 1035  OE1 GLN D 308     7863   9241  14982   1694   -802  -2449       O  
ATOM   1036  NE2 GLN D 308      29.260  13.782 -23.415  1.00 88.66           N  
ANISOU 1036  NE2 GLN D 308     8352  10022  15313   2421   -827  -3823       N  
ATOM   1037  N   VAL D 309      27.808  18.545 -19.466  1.00 52.11           N  
ANISOU 1037  N   VAL D 309     4733   5675   9391   -218   -116   -679       N  
ATOM   1038  CA  VAL D 309      28.410  19.501 -18.585  1.00 52.01           C  
ANISOU 1038  CA  VAL D 309     4707   5766   9288   -392   -284   -432       C  
ATOM   1039  C   VAL D 309      29.559  18.852 -17.775  1.00 54.06           C  
ANISOU 1039  C   VAL D 309     4726   5973   9842   -414   -391   -119       C  
ATOM   1040  O   VAL D 309      29.415  17.747 -17.259  1.00 53.18           O  
ANISOU 1040  O   VAL D 309     4565   5639  10000   -433   -573      9       O  
ATOM   1041  CB  VAL D 309      27.347  20.075 -17.647  1.00 50.87           C  
ANISOU 1041  CB  VAL D 309     4693   5794   8839   -442   -474   -624       C  
ATOM   1042  CG1 VAL D 309      27.939  21.176 -16.795  1.00 53.16           C  
ANISOU 1042  CG1 VAL D 309     5019   6111   9068   -469   -850   -650       C  
ATOM   1043  CG2 VAL D 309      26.150  20.575 -18.449  1.00 51.30           C  
ANISOU 1043  CG2 VAL D 309     4910   5851   8729   -296   -474  -1012       C  
ATOM   1044  N   ARG D 310      30.691  19.551 -17.685  1.00 53.87           N  
ANISOU 1044  N   ARG D 310     4539   6112   9817   -520   -458    130       N  
ATOM   1045  CA  ARG D 310      31.848  19.095 -16.912  1.00 58.31           C  
ANISOU 1045  CA  ARG D 310     4822   6672  10658   -541   -600    453       C  
ATOM   1046  C   ARG D 310      31.925  19.845 -15.573  1.00 57.09           C  
ANISOU 1046  C   ARG D 310     4840   6515  10334   -875   -907    723       C  
ATOM   1047  O   ARG D 310      32.018  21.078 -15.535  1.00 56.18           O  
ANISOU 1047  O   ARG D 310     4906   6404  10034  -1030  -1155    721       O  
ATOM   1048  CB  ARG D 310      33.128  19.278 -17.740  1.00 63.58           C  
ANISOU 1048  CB  ARG D 310     4985   7866  11306   -459   -466    555       C  
ATOM   1049  CG  ARG D 310      34.334  18.466 -17.272  1.00 71.66           C  
ANISOU 1049  CG  ARG D 310     5520   8974  12734   -200   -593    647       C  
ATOM   1050  CD  ARG D 310      35.586  18.691 -18.134  1.00 80.17           C  
ANISOU 1050  CD  ARG D 310     5792  11129  13537    -88   -392    655       C  
ATOM   1051  NE  ARG D 310      35.312  18.661 -19.586  1.00 86.73           N  
ANISOU 1051  NE  ARG D 310     6264  12800  13887    118    -27    169       N  
ATOM   1052  CZ  ARG D 310      35.387  19.704 -20.430  1.00 90.74           C  
ANISOU 1052  CZ  ARG D 310     6553  14236  13687   -507     91    619       C  
ATOM   1053  NH1 ARG D 310      35.746  20.921 -20.022  1.00 91.28           N  
ANISOU 1053  NH1 ARG D 310     6800  14291  13589  -1359   -294   1563       N  
ATOM   1054  NH2 ARG D 310      35.112  19.524 -21.718  1.00 95.66           N  
ANISOU 1054  NH2 ARG D 310     6757  15817  13771   -364    414    176       N  
ATOM   1055  N   GLY D 311      31.818  19.106 -14.472  1.00 58.88           N  
ANISOU 1055  N   GLY D 311     5005   6751  10615  -1036  -1079    945       N  
ATOM   1056  CA  GLY D 311      31.984  19.683 -13.137  1.00 62.06           C  
ANISOU 1056  CA  GLY D 311     5413   7478  10688  -1351  -1358   1114       C  
ATOM   1057  C   GLY D 311      30.660  19.988 -12.466  1.00 64.18           C  
ANISOU 1057  C   GLY D 311     5703   8391  10292  -1421  -1388    703       C  
ATOM   1058  O   GLY D 311      29.689  20.328 -13.141  1.00 63.84           O  
ANISOU 1058  O   GLY D 311     5790   8381  10084  -1149  -1237    198       O  
ATOM   1059  N   ARG D 312      30.634  19.882 -11.136  1.00 68.43           N  
ANISOU 1059  N   ARG D 312     5582   8655  11762    461   -906   3975       N  
ATOM   1060  CA  ARG D 312      29.400  19.998 -10.348  1.00 70.11           C  
ANISOU 1060  CA  ARG D 312     5963   9367  11309    448   -961   4246       C  
ATOM   1061  C   ARG D 312      28.934  21.438 -10.178  1.00 64.58           C  
ANISOU 1061  C   ARG D 312     5678   9260   9597    247  -1153   3503       C  
ATOM   1062  O   ARG D 312      27.719  21.697 -10.105  1.00 61.08           O  
ANISOU 1062  O   ARG D 312     5532   8892   8781    162  -1056   3319       O  
ATOM   1063  CB  ARG D 312      29.529  19.298  -8.966  1.00 79.76           C  
ANISOU 1063  CB  ARG D 312     6646  11294  12364    687  -1153   5436       C  
ATOM   1064  CG  ARG D 312      30.185  20.120  -7.849  1.00 86.23           C  
ANISOU 1064  CG  ARG D 312     7233  13420  12109    707  -1636   5515       C  
ATOM   1065  CD  ARG D 312      30.916  19.255  -6.819  1.00100.03           C  
ANISOU 1065  CD  ARG D 312     8237  15839  13927   1009  -1856   6814       C  
ATOM   1066  NE  ARG D 312      32.014  19.971  -6.150  1.00105.64           N  
ANISOU 1066  NE  ARG D 312     8603  17638  13897   1016  -2344   6635       N  
ATOM   1067  CZ  ARG D 312      33.017  19.396  -5.479  1.00117.64           C  
ANISOU 1067  CZ  ARG D 312     9413  19762  15521   1275  -2627   7598       C  
ATOM   1068  NH1 ARG D 312      33.096  18.074  -5.358  1.00126.08           N  
ANISOU 1068  NH1 ARG D 312    10006  20360  17537   1580  -2438   8955       N  
ATOM   1069  NH2 ARG D 312      33.961  20.147  -4.913  1.00122.41           N  
ANISOU 1069  NH2 ARG D 312     9683  21443  15384   1236  -3099   7213       N  
ATOM   1070  N   GLU D 313      29.879  22.369 -10.125  1.00 62.59           N  
ANISOU 1070  N   GLU D 313     5374   9341   9063    167  -1387   3047       N  
ATOM   1071  CA  GLU D 313      29.559  23.775  -9.891  1.00 62.88           C  
ANISOU 1071  CA  GLU D 313     5634   9829   8426    -25  -1533   2293       C  
ATOM   1072  C   GLU D 313      28.692  24.285 -11.061  1.00 57.72           C  
ANISOU 1072  C   GLU D 313     5478   8478   7975   -171  -1237   1748       C  
ATOM   1073  O   GLU D 313      27.689  25.006 -10.867  1.00 56.14           O  
ANISOU 1073  O   GLU D 313     5504   8451   7375   -269  -1222   1404       O  
ATOM   1074  CB  GLU D 313      30.828  24.626  -9.756  1.00 67.67           C  
ANISOU 1074  CB  GLU D 313     5979  10717   9015   -107  -1771   1839       C  
ATOM   1075  CG  GLU D 313      31.945  24.066  -8.840  1.00 77.05           C  
ANISOU 1075  CG  GLU D 313     6574  12595  10105     57  -2102   2390       C  
ATOM   1076  CD  GLU D 313      31.992  24.683  -7.438  1.00 85.56           C  
ANISOU 1076  CD  GLU D 313     7267  15021  10219     19  -2503   2192       C  
ATOM   1077  OE1 GLU D 313      31.680  25.889  -7.285  1.00 88.23           O  
ANISOU 1077  OE1 GLU D 313     7699  15596  10227   -205  -2541   1241       O  
ATOM   1078  OE2 GLU D 313      32.367  23.967  -6.476  1.00 92.24           O  
ANISOU 1078  OE2 GLU D 313     7617  16759  10668    217  -2770   2979       O  
ATOM   1079  N   ARG D 314      29.063  23.839 -12.261  1.00 54.16           N  
ANISOU 1079  N   ARG D 314     5113   7329   8133   -167   -994   1702       N  
ATOM   1080  CA  ARG D 314      28.475  24.287 -13.517  1.00 49.04           C  
ANISOU 1080  CA  ARG D 314     4810   6229   7592   -284   -737   1268       C  
ATOM   1081  C   ARG D 314      27.145  23.582 -13.755  1.00 47.66           C  
ANISOU 1081  C   ARG D 314     4816   5875   7415   -263   -565   1365       C  
ATOM   1082  O   ARG D 314      26.196  24.206 -14.229  1.00 40.16           O  
ANISOU 1082  O   ARG D 314     4137   4905   6216   -348   -495   1074       O  
ATOM   1083  CB  ARG D 314      29.432  23.960 -14.643  1.00 48.46           C  
ANISOU 1083  CB  ARG D 314     4636   5743   8031   -292   -528   1146       C  
ATOM   1084  CG  ARG D 314      29.327  24.783 -15.892  1.00 48.43           C  
ANISOU 1084  CG  ARG D 314     4837   5594   7967   -416   -319    773       C  
ATOM   1085  CD  ARG D 314      30.509  24.463 -16.783  1.00 51.81           C  
ANISOU 1085  CD  ARG D 314     5052   5821   8812   -424   -110    672       C  
ATOM   1086  NE  ARG D 314      31.735  24.865 -16.134  1.00 53.32           N  
ANISOU 1086  NE  ARG D 314     4983   6073   9201   -415   -294    753       N  
ATOM   1087  CZ  ARG D 314      32.919  24.302 -16.304  1.00 58.30           C  
ANISOU 1087  CZ  ARG D 314     5292   6548  10311   -361   -228    800       C  
ATOM   1088  NH1 ARG D 314      33.086  23.270 -17.112  1.00 63.90           N  
ANISOU 1088  NH1 ARG D 314     5870   6975  11432   -314     66    714       N  
ATOM   1089  NH2 ARG D 314      33.960  24.795 -15.654  1.00 61.41           N  
ANISOU 1089  NH2 ARG D 314     5413   7082  10838   -365   -449    836       N  
ATOM   1090  N   TYR D 315      27.098  22.285 -13.435  1.00 49.03           N  
ANISOU 1090  N   TYR D 315     4757   5872   7999   -142   -482   1810       N  
ATOM   1091  CA  TYR D 315      25.878  21.488 -13.574  1.00 49.63           C  
ANISOU 1091  CA  TYR D 315     4880   5691   8286   -136   -283   1897       C  
ATOM   1092  C   TYR D 315      24.732  22.020 -12.715  1.00 50.25           C  
ANISOU 1092  C   TYR D 315     5143   6211   7739   -162   -399   1998       C  
ATOM   1093  O   TYR D 315      23.585  22.145 -13.183  1.00 48.52           O  
ANISOU 1093  O   TYR D 315     5137   5861   7436   -240   -278   1710       O  
ATOM   1094  CB  TYR D 315      26.151  20.031 -13.253  1.00 55.02           C  
ANISOU 1094  CB  TYR D 315     5128   5980   9794      7   -125   2466       C  
ATOM   1095  CG  TYR D 315      24.909  19.180 -13.054  1.00 57.84           C  
ANISOU 1095  CG  TYR D 315     5397   6061  10518     18     88   2707       C  
ATOM   1096  CD1 TYR D 315      24.159  18.742 -14.144  1.00 56.50           C  
ANISOU 1096  CD1 TYR D 315     5261   5398  10807   -101    365   2079       C  
ATOM   1097  CD2 TYR D 315      24.507  18.772 -11.766  1.00 60.77           C  
ANISOU 1097  CD2 TYR D 315     5552   6751  10784    143     33   3576       C  
ATOM   1098  CE1 TYR D 315      23.044  17.937 -13.965  1.00 58.59           C  
ANISOU 1098  CE1 TYR D 315     5355   5333  11571   -115    583   2227       C  
ATOM   1099  CE2 TYR D 315      23.393  17.970 -11.584  1.00 63.54           C  
ANISOU 1099  CE2 TYR D 315     5754   6776  11612    146    292   3876       C  
ATOM   1100  CZ  TYR D 315      22.666  17.558 -12.686  1.00 62.72           C  
ANISOU 1100  CZ  TYR D 315     5692   6020  12119      8    568   3161       C  
ATOM   1101  OH  TYR D 315      21.549  16.767 -12.522  1.00 67.21           O  
ANISOU 1101  OH  TYR D 315     6041   6202  13293    -17    843   3363       O  
ATOM   1102  N   GLU D 316      25.067  22.350 -11.473  1.00 52.35           N  
ANISOU 1102  N   GLU D 316     5261   7099   7529   -104   -636   2339       N  
ATOM   1103  CA  GLU D 316      24.160  22.943 -10.479  1.00 53.13           C  
ANISOU 1103  CA  GLU D 316     5428   7832   6925   -138   -741   2333       C  
ATOM   1104  C   GLU D 316      23.455  24.176 -11.021  1.00 48.98           C  
ANISOU 1104  C   GLU D 316     5240   7218   6150   -286   -726   1597       C  
ATOM   1105  O   GLU D 316      22.221  24.267 -11.045  1.00 45.92           O  
ANISOU 1105  O   GLU D 316     5008   6791   5647   -324   -612   1486       O  
ATOM   1106  CB  GLU D 316      25.003  23.322  -9.250  1.00 61.57           C  
ANISOU 1106  CB  GLU D 316     6182   9795   7416    -90  -1041   2526       C  
ATOM   1107  CG  GLU D 316      24.262  23.799  -8.029  1.00 67.79           C  
ANISOU 1107  CG  GLU D 316     6864  11529   7362   -120  -1141   2489       C  
ATOM   1108  CD  GLU D 316      23.906  22.633  -7.143  1.00 77.61           C  
ANISOU 1108  CD  GLU D 316     7789  13235   8465     44  -1070   3528       C  
ATOM   1109  OE1 GLU D 316      23.242  21.710  -7.680  1.00 79.89           O  
ANISOU 1109  OE1 GLU D 316     8159  12769   9426     94   -783   3942       O  
ATOM   1110  OE2 GLU D 316      24.307  22.625  -5.948  1.00 83.99           O  
ANISOU 1110  OE2 GLU D 316     8187  15184   8542    123  -1285   3943       O  
ATOM   1111  N   ILE D 317      24.265  25.121 -11.481  1.00 47.13           N  
ANISOU 1111  N   ILE D 317     5047   6897   5962   -359   -818   1165       N  
ATOM   1112  CA  ILE D 317      23.772  26.358 -12.039  1.00 45.64           C  
ANISOU 1112  CA  ILE D 317     5051   6520   5769   -468   -774    635       C  
ATOM   1113  C   ILE D 317      22.872  26.069 -13.217  1.00 40.04           C  
ANISOU 1113  C   ILE D 317     4573   5365   5274   -468   -577    645       C  
ATOM   1114  O   ILE D 317      21.719  26.548 -13.271  1.00 38.27           O  
ANISOU 1114  O   ILE D 317     4467   5135   4938   -494   -529    485       O  
ATOM   1115  CB  ILE D 317      24.934  27.267 -12.483  1.00 47.25           C  
ANISOU 1115  CB  ILE D 317     5158   6556   6236   -535   -824    346       C  
ATOM   1116  CG1 ILE D 317      25.722  27.720 -11.269  1.00 52.86           C  
ANISOU 1116  CG1 ILE D 317     5545   7827   6710   -574  -1058    111       C  
ATOM   1117  CG2 ILE D 317      24.396  28.486 -13.178  1.00 47.28           C  
ANISOU 1117  CG2 ILE D 317     5265   6228   6471   -613   -706     32       C  
ATOM   1118  CD1 ILE D 317      27.193  28.006 -11.546  1.00 55.50           C  
ANISOU 1118  CD1 ILE D 317     5662   8036   7387   -609  -1134      8       C  
ATOM   1119  N   LEU D 318      23.360  25.237 -14.133  1.00 38.36           N  
ANISOU 1119  N   LEU D 318     4347   4857   5370   -440   -460    769       N  
ATOM   1120  CA  LEU D 318      22.604  24.980 -15.368  1.00 36.42           C  
ANISOU 1120  CA  LEU D 318     4211   4403   5222   -465   -294    613       C  
ATOM   1121  C   LEU D 318      21.296  24.207 -15.158  1.00 37.16           C  
ANISOU 1121  C   LEU D 318     4318   4461   5339   -458   -217    644       C  
ATOM   1122  O   LEU D 318      20.295  24.493 -15.807  1.00 36.12           O  
ANISOU 1122  O   LEU D 318     4273   4355   5094   -491   -179    444       O  
ATOM   1123  CB  LEU D 318      23.498  24.350 -16.423  1.00 37.83           C  
ANISOU 1123  CB  LEU D 318     4272   4416   5686   -472   -149    517       C  
ATOM   1124  CG  LEU D 318      24.595  25.254 -17.012  1.00 39.22           C  
ANISOU 1124  CG  LEU D 318     4427   4633   5840   -503   -143    476       C  
ATOM   1125  CD1 LEU D 318      25.501  24.452 -17.940  1.00 42.09           C  
ANISOU 1125  CD1 LEU D 318     4607   4912   6472   -511     51    331       C  
ATOM   1126  CD2 LEU D 318      24.066  26.463 -17.767  1.00 40.22           C  
ANISOU 1126  CD2 LEU D 318     4655   4889   5735   -536   -115    469       C  
ATOM   1127  N   LYS D 319      21.304  23.244 -14.230  1.00 40.88           N  
ANISOU 1127  N   LYS D 319     4631   4899   6000   -404   -187    981       N  
ATOM   1128  CA  LYS D 319      20.119  22.479 -13.844  1.00 41.81           C  
ANISOU 1128  CA  LYS D 319     4677   4933   6275   -402    -60   1131       C  
ATOM   1129  C   LYS D 319      19.123  23.385 -13.137  1.00 41.49           C  
ANISOU 1129  C   LYS D 319     4786   5245   5729   -424   -145   1076       C  
ATOM   1130  O   LYS D 319      17.896  23.255 -13.292  1.00 40.10           O  
ANISOU 1130  O   LYS D 319     4636   5001   5598   -459    -49    957       O  
ATOM   1131  CB  LYS D 319      20.522  21.340 -12.900  1.00 46.54           C  
ANISOU 1131  CB  LYS D 319     4970   5452   7261   -305     22   1765       C  
ATOM   1132  CG  LYS D 319      19.403  20.431 -12.386  1.00 50.40           C  
ANISOU 1132  CG  LYS D 319     5266   5780   8102   -294    234   2123       C  
ATOM   1133  CD  LYS D 319      19.922  19.565 -11.220  1.00 58.02           C  
ANISOU 1133  CD  LYS D 319     5855   6862   9325   -148    292   3075       C  
ATOM   1134  CE  LYS D 319      18.896  18.574 -10.659  1.00 62.54           C  
ANISOU 1134  CE  LYS D 319     6121   7214  10425   -122    588   3664       C  
ATOM   1135  NZ  LYS D 319      17.545  19.191 -10.555  1.00 60.86           N  
ANISOU 1135  NZ  LYS D 319     6150   7268   9706   -231    612   3294       N  
ATOM   1136  N   LYS D 320      19.637  24.291 -12.323  1.00 42.93           N  
ANISOU 1136  N   LYS D 320     4990   5823   5498   -417   -306   1068       N  
ATOM   1137  CA  LYS D 320      18.760  25.239 -11.672  1.00 42.54           C  
ANISOU 1137  CA  LYS D 320     4993   6095   5075   -456   -340    817       C  
ATOM   1138  C   LYS D 320      18.078  26.122 -12.704  1.00 38.50           C  
ANISOU 1138  C   LYS D 320     4636   5282   4710   -493   -322    438       C  
ATOM   1139  O   LYS D 320      16.893  26.347 -12.625  1.00 40.23           O  
ANISOU 1139  O   LYS D 320     4872   5511   4902   -502   -259    318       O  
ATOM   1140  CB  LYS D 320      19.504  26.074 -10.655  1.00 46.43           C  
ANISOU 1140  CB  LYS D 320     5351   7111   5179   -477   -497    635       C  
ATOM   1141  CG  LYS D 320      18.582  27.010  -9.914  1.00 50.46           C  
ANISOU 1141  CG  LYS D 320     5802   7974   5397   -538   -468    193       C  
ATOM   1142  CD  LYS D 320      19.305  27.736  -8.805  1.00 58.49           C  
ANISOU 1142  CD  LYS D 320     6544   9680   5998   -596   -608   -199       C  
ATOM   1143  CE  LYS D 320      18.397  28.737  -8.116  1.00 62.33           C  
ANISOU 1143  CE  LYS D 320     6873  10491   6318   -684   -517   -884       C  
ATOM   1144  NZ  LYS D 320      17.956  28.246  -6.793  1.00 66.58           N  
ANISOU 1144  NZ  LYS D 320     7173  12043   6079   -683   -475   -757       N  
ATOM   1145  N   LEU D 321      18.804  26.599 -13.696  1.00 36.93           N  
ANISOU 1145  N   LEU D 321     4489   4861   4681   -496   -363    347       N  
ATOM   1146  CA  LEU D 321      18.179  27.406 -14.755  1.00 35.01           C  
ANISOU 1146  CA  LEU D 321     4293   4453   4555   -489   -343    235       C  
ATOM   1147  C   LEU D 321      17.157  26.615 -15.583  1.00 37.26           C  
ANISOU 1147  C   LEU D 321     4585   4732   4838   -482   -284    239       C  
ATOM   1148  O   LEU D 321      16.007  27.080 -15.797  1.00 34.40           O  
ANISOU 1148  O   LEU D 321     4196   4400   4473   -460   -293    178       O  
ATOM   1149  CB  LEU D 321      19.218  28.026 -15.667  1.00 34.88           C  
ANISOU 1149  CB  LEU D 321     4251   4321   4679   -487   -349    305       C  
ATOM   1150  CG  LEU D 321      20.251  28.931 -14.983  1.00 36.19           C  
ANISOU 1150  CG  LEU D 321     4312   4416   5020   -524   -396    186       C  
ATOM   1151  CD1 LEU D 321      21.315  29.277 -15.999  1.00 35.91           C  
ANISOU 1151  CD1 LEU D 321     4219   4233   5189   -527   -338    361       C  
ATOM   1152  CD2 LEU D 321      19.622  30.201 -14.404  1.00 39.77           C  
ANISOU 1152  CD2 LEU D 321     4627   4751   5732   -543   -382    -83       C  
ATOM   1153  N   ASN D 322      17.561  25.410 -15.994  1.00 36.35           N  
ANISOU 1153  N   ASN D 322     4419   4565   4826   -506   -213    236       N  
ATOM   1154  CA  ASN D 322      16.720  24.531 -16.770  1.00 37.05           C  
ANISOU 1154  CA  ASN D 322     4389   4658   5030   -544   -133     22       C  
ATOM   1155  C   ASN D 322      15.442  24.160 -16.033  1.00 39.61           C  
ANISOU 1155  C   ASN D 322     4665   4915   5468   -560    -77     26       C  
ATOM   1156  O   ASN D 322      14.335  24.261 -16.616  1.00 39.74           O  
ANISOU 1156  O   ASN D 322     4600   5043   5454   -577   -101   -182       O  
ATOM   1157  CB  ASN D 322      17.509  23.274 -17.199  1.00 38.70           C  
ANISOU 1157  CB  ASN D 322     4426   4690   5587   -587      5   -128       C  
ATOM   1158  CG  ASN D 322      16.812  22.469 -18.270  1.00 40.84           C  
ANISOU 1158  CG  ASN D 322     4446   5044   6025   -672    104   -640       C  
ATOM   1159  OD1 ASN D 322      16.444  22.980 -19.318  1.00 40.66           O  
ANISOU 1159  OD1 ASN D 322     4376   5478   5595   -686     17   -878       O  
ATOM   1160  ND2 ASN D 322      16.659  21.175 -18.020  1.00 45.86           N  
ANISOU 1160  ND2 ASN D 322     4820   5278   7325   -729    302   -810       N  
ATOM   1161  N   ASP D 323      15.560  23.757 -14.763  1.00 40.92           N  
ANISOU 1161  N   ASP D 323     4821   5006   5718   -547     -3    312       N  
ATOM   1162  CA  ASP D 323      14.369  23.413 -13.968  1.00 42.28           C  
ANISOU 1162  CA  ASP D 323     4904   5189   5970   -565    115    415       C  
ATOM   1163  C   ASP D 323      13.428  24.610 -13.809  1.00 39.64           C  
ANISOU 1163  C   ASP D 323     4656   5054   5348   -550     35    229       C  
ATOM   1164  O   ASP D 323      12.226  24.463 -13.899  1.00 38.29           O  
ANISOU 1164  O   ASP D 323     4388   4854   5306   -574    102    108       O  
ATOM   1165  CB  ASP D 323      14.732  22.859 -12.588  1.00 48.86           C  
ANISOU 1165  CB  ASP D 323     5636   6149   6779   -530    223    925       C  
ATOM   1166  CG  ASP D 323      15.351  21.451 -12.644  1.00 54.16           C  
ANISOU 1166  CG  ASP D 323     6061   6451   8064   -513    385   1280       C  
ATOM   1167  OD1 ASP D 323      15.646  20.936 -13.750  1.00 59.35           O  
ANISOU 1167  OD1 ASP D 323     6637   6741   9171   -555    425    933       O  
ATOM   1168  OD2 ASP D 323      15.566  20.859 -11.567  1.00 58.70           O  
ANISOU 1168  OD2 ASP D 323     6443   7154   8705   -449    496   1924       O  
ATOM   1169  N   SER D 324      13.977  25.798 -13.599  1.00 38.13           N  
ANISOU 1169  N   SER D 324     4570   4993   4923   -514    -83    162       N  
ATOM   1170  CA  SER D 324      13.145  26.965 -13.467  1.00 40.88           C  
ANISOU 1170  CA  SER D 324     4888   5377   5266   -489   -105    -46       C  
ATOM   1171  C   SER D 324      12.448  27.292 -14.786  1.00 39.40           C  
ANISOU 1171  C   SER D 324     4645   5084   5239   -442   -190    -80       C  
ATOM   1172  O   SER D 324      11.259  27.606 -14.803  1.00 38.82           O  
ANISOU 1172  O   SER D 324     4453   5009   5287   -414   -175   -169       O  
ATOM   1173  CB  SER D 324      13.910  28.167 -12.903  1.00 41.75           C  
ANISOU 1173  CB  SER D 324     4981   5538   5344   -484   -155   -220       C  
ATOM   1174  OG  SER D 324      14.446  28.954 -13.940  1.00 47.04           O  
ANISOU 1174  OG  SER D 324     5653   5964   6256   -440   -241   -162       O  
ATOM   1175  N   LEU D 325      13.161  27.193 -15.896  1.00 38.02           N  
ANISOU 1175  N   LEU D 325     4491   4939   5013   -427   -278      9       N  
ATOM   1176  CA  LEU D 325      12.511  27.374 -17.197  1.00 38.54           C  
ANISOU 1176  CA  LEU D 325     4407   5213   5023   -376   -382     39       C  
ATOM   1177  C   LEU D 325      11.426  26.327 -17.547  1.00 41.24           C  
ANISOU 1177  C   LEU D 325     4585   5701   5382   -439   -372   -234       C  
ATOM   1178  O   LEU D 325      10.456  26.651 -18.247  1.00 42.04           O  
ANISOU 1178  O   LEU D 325     4481   6066   5426   -386   -490   -254       O  
ATOM   1179  CB  LEU D 325      13.540  27.405 -18.297  1.00 38.26           C  
ANISOU 1179  CB  LEU D 325     4358   5399   4781   -363   -433    168       C  
ATOM   1180  CG  LEU D 325      14.442  28.615 -18.362  1.00 38.47           C  
ANISOU 1180  CG  LEU D 325     4410   5290   4916   -292   -436    510       C  
ATOM   1181  CD1 LEU D 325      15.565  28.292 -19.327  1.00 38.92           C  
ANISOU 1181  CD1 LEU D 325     4452   5612   4723   -316   -414    602       C  
ATOM   1182  CD2 LEU D 325      13.676  29.856 -18.799  1.00 41.76           C  
ANISOU 1182  CD2 LEU D 325     4608   5708   5550   -156   -491    878       C  
ATOM   1183  N   GLU D 326      11.586  25.090 -17.078  1.00 42.32           N  
ANISOU 1183  N   GLU D 326     4721   5655   5701   -544   -224   -411       N  
ATOM   1184  CA  GLU D 326      10.544  24.072 -17.262  1.00 46.23           C  
ANISOU 1184  CA  GLU D 326     4965   6122   6477   -637   -141   -734       C  
ATOM   1185  C   GLU D 326       9.317  24.382 -16.401  1.00 48.35           C  
ANISOU 1185  C   GLU D 326     5192   6290   6888   -621    -76   -659       C  
ATOM   1186  O   GLU D 326       8.181  24.146 -16.839  1.00 56.15           O  
ANISOU 1186  O   GLU D 326     5926   7380   8029   -655   -107   -918       O  
ATOM   1187  CB  GLU D 326      11.074  22.648 -17.010  1.00 48.52           C  
ANISOU 1187  CB  GLU D 326     5136   6067   7231   -746     79   -859       C  
ATOM   1188  CG  GLU D 326      12.097  22.219 -18.052  1.00 51.17           C  
ANISOU 1188  CG  GLU D 326     5383   6523   7535   -785     58  -1160       C  
ATOM   1189  CD  GLU D 326      12.473  20.749 -18.005  1.00 56.59           C  
ANISOU 1189  CD  GLU D 326     5776   6748   8975   -895    321  -1431       C  
ATOM   1190  OE1 GLU D 326      11.958  20.021 -17.138  1.00 62.61           O  
ANISOU 1190  OE1 GLU D 326     6392   7056  10338   -929    532  -1225       O  
ATOM   1191  OE2 GLU D 326      13.265  20.302 -18.869  1.00 61.50           O  
ANISOU 1191  OE2 GLU D 326     6232   7450   9682   -948    363  -1847       O  
ATOM   1192  N   LEU D 327       9.535  24.944 -15.204  1.00 45.17           N  
ANISOU 1192  N   LEU D 327     4968   5788   6405   -578     13   -392       N  
ATOM   1193  CA  LEU D 327       8.434  25.436 -14.376  1.00 43.99           C  
ANISOU 1193  CA  LEU D 327     4742   5651   6320   -560    112   -406       C  
ATOM   1194  C   LEU D 327       7.681  26.575 -15.048  1.00 44.18           C  
ANISOU 1194  C   LEU D 327     4651   5755   6378   -455    -62   -498       C  
ATOM   1195  O   LEU D 327       6.447  26.513 -15.168  1.00 42.97           O  
ANISOU 1195  O   LEU D 327     4274   5626   6427   -453    -50   -633       O  
ATOM   1196  CB  LEU D 327       8.896  25.822 -12.952  1.00 42.72           C  
ANISOU 1196  CB  LEU D 327     4694   5595   5940   -557    257   -261       C  
ATOM   1197  CG  LEU D 327       7.820  26.181 -11.917  1.00 43.29           C  
ANISOU 1197  CG  LEU D 327     4619   5821   6005   -569    455   -373       C  
ATOM   1198  CD1 LEU D 327       6.887  25.032 -11.539  1.00 44.45           C  
ANISOU 1198  CD1 LEU D 327     4575   5937   6377   -649    701   -217       C  
ATOM   1199  CD2 LEU D 327       8.461  26.733 -10.642  1.00 45.50           C  
ANISOU 1199  CD2 LEU D 327     4928   6479   5881   -579    552   -416       C  
ATOM   1200  N   SER D 328       8.391  27.594 -15.515  1.00 43.84           N  
ANISOU 1200  N   SER D 328     4682   5726   6248   -357   -208   -351       N  
ATOM   1201  CA  SER D 328       7.721  28.679 -16.264  1.00 49.45           C  
ANISOU 1201  CA  SER D 328     5168   6475   7145   -210   -359   -203       C  
ATOM   1202  C   SER D 328       6.799  28.153 -17.377  1.00 52.59           C  
ANISOU 1202  C   SER D 328     5299   7236   7444   -192   -538   -236       C  
ATOM   1203  O   SER D 328       5.779  28.761 -17.687  1.00 54.00           O  
ANISOU 1203  O   SER D 328     5190   7498   7829    -76   -640   -126       O  
ATOM   1204  CB  SER D 328       8.730  29.625 -16.893  1.00 49.60           C  
ANISOU 1204  CB  SER D 328     5209   6461   7174   -109   -459    140       C  
ATOM   1205  OG  SER D 328       9.380  30.327 -15.882  1.00 53.08           O  
ANISOU 1205  OG  SER D 328     5746   6567   7853   -130   -312     23       O  
ATOM   1206  N   ASP D 329       7.188  27.026 -17.966  1.00 52.84           N  
ANISOU 1206  N   ASP D 329     5347   7509   7220   -311   -571   -455       N  
ATOM   1207  CA  ASP D 329       6.442  26.417 -19.061  1.00 56.86           C  
ANISOU 1207  CA  ASP D 329     5507   8520   7576   -346   -745   -732       C  
ATOM   1208  C   ASP D 329       5.140  25.738 -18.645  1.00 55.75           C  
ANISOU 1208  C   ASP D 329     5125   8251   7806   -443   -658  -1110       C  
ATOM   1209  O   ASP D 329       4.231  25.726 -19.441  1.00 58.51           O  
ANISOU 1209  O   ASP D 329     5091   9053   8088   -419   -863  -1288       O  
ATOM   1210  CB  ASP D 329       7.301  25.367 -19.783  1.00 58.57           C  
ANISOU 1210  CB  ASP D 329     5702   8995   7555   -485   -733  -1100       C  
ATOM   1211  CG  ASP D 329       8.258  25.973 -20.780  1.00 61.38           C  
ANISOU 1211  CG  ASP D 329     6073   9860   7388   -390   -885   -801       C  
ATOM   1212  OD1 ASP D 329       8.034  27.122 -21.249  1.00 67.33           O  
ANISOU 1212  OD1 ASP D 329     6709  10925   7948   -204  -1058   -248       O  
ATOM   1213  OD2 ASP D 329       9.231  25.268 -21.121  1.00 58.81           O  
ANISOU 1213  OD2 ASP D 329     5802   9613   6927   -496   -796  -1077       O  
ATOM   1214  N   VAL D 330       5.078  25.157 -17.440  1.00 50.61           N  
ANISOU 1214  N   VAL D 330     4630   7087   7512   -551   -355  -1180       N  
ATOM   1215  CA  VAL D 330       3.911  24.374 -16.977  1.00 52.63           C  
ANISOU 1215  CA  VAL D 330     4615   7152   8230   -670   -173  -1468       C  
ATOM   1216  C   VAL D 330       2.953  25.152 -16.071  1.00 50.56           C  
ANISOU 1216  C   VAL D 330     4319   6738   8150   -589    -56  -1302       C  
ATOM   1217  O   VAL D 330       1.864  24.687 -15.792  1.00 54.97           O  
ANISOU 1217  O   VAL D 330     4597   7202   9084   -668     82  -1503       O  
ATOM   1218  CB  VAL D 330       4.324  23.101 -16.204  1.00 53.99           C  
ANISOU 1218  CB  VAL D 330     4827   6887   8800   -836    175  -1496       C  
ATOM   1219  CG1 VAL D 330       5.039  22.114 -17.114  1.00 58.01           C  
ANISOU 1219  CG1 VAL D 330     5186   7407   9448   -951    144  -1876       C  
ATOM   1220  CG2 VAL D 330       5.218  23.423 -15.022  1.00 52.83           C  
ANISOU 1220  CG2 VAL D 330     5055   6571   8447   -780    353  -1005       C  
ATOM   1221  N   VAL D 331       3.360  26.318 -15.594  1.00 46.03           N  
ANISOU 1221  N   VAL D 331     3962   6112   7416   -452    -66  -1023       N  
ATOM   1222  CA  VAL D 331       2.500  27.117 -14.757  1.00 46.55           C  
ANISOU 1222  CA  VAL D 331     3909   6042   7735   -383     87  -1038       C  
ATOM   1223  C   VAL D 331       1.661  28.064 -15.648  1.00 49.02           C  
ANISOU 1223  C   VAL D 331     3882   6469   8275   -201   -183   -958       C  
ATOM   1224  O   VAL D 331       2.218  28.997 -16.248  1.00 47.98           O  
ANISOU 1224  O   VAL D 331     3759   6375   8092    -42   -380   -642       O  
ATOM   1225  CB  VAL D 331       3.312  27.917 -13.724  1.00 45.53           C  
ANISOU 1225  CB  VAL D 331     4025   5799   7473   -352    258   -976       C  
ATOM   1226  CG1 VAL D 331       2.382  28.703 -12.818  1.00 48.28           C  
ANISOU 1226  CG1 VAL D 331     4147   6065   8130   -313    487  -1212       C  
ATOM   1227  CG2 VAL D 331       4.176  26.984 -12.873  1.00 44.31           C  
ANISOU 1227  CG2 VAL D 331     4121   5717   6996   -490    464   -891       C  
ATOM   1228  N   PRO D 332       0.327  27.832 -15.731  1.00 54.80           N  
ANISOU 1228  N   PRO D 332     5394   6714   8710   -126  -1276    655       N  
ATOM   1229  CA  PRO D 332      -0.536  28.744 -16.503  1.00 57.47           C  
ANISOU 1229  CA  PRO D 332     5663   7019   9153   -331  -1699   1020       C  
ATOM   1230  C   PRO D 332      -0.263  30.195 -16.158  1.00 55.74           C  
ANISOU 1230  C   PRO D 332     5379   6861   8938   -156  -1412   1178       C  
ATOM   1231  O   PRO D 332      -0.053  30.521 -14.991  1.00 52.50           O  
ANISOU 1231  O   PRO D 332     4650   6501   8795    126   -944   1135       O  
ATOM   1232  CB  PRO D 332      -1.967  28.348 -16.081  1.00 60.39           C  
ANISOU 1232  CB  PRO D 332     5417   7259  10270   -432  -2037   1354       C  
ATOM   1233  CG  PRO D 332      -1.864  26.934 -15.634  1.00 61.04           C  
ANISOU 1233  CG  PRO D 332     5657   7144  10388   -632  -1970   1206       C  
ATOM   1234  CD  PRO D 332      -0.456  26.772 -15.063  1.00 56.56           C  
ANISOU 1234  CD  PRO D 332     5478   6626   9383   -237  -1434    830       C  
ATOM   1235  N   ALA D 333      -0.252  31.045 -17.175  1.00 59.51           N  
ANISOU 1235  N   ALA D 333     6347   7240   9023   -373  -1759   1362       N  
ATOM   1236  CA  ALA D 333       0.097  32.453 -17.015  1.00 61.17           C  
ANISOU 1236  CA  ALA D 333     6849   7269   9120   -361  -1623   1542       C  
ATOM   1237  C   ALA D 333      -0.597  33.106 -15.827  1.00 59.97           C  
ANISOU 1237  C   ALA D 333     6166   6894   9722    206  -1541   1645       C  
ATOM   1238  O   ALA D 333       0.046  33.823 -15.078  1.00 59.86           O  
ANISOU 1238  O   ALA D 333     6264   6810   9669    288  -1121   1509       O  
ATOM   1239  CB  ALA D 333      -0.212  33.228 -18.295  1.00 68.26           C  
ANISOU 1239  CB  ALA D 333     8552   7842   9539   -669  -2296   1933       C  
ATOM   1240  N   SER D 334      -1.889  32.842 -15.650  1.00 62.70           N  
ANISOU 1240  N   SER D 334     5879   7222  10722    562  -1916   1798       N  
ATOM   1241  CA  SER D 334      -2.693  33.497 -14.606  1.00 64.77           C  
ANISOU 1241  CA  SER D 334     5502   7440  11666   1211  -1769   1783       C  
ATOM   1242  C   SER D 334      -2.257  33.028 -13.208  1.00 60.89           C  
ANISOU 1242  C   SER D 334     4651   7265  11218   1293   -895   1513       C  
ATOM   1243  O   SER D 334      -2.121  33.841 -12.294  1.00 61.14           O  
ANISOU 1243  O   SER D 334     4694   7204  11331   1708   -535   1339       O  
ATOM   1244  CB  SER D 334      -4.208  33.282 -14.848  1.00 71.21           C  
ANISOU 1244  CB  SER D 334     5438   8428  13189   1510  -2347   1927       C  
ATOM   1245  OG  SER D 334      -4.619  31.919 -14.727  1.00 69.58           O  
ANISOU 1245  OG  SER D 334     4623   8643  13170   1039  -2203   1920       O  
ATOM   1246  N   ASP D 335      -1.997  31.730 -13.053  1.00 58.26           N  
ANISOU 1246  N   ASP D 335     4203   7193  10739    919   -658   1465       N  
ATOM   1247  CA  ASP D 335      -1.402  31.215 -11.809  1.00 56.23           C  
ANISOU 1247  CA  ASP D 335     3932   7117  10315    973     -8   1281       C  
ATOM   1248  C   ASP D 335      -0.031  31.882 -11.511  1.00 52.53           C  
ANISOU 1248  C   ASP D 335     3984   6599   9376   1047    228    987       C  
ATOM   1249  O   ASP D 335       0.221  32.337 -10.391  1.00 51.86           O  
ANISOU 1249  O   ASP D 335     3897   6562   9245   1327    607    815       O  
ATOM   1250  CB  ASP D 335      -1.213  29.701 -11.887  1.00 55.93           C  
ANISOU 1250  CB  ASP D 335     4033   7098  10119    598    -53   1300       C  
ATOM   1251  CG  ASP D 335      -2.526  28.934 -12.003  1.00 62.18           C  
ANISOU 1251  CG  ASP D 335     4308   7943  11375    239   -254   1591       C  
ATOM   1252  OD1 ASP D 335      -3.598  29.549 -11.879  1.00 65.46           O  
ANISOU 1252  OD1 ASP D 335     3984   8599  12288    379   -247   1719       O  
ATOM   1253  OD2 ASP D 335      -2.472  27.701 -12.220  1.00 63.77           O  
ANISOU 1253  OD2 ASP D 335     4825   7939  11466   -182   -465   1634       O  
ATOM   1254  N   ALA D 336       0.844  31.953 -12.512  1.00 51.38           N  
ANISOU 1254  N   ALA D 336     4244   6444   8832    717     24    884       N  
ATOM   1255  CA  ALA D 336       2.182  32.587 -12.324  1.00 50.30           C  
ANISOU 1255  CA  ALA D 336     4384   6442   8285    555    269    569       C  
ATOM   1256  C   ALA D 336       2.090  33.982 -11.672  1.00 52.33           C  
ANISOU 1256  C   ALA D 336     4838   6370   8676    700    329    574       C  
ATOM   1257  O   ALA D 336       2.807  34.284 -10.688  1.00 52.13           O  
ANISOU 1257  O   ALA D 336     4834   6448   8522    775    587    263       O  
ATOM   1258  CB  ALA D 336       2.931  32.680 -13.642  1.00 50.17           C  
ANISOU 1258  CB  ALA D 336     4691   6596   7773     10    169    500       C  
ATOM   1259  N   GLU D 337       1.204  34.815 -12.209  1.00 54.93           N  
ANISOU 1259  N   GLU D 337     5387   6233   9248    816    -38    873       N  
ATOM   1260  CA  GLU D 337       1.037  36.193 -11.706  1.00 60.11           C  
ANISOU 1260  CA  GLU D 337     6452   6329  10054   1098   -144    823       C  
ATOM   1261  C   GLU D 337       0.515  36.214 -10.264  1.00 60.09           C  
ANISOU 1261  C   GLU D 337     6041   6438  10353   1798    239    532       C  
ATOM   1262  O   GLU D 337       0.948  37.016  -9.455  1.00 59.85           O  
ANISOU 1262  O   GLU D 337     6386   6152  10202   1940    368    219       O  
ATOM   1263  CB  GLU D 337       0.106  37.016 -12.611  1.00 67.07           C  
ANISOU 1263  CB  GLU D 337     7737   6573  11173   1328   -825   1187       C  
ATOM   1264  CG  GLU D 337       0.265  36.703 -14.093  1.00 68.96           C  
ANISOU 1264  CG  GLU D 337     8368   6830  11003    690  -1233   1562       C  
ATOM   1265  CD  GLU D 337      -0.016  37.879 -15.014  1.00 78.32           C  
ANISOU 1265  CD  GLU D 337    10582   7166  12010    585  -1994   1980       C  
ATOM   1266  OE1 GLU D 337       0.223  39.041 -14.615  1.00 82.83           O  
ANISOU 1266  OE1 GLU D 337    11864   7018  12587    646  -2128   1955       O  
ATOM   1267  OE2 GLU D 337      -0.465  37.625 -16.160  1.00 82.46           O  
ANISOU 1267  OE2 GLU D 337    11368   7646  12315    412  -2560   2345       O  
ATOM   1268  N   LYS D 338      -0.409  35.307  -9.958  1.00 61.68           N  
ANISOU 1268  N   LYS D 338     5526   7052  10856   2110    443    624       N  
ATOM   1269  CA  LYS D 338      -0.932  35.166  -8.603  1.00 64.53           C  
ANISOU 1269  CA  LYS D 338     5484   7724  11308   2601   1001    391       C  
ATOM   1270  C   LYS D 338       0.223  34.916  -7.644  1.00 60.44           C  
ANISOU 1270  C   LYS D 338     5351   7375  10238   2408   1332    117       C  
ATOM   1271  O   LYS D 338       0.411  35.655  -6.688  1.00 63.35           O  
ANISOU 1271  O   LYS D 338     6026   7626  10415   2735   1535   -240       O  
ATOM   1272  CB  LYS D 338      -1.949  34.022  -8.556  1.00 67.22           C  
ANISOU 1272  CB  LYS D 338     5024   8579  11937   2531   1224    643       C  
ATOM   1273  CG  LYS D 338      -2.515  33.718  -7.179  1.00 73.70           C  
ANISOU 1273  CG  LYS D 338     5441   9894  12668   2776   1984    496       C  
ATOM   1274  CD  LYS D 338      -3.654  32.718  -7.286  1.00 79.58           C  
ANISOU 1274  CD  LYS D 338     5315  11149  13772   2442   2191    811       C  
ATOM   1275  CE  LYS D 338      -4.137  32.247  -5.925  1.00 86.49           C  
ANISOU 1275  CE  LYS D 338     5899  12625  14336   2356   3109    781       C  
ATOM   1276  NZ  LYS D 338      -5.544  31.767  -6.014  1.00 96.21           N  
ANISOU 1276  NZ  LYS D 338     5931  14520  16103   2073   3424    957       N  
ATOM   1277  N   TYR D 339       1.013  33.887  -7.932  1.00 53.62           N  
ANISOU 1277  N   TYR D 339     4510   6756   9104   1964   1268    209       N  
ATOM   1278  CA  TYR D 339       2.190  33.582  -7.122  1.00 52.46           C  
ANISOU 1278  CA  TYR D 339     4639   6813   8480   1895   1350    -87       C  
ATOM   1279  C   TYR D 339       3.176  34.740  -6.982  1.00 53.42           C  
ANISOU 1279  C   TYR D 339     5132   6757   8408   1730   1185   -467       C  
ATOM   1280  O   TYR D 339       3.671  34.992  -5.895  1.00 54.57           O  
ANISOU 1280  O   TYR D 339     5515   6977   8241   1888   1250   -803       O  
ATOM   1281  CB  TYR D 339       2.941  32.384  -7.682  1.00 48.06           C  
ANISOU 1281  CB  TYR D 339     4006   6487   7765   1644   1141    -55       C  
ATOM   1282  CG  TYR D 339       2.310  31.057  -7.389  1.00 47.87           C  
ANISOU 1282  CG  TYR D 339     3943   6495   7749   1710   1212    243       C  
ATOM   1283  CD1 TYR D 339       2.205  30.584  -6.087  1.00 52.23           C  
ANISOU 1283  CD1 TYR D 339     4760   7113   7969   1901   1442    302       C  
ATOM   1284  CD2 TYR D 339       1.860  30.250  -8.409  1.00 47.12           C  
ANISOU 1284  CD2 TYR D 339     3722   6300   7881   1466    996    481       C  
ATOM   1285  CE1 TYR D 339       1.627  29.350  -5.808  1.00 54.24           C  
ANISOU 1285  CE1 TYR D 339     5193   7272   8144   1731   1497    693       C  
ATOM   1286  CE2 TYR D 339       1.310  29.007  -8.146  1.00 50.56           C  
ANISOU 1286  CE2 TYR D 339     4281   6608   8322   1336    974    772       C  
ATOM   1287  CZ  TYR D 339       1.188  28.562  -6.850  1.00 53.36           C  
ANISOU 1287  CZ  TYR D 339     4939   6966   8368   1411   1241    925       C  
ATOM   1288  OH  TYR D 339       0.642  27.320  -6.617  1.00 57.72           O  
ANISOU 1288  OH  TYR D 339     5817   7260   8852   1061   1196   1324       O  
ATOM   1289  N   ARG D 340       3.491  35.422  -8.073  1.00 54.82           N  
ANISOU 1289  N   ARG D 340     5459   6687   8683   1281    932   -396       N  
ATOM   1290  CA  ARG D 340       4.385  36.574  -7.972  1.00 59.47           C  
ANISOU 1290  CA  ARG D 340     6489   7016   9088    841    771   -689       C  
ATOM   1291  C   ARG D 340       3.862  37.609  -6.965  1.00 65.10           C  
ANISOU 1291  C   ARG D 340     7701   7174   9858   1323    765   -934       C  
ATOM   1292  O   ARG D 340       4.626  38.217  -6.213  1.00 66.99           O  
ANISOU 1292  O   ARG D 340     8304   7310   9839   1130    662  -1357       O  
ATOM   1293  CB  ARG D 340       4.577  37.215  -9.338  1.00 62.33           C  
ANISOU 1293  CB  ARG D 340     7176   7068   9439    142    545   -408       C  
ATOM   1294  CG  ARG D 340       5.469  36.383 -10.241  1.00 61.16           C  
ANISOU 1294  CG  ARG D 340     6592   7630   9016   -442    669   -429       C  
ATOM   1295  CD  ARG D 340       5.697  37.054 -11.578  1.00 65.88           C  
ANISOU 1295  CD  ARG D 340     7660   8018   9353  -1308    571   -120       C  
ATOM   1296  NE  ARG D 340       6.068  36.065 -12.587  1.00 65.20           N  
ANISOU 1296  NE  ARG D 340     7164   8633   8975  -1570    768   -130       N  
ATOM   1297  CZ  ARG D 340       7.295  35.577 -12.778  1.00 67.16           C  
ANISOU 1297  CZ  ARG D 340     6826   9784   8907  -1993   1104   -594       C  
ATOM   1298  NH1 ARG D 340       8.328  35.980 -12.031  1.00 70.12           N  
ANISOU 1298  NH1 ARG D 340     6831  10552   9257  -2332   1213  -1047       N  
ATOM   1299  NH2 ARG D 340       7.490  34.681 -13.739  1.00 67.13           N  
ANISOU 1299  NH2 ARG D 340     6550  10347   8607  -2034   1287   -700       N  
ATOM   1300  N   GLN D 341       2.547  37.797  -6.957  1.00 68.26           N  
ANISOU 1300  N   GLN D 341     8058   7273  10602   1995    844   -765       N  
ATOM   1301  CA  GLN D 341       1.927  38.737  -6.052  1.00 75.11           C  
ANISOU 1301  CA  GLN D 341     9320   7683  11534   2699    910  -1141       C  
ATOM   1302  C   GLN D 341       1.568  38.030  -4.771  1.00 75.09           C  
ANISOU 1302  C   GLN D 341     8968   8308  11253   3204   1488  -1378       C  
ATOM   1303  O   GLN D 341       1.693  38.617  -3.708  1.00 83.00           O  
ANISOU 1303  O   GLN D 341    10443   9176  11915   3549   1620  -1884       O  
ATOM   1304  CB  GLN D 341       0.694  39.332  -6.697  1.00 81.40           C  
ANISOU 1304  CB  GLN D 341    10090   7965  12871   3326    672   -960       C  
ATOM   1305  CG  GLN D 341       0.987  40.033  -8.013  1.00 84.29           C  
ANISOU 1305  CG  GLN D 341    11102   7584  13340   2777     -3   -579       C  
ATOM   1306  CD  GLN D 341      -0.167  40.885  -8.490  1.00 93.86           C  
ANISOU 1306  CD  GLN D 341    12592   8019  15048   3628   -536   -493       C  
ATOM   1307  OE1 GLN D 341      -1.021  41.287  -7.698  1.00101.43           O  
ANISOU 1307  OE1 GLN D 341    13343   8888  16304   4717   -392   -947       O  
ATOM   1308  NE2 GLN D 341      -0.201  41.171  -9.789  1.00 96.16           N  
ANISOU 1308  NE2 GLN D 341    13373   7787  15374   3213  -1184     43       N  
TER    1309      GLN D 341                                                      
ATOM   1310  N   GLU E 303      35.701  14.966  -3.237  1.00 91.74           N  
ANISOU 1310  N   GLU E 303    12701  11033  11123   -857   4406   -137       N  
ATOM   1311  CA  GLU E 303      36.193  16.041  -2.324  1.00 89.14           C  
ANISOU 1311  CA  GLU E 303    11897  11009  10960   -464   3526    609       C  
ATOM   1312  C   GLU E 303      35.380  16.056  -1.026  1.00 85.15           C  
ANISOU 1312  C   GLU E 303    11362  10445  10545   -571   3252    483       C  
ATOM   1313  O   GLU E 303      34.886  15.017  -0.584  1.00 89.60           O  
ANISOU 1313  O   GLU E 303    12298  10517  11226   -651   3948    206       O  
ATOM   1314  CB  GLU E 303      36.182  17.423  -3.029  1.00 90.49           C  
ANISOU 1314  CB  GLU E 303    11730  11751  10899   -529   2763    669       C  
ATOM   1315  CG  GLU E 303      37.316  18.379  -2.595  1.00 90.28           C  
ANISOU 1315  CG  GLU E 303    11341  11861  11101   -299   2396   1363       C  
ATOM   1316  CD  GLU E 303      37.210  19.795  -3.173  1.00 89.86           C  
ANISOU 1316  CD  GLU E 303    11173  12020  10949   -373   2020   1425       C  
ATOM   1317  OE1 GLU E 303      36.078  20.291  -3.383  1.00 91.59           O  
ANISOU 1317  OE1 GLU E 303    11475  12409  10914   -407   1818   1146       O  
ATOM   1318  OE2 GLU E 303      38.267  20.422  -3.406  1.00 89.17           O  
ANISOU 1318  OE2 GLU E 303    10900  11965  11014   -337   2067   1820       O  
ATOM   1319  N   ILE E 304      35.226  17.231  -0.425  1.00 78.66           N  
ANISOU 1319  N   ILE E 304    10183  10013   9689   -610   2417    645       N  
ATOM   1320  CA  ILE E 304      34.716  17.348   0.924  1.00 74.55           C  
ANISOU 1320  CA  ILE E 304     9573   9500   9251   -639   2133    658       C  
ATOM   1321  C   ILE E 304      33.822  18.567   0.987  1.00 71.11           C  
ANISOU 1321  C   ILE E 304     9033   9324   8660   -916   1472    366       C  
ATOM   1322  O   ILE E 304      34.178  19.642   0.483  1.00 69.51           O  
ANISOU 1322  O   ILE E 304     8712   9280   8419   -909   1225    546       O  
ATOM   1323  CB  ILE E 304      35.879  17.456   1.931  1.00 75.74           C  
ANISOU 1323  CB  ILE E 304     9306   9989   9481   -285   2056   1361       C  
ATOM   1324  CG1 ILE E 304      36.250  16.061   2.458  1.00 80.89           C  
ANISOU 1324  CG1 ILE E 304    10098  10411  10222    311   2903   1841       C  
ATOM   1325  CG2 ILE E 304      35.543  18.403   3.080  1.00 73.32           C  
ANISOU 1325  CG2 ILE E 304     8703  10055   9098   -564   1421   1259       C  
ATOM   1326  CD1 ILE E 304      37.740  15.826   2.577  1.00 86.35           C  
ANISOU 1326  CD1 ILE E 304    10306  11698  10803    960   3195   2756       C  
ATOM   1327  N   PHE E 305      32.640  18.375   1.573  1.00 68.39           N  
ANISOU 1327  N   PHE E 305     8791   8957   8237  -1093   1375    -29       N  
ATOM   1328  CA  PHE E 305      31.747  19.476   1.862  1.00 65.04           C  
ANISOU 1328  CA  PHE E 305     8287   8759   7665  -1167    896   -141       C  
ATOM   1329  C   PHE E 305      31.630  19.545   3.376  1.00 61.97           C  
ANISOU 1329  C   PHE E 305     7873   8211   7458  -1217    710    -77       C  
ATOM   1330  O   PHE E 305      31.932  18.583   4.073  1.00 63.85           O  
ANISOU 1330  O   PHE E 305     8122   8313   7824  -1120    971     28       O  
ATOM   1331  CB  PHE E 305      30.382  19.274   1.195  1.00 67.14           C  
ANISOU 1331  CB  PHE E 305     8508   9510   7491  -1303    901   -645       C  
ATOM   1332  CG  PHE E 305      30.453  19.079  -0.302  1.00 70.74           C  
ANISOU 1332  CG  PHE E 305     8841  10491   7543  -1317   1106   -815       C  
ATOM   1333  CD1 PHE E 305      30.717  17.824  -0.844  1.00 73.18           C  
ANISOU 1333  CD1 PHE E 305     9306  10667   7831  -1671   1666  -1276       C  
ATOM   1334  CD2 PHE E 305      30.249  20.152  -1.176  1.00 72.63           C  
ANISOU 1334  CD2 PHE E 305     8851  11357   7384   -921    918   -480       C  
ATOM   1335  CE1 PHE E 305      30.776  17.642  -2.218  1.00 77.11           C  
ANISOU 1335  CE1 PHE E 305     9662  11777   7857  -1802   1883  -1564       C  
ATOM   1336  CE2 PHE E 305      30.310  19.972  -2.555  1.00 76.57           C  
ANISOU 1336  CE2 PHE E 305     9128  12603   7362   -865   1088   -596       C  
ATOM   1337  CZ  PHE E 305      30.571  18.715  -3.074  1.00 78.46           C  
ANISOU 1337  CZ  PHE E 305     9453  12837   7522  -1393   1495  -1222       C  
ATOM   1338  N   THR E 306      31.227  20.700   3.883  1.00 60.63           N  
ANISOU 1338  N   THR E 306     7701   8061   7272  -1289    413    -71       N  
ATOM   1339  CA  THR E 306      31.017  20.862   5.303  1.00 59.64           C  
ANISOU 1339  CA  THR E 306     7539   7900   7219  -1426    234   -127       C  
ATOM   1340  C   THR E 306      29.655  21.466   5.551  1.00 58.56           C  
ANISOU 1340  C   THR E 306     7575   7705   6970  -1401    111   -335       C  
ATOM   1341  O   THR E 306      29.095  22.176   4.701  1.00 58.39           O  
ANISOU 1341  O   THR E 306     7634   7772   6780  -1183    188   -253       O  
ATOM   1342  CB  THR E 306      32.096  21.732   5.962  1.00 61.97           C  
ANISOU 1342  CB  THR E 306     7633   8347   7565  -1730    171    -24       C  
ATOM   1343  OG1 THR E 306      32.212  22.985   5.268  1.00 62.88           O  
ANISOU 1343  OG1 THR E 306     7969   8159   7762  -1883    372    -41       O  
ATOM   1344  CG2 THR E 306      33.427  21.000   5.937  1.00 64.58           C  
ANISOU 1344  CG2 THR E 306     7558   9132   7846  -1629    261    306       C  
ATOM   1345  N   LEU E 307      29.142  21.176   6.735  1.00 56.67           N  
ANISOU 1345  N   LEU E 307     7336   7438   6754  -1482    -10   -476       N  
ATOM   1346  CA  LEU E 307      27.803  21.551   7.101  1.00 57.56           C  
ANISOU 1346  CA  LEU E 307     7566   7559   6744  -1409    -99   -642       C  
ATOM   1347  C   LEU E 307      27.818  22.159   8.498  1.00 55.48           C  
ANISOU 1347  C   LEU E 307     7385   7125   6567  -1594   -195   -697       C  
ATOM   1348  O   LEU E 307      28.362  21.561   9.402  1.00 55.41           O  
ANISOU 1348  O   LEU E 307     7195   7285   6574  -1708   -279   -694       O  
ATOM   1349  CB  LEU E 307      26.937  20.279   7.086  1.00 57.53           C  
ANISOU 1349  CB  LEU E 307     7489   7731   6639  -1453    -21   -943       C  
ATOM   1350  CG  LEU E 307      25.548  20.360   6.473  1.00 60.93           C  
ANISOU 1350  CG  LEU E 307     7756   8720   6673  -1419    -49  -1201       C  
ATOM   1351  CD1 LEU E 307      25.593  21.117   5.155  1.00 62.99           C  
ANISOU 1351  CD1 LEU E 307     7853   9482   6595  -1118    -40   -958       C  
ATOM   1352  CD2 LEU E 307      24.954  18.961   6.280  1.00 62.74           C  
ANISOU 1352  CD2 LEU E 307     7893   9151   6794  -1847    263  -1784       C  
ATOM   1353  N   GLN E 308      27.223  23.327   8.671  1.00 57.12           N  
ANISOU 1353  N   GLN E 308     7860   7082   6761  -1551    -49   -697       N  
ATOM   1354  CA  GLN E 308      26.997  23.878  10.029  1.00 59.23           C  
ANISOU 1354  CA  GLN E 308     8282   7165   7055  -1826    -24   -914       C  
ATOM   1355  C   GLN E 308      25.683  23.324  10.626  1.00 56.56           C  
ANISOU 1355  C   GLN E 308     7925   6953   6610  -1562   -210   -964       C  
ATOM   1356  O   GLN E 308      24.598  23.659  10.160  1.00 55.69           O  
ANISOU 1356  O   GLN E 308     7900   6893   6367  -1170    -96   -821       O  
ATOM   1357  CB  GLN E 308      26.977  25.419  10.036  1.00 65.80           C  
ANISOU 1357  CB  GLN E 308     9607   7393   8001  -1959    570   -945       C  
ATOM   1358  CG  GLN E 308      26.182  26.067   8.888  1.00 71.25           C  
ANISOU 1358  CG  GLN E 308    10572   7853   8647  -1211   1017   -440       C  
ATOM   1359  CD  GLN E 308      25.647  27.472   9.173  1.00 79.58           C  
ANISOU 1359  CD  GLN E 308    12294   8118   9823   -972   1932   -258       C  
ATOM   1360  OE1 GLN E 308      25.612  27.944  10.322  1.00 82.70           O  
ANISOU 1360  OE1 GLN E 308    13017   8063  10342  -1486   2204   -682       O  
ATOM   1361  NE2 GLN E 308      25.204  28.145   8.110  1.00 85.28           N  
ANISOU 1361  NE2 GLN E 308    13235   8718  10450    -99   2567    433       N  
ATOM   1362  N   VAL E 309      25.801  22.501  11.664  1.00 55.29           N  
ANISOU 1362  N   VAL E 309     7580   6992   6433  -1703   -418  -1087       N  
ATOM   1363  CA  VAL E 309      24.655  21.886  12.332  1.00 54.27           C  
ANISOU 1363  CA  VAL E 309     7449   6912   6256  -1534   -493  -1166       C  
ATOM   1364  C   VAL E 309      24.494  22.478  13.732  1.00 57.50           C  
ANISOU 1364  C   VAL E 309     7970   7279   6595  -1695   -532  -1302       C  
ATOM   1365  O   VAL E 309      25.473  22.514  14.492  1.00 61.85           O  
ANISOU 1365  O   VAL E 309     8319   8161   7017  -1980   -602  -1372       O  
ATOM   1366  CB  VAL E 309      24.884  20.374  12.461  1.00 52.78           C  
ANISOU 1366  CB  VAL E 309     7082   6837   6135  -1456   -400  -1114       C  
ATOM   1367  CG1 VAL E 309      23.687  19.687  13.134  1.00 52.52           C  
ANISOU 1367  CG1 VAL E 309     7105   6736   6112  -1388   -279  -1266       C  
ATOM   1368  CG2 VAL E 309      25.189  19.778  11.098  1.00 52.26           C  
ANISOU 1368  CG2 VAL E 309     6975   6760   6122  -1466   -207  -1130       C  
ATOM   1369  N   ARG E 310      23.287  22.956  14.065  1.00 57.29           N  
ANISOU 1369  N   ARG E 310     8169   7060   6538  -1519   -453  -1346       N  
ATOM   1370  CA  ARG E 310      22.983  23.552  15.375  1.00 58.53           C  
ANISOU 1370  CA  ARG E 310     8522   7100   6616  -1684   -388  -1537       C  
ATOM   1371  C   ARG E 310      22.480  22.497  16.392  1.00 57.96           C  
ANISOU 1371  C   ARG E 310     8235   7317   6466  -1545   -593  -1528       C  
ATOM   1372  O   ARG E 310      21.417  21.897  16.176  1.00 58.04           O  
ANISOU 1372  O   ARG E 310     8216   7303   6530  -1278   -578  -1467       O  
ATOM   1373  CB  ARG E 310      21.906  24.638  15.244  1.00 60.95           C  
ANISOU 1373  CB  ARG E 310     9257   6963   6938  -1381      3  -1436       C  
ATOM   1374  CG  ARG E 310      22.100  25.718  14.180  1.00 64.66           C  
ANISOU 1374  CG  ARG E 310    10067   7007   7493  -1176    538  -1191       C  
ATOM   1375  CD  ARG E 310      20.790  26.504  14.052  1.00 69.64           C  
ANISOU 1375  CD  ARG E 310    11002   7434   8024   -434   1053   -753       C  
ATOM   1376  NE  ARG E 310      20.820  27.677  13.173  1.00 77.04           N  
ANISOU 1376  NE  ARG E 310    12396   7859   9015     91   1926   -259       N  
ATOM   1377  CZ  ARG E 310      19.770  28.482  12.939  1.00 85.36           C  
ANISOU 1377  CZ  ARG E 310    13725   8798   9909   1061   2656    422       C  
ATOM   1378  NH1 ARG E 310      18.585  28.260  13.511  1.00 85.87           N  
ANISOU 1378  NH1 ARG E 310    13577   9322   9727   1501   2487    598       N  
ATOM   1379  NH2 ARG E 310      19.897  29.532  12.127  1.00 93.11           N  
ANISOU 1379  NH2 ARG E 310    15193   9233  10950   1724   3702   1051       N  
ATOM   1380  N   GLY E 311      23.231  22.314  17.495  1.00 58.01           N  
ANISOU 1380  N   GLY E 311     8023   7761   6256  -1740   -696  -1597       N  
ATOM   1381  CA  GLY E 311      22.897  21.418  18.605  1.00 56.77           C  
ANISOU 1381  CA  GLY E 311     7673   7940   5955  -1454   -738  -1433       C  
ATOM   1382  C   GLY E 311      23.645  20.086  18.614  1.00 58.78           C  
ANISOU 1382  C   GLY E 311     7578   8581   6175  -1047   -603   -968       C  
ATOM   1383  O   GLY E 311      23.836  19.478  17.575  1.00 58.83           O  
ANISOU 1383  O   GLY E 311     7641   8263   6447   -936   -411   -832       O  
ATOM   1384  N   ARG E 312      24.072  19.627  19.787  1.00 62.86           N  
ANISOU 1384  N   ARG E 312     8290   9723   5871  -1530  -1503  -1037       N  
ATOM   1385  CA  ARG E 312      24.691  18.287  19.918  1.00 65.72           C  
ANISOU 1385  CA  ARG E 312     8599  10302   6069  -1046  -1749  -1141       C  
ATOM   1386  C   ARG E 312      23.786  17.174  19.352  1.00 59.32           C  
ANISOU 1386  C   ARG E 312     7990   9321   5226  -1030  -1178   -645       C  
ATOM   1387  O   ARG E 312      24.256  16.305  18.617  1.00 56.76           O  
ANISOU 1387  O   ARG E 312     7325   9205   5036  -1033  -1184   -648       O  
ATOM   1388  CB  ARG E 312      25.008  17.912  21.380  1.00 70.79           C  
ANISOU 1388  CB  ARG E 312    10009  10836   6051   -119  -2261  -1390       C  
ATOM   1389  CG  ARG E 312      26.277  18.480  22.002  1.00 81.57           C  
ANISOU 1389  CG  ARG E 312    10954  12575   7461    245  -3203  -2324       C  
ATOM   1390  CD  ARG E 312      26.070  19.929  22.442  1.00 82.67           C  
ANISOU 1390  CD  ARG E 312    11059  12568   7782   -177  -3228  -2524       C  
ATOM   1391  NE  ARG E 312      27.085  20.435  23.353  1.00 90.69           N  
ANISOU 1391  NE  ARG E 312    11814  13857   8786    333  -4178  -3595       N  
ATOM   1392  CZ  ARG E 312      27.144  21.700  23.770  1.00 94.69           C  
ANISOU 1392  CZ  ARG E 312    12172  14263   9541    -51  -4285  -4022       C  
ATOM   1393  NH1 ARG E 312      26.247  22.585  23.344  1.00 89.11           N  
ANISOU 1393  NH1 ARG E 312    11722  13148   8985   -865  -3486  -3349       N  
ATOM   1394  NH2 ARG E 312      28.101  22.091  24.617  1.00104.70           N  
ANISOU 1394  NH2 ARG E 312    13051  15840  10890    488  -5273  -5265       N  
ATOM   1395  N   GLU E 313      22.514  17.171  19.745  1.00 58.92           N  
ANISOU 1395  N   GLU E 313     8420   8886   5080  -1027   -640   -385       N  
ATOM   1396  CA  GLU E 313      21.601  16.076  19.373  1.00 59.00           C  
ANISOU 1396  CA  GLU E 313     8504   8666   5247  -1103     54   -243       C  
ATOM   1397  C   GLU E 313      21.455  16.003  17.865  1.00 52.73           C  
ANISOU 1397  C   GLU E 313     6884   8190   4958  -1477     12   -285       C  
ATOM   1398  O   GLU E 313      21.573  14.921  17.297  1.00 54.24           O  
ANISOU 1398  O   GLU E 313     6922   8426   5260  -1480    189   -265       O  
ATOM   1399  CB  GLU E 313      20.218  16.214  20.030  1.00 64.55           C  
ANISOU 1399  CB  GLU E 313     9580   8906   6038  -1194    817   -302       C  
ATOM   1400  CG  GLU E 313      20.195  15.937  21.529  1.00 74.20           C  
ANISOU 1400  CG  GLU E 313    12070   9529   6592   -727   1231   -189       C  
ATOM   1401  CD  GLU E 313      18.780  15.723  22.079  1.00 84.60           C  
ANISOU 1401  CD  GLU E 313    13781  10212   8150   -996   2491   -361       C  
ATOM   1402  OE1 GLU E 313      18.038  14.863  21.522  1.00 89.60           O  
ANISOU 1402  OE1 GLU E 313    14010  10664   9368  -1433   3339   -649       O  
ATOM   1403  OE2 GLU E 313      18.416  16.396  23.086  1.00 86.17           O  
ANISOU 1403  OE2 GLU E 313    14646  10063   8028   -808   2719   -344       O  
ATOM   1404  N   ARG E 314      21.232  17.153  17.221  1.00 48.49           N  
ANISOU 1404  N   ARG E 314     6053   7781   4588  -1663   -220   -346       N  
ATOM   1405  CA  ARG E 314      21.066  17.193  15.786  1.00 46.75           C  
ANISOU 1405  CA  ARG E 314     5460   7717   4583  -1738   -306   -402       C  
ATOM   1406  C   ARG E 314      22.365  16.768  15.085  1.00 45.24           C  
ANISOU 1406  C   ARG E 314     5083   7724   4382  -1884   -442   -295       C  
ATOM   1407  O   ARG E 314      22.344  16.075  14.080  1.00 41.10           O  
ANISOU 1407  O   ARG E 314     4339   7299   3976  -1854   -393   -285       O  
ATOM   1408  CB  ARG E 314      20.608  18.577  15.295  1.00 47.38           C  
ANISOU 1408  CB  ARG E 314     5788   7681   4533  -1640   -486   -474       C  
ATOM   1409  CG  ARG E 314      20.410  18.625  13.760  1.00 47.02           C  
ANISOU 1409  CG  ARG E 314     5809   7642   4412  -1375   -632   -559       C  
ATOM   1410  CD  ARG E 314      19.825  19.932  13.243  1.00 50.68           C  
ANISOU 1410  CD  ARG E 314     6970   7824   4460   -915   -837   -673       C  
ATOM   1411  NE  ARG E 314      18.614  20.308  13.972  1.00 53.83           N  
ANISOU 1411  NE  ARG E 314     7184   8287   4982   -579  -1011  -1049       N  
ATOM   1412  CZ  ARG E 314      18.054  21.522  13.987  1.00 57.71           C  
ANISOU 1412  CZ  ARG E 314     8299   8549   5077   -101  -1243  -1188       C  
ATOM   1413  NH1 ARG E 314      18.563  22.547  13.295  1.00 61.96           N  
ANISOU 1413  NH1 ARG E 314     9979   8614   4948    108  -1221   -918       N  
ATOM   1414  NH2 ARG E 314      16.951  21.706  14.682  1.00 58.46           N  
ANISOU 1414  NH2 ARG E 314     7995   8790   5427    185  -1362  -1668       N  
ATOM   1415  N   TYR E 315      23.492  17.189  15.637  1.00 47.97           N  
ANISOU 1415  N   TYR E 315     5419   8146   4658  -2017   -622   -384       N  
ATOM   1416  CA  TYR E 315      24.771  16.796  15.095  1.00 49.55           C  
ANISOU 1416  CA  TYR E 315     5207   8593   5025  -2179   -692   -570       C  
ATOM   1417  C   TYR E 315      24.959  15.271  15.146  1.00 48.12           C  
ANISOU 1417  C   TYR E 315     4912   8601   4768  -1819   -789   -511       C  
ATOM   1418  O   TYR E 315      25.340  14.669  14.146  1.00 47.36           O  
ANISOU 1418  O   TYR E 315     4529   8645   4818  -1904   -686   -485       O  
ATOM   1419  CB  TYR E 315      25.904  17.514  15.824  1.00 55.37           C  
ANISOU 1419  CB  TYR E 315     5668   9461   5906  -2345   -940  -1094       C  
ATOM   1420  CG  TYR E 315      27.244  16.951  15.457  1.00 61.91           C  
ANISOU 1420  CG  TYR E 315     5782  10666   7074  -2417  -1066  -1629       C  
ATOM   1421  CD1 TYR E 315      27.857  17.301  14.262  1.00 64.82           C  
ANISOU 1421  CD1 TYR E 315     5833  10946   7846  -3041   -480  -1813       C  
ATOM   1422  CD2 TYR E 315      27.888  16.032  16.289  1.00 67.78           C  
ANISOU 1422  CD2 TYR E 315     6320  11780   7650  -1731  -1719  -2025       C  
ATOM   1423  CE1 TYR E 315      29.091  16.775  13.910  1.00 71.77           C  
ANISOU 1423  CE1 TYR E 315     5887  12197   9183  -3166   -474  -2474       C  
ATOM   1424  CE2 TYR E 315      29.131  15.507  15.952  1.00 74.81           C  
ANISOU 1424  CE2 TYR E 315     6399  13123   8900  -1639  -1970  -2739       C  
ATOM   1425  CZ  TYR E 315      29.720  15.880  14.753  1.00 75.88           C  
ANISOU 1425  CZ  TYR E 315     5912  13260   9659  -2452  -1307  -2997       C  
ATOM   1426  OH  TYR E 315      30.931  15.361  14.393  1.00 83.99           O  
ANISOU 1426  OH  TYR E 315     5988  14745  11179  -2435  -1417  -3843       O  
ATOM   1427  N   GLU E 316      24.675  14.654  16.292  1.00 48.74           N  
ANISOU 1427  N   GLU E 316     5455   8551   4512  -1366   -873   -469       N  
ATOM   1428  CA  GLU E 316      24.805  13.207  16.433  1.00 51.33           C  
ANISOU 1428  CA  GLU E 316     6110   8817   4575   -930   -792   -383       C  
ATOM   1429  C   GLU E 316      23.911  12.414  15.464  1.00 48.89           C  
ANISOU 1429  C   GLU E 316     5685   8357   4533  -1204   -258   -174       C  
ATOM   1430  O   GLU E 316      24.298  11.356  14.964  1.00 46.72           O  
ANISOU 1430  O   GLU E 316     5386   8144   4219  -1058   -212   -141       O  
ATOM   1431  CB  GLU E 316      24.518  12.794  17.876  1.00 56.44           C  
ANISOU 1431  CB  GLU E 316     7821   9025   4596   -316   -693   -331       C  
ATOM   1432  CG  GLU E 316      25.714  12.972  18.807  1.00 64.03           C  
ANISOU 1432  CG  GLU E 316     9025  10220   5083    459  -1547   -768       C  
ATOM   1433  CD  GLU E 316      25.322  13.022  20.276  1.00 71.96           C  
ANISOU 1433  CD  GLU E 316    11354  10677   5309   1172  -1505   -710       C  
ATOM   1434  OE1 GLU E 316      24.205  12.564  20.600  1.00 75.16           O  
ANISOU 1434  OE1 GLU E 316    12661  10392   5501   1044   -536   -286       O  
ATOM   1435  OE2 GLU E 316      26.124  13.503  21.120  1.00 79.19           O  
ANISOU 1435  OE2 GLU E 316    12438  11800   5848   1882  -2374  -1221       O  
ATOM   1436  N   ILE E 317      22.712  12.939  15.228  1.00 48.13           N  
ANISOU 1436  N   ILE E 317     5463   8093   4730  -1508     57   -196       N  
ATOM   1437  CA  ILE E 317      21.766  12.351  14.279  1.00 47.30           C  
ANISOU 1437  CA  ILE E 317     4997   7943   5031  -1682    375   -368       C  
ATOM   1438  C   ILE E 317      22.313  12.466  12.867  1.00 43.91           C  
ANISOU 1438  C   ILE E 317     4166   7835   4682  -1689      0   -333       C  
ATOM   1439  O   ILE E 317      22.388  11.470  12.150  1.00 42.83           O  
ANISOU 1439  O   ILE E 317     3870   7749   4651  -1653     84   -370       O  
ATOM   1440  CB  ILE E 317      20.378  13.034  14.397  1.00 49.05           C  
ANISOU 1440  CB  ILE E 317     4996   8035   5605  -1795    581   -745       C  
ATOM   1441  CG1 ILE E 317      19.670  12.512  15.644  1.00 52.73           C  
ANISOU 1441  CG1 ILE E 317     5906   7999   6128  -1923   1403   -892       C  
ATOM   1442  CG2 ILE E 317      19.531  12.791  13.147  1.00 52.24           C  
ANISOU 1442  CG2 ILE E 317     4755   8614   6477  -1740    457  -1269       C  
ATOM   1443  CD1 ILE E 317      18.586  13.417  16.199  1.00 55.36           C  
ANISOU 1443  CD1 ILE E 317     6086   8210   6736  -2011   1630  -1269       C  
ATOM   1444  N   LEU E 318      22.711  13.667  12.457  1.00 42.36           N  
ANISOU 1444  N   LEU E 318     3994   7724   4376  -1739   -264   -268       N  
ATOM   1445  CA  LEU E 318      23.176  13.817  11.101  1.00 43.65           C  
ANISOU 1445  CA  LEU E 318     4162   7942   4481  -1715   -331   -220       C  
ATOM   1446  C   LEU E 318      24.488  13.058  10.862  1.00 44.45           C  
ANISOU 1446  C   LEU E 318     4037   8244   4607  -1837   -266   -139       C  
ATOM   1447  O   LEU E 318      24.721  12.592   9.724  1.00 45.02           O  
ANISOU 1447  O   LEU E 318     4098   8340   4666  -1769   -190    -99       O  
ATOM   1448  CB  LEU E 318      23.343  15.289  10.691  1.00 46.38           C  
ANISOU 1448  CB  LEU E 318     4992   8044   4586  -1770   -283   -175       C  
ATOM   1449  CG  LEU E 318      22.061  16.114  10.563  1.00 47.62           C  
ANISOU 1449  CG  LEU E 318     5527   8008   4556  -1349   -509   -345       C  
ATOM   1450  CD1 LEU E 318      22.381  17.472   9.987  1.00 50.43           C  
ANISOU 1450  CD1 LEU E 318     6821   7906   4432  -1277   -315   -217       C  
ATOM   1451  CD2 LEU E 318      21.018  15.407   9.715  1.00 49.59           C  
ANISOU 1451  CD2 LEU E 318     5564   8382   4895   -795   -839   -730       C  
ATOM   1452  N   LYS E 319      25.336  12.962  11.894  1.00 44.47           N  
ANISOU 1452  N   LYS E 319     3885   8406   4606  -1867   -384   -238       N  
ATOM   1453  CA  LYS E 319      26.600  12.225  11.798  1.00 46.53           C  
ANISOU 1453  CA  LYS E 319     3782   8972   4923  -1768   -506   -437       C  
ATOM   1454  C   LYS E 319      26.339  10.731  11.633  1.00 45.44           C  
ANISOU 1454  C   LYS E 319     3800   8833   4629  -1409   -502   -269       C  
ATOM   1455  O   LYS E 319      26.906  10.094  10.741  1.00 46.61           O  
ANISOU 1455  O   LYS E 319     3720   9142   4848  -1379   -458   -286       O  
ATOM   1456  CB  LYS E 319      27.501  12.474  13.019  1.00 52.07           C  
ANISOU 1456  CB  LYS E 319     4280   9909   5595  -1550   -920   -885       C  
ATOM   1457  CG  LYS E 319      28.603  11.442  13.141  1.00 56.62           C  
ANISOU 1457  CG  LYS E 319     4531  10869   6114  -1034  -1311  -1289       C  
ATOM   1458  CD  LYS E 319      29.681  11.858  14.109  1.00 66.69           C  
ANISOU 1458  CD  LYS E 319     5333  12526   7480   -665  -1946  -2152       C  
ATOM   1459  CE  LYS E 319      30.919  10.977  13.964  1.00 73.97           C  
ANISOU 1459  CE  LYS E 319     5638  13974   8494    -72  -2441  -2884       C  
ATOM   1460  NZ  LYS E 319      31.667  11.233  12.702  1.00 75.43           N  
ANISOU 1460  NZ  LYS E 319     4838  14376   9445   -854  -1876  -3269       N  
ATOM   1461  N   LYS E 320      25.478  10.175  12.479  1.00 44.59           N  
ANISOU 1461  N   LYS E 320     4188   8435   4318  -1196   -372   -146       N  
ATOM   1462  CA  LYS E 320      25.067   8.790  12.340  1.00 45.57           C  
ANISOU 1462  CA  LYS E 320     4658   8317   4338  -1015    -53    -53       C  
ATOM   1463  C   LYS E 320      24.476   8.509  10.919  1.00 44.66           C  
ANISOU 1463  C   LYS E 320     4132   8244   4593  -1284     94    -89       C  
ATOM   1464  O   LYS E 320      24.818   7.506  10.273  1.00 46.26           O  
ANISOU 1464  O   LYS E 320     4324   8486   4763  -1156    141    -62       O  
ATOM   1465  CB  LYS E 320      24.085   8.462  13.463  1.00 49.20           C  
ANISOU 1465  CB  LYS E 320     5855   8209   4628   -973    486    -34       C  
ATOM   1466  CG  LYS E 320      23.361   7.146  13.286  1.00 53.46           C  
ANISOU 1466  CG  LYS E 320     6807   8246   5257  -1087   1243    -98       C  
ATOM   1467  CD  LYS E 320      22.593   6.698  14.520  1.00 61.08           C  
ANISOU 1467  CD  LYS E 320     8848   8382   5975  -1095   2192   -135       C  
ATOM   1468  CE  LYS E 320      22.163   5.243  14.309  1.00 67.09           C  
ANISOU 1468  CE  LYS E 320    10216   8484   6790  -1267   3174   -271       C  
ATOM   1469  NZ  LYS E 320      21.721   4.568  15.552  1.00 75.45           N  
ANISOU 1469  NZ  LYS E 320    12934   8415   7318  -1162   4435   -228       N  
ATOM   1470  N   LEU E 321      23.631   9.410  10.411  1.00 41.62           N  
ANISOU 1470  N   LEU E 321     3501   7853   4460  -1473     43   -226       N  
ATOM   1471  CA  LEU E 321      23.108   9.264   9.058  1.00 41.03           C  
ANISOU 1471  CA  LEU E 321     3196   7831   4559  -1386    -80   -428       C  
ATOM   1472  C   LEU E 321      24.193   9.309   8.012  1.00 40.91           C  
ANISOU 1472  C   LEU E 321     3244   7979   4319  -1284   -208   -200       C  
ATOM   1473  O   LEU E 321      24.170   8.541   7.043  1.00 40.71           O  
ANISOU 1473  O   LEU E 321     3194   7976   4298  -1106   -244   -264       O  
ATOM   1474  CB  LEU E 321      22.057  10.331   8.734  1.00 41.87           C  
ANISOU 1474  CB  LEU E 321     3243   7900   4765  -1236   -328   -762       C  
ATOM   1475  CG  LEU E 321      20.755  10.219   9.520  1.00 44.15           C  
ANISOU 1475  CG  LEU E 321     3206   8058   5510  -1362   -103  -1301       C  
ATOM   1476  CD1 LEU E 321      19.873  11.396   9.171  1.00 47.13           C  
ANISOU 1476  CD1 LEU E 321     3496   8510   5899   -981   -566  -1739       C  
ATOM   1477  CD2 LEU E 321      20.047   8.906   9.210  1.00 46.89           C  
ANISOU 1477  CD2 LEU E 321     3122   8308   6385  -1493    230  -1894       C  
ATOM   1478  N   ASN E 322      25.121  10.243   8.178  1.00 42.12           N  
ANISOU 1478  N   ASN E 322     3470   8185   4345  -1453   -161    -53       N  
ATOM   1479  CA  ASN E 322      26.216  10.339   7.275  1.00 43.70           C  
ANISOU 1479  CA  ASN E 322     3696   8427   4480  -1540     55      0       C  
ATOM   1480  C   ASN E 322      27.031   9.046   7.211  1.00 42.75           C  
ANISOU 1480  C   ASN E 322     3237   8580   4424  -1421     28    -28       C  
ATOM   1481  O   ASN E 322      27.350   8.585   6.121  1.00 42.34           O  
ANISOU 1481  O   ASN E 322     3267   8510   4308  -1324    180     21       O  
ATOM   1482  CB  ASN E 322      27.124  11.478   7.666  1.00 48.26           C  
ANISOU 1482  CB  ASN E 322     4196   8970   5169  -1950    341   -137       C  
ATOM   1483  CG  ASN E 322      28.281  11.625   6.716  1.00 52.17           C  
ANISOU 1483  CG  ASN E 322     4662   9379   5781  -2245    935   -293       C  
ATOM   1484  OD1 ASN E 322      28.097  11.792   5.531  1.00 54.09           O  
ANISOU 1484  OD1 ASN E 322     5604   9225   5720  -2134   1317    -97       O  
ATOM   1485  ND2 ASN E 322      29.474  11.547   7.237  1.00 56.54           N  
ANISOU 1485  ND2 ASN E 322     4440  10274   6767  -2530   1029   -790       N  
ATOM   1486  N   ASP E 323      27.377   8.493   8.375  1.00 42.68           N  
ANISOU 1486  N   ASP E 323     3049   8757   4409  -1271   -187   -127       N  
ATOM   1487  CA  ASP E 323      28.158   7.253   8.441  1.00 45.13           C  
ANISOU 1487  CA  ASP E 323     3268   9282   4597   -891   -327   -215       C  
ATOM   1488  C   ASP E 323      27.396   6.053   7.861  1.00 43.25           C  
ANISOU 1488  C   ASP E 323     3379   8806   4246   -733   -183     -5       C  
ATOM   1489  O   ASP E 323      27.993   5.153   7.265  1.00 41.75           O  
ANISOU 1489  O   ASP E 323     3159   8736   3967   -498   -191     -7       O  
ATOM   1490  CB  ASP E 323      28.553   6.949   9.883  1.00 49.95           C  
ANISOU 1490  CB  ASP E 323     4073   9976   4926   -411   -689   -412       C  
ATOM   1491  CG  ASP E 323      29.470   8.013  10.487  1.00 55.16           C  
ANISOU 1491  CG  ASP E 323     4164  10986   5807   -469   -999   -935       C  
ATOM   1492  OD1 ASP E 323      29.941   8.895   9.765  1.00 57.13           O  
ANISOU 1492  OD1 ASP E 323     3845  11349   6511  -1040   -700  -1163       O  
ATOM   1493  OD2 ASP E 323      29.733   7.957  11.703  1.00 64.49           O  
ANISOU 1493  OD2 ASP E 323     5585  12240   6679     95  -1476  -1215       O  
ATOM   1494  N   SER E 324      26.086   6.022   8.090  1.00 42.58           N  
ANISOU 1494  N   SER E 324     3535   8385   4257   -886    -10     14       N  
ATOM   1495  CA  SER E 324      25.228   4.955   7.564  1.00 42.92           C  
ANISOU 1495  CA  SER E 324     3707   8160   4441   -900    236   -107       C  
ATOM   1496  C   SER E 324      25.125   4.992   6.059  1.00 40.95           C  
ANISOU 1496  C   SER E 324     3220   8044   4292   -825     37   -202       C  
ATOM   1497  O   SER E 324      25.178   3.958   5.411  1.00 42.81           O  
ANISOU 1497  O   SER E 324     3511   8230   4521   -690     93   -263       O  
ATOM   1498  CB  SER E 324      23.826   5.077   8.164  1.00 45.28           C  
ANISOU 1498  CB  SER E 324     4018   8102   5085  -1196    581   -434       C  
ATOM   1499  OG  SER E 324      23.796   4.397   9.380  1.00 50.30           O  
ANISOU 1499  OG  SER E 324     5317   8296   5497  -1193   1115   -349       O  
ATOM   1500  N   LEU E 325      24.977   6.185   5.486  1.00 41.19           N  
ANISOU 1500  N   LEU E 325     3221   8142   4287   -798   -169   -218       N  
ATOM   1501  CA  LEU E 325      24.951   6.333   4.015  1.00 40.74           C  
ANISOU 1501  CA  LEU E 325     3407   8045   4025   -456   -345   -275       C  
ATOM   1502  C   LEU E 325      26.289   5.967   3.391  1.00 41.31           C  
ANISOU 1502  C   LEU E 325     3604   8208   3881   -440    -88     22       C  
ATOM   1503  O   LEU E 325      26.358   5.290   2.359  1.00 39.76           O  
ANISOU 1503  O   LEU E 325     3613   7962   3530   -140   -129      0       O  
ATOM   1504  CB  LEU E 325      24.499   7.733   3.617  1.00 42.31           C  
ANISOU 1504  CB  LEU E 325     4036   8069   3968   -225   -512   -338       C  
ATOM   1505  CG  LEU E 325      23.008   8.009   3.944  1.00 43.76           C  
ANISOU 1505  CG  LEU E 325     3954   8251   4419     -5   -938   -923       C  
ATOM   1506  CD1 LEU E 325      22.731   9.501   3.865  1.00 45.91           C  
ANISOU 1506  CD1 LEU E 325     4806   8335   4301    303  -1110   -902       C  
ATOM   1507  CD2 LEU E 325      22.064   7.236   3.031  1.00 46.58           C  
ANISOU 1507  CD2 LEU E 325     4082   8658   4956    521  -1420  -1655       C  
ATOM   1508  N   GLU E 326      27.361   6.397   4.025  1.00 42.27           N  
ANISOU 1508  N   GLU E 326     3504   8490   4065   -736    164    135       N  
ATOM   1509  CA  GLU E 326      28.687   5.982   3.598  1.00 46.66           C  
ANISOU 1509  CA  GLU E 326     3849   9237   4640   -762    449    113       C  
ATOM   1510  C   GLU E 326      28.770   4.457   3.495  1.00 45.22           C  
ANISOU 1510  C   GLU E 326     3599   9196   4384   -419    242    133       C  
ATOM   1511  O   GLU E 326      29.148   3.932   2.460  1.00 45.12           O  
ANISOU 1511  O   GLU E 326     3730   9162   4251   -242    389    176       O  
ATOM   1512  CB  GLU E 326      29.745   6.496   4.566  1.00 52.01           C  
ANISOU 1512  CB  GLU E 326     3932  10221   5608  -1036    536   -189       C  
ATOM   1513  CG  GLU E 326      30.184   7.932   4.353  1.00 57.96           C  
ANISOU 1513  CG  GLU E 326     4707  10757   6557  -1562   1117   -368       C  
ATOM   1514  CD  GLU E 326      31.318   8.333   5.291  1.00 65.02           C  
ANISOU 1514  CD  GLU E 326     4689  12052   7962  -1853   1140  -1039       C  
ATOM   1515  OE1 GLU E 326      31.632   7.578   6.244  1.00 65.81           O  
ANISOU 1515  OE1 GLU E 326     4315  12617   8071  -1391    456  -1313       O  
ATOM   1516  OE2 GLU E 326      31.924   9.397   5.052  1.00 73.63           O  
ANISOU 1516  OE2 GLU E 326     5630  12925   9420  -2473   1883  -1429       O  
ATOM   1517  N   LEU E 327      28.398   3.755   4.576  1.00 43.88           N  
ANISOU 1517  N   LEU E 327     3440   9034   4197   -295     25    113       N  
ATOM   1518  CA  LEU E 327      28.426   2.288   4.594  1.00 43.21           C  
ANISOU 1518  CA  LEU E 327     3629   8863   3925     42      9    139       C  
ATOM   1519  C   LEU E 327      27.596   1.665   3.467  1.00 41.88           C  
ANISOU 1519  C   LEU E 327     3638   8450   3823     37     76    105       C  
ATOM   1520  O   LEU E 327      28.068   0.812   2.695  1.00 42.59           O  
ANISOU 1520  O   LEU E 327     3841   8576   3765    293     92    143       O  
ATOM   1521  CB  LEU E 327      27.961   1.770   5.967  1.00 45.04           C  
ANISOU 1521  CB  LEU E 327     4344   8793   3974    164     85    140       C  
ATOM   1522  CG  LEU E 327      28.274   0.297   6.193  1.00 48.01           C  
ANISOU 1522  CG  LEU E 327     5408   8909   3923    659    215    185       C  
ATOM   1523  CD1 LEU E 327      29.768   0.019   6.006  1.00 51.02           C  
ANISOU 1523  CD1 LEU E 327     5539   9813   4033   1287   -222     65       C  
ATOM   1524  CD2 LEU E 327      27.786  -0.130   7.555  1.00 51.31           C  
ANISOU 1524  CD2 LEU E 327     6809   8730   3955    845    572    226       C  
ATOM   1525  N   SER E 328      26.360   2.124   3.331  1.00 41.13           N  
ANISOU 1525  N   SER E 328     3495   8153   3979   -157     22   -124       N  
ATOM   1526  CA  SER E 328      25.533   1.709   2.217  1.00 41.37           C  
ANISOU 1526  CA  SER E 328     3524   8054   4139     11   -161   -490       C  
ATOM   1527  C   SER E 328      26.166   1.895   0.856  1.00 41.34           C  
ANISOU 1527  C   SER E 328     3805   8137   3763    422   -329   -323       C  
ATOM   1528  O   SER E 328      25.961   1.070  -0.033  1.00 43.02           O  
ANISOU 1528  O   SER E 328     4157   8270   3917    722   -479   -531       O  
ATOM   1529  CB  SER E 328      24.207   2.454   2.243  1.00 43.81           C  
ANISOU 1529  CB  SER E 328     3566   8289   4791    -28   -422  -1045       C  
ATOM   1530  OG  SER E 328      23.594   2.150   3.458  1.00 45.54           O  
ANISOU 1530  OG  SER E 328     3584   8304   5415   -500      0  -1269       O  
ATOM   1531  N   ASP E 329      26.920   2.968   0.662  1.00 40.94           N  
ANISOU 1531  N   ASP E 329     3958   8136   3461    411   -161    -18       N  
ATOM   1532  CA  ASP E 329      27.551   3.164  -0.632  1.00 44.34           C  
ANISOU 1532  CA  ASP E 329     4965   8412   3469    745     44    141       C  
ATOM   1533  C   ASP E 329      28.697   2.202  -0.953  1.00 43.53           C  
ANISOU 1533  C   ASP E 329     4726   8476   3337    751    364    297       C  
ATOM   1534  O   ASP E 329      28.976   1.979  -2.118  1.00 44.28           O  
ANISOU 1534  O   ASP E 329     5360   8377   3088   1103    528    361       O  
ATOM   1535  CB  ASP E 329      28.027   4.594  -0.827  1.00 49.55           C  
ANISOU 1535  CB  ASP E 329     6124   8816   3887    603    530    321       C  
ATOM   1536  CG  ASP E 329      27.131   5.348  -1.721  1.00 55.77           C  
ANISOU 1536  CG  ASP E 329     7931   9151   4107   1258    254    217       C  
ATOM   1537  OD1 ASP E 329      26.011   5.687  -1.264  1.00 59.53           O  
ANISOU 1537  OD1 ASP E 329     8215   9699   4705   1451   -365   -105       O  
ATOM   1538  OD2 ASP E 329      27.509   5.586  -2.874  1.00 63.55           O  
ANISOU 1538  OD2 ASP E 329    10008   9670   4467   1707    644    366       O  
ATOM   1539  N   VAL E 330      29.367   1.667   0.055  1.00 40.99           N  
ANISOU 1539  N   VAL E 330     3825   8479   3269    532    409    295       N  
ATOM   1540  CA  VAL E 330      30.532   0.811  -0.222  1.00 43.93           C  
ANISOU 1540  CA  VAL E 330     4006   9091   3591    723    599    278       C  
ATOM   1541  C   VAL E 330      30.265  -0.701  -0.029  1.00 44.32           C  
ANISOU 1541  C   VAL E 330     4213   9121   3504   1069    303    286       C  
ATOM   1542  O   VAL E 330      31.077  -1.511  -0.422  1.00 47.03           O  
ANISOU 1542  O   VAL E 330     4559   9613   3695   1390    367    271       O  
ATOM   1543  CB  VAL E 330      31.777   1.260   0.575  1.00 45.84           C  
ANISOU 1543  CB  VAL E 330     3533   9753   4131    541    786    -17       C  
ATOM   1544  CG1 VAL E 330      32.224   2.650   0.150  1.00 48.92           C  
ANISOU 1544  CG1 VAL E 330     3848   9989   4751     26   1467   -154       C  
ATOM   1545  CG2 VAL E 330      31.510   1.225   2.049  1.00 44.00           C  
ANISOU 1545  CG2 VAL E 330     3098   9677   3942    604    328   -110       C  
ATOM   1546  N   VAL E 331      29.123  -1.077   0.547  1.00 44.74           N  
ANISOU 1546  N   VAL E 331     4457   8901   3641    959    138    224       N  
ATOM   1547  CA  VAL E 331      28.725  -2.478   0.618  1.00 46.24           C  
ANISOU 1547  CA  VAL E 331     5031   8795   3741   1115    193    143       C  
ATOM   1548  C   VAL E 331      27.860  -2.901  -0.587  1.00 48.13           C  
ANISOU 1548  C   VAL E 331     5377   8803   4107   1154     73   -142       C  
ATOM   1549  O   VAL E 331      26.810  -2.346  -0.832  1.00 50.02           O  
ANISOU 1549  O   VAL E 331     5422   8941   4641   1011   -134   -521       O  
ATOM   1550  CB  VAL E 331      27.955  -2.773   1.908  1.00 47.21           C  
ANISOU 1550  CB  VAL E 331     5436   8529   3971    854    446     33       C  
ATOM   1551  CG1 VAL E 331      27.525  -4.236   1.945  1.00 51.01           C  
ANISOU 1551  CG1 VAL E 331     6578   8436   4366    875    872   -121       C  
ATOM   1552  CG2 VAL E 331      28.784  -2.426   3.139  1.00 48.55           C  
ANISOU 1552  CG2 VAL E 331     5722   8889   3836   1108    373    217       C  
ATOM   1553  N   PRO E 332      28.278  -3.930  -1.323  1.00 42.14           N  
ANISOU 1553  N   PRO E 332     4483   5061   6467    389  -1214    394       N  
ATOM   1554  CA  PRO E 332      27.448  -4.444  -2.421  1.00 42.53           C  
ANISOU 1554  CA  PRO E 332     4934   5000   6222    599  -1180    319       C  
ATOM   1555  C   PRO E 332      26.077  -4.924  -1.937  1.00 41.71           C  
ANISOU 1555  C   PRO E 332     4706   5305   5835    461  -1579    262       C  
ATOM   1556  O   PRO E 332      26.000  -5.517  -0.876  1.00 42.05           O  
ANISOU 1556  O   PRO E 332     4506   5449   6019    250  -1725    352       O  
ATOM   1557  CB  PRO E 332      28.250  -5.655  -2.943  1.00 45.21           C  
ANISOU 1557  CB  PRO E 332     5385   4979   6813    669   -921    420       C  
ATOM   1558  CG  PRO E 332      29.614  -5.550  -2.354  1.00 47.10           C  
ANISOU 1558  CG  PRO E 332     5081   5263   7550    718   -747    646       C  
ATOM   1559  CD  PRO E 332      29.545  -4.658  -1.156  1.00 44.93           C  
ANISOU 1559  CD  PRO E 332     4401   5409   7260    404  -1122    592       C  
ATOM   1560  N   ALA E 333      25.020  -4.673  -2.701  1.00 43.64           N  
ANISOU 1560  N   ALA E 333     5058   5872   5649    597  -1733    149       N  
ATOM   1561  CA  ALA E 333      23.677  -5.135  -2.347  1.00 47.12           C  
ANISOU 1561  CA  ALA E 333     5093   6933   5875    348  -2086     83       C  
ATOM   1562  C   ALA E 333      23.674  -6.623  -1.989  1.00 49.72           C  
ANISOU 1562  C   ALA E 333     5461   7037   6392   -276  -2084    -16       C  
ATOM   1563  O   ALA E 333      23.027  -7.022  -1.055  1.00 54.10           O  
ANISOU 1563  O   ALA E 333     5704   7831   7020   -599  -2125     19       O  
ATOM   1564  CB  ALA E 333      22.682  -4.880  -3.488  1.00 50.51           C  
ANISOU 1564  CB  ALA E 333     5462   7981   5746    553  -2390    -30       C  
ATOM   1565  N   SER E 334      24.382  -7.444  -2.750  1.00 52.16           N  
ANISOU 1565  N   SER E 334     6329   6765   6722   -394  -1867   -114       N  
ATOM   1566  CA  SER E 334      24.447  -8.867  -2.453  1.00 55.75           C  
ANISOU 1566  CA  SER E 334     7184   6735   7262   -871  -1620   -166       C  
ATOM   1567  C   SER E 334      24.975  -9.133  -1.034  1.00 53.30           C  
ANISOU 1567  C   SER E 334     6715   6232   7302   -685  -1449    189       C  
ATOM   1568  O   SER E 334      24.426  -9.976  -0.332  1.00 54.25           O  
ANISOU 1568  O   SER E 334     6993   6229   7390  -1095  -1304    198       O  
ATOM   1569  CB  SER E 334      25.324  -9.600  -3.451  1.00 59.29           C  
ANISOU 1569  CB  SER E 334     8482   6397   7645   -749  -1176   -221       C  
ATOM   1570  OG  SER E 334      25.078 -10.998  -3.330  1.00 68.17           O  
ANISOU 1570  OG  SER E 334    10314   6940   8647  -1301   -815   -357       O  
ATOM   1571  N   ASP E 335      26.015  -8.395  -0.633  1.00 49.60           N  
ANISOU 1571  N   ASP E 335     5968   5788   7089   -143  -1465    456       N  
ATOM   1572  CA  ASP E 335      26.584  -8.510   0.707  1.00 51.05           C  
ANISOU 1572  CA  ASP E 335     5936   6030   7427     77  -1512    786       C  
ATOM   1573  C   ASP E 335      25.598  -8.003   1.733  1.00 49.85           C  
ANISOU 1573  C   ASP E 335     5542   6303   7094   -165  -1748    745       C  
ATOM   1574  O   ASP E 335      25.436  -8.602   2.789  1.00 55.06           O  
ANISOU 1574  O   ASP E 335     6355   6894   7670   -198  -1677    943       O  
ATOM   1575  CB  ASP E 335      27.903  -7.733   0.845  1.00 50.74           C  
ANISOU 1575  CB  ASP E 335     5467   6173   7637    455  -1606    966       C  
ATOM   1576  CG  ASP E 335      29.089  -8.470   0.270  1.00 55.85           C  
ANISOU 1576  CG  ASP E 335     6165   6500   8552    917  -1227   1234       C  
ATOM   1577  OD1 ASP E 335      28.911  -9.586  -0.249  1.00 59.12           O  
ANISOU 1577  OD1 ASP E 335     7231   6348   8883   1021   -809   1277       O  
ATOM   1578  OD2 ASP E 335      30.221  -7.938   0.359  1.00 60.13           O  
ANISOU 1578  OD2 ASP E 335     6103   7366   9376   1147  -1268   1404       O  
ATOM   1579  N   ALA E 336      24.933  -6.909   1.420  1.00 47.86           N  
ANISOU 1579  N   ALA E 336     5035   6431   6719   -199  -1899    557       N  
ATOM   1580  CA  ALA E 336      23.884  -6.370   2.288  1.00 49.69           C  
ANISOU 1580  CA  ALA E 336     5061   7062   6756   -266  -1934    569       C  
ATOM   1581  C   ALA E 336      22.825  -7.395   2.651  1.00 54.22           C  
ANISOU 1581  C   ALA E 336     5571   7737   7293   -714  -1770    556       C  
ATOM   1582  O   ALA E 336      22.519  -7.567   3.820  1.00 54.76           O  
ANISOU 1582  O   ALA E 336     5718   7798   7287   -764  -1597    723       O  
ATOM   1583  CB  ALA E 336      23.216  -5.171   1.651  1.00 48.28           C  
ANISOU 1583  CB  ALA E 336     4693   7261   6388     11  -1960    469       C  
ATOM   1584  N   GLU E 337      22.261  -8.061   1.655  1.00 58.91           N  
ANISOU 1584  N   GLU E 337     6099   8413   7871  -1149  -1775    316       N  
ATOM   1585  CA  GLU E 337      21.203  -9.034   1.911  1.00 66.10           C  
ANISOU 1585  CA  GLU E 337     6902   9455   8757  -1909  -1549    183       C  
ATOM   1586  C   GLU E 337      21.721 -10.217   2.703  1.00 66.40           C  
ANISOU 1586  C   GLU E 337     7712   8659   8857  -2102  -1077    358       C  
ATOM   1587  O   GLU E 337      20.972 -10.809   3.466  1.00 70.45           O  
ANISOU 1587  O   GLU E 337     8294   9121   9352  -2598   -678    391       O  
ATOM   1588  CB  GLU E 337      20.533  -9.514   0.616  1.00 73.41           C  
ANISOU 1588  CB  GLU E 337     7659  10714   9517  -2586  -1752   -238       C  
ATOM   1589  CG  GLU E 337      19.588  -8.508  -0.036  1.00 79.45           C  
ANISOU 1589  CG  GLU E 337     7486  12632  10067  -2369  -2232   -320       C  
ATOM   1590  CD  GLU E 337      18.810  -7.660   0.970  1.00 82.15           C  
ANISOU 1590  CD  GLU E 337     7082  13640  10489  -1923  -2097     -5       C  
ATOM   1591  OE1 GLU E 337      19.436  -6.752   1.580  1.00 78.82           O  
ANISOU 1591  OE1 GLU E 337     6975  12877  10095  -1123  -1960    279       O  
ATOM   1592  OE2 GLU E 337      17.590  -7.896   1.152  1.00 88.55           O  
ANISOU 1592  OE2 GLU E 337     7019  15315  11311  -2426  -2060    -62       O  
ATOM   1593  N   LYS E 338      22.992 -10.562   2.527  1.00 63.27           N  
ANISOU 1593  N   LYS E 338     7899   7630   8508  -1615  -1017    538       N  
ATOM   1594  CA  LYS E 338      23.592 -11.608   3.345  1.00 66.97           C  
ANISOU 1594  CA  LYS E 338     9150   7367   8926  -1391   -545    889       C  
ATOM   1595  C   LYS E 338      23.647 -11.192   4.816  1.00 64.78           C  
ANISOU 1595  C   LYS E 338     8778   7322   8512   -979   -621   1251       C  
ATOM   1596  O   LYS E 338      23.342 -11.984   5.689  1.00 69.18           O  
ANISOU 1596  O   LYS E 338     9927   7469   8887  -1076   -135   1473       O  
ATOM   1597  CB  LYS E 338      24.978 -11.995   2.835  1.00 68.45           C  
ANISOU 1597  CB  LYS E 338     9763   7053   9189   -686   -447   1136       C  
ATOM   1598  CG  LYS E 338      24.913 -12.872   1.605  1.00 73.08           C  
ANISOU 1598  CG  LYS E 338    11064   6980   9722  -1100     -9    837       C  
ATOM   1599  CD  LYS E 338      26.200 -13.631   1.356  1.00 77.54           C  
ANISOU 1599  CD  LYS E 338    12358   6792  10312   -234    505   1251       C  
ATOM   1600  CE  LYS E 338      26.198 -14.158  -0.067  1.00 81.88           C  
ANISOU 1600  CE  LYS E 338    13674   6707  10730   -603    911    861       C  
ATOM   1601  NZ  LYS E 338      27.134 -15.299  -0.233  1.00 91.06           N  
ANISOU 1601  NZ  LYS E 338    16023   6780  11793    156   1847   1274       N  
ATOM   1602  N   TYR E 339      24.016  -9.943   5.087  1.00 58.71           N  
ANISOU 1602  N   TYR E 339     7459   7114   7731   -583  -1141   1277       N  
ATOM   1603  CA  TYR E 339      23.994  -9.446   6.455  1.00 58.14           C  
ANISOU 1603  CA  TYR E 339     7472   7259   7358   -325  -1240   1503       C  
ATOM   1604  C   TYR E 339      22.553  -9.312   6.988  1.00 61.44           C  
ANISOU 1604  C   TYR E 339     7806   7854   7683   -760   -842   1409       C  
ATOM   1605  O   TYR E 339      22.298  -9.727   8.116  1.00 63.64           O  
ANISOU 1605  O   TYR E 339     8596   7909   7676   -707   -480   1663       O  
ATOM   1606  CB  TYR E 339      24.726  -8.121   6.585  1.00 53.68           C  
ANISOU 1606  CB  TYR E 339     6551   7129   6714    -39  -1786   1428       C  
ATOM   1607  CG  TYR E 339      26.241  -8.169   6.471  1.00 54.89           C  
ANISOU 1607  CG  TYR E 339     6552   7369   6934    352  -2181   1600       C  
ATOM   1608  CD1 TYR E 339      27.010  -8.756   7.449  1.00 60.63           C  
ANISOU 1608  CD1 TYR E 339     7507   8182   7345    807  -2371   2010       C  
ATOM   1609  CD2 TYR E 339      26.901  -7.563   5.402  1.00 52.56           C  
ANISOU 1609  CD2 TYR E 339     5806   7189   6975    328  -2338   1402       C  
ATOM   1610  CE1 TYR E 339      28.403  -8.778   7.363  1.00 65.21           C  
ANISOU 1610  CE1 TYR E 339     7611   9162   8002   1242  -2793   2239       C  
ATOM   1611  CE2 TYR E 339      28.287  -7.582   5.304  1.00 56.22           C  
ANISOU 1611  CE2 TYR E 339     5877   7892   7589    631  -2604   1585       C  
ATOM   1612  CZ  TYR E 339      29.033  -8.174   6.287  1.00 61.70           C  
ANISOU 1612  CZ  TYR E 339     6537   8881   8024   1083  -2880   2005       C  
ATOM   1613  OH  TYR E 339      30.404  -8.192   6.193  1.00 68.34           O  
ANISOU 1613  OH  TYR E 339     6673  10257   9034   1455  -3196   2254       O  
ATOM   1614  N   ARG E 340      21.633  -8.743   6.192  1.00 60.98           N  
ANISOU 1614  N   ARG E 340     7080   8269   7819  -1079   -865   1117       N  
ATOM   1615  CA  ARG E 340      20.205  -8.570   6.588  1.00 67.58           C  
ANISOU 1615  CA  ARG E 340     7466   9557   8653  -1402   -448   1092       C  
ATOM   1616  C   ARG E 340      19.502  -9.888   6.923  1.00 75.41           C  
ANISOU 1616  C   ARG E 340     8690  10237   9725  -2160    191   1098       C  
ATOM   1617  O   ARG E 340      18.598  -9.925   7.764  1.00 78.51           O  
ANISOU 1617  O   ARG E 340     8965  10791  10074  -2364    760   1229       O  
ATOM   1618  CB  ARG E 340      19.371  -7.831   5.511  1.00 68.34           C  
ANISOU 1618  CB  ARG E 340     6607  10468   8892  -1446   -684    867       C  
ATOM   1619  CG  ARG E 340      19.627  -6.323   5.443  1.00 66.14           C  
ANISOU 1619  CG  ARG E 340     6268  10427   8432   -640   -909    942       C  
ATOM   1620  CD  ARG E 340      18.636  -5.559   4.566  1.00 69.70           C  
ANISOU 1620  CD  ARG E 340     5871  11745   8867   -332   -985    919       C  
ATOM   1621  NE  ARG E 340      19.299  -4.463   3.824  1.00 67.79           N  
ANISOU 1621  NE  ARG E 340     5924  11377   8457    316  -1247    894       N  
ATOM   1622  CZ  ARG E 340      19.381  -3.174   4.194  1.00 64.97           C  
ANISOU 1622  CZ  ARG E 340     5996  10865   7825   1038   -967   1049       C  
ATOM   1623  NH1 ARG E 340      18.854  -2.725   5.318  1.00 68.20           N  
ANISOU 1623  NH1 ARG E 340     6625  11248   8039   1336   -446   1252       N  
ATOM   1624  NH2 ARG E 340      20.011  -2.311   3.413  1.00 63.27           N  
ANISOU 1624  NH2 ARG E 340     6193  10380   7466   1443  -1063    986       N  
ATOM   1625  N   GLN E 341      19.909 -10.964   6.264  1.00 79.61           N  
ANISOU 1625  N   GLN E 341     9685  10215  10347  -2605    267    953       N  
ATOM   1626  CA  GLN E 341      19.253 -12.244   6.473  1.00 91.46           C  
ANISOU 1626  CA  GLN E 341    11667  11205  11876  -3532   1043    866       C  
ATOM   1627  C   GLN E 341      19.810 -12.951   7.712  1.00 97.99           C  
ANISOU 1627  C   GLN E 341    13729  11106  12396  -3077   1653   1345       C  
ATOM   1628  O   GLN E 341      19.051 -13.528   8.508  1.00106.81           O  
ANISOU 1628  O   GLN E 341    15239  11908  13435  -3582   2491   1453       O  
ATOM   1629  CB  GLN E 341      19.342 -13.135   5.214  1.00 94.81           C  
ANISOU 1629  CB  GLN E 341    12394  11253  12375  -4319   1053    439       C  
ATOM   1630  CG  GLN E 341      20.705 -13.751   4.915  1.00 92.69           C  
ANISOU 1630  CG  GLN E 341    13255   9993  11970  -3668   1110    639       C  
ATOM   1631  CD  GLN E 341      20.650 -14.862   3.877  1.00100.29           C  
ANISOU 1631  CD  GLN E 341    15023  10221  12859  -4556   1533    219       C  
ATOM   1632  OE1 GLN E 341      19.627 -15.532   3.707  1.00108.95           O  
ANISOU 1632  OE1 GLN E 341    16211  11248  13933  -5917   1999   -215       O  
ATOM   1633  NE2 GLN E 341      21.766 -15.077   3.190  1.00 98.02           N  
ANISOU 1633  NE2 GLN E 341    15379   9362  12500  -3863   1461    326       N  
ATOM   1634  N   LYS E 342      21.128 -12.886   7.884  1.00 96.28           N  
ANISOU 1634  N   LYS E 342    14066  10553  11963  -2081   1254   1673       N  
ATOM   1635  CA  LYS E 342      21.805 -13.685   8.906  1.00103.02           C  
ANISOU 1635  CA  LYS E 342    16129  10632  12379  -1412   1708   2222       C  
ATOM   1636  C   LYS E 342      21.781 -13.067  10.308  1.00103.49           C  
ANISOU 1636  C   LYS E 342    16369  10973  11976   -825   1621   2579       C  
ATOM   1637  O   LYS E 342      21.815 -13.801  11.294  1.00108.47           O  
ANISOU 1637  O   LYS E 342    18088  10987  12137   -498   2247   3013       O  
ATOM   1638  CB  LYS E 342      23.238 -14.026   8.463  1.00102.64           C  
ANISOU 1638  CB  LYS E 342    16448  10293  12256   -502   1345   2510       C  
ATOM   1639  CG  LYS E 342      23.320 -15.370   7.744  1.00110.22           C  
ANISOU 1639  CG  LYS E 342    18417  10196  13265   -796   2172   2487       C  
ATOM   1640  CD  LYS E 342      23.244 -16.536   8.736  1.00121.43           C  
ANISOU 1640  CD  LYS E 342    21370  10562  14206   -513   3242   2998       C  
ATOM   1641  CE  LYS E 342      22.342 -17.673   8.265  1.00130.23           C  
ANISOU 1641  CE  LYS E 342    23498  10590  15391  -1818   4445   2612       C  
ATOM   1642  NZ  LYS E 342      22.688 -18.150   6.899  1.00130.98           N  
ANISOU 1642  NZ  LYS E 342    23892  10202  15670  -2173   4545   2231       N  
ATOM   1643  N   PHE E 343      21.697 -11.735  10.392  1.00 97.72           N  
ANISOU 1643  N   PHE E 343    14808  11053  11269   -681    964   2395       N  
ATOM   1644  CA  PHE E 343      21.670 -11.028  11.680  1.00100.37           C  
ANISOU 1644  CA  PHE E 343    15506  11597  11030   -217    892   2620       C  
ATOM   1645  C   PHE E 343      20.291 -10.414  12.005  1.00100.65           C  
ANISOU 1645  C   PHE E 343    15141  11923  11177   -668   1488   2455       C  
ATOM   1646  O   PHE E 343      20.211  -9.408  12.706  1.00 99.49           O  
ANISOU 1646  O   PHE E 343    15112  12051  10638   -305   1362   2477       O  
ATOM   1647  CB  PHE E 343      22.767  -9.939  11.720  1.00 97.29           C  
ANISOU 1647  CB  PHE E 343    14809  11760  10394    313   -156   2552       C  
ATOM   1648  CG  PHE E 343      24.174 -10.463  11.978  1.00102.53           C  
ANISOU 1648  CG  PHE E 343    15826  12424  10705   1011   -727   2920       C  
ATOM   1649  CD1 PHE E 343      24.492 -11.113  13.179  1.00112.57           C  
ANISOU 1649  CD1 PHE E 343    18099  13466  11204   1636   -591   3442       C  
ATOM   1650  CD2 PHE E 343      25.195 -10.266  11.039  1.00 98.14           C  
ANISOU 1650  CD2 PHE E 343    14552  12206  10529   1171  -1374   2817       C  
ATOM   1651  CE1 PHE E 343      25.784 -11.579  13.421  1.00117.93           C  
ANISOU 1651  CE1 PHE E 343    18907  14414  11487   2508  -1193   3900       C  
ATOM   1652  CE2 PHE E 343      26.484 -10.724  11.279  1.00103.76           C  
ANISOU 1652  CE2 PHE E 343    15296  13164  10964   1936  -1868   3244       C  
ATOM   1653  CZ  PHE E 343      26.779 -11.384  12.470  1.00114.59           C  
ANISOU 1653  CZ  PHE E 343    17514  14472  11550   2660  -1838   3810       C  
ATOM   1654  N   MET E 344      19.208 -11.033  11.532  1.00104.57           N  
ANISOU 1654  N   MET E 344    15191  12387  12152  -1477   2205   2296       N  
ATOM   1655  CA  MET E 344      17.859 -10.491  11.745  1.00107.95           C  
ANISOU 1655  CA  MET E 344    14858  13363  12794  -1836   2811   2216       C  
ATOM   1656  C   MET E 344      16.797 -11.556  11.460  1.00115.09           C  
ANISOU 1656  C   MET E 344    15395  14191  14142  -2975   3703   2077       C  
ATOM   1657  O   MET E 344      15.744 -11.277  10.888  1.00116.09           O  
ANISOU 1657  O   MET E 344    14194  15184  14728  -3570   3842   1838       O  
ATOM   1658  CB  MET E 344      17.650  -9.253  10.854  1.00102.80           C  
ANISOU 1658  CB  MET E 344    13029  13604  12425  -1609   2154   1953       C  
ATOM   1659  CG  MET E 344      16.580  -8.277  11.325  1.00107.35           C  
ANISOU 1659  CG  MET E 344    13031  14784  12972  -1283   2697   2080       C  
ATOM   1660  SD  MET E 344      16.948  -6.566  10.857  1.00102.93           S  
ANISOU 1660  SD  MET E 344    12230  14657  12221   -366   2044   1993       S  
ATOM   1661  CE  MET E 344      17.564  -5.884  12.397  1.00102.50           C  
ANISOU 1661  CE  MET E 344    13765  13892  11285    257   2279   2177       C  
TER    1662      MET E 344                                                      
ATOM   1663  N   GLU F 303      26.415  26.774  20.108  1.00 75.25           N  
ANISOU 1663  N   GLU F 303     9911  10358   8319   -969   -253  -1381       N  
ATOM   1664  CA  GLU F 303      26.188  25.308  20.220  1.00 72.04           C  
ANISOU 1664  CA  GLU F 303     9099  10311   7961   -893   -482  -1196       C  
ATOM   1665  C   GLU F 303      26.327  24.676  18.814  1.00 69.55           C  
ANISOU 1665  C   GLU F 303     8291  10146   7988   -908   -551  -1039       C  
ATOM   1666  O   GLU F 303      25.535  23.836  18.394  1.00 68.50           O  
ANISOU 1666  O   GLU F 303     7882  10233   7909   -820   -453   -886       O  
ATOM   1667  CB  GLU F 303      24.813  25.049  20.858  1.00 74.59           C  
ANISOU 1667  CB  GLU F 303     9526  10735   8078   -683   -120  -1107       C  
ATOM   1668  CG  GLU F 303      23.659  25.859  20.250  1.00 77.34           C  
ANISOU 1668  CG  GLU F 303     9679  11224   8483   -259    217  -1129       C  
ATOM   1669  CD  GLU F 303      22.280  25.442  20.767  1.00 80.03           C  
ANISOU 1669  CD  GLU F 303     9699  11998   8709   -148    631  -1292       C  
ATOM   1670  OE1 GLU F 303      22.077  25.434  21.998  1.00 82.18           O  
ANISOU 1670  OE1 GLU F 303    10405  12114   8705   -299    898  -1379       O  
ATOM   1671  OE2 GLU F 303      21.392  25.137  19.937  1.00 80.56           O  
ANISOU 1671  OE2 GLU F 303     9045  12637   8925     47    726  -1444       O  
ATOM   1672  N   ILE F 304      27.371  25.082  18.101  1.00 68.01           N  
ANISOU 1672  N   ILE F 304     8005   9842   7992  -1151   -635  -1188       N  
ATOM   1673  CA  ILE F 304      27.487  24.844  16.673  1.00 66.28           C  
ANISOU 1673  CA  ILE F 304     7546   9610   8025  -1159   -562  -1057       C  
ATOM   1674  C   ILE F 304      28.608  23.862  16.351  1.00 65.46           C  
ANISOU 1674  C   ILE F 304     6987   9747   8138  -1368   -853  -1169       C  
ATOM   1675  O   ILE F 304      29.693  23.887  16.944  1.00 69.04           O  
ANISOU 1675  O   ILE F 304     7235  10403   8591  -1554  -1100  -1552       O  
ATOM   1676  CB  ILE F 304      27.690  26.175  15.926  1.00 69.83           C  
ANISOU 1676  CB  ILE F 304     8544   9568   8417  -1255   -159  -1153       C  
ATOM   1677  CG1 ILE F 304      26.411  27.021  16.037  1.00 73.05           C  
ANISOU 1677  CG1 ILE F 304     9498   9770   8484   -619     69   -981       C  
ATOM   1678  CG2 ILE F 304      28.051  25.930  14.474  1.00 69.90           C  
ANISOU 1678  CG2 ILE F 304     8505   9465   8588  -1325    -37  -1060       C  
ATOM   1679  CD1 ILE F 304      26.625  28.368  16.694  1.00 78.30           C  
ANISOU 1679  CD1 ILE F 304    11046   9856   8846   -745    453  -1188       C  
ATOM   1680  N   PHE F 305      28.301  22.982  15.411  1.00 61.89           N  
ANISOU 1680  N   PHE F 305     6329   9373   7814  -1253   -854   -924       N  
ATOM   1681  CA  PHE F 305      29.208  21.967  14.947  1.00 61.66           C  
ANISOU 1681  CA  PHE F 305     5978   9510   7940  -1282  -1054   -973       C  
ATOM   1682  C   PHE F 305      29.253  22.075  13.428  1.00 61.98           C  
ANISOU 1682  C   PHE F 305     5960   9401   8188  -1413   -801   -883       C  
ATOM   1683  O   PHE F 305      28.341  22.636  12.793  1.00 64.76           O  
ANISOU 1683  O   PHE F 305     6583   9583   8437  -1285   -600   -707       O  
ATOM   1684  CB  PHE F 305      28.720  20.579  15.388  1.00 60.29           C  
ANISOU 1684  CB  PHE F 305     5981   9385   7540  -1038  -1175   -740       C  
ATOM   1685  CG  PHE F 305      28.532  20.441  16.881  1.00 63.95           C  
ANISOU 1685  CG  PHE F 305     6866   9820   7611   -849  -1302   -767       C  
ATOM   1686  CD1 PHE F 305      27.406  20.968  17.513  1.00 63.58           C  
ANISOU 1686  CD1 PHE F 305     7049   9691   7415   -955  -1018   -710       C  
ATOM   1687  CD2 PHE F 305      29.478  19.774  17.654  1.00 68.46           C  
ANISOU 1687  CD2 PHE F 305     7667  10483   7862   -419  -1717   -897       C  
ATOM   1688  CE1 PHE F 305      27.246  20.848  18.882  1.00 67.97           C  
ANISOU 1688  CE1 PHE F 305     8150  10130   7544   -825  -1032   -739       C  
ATOM   1689  CE2 PHE F 305      29.317  19.646  19.025  1.00 72.97           C  
ANISOU 1689  CE2 PHE F 305     8888  10943   7895   -124  -1852   -905       C  
ATOM   1690  CZ  PHE F 305      28.203  20.187  19.639  1.00 71.57           C  
ANISOU 1690  CZ  PHE F 305     9032  10556   7604   -421  -1451   -803       C  
ATOM   1691  N   THR F 306      30.330  21.565  12.851  1.00 63.82           N  
ANISOU 1691  N   THR F 306     5878   9743   8625  -1537   -832  -1063       N  
ATOM   1692  CA  THR F 306      30.433  21.402  11.416  1.00 63.06           C  
ANISOU 1692  CA  THR F 306     5832   9465   8660  -1652   -563   -960       C  
ATOM   1693  C   THR F 306      30.611  19.901  11.152  1.00 61.58           C  
ANISOU 1693  C   THR F 306     5466   9441   8490  -1418   -762   -824       C  
ATOM   1694  O   THR F 306      31.354  19.194  11.860  1.00 58.01           O  
ANISOU 1694  O   THR F 306     4804   9236   8001  -1144  -1047   -990       O  
ATOM   1695  CB  THR F 306      31.593  22.221  10.782  1.00 70.04           C  
ANISOU 1695  CB  THR F 306     6654  10211   9745  -2160   -130  -1393       C  
ATOM   1696  OG1 THR F 306      32.841  21.800  11.343  1.00 69.30           O  
ANISOU 1696  OG1 THR F 306     5800  10667   9864  -2256   -344  -1933       O  
ATOM   1697  CG2 THR F 306      31.397  23.750  10.979  1.00 72.09           C  
ANISOU 1697  CG2 THR F 306     7540  10020   9828  -2488    296  -1534       C  
ATOM   1698  N   LEU F 307      29.884  19.432  10.145  1.00 58.28           N  
ANISOU 1698  N   LEU F 307     5262   8877   8005  -1421   -629   -564       N  
ATOM   1699  CA  LEU F 307      29.891  18.038   9.752  1.00 58.11           C  
ANISOU 1699  CA  LEU F 307     5328   8838   7912  -1330   -653   -440       C  
ATOM   1700  C   LEU F 307      30.646  17.914   8.441  1.00 58.79           C  
ANISOU 1700  C   LEU F 307     5374   8798   8163  -1426   -427   -504       C  
ATOM   1701  O   LEU F 307      30.365  18.665   7.491  1.00 58.13           O  
ANISOU 1701  O   LEU F 307     5491   8540   8056  -1585   -211   -467       O  
ATOM   1702  CB  LEU F 307      28.456  17.578   9.533  1.00 57.25           C  
ANISOU 1702  CB  LEU F 307     5408   8769   7573  -1473   -591   -299       C  
ATOM   1703  CG  LEU F 307      28.242  16.085   9.295  1.00 60.13           C  
ANISOU 1703  CG  LEU F 307     6115   8988   7741  -1627   -432   -252       C  
ATOM   1704  CD1 LEU F 307      28.546  15.303  10.568  1.00 62.55           C  
ANISOU 1704  CD1 LEU F 307     6904   9068   7794  -1427   -417   -198       C  
ATOM   1705  CD2 LEU F 307      26.812  15.813   8.806  1.00 61.16           C  
ANISOU 1705  CD2 LEU F 307     6155   9391   7690  -2046   -287   -409       C  
ATOM   1706  N   GLN F 308      31.562  16.950   8.374  1.00 59.19           N  
ANISOU 1706  N   GLN F 308     5328   8894   8266  -1200   -447   -603       N  
ATOM   1707  CA  GLN F 308      32.270  16.656   7.132  1.00 61.53           C  
ANISOU 1707  CA  GLN F 308     5595   9079   8703  -1280   -143   -700       C  
ATOM   1708  C   GLN F 308      31.531  15.629   6.296  1.00 58.41           C  
ANISOU 1708  C   GLN F 308     5738   8395   8059  -1321    -35   -418       C  
ATOM   1709  O   GLN F 308      31.326  14.501   6.739  1.00 55.69           O  
ANISOU 1709  O   GLN F 308     5756   7928   7473  -1115    -96   -306       O  
ATOM   1710  CB  GLN F 308      33.677  16.123   7.412  1.00 67.35           C  
ANISOU 1710  CB  GLN F 308     5833  10161   9595   -861   -215  -1092       C  
ATOM   1711  CG  GLN F 308      34.688  17.208   7.706  1.00 72.76           C  
ANISOU 1711  CG  GLN F 308     5722  11309  10611  -1137   -118  -1708       C  
ATOM   1712  CD  GLN F 308      36.105  16.665   7.757  1.00 80.58           C  
ANISOU 1712  CD  GLN F 308     5880  12964  11772   -678   -197  -2354       C  
ATOM   1713  OE1 GLN F 308      36.563  15.966   6.847  1.00 81.23           O  
ANISOU 1713  OE1 GLN F 308     5967  12987  11908   -496     84  -2402       O  
ATOM   1714  NE2 GLN F 308      36.804  16.980   8.833  1.00 87.98           N  
ANISOU 1714  NE2 GLN F 308     6039  14645  12742   -398   -624  -2944       N  
ATOM   1715  N   VAL F 309      31.184  16.009   5.065  1.00 58.87           N  
ANISOU 1715  N   VAL F 309     6020   8280   8066  -1588    186   -360       N  
ATOM   1716  CA  VAL F 309      30.474  15.107   4.167  1.00 59.01           C  
ANISOU 1716  CA  VAL F 309     6474   8147   7798  -1718    249   -242       C  
ATOM   1717  C   VAL F 309      31.314  14.788   2.935  1.00 61.52           C  
ANISOU 1717  C   VAL F 309     7042   8185   8145  -1736    614   -290       C  
ATOM   1718  O   VAL F 309      31.797  15.693   2.255  1.00 67.81           O  
ANISOU 1718  O   VAL F 309     7898   8844   9020  -1839    890   -372       O  
ATOM   1719  CB  VAL F 309      29.129  15.704   3.745  1.00 57.44           C  
ANISOU 1719  CB  VAL F 309     6344   8163   7315  -1831     40   -233       C  
ATOM   1720  CG1 VAL F 309      28.287  14.662   3.037  1.00 60.45           C  
ANISOU 1720  CG1 VAL F 309     6946   8651   7370  -2110     28   -347       C  
ATOM   1721  CG2 VAL F 309      28.401  16.237   4.958  1.00 57.05           C  
ANISOU 1721  CG2 VAL F 309     5949   8434   7290  -1776   -210   -262       C  
ATOM   1722  N   ARG F 310      31.452  13.492   2.668  1.00 62.62           N  
ANISOU 1722  N   ARG F 310     7524   8130   8137  -1678    741   -261       N  
ATOM   1723  CA  ARG F 310      32.275  12.935   1.603  1.00 65.09           C  
ANISOU 1723  CA  ARG F 310     8126   8158   8446  -1612   1137   -325       C  
ATOM   1724  C   ARG F 310      31.407  12.609   0.389  1.00 65.94           C  
ANISOU 1724  C   ARG F 310     8843   8057   8151  -1970   1213   -265       C  
ATOM   1725  O   ARG F 310      30.715  11.585   0.373  1.00 65.60           O  
ANISOU 1725  O   ARG F 310     9205   7918   7800  -2197   1197   -279       O  
ATOM   1726  CB  ARG F 310      32.917  11.650   2.144  1.00 70.75           C  
ANISOU 1726  CB  ARG F 310     9073   8722   9084  -1117   1208   -338       C  
ATOM   1727  CG  ARG F 310      34.066  11.059   1.344  1.00 77.97           C  
ANISOU 1727  CG  ARG F 310    10084   9478  10061   -743   1615   -503       C  
ATOM   1728  CD  ARG F 310      34.847  10.039   2.184  1.00 85.81           C  
ANISOU 1728  CD  ARG F 310    11227  10476  10898    216   1519   -576       C  
ATOM   1729  NE  ARG F 310      35.571  10.665   3.303  1.00 89.98           N  
ANISOU 1729  NE  ARG F 310    10808  11675  11705    757   1107   -866       N  
ATOM   1730  CZ  ARG F 310      35.221  10.628   4.595  1.00 92.07           C  
ANISOU 1730  CZ  ARG F 310    11194  12032  11757   1100    654   -747       C  
ATOM   1731  NH1 ARG F 310      34.142   9.966   5.019  1.00 90.46           N  
ANISOU 1731  NH1 ARG F 310    12055  11240  11074    883    683   -357       N  
ATOM   1732  NH2 ARG F 310      35.973  11.262   5.489  1.00 95.42           N  
ANISOU 1732  NH2 ARG F 310    10673  13175  12404   1576    242  -1131       N  
ATOM   1733  N   GLY F 311      31.412  13.489  -0.616  1.00 64.71           N  
ANISOU 1733  N   GLY F 311     8888   7813   7887  -2055   1336   -274       N  
ATOM   1734  CA  GLY F 311      30.654  13.257  -1.861  1.00 65.10           C  
ANISOU 1734  CA  GLY F 311     9567   7759   7405  -2205   1283   -291       C  
ATOM   1735  C   GLY F 311      29.459  14.178  -1.998  1.00 66.98           C  
ANISOU 1735  C   GLY F 311     9797   8394   7258  -2054    757   -327       C  
ATOM   1736  O   GLY F 311      28.874  14.594  -1.000  1.00 66.35           O  
ANISOU 1736  O   GLY F 311     9170   8720   7317  -1980    411   -351       O  
ATOM   1737  N   ARG F 312      29.096  14.501  -3.236  1.00 66.81           N  
ANISOU 1737  N   ARG F 312     9192   8393   7799   -946   3227     34       N  
ATOM   1738  CA  ARG F 312      28.006  15.452  -3.511  1.00 68.86           C  
ANISOU 1738  CA  ARG F 312     9908   8513   7739   -731   3306    325       C  
ATOM   1739  C   ARG F 312      26.591  14.899  -3.170  1.00 62.33           C  
ANISOU 1739  C   ARG F 312     9169   7987   6527   -588   2492    151       C  
ATOM   1740  O   ARG F 312      25.733  15.634  -2.692  1.00 58.88           O  
ANISOU 1740  O   ARG F 312     8813   7478   6079   -625   2348    228       O  
ATOM   1741  CB  ARG F 312      28.112  15.947  -4.974  1.00 76.32           C  
ANISOU 1741  CB  ARG F 312    11468   9359   8171   -106   4036    783       C  
ATOM   1742  CG  ARG F 312      26.841  16.498  -5.640  1.00 81.68           C  
ANISOU 1742  CG  ARG F 312    12759  10238   8037    631   3944   1085       C  
ATOM   1743  CD  ARG F 312      26.635  18.019  -5.576  1.00 86.76           C  
ANISOU 1743  CD  ARG F 312    13776  10342   8844    759   4741   1609       C  
ATOM   1744  NE  ARG F 312      25.381  18.372  -6.262  1.00 90.56           N  
ANISOU 1744  NE  ARG F 312    14847  11239   8320   1739   4518   1881       N  
ATOM   1745  CZ  ARG F 312      24.585  19.409  -5.985  1.00 91.10           C  
ANISOU 1745  CZ  ARG F 312    15209  11101   8302   1987   4703   2194       C  
ATOM   1746  NH1 ARG F 312      24.886  20.287  -5.028  1.00 89.26           N  
ANISOU 1746  NH1 ARG F 312    14768  10132   9014   1241   5194   2263       N  
ATOM   1747  NH2 ARG F 312      23.456  19.559  -6.683  1.00 93.78           N  
ANISOU 1747  NH2 ARG F 312    15996  12068   7567   3075   4349   2323       N  
ATOM   1748  N   GLU F 313      26.348  13.623  -3.425  1.00 62.52           N  
ANISOU 1748  N   GLU F 313     9126   8271   6357   -457   2072   -152       N  
ATOM   1749  CA  GLU F 313      25.010  13.043  -3.228  1.00 60.66           C  
ANISOU 1749  CA  GLU F 313     8844   8214   5990   -392   1501   -502       C  
ATOM   1750  C   GLU F 313      24.644  13.038  -1.740  1.00 53.31           C  
ANISOU 1750  C   GLU F 313     7635   7079   5540   -820   1286   -509       C  
ATOM   1751  O   GLU F 313      23.515  13.340  -1.360  1.00 50.95           O  
ANISOU 1751  O   GLU F 313     7330   6800   5226   -839   1024   -598       O  
ATOM   1752  CB  GLU F 313      24.941  11.612  -3.790  1.00 64.64           C  
ANISOU 1752  CB  GLU F 313     9232   8857   6469   -272   1313   -996       C  
ATOM   1753  CG  GLU F 313      25.161  11.492  -5.304  1.00 74.75           C  
ANISOU 1753  CG  GLU F 313    10777  10513   7111    316   1411  -1142       C  
ATOM   1754  CD  GLU F 313      23.900  11.696  -6.154  1.00 82.02           C  
ANISOU 1754  CD  GLU F 313    11786  11999   7378    925    992  -1603       C  
ATOM   1755  OE1 GLU F 313      22.962  12.410  -5.705  1.00 83.65           O  
ANISOU 1755  OE1 GLU F 313    11969  12271   7542    936    762  -1561       O  
ATOM   1756  OE2 GLU F 313      23.854  11.146  -7.287  1.00 86.38           O  
ANISOU 1756  OE2 GLU F 313    12386  13036   7395   1495    854  -2091       O  
ATOM   1757  N   ARG F 314      25.606  12.684  -0.900  1.00 51.27           N  
ANISOU 1757  N   ARG F 314     7134   6717   5627  -1028   1398   -440       N  
ATOM   1758  CA  ARG F 314      25.396  12.726   0.543  1.00 49.95           C  
ANISOU 1758  CA  ARG F 314     6760   6504   5714  -1175   1233   -406       C  
ATOM   1759  C   ARG F 314      25.269  14.139   1.059  1.00 49.13           C  
ANISOU 1759  C   ARG F 314     6608   6388   5671  -1346   1239   -324       C  
ATOM   1760  O   ARG F 314      24.475  14.394   1.944  1.00 46.85           O  
ANISOU 1760  O   ARG F 314     6294   6082   5422  -1392   1030   -315       O  
ATOM   1761  CB  ARG F 314      26.526  12.045   1.278  1.00 51.55           C  
ANISOU 1761  CB  ARG F 314     6701   6831   6053  -1052   1302   -410       C  
ATOM   1762  CG  ARG F 314      26.189  10.655   1.742  1.00 52.70           C  
ANISOU 1762  CG  ARG F 314     6937   6810   6274   -806   1365   -354       C  
ATOM   1763  CD  ARG F 314      27.437   9.976   2.239  1.00 55.88           C  
ANISOU 1763  CD  ARG F 314     7167   7437   6626   -418   1486   -281       C  
ATOM   1764  NE  ARG F 314      27.801   8.997   1.261  1.00 59.66           N  
ANISOU 1764  NE  ARG F 314     7771   7724   7171   -355   1730   -338       N  
ATOM   1765  CZ  ARG F 314      29.022   8.694   0.872  1.00 60.30           C  
ANISOU 1765  CZ  ARG F 314     7693   8025   7191   -167   1843   -382       C  
ATOM   1766  NH1 ARG F 314      30.079   9.294   1.379  1.00 64.38           N  
ANISOU 1766  NH1 ARG F 314     7795   9016   7649    -44   1726   -487       N  
ATOM   1767  NH2 ARG F 314      29.156   7.768  -0.052  1.00 60.19           N  
ANISOU 1767  NH2 ARG F 314     7853   7776   7239   -112   2081   -461       N  
ATOM   1768  N   TYR F 315      26.086  15.051   0.535  1.00 50.99           N  
ANISOU 1768  N   TYR F 315     6817   6541   6014  -1450   1613   -287       N  
ATOM   1769  CA  TYR F 315      25.973  16.448   0.897  1.00 52.31           C  
ANISOU 1769  CA  TYR F 315     6954   6500   6420  -1657   1842   -275       C  
ATOM   1770  C   TYR F 315      24.552  16.974   0.672  1.00 50.23           C  
ANISOU 1770  C   TYR F 315     7098   6145   5840  -1482   1707    -41       C  
ATOM   1771  O   TYR F 315      23.976  17.554   1.589  1.00 52.03           O  
ANISOU 1771  O   TYR F 315     7240   6327   6203  -1617   1536   -100       O  
ATOM   1772  CB  TYR F 315      27.037  17.304   0.175  1.00 57.70           C  
ANISOU 1772  CB  TYR F 315     7590   6861   7469  -1808   2609   -257       C  
ATOM   1773  CG  TYR F 315      26.878  18.800   0.385  1.00 61.62           C  
ANISOU 1773  CG  TYR F 315     8132   6885   8396  -2037   3147   -241       C  
ATOM   1774  CD1 TYR F 315      27.068  19.382   1.636  1.00 63.26           C  
ANISOU 1774  CD1 TYR F 315     7798   7111   9124  -2419   2992   -772       C  
ATOM   1775  CD2 TYR F 315      26.516  19.630  -0.666  1.00 66.65           C  
ANISOU 1775  CD2 TYR F 315     9388   7067   8868  -1737   3872    289       C  
ATOM   1776  CE1 TYR F 315      26.915  20.758   1.820  1.00 68.47           C  
ANISOU 1776  CE1 TYR F 315     8476   7215  10323  -2683   3591   -864       C  
ATOM   1777  CE2 TYR F 315      26.364  20.998  -0.494  1.00 71.79           C  
ANISOU 1777  CE2 TYR F 315    10175   7105   9997  -1885   4586    386       C  
ATOM   1778  CZ  TYR F 315      26.566  21.557   0.744  1.00 72.97           C  
ANISOU 1778  CZ  TYR F 315     9724   7147  10851  -2450   4464   -233       C  
ATOM   1779  OH  TYR F 315      26.410  22.921   0.877  1.00 82.28           O  
ANISOU 1779  OH  TYR F 315    11031   7593  12639  -2639   5292   -220       O  
ATOM   1780  N   GLU F 316      23.973  16.722  -0.499  1.00 51.47           N  
ANISOU 1780  N   GLU F 316     7634   6404   5518  -1082   1712    123       N  
ATOM   1781  CA  GLU F 316      22.640  17.270  -0.861  1.00 53.23           C  
ANISOU 1781  CA  GLU F 316     8169   6737   5318   -704   1540    238       C  
ATOM   1782  C   GLU F 316      21.539  16.698   0.009  1.00 49.11           C  
ANISOU 1782  C   GLU F 316     7387   6377   4895   -856    959    -57       C  
ATOM   1783  O   GLU F 316      20.692  17.441   0.501  1.00 49.10           O  
ANISOU 1783  O   GLU F 316     7432   6338   4884   -831    857      6       O  
ATOM   1784  CB  GLU F 316      22.296  17.028  -2.350  1.00 59.30           C  
ANISOU 1784  CB  GLU F 316     9291   7863   5376      5   1551    277       C  
ATOM   1785  CG  GLU F 316      22.509  18.217  -3.288  1.00 67.16           C  
ANISOU 1785  CG  GLU F 316    10876   8696   5946    625   2275    846       C  
ATOM   1786  CD  GLU F 316      21.958  17.954  -4.697  1.00 76.57           C  
ANISOU 1786  CD  GLU F 316    12445  10529   6116   1681   2130    833       C  
ATOM   1787  OE1 GLU F 316      21.879  16.781  -5.137  1.00 75.52           O  
ANISOU 1787  OE1 GLU F 316    12043  10878   5771   1762   1604    278       O  
ATOM   1788  OE2 GLU F 316      21.612  18.928  -5.395  1.00 89.57           O  
ANISOU 1788  OE2 GLU F 316    14674  12233   7123   2562   2594   1343       O  
ATOM   1789  N   ILE F 317      21.560  15.380   0.205  1.00 47.59           N  
ANISOU 1789  N   ILE F 317     6940   6266   4873   -997    727   -356       N  
ATOM   1790  CA  ILE F 317      20.663  14.729   1.168  1.00 45.85           C  
ANISOU 1790  CA  ILE F 317     6477   5977   4967  -1186    497   -572       C  
ATOM   1791  C   ILE F 317      20.786  15.397   2.545  1.00 42.99           C  
ANISOU 1791  C   ILE F 317     6061   5471   4802  -1376    536   -333       C  
ATOM   1792  O   ILE F 317      19.784  15.834   3.124  1.00 40.01           O  
ANISOU 1792  O   ILE F 317     5665   5069   4466  -1390    410   -339       O  
ATOM   1793  CB  ILE F 317      20.929  13.209   1.263  1.00 46.81           C  
ANISOU 1793  CB  ILE F 317     6422   5953   5408  -1282    595   -803       C  
ATOM   1794  CG1 ILE F 317      20.415  12.518  -0.002  1.00 52.54           C  
ANISOU 1794  CG1 ILE F 317     7052   6868   6043  -1124    465  -1355       C  
ATOM   1795  CG2 ILE F 317      20.224  12.599   2.456  1.00 47.89           C  
ANISOU 1795  CG2 ILE F 317     6417   5793   5984  -1420    725   -811       C  
ATOM   1796  CD1 ILE F 317      21.059  11.177  -0.310  1.00 53.98           C  
ANISOU 1796  CD1 ILE F 317     7147   6851   6511  -1184    698  -1591       C  
ATOM   1797  N   LEU F 318      22.008  15.505   3.059  1.00 42.52           N  
ANISOU 1797  N   LEU F 318     5903   5412   4840  -1460    675   -244       N  
ATOM   1798  CA  LEU F 318      22.188  15.936   4.450  1.00 42.32           C  
ANISOU 1798  CA  LEU F 318     5702   5460   4918  -1488    601   -253       C  
ATOM   1799  C   LEU F 318      21.967  17.431   4.617  1.00 43.55           C  
ANISOU 1799  C   LEU F 318     5882   5521   5142  -1642    651   -288       C  
ATOM   1800  O   LEU F 318      21.454  17.840   5.645  1.00 42.12           O  
ANISOU 1800  O   LEU F 318     5634   5394   4977  -1622    508   -340       O  
ATOM   1801  CB  LEU F 318      23.559  15.530   5.007  1.00 44.44           C  
ANISOU 1801  CB  LEU F 318     5684   5986   5214  -1366    620   -393       C  
ATOM   1802  CG  LEU F 318      23.823  14.036   5.184  1.00 45.02           C  
ANISOU 1802  CG  LEU F 318     5797   6107   5198  -1035    688   -255       C  
ATOM   1803  CD1 LEU F 318      25.274  13.762   5.557  1.00 48.97           C  
ANISOU 1803  CD1 LEU F 318     5978   7022   5606   -750    659   -434       C  
ATOM   1804  CD2 LEU F 318      22.901  13.431   6.219  1.00 45.72           C  
ANISOU 1804  CD2 LEU F 318     6045   6086   5238   -739    767    -20       C  
ATOM   1805  N   LYS F 319      22.373  18.236   3.617  1.00 47.91           N  
ANISOU 1805  N   LYS F 319     6581   5866   5754  -1725    987   -224       N  
ATOM   1806  CA  LYS F 319      22.011  19.658   3.559  1.00 49.69           C  
ANISOU 1806  CA  LYS F 319     6985   5782   6112  -1785   1294   -138       C  
ATOM   1807  C   LYS F 319      20.490  19.819   3.579  1.00 48.15           C  
ANISOU 1807  C   LYS F 319     7046   5647   5602  -1534   1025     48       C  
ATOM   1808  O   LYS F 319      19.962  20.659   4.297  1.00 49.93           O  
ANISOU 1808  O   LYS F 319     7279   5747   5943  -1588   1030     26       O  
ATOM   1809  CB  LYS F 319      22.585  20.338   2.298  1.00 53.15           C  
ANISOU 1809  CB  LYS F 319     7730   5857   6606  -1694   1979    115       C  
ATOM   1810  CG  LYS F 319      22.290  21.831   2.189  1.00 58.70           C  
ANISOU 1810  CG  LYS F 319     8734   6026   7542  -1657   2612    322       C  
ATOM   1811  CD  LYS F 319      22.719  22.413   0.843  1.00 65.99           C  
ANISOU 1811  CD  LYS F 319    10168   6503   8398  -1300   3538    809       C  
ATOM   1812  CE  LYS F 319      22.697  23.938   0.817  1.00 74.24           C  
ANISOU 1812  CE  LYS F 319    11536   6736   9936  -1291   4555   1053       C  
ATOM   1813  NZ  LYS F 319      21.371  24.571   1.079  1.00 73.76           N  
ANISOU 1813  NZ  LYS F 319    11839   6697   9490   -878   4346   1322       N  
ATOM   1814  N   LYS F 320      19.793  19.032   2.765  1.00 47.10           N  
ANISOU 1814  N   LYS F 320     7035   5746   5114  -1245    790     96       N  
ATOM   1815  CA  LYS F 320      18.335  19.128   2.670  1.00 47.82           C  
ANISOU 1815  CA  LYS F 320     7180   6027   4962   -966    495     51       C  
ATOM   1816  C   LYS F 320      17.662  18.870   4.013  1.00 44.76           C  
ANISOU 1816  C   LYS F 320     6533   5616   4855  -1207    274    -83       C  
ATOM   1817  O   LYS F 320      16.714  19.564   4.383  1.00 43.82           O  
ANISOU 1817  O   LYS F 320     6452   5500   4694  -1097    197    -53       O  
ATOM   1818  CB  LYS F 320      17.808  18.130   1.625  1.00 50.93           C  
ANISOU 1818  CB  LYS F 320     7483   6800   5069   -662    216   -245       C  
ATOM   1819  CG  LYS F 320      16.301  18.133   1.448  1.00 54.14           C  
ANISOU 1819  CG  LYS F 320     7700   7566   5303   -346   -157   -596       C  
ATOM   1820  CD  LYS F 320      15.889  17.193   0.324  1.00 62.62           C  
ANISOU 1820  CD  LYS F 320     8509   9141   6140    -13   -472  -1213       C  
ATOM   1821  CE  LYS F 320      14.519  17.572  -0.226  1.00 68.52           C  
ANISOU 1821  CE  LYS F 320     9037  10528   6469    618   -897  -1687       C  
ATOM   1822  NZ  LYS F 320      14.188  16.733  -1.389  1.00 77.03           N  
ANISOU 1822  NZ  LYS F 320     9740  12286   7241   1066  -1292  -2540       N  
ATOM   1823  N   LEU F 321      18.150  17.860   4.737  1.00 41.56           N  
ANISOU 1823  N   LEU F 321     5922   5190   4679  -1405    261   -166       N  
ATOM   1824  CA  LEU F 321      17.544  17.497   5.985  1.00 40.42           C  
ANISOU 1824  CA  LEU F 321     5648   4999   4709  -1433    241   -162       C  
ATOM   1825  C   LEU F 321      17.827  18.600   6.988  1.00 40.40           C  
ANISOU 1825  C   LEU F 321     5673   5018   4658  -1439    231   -107       C  
ATOM   1826  O   LEU F 321      16.959  18.978   7.779  1.00 39.59           O  
ANISOU 1826  O   LEU F 321     5574   4905   4563  -1369    192    -78       O  
ATOM   1827  CB  LEU F 321      18.077  16.147   6.505  1.00 40.74           C  
ANISOU 1827  CB  LEU F 321     5608   4972   4897  -1383    427   -113       C  
ATOM   1828  CG  LEU F 321      17.896  14.900   5.645  1.00 40.96           C  
ANISOU 1828  CG  LEU F 321     5550   4843   5170  -1448    574   -304       C  
ATOM   1829  CD1 LEU F 321      18.699  13.773   6.264  1.00 42.18           C  
ANISOU 1829  CD1 LEU F 321     5759   4837   5430  -1273    921    -94       C  
ATOM   1830  CD2 LEU F 321      16.432  14.478   5.510  1.00 43.73           C  
ANISOU 1830  CD2 LEU F 321     5671   5025   5918  -1562    660   -642       C  
ATOM   1831  N   ASN F 322      19.047  19.125   6.948  1.00 38.76           N  
ANISOU 1831  N   ASN F 322     5404   4840   4483  -1540    304   -220       N  
ATOM   1832  CA  ASN F 322      19.464  20.100   7.912  1.00 39.90           C  
ANISOU 1832  CA  ASN F 322     5385   5048   4727  -1595    295   -482       C  
ATOM   1833  C   ASN F 322      18.682  21.395   7.728  1.00 40.96           C  
ANISOU 1833  C   ASN F 322     5718   4873   4971  -1679    451   -427       C  
ATOM   1834  O   ASN F 322      18.161  21.975   8.698  1.00 40.21           O  
ANISOU 1834  O   ASN F 322     5578   4819   4881  -1625    363   -557       O  
ATOM   1835  CB  ASN F 322      20.973  20.327   7.775  1.00 43.43           C  
ANISOU 1835  CB  ASN F 322     5521   5573   5407  -1770    420   -866       C  
ATOM   1836  CG  ASN F 322      21.545  21.120   8.914  1.00 46.82           C  
ANISOU 1836  CG  ASN F 322     5520   6253   6017  -1800    317  -1507       C  
ATOM   1837  OD1 ASN F 322      21.305  20.826  10.083  1.00 45.56           O  
ANISOU 1837  OD1 ASN F 322     5247   6553   5512  -1414    -15  -1641       O  
ATOM   1838  ND2 ASN F 322      22.335  22.122   8.580  1.00 51.83           N  
ANISOU 1838  ND2 ASN F 322     5877   6586   7228  -2202    689  -1988       N  
ATOM   1839  N   ASP F 323      18.597  21.840   6.479  1.00 42.79           N  
ANISOU 1839  N   ASP F 323     6227   4822   5209  -1667    739   -191       N  
ATOM   1840  CA  ASP F 323      17.831  23.036   6.113  1.00 46.69           C  
ANISOU 1840  CA  ASP F 323     7051   4997   5692  -1504   1025     23       C  
ATOM   1841  C   ASP F 323      16.349  22.904   6.527  1.00 44.48           C  
ANISOU 1841  C   ASP F 323     6806   4945   5146  -1249    659    118       C  
ATOM   1842  O   ASP F 323      15.720  23.870   6.990  1.00 43.37           O  
ANISOU 1842  O   ASP F 323     6784   4634   5058  -1161    767    150       O  
ATOM   1843  CB  ASP F 323      17.916  23.320   4.595  1.00 51.24           C  
ANISOU 1843  CB  ASP F 323     8043   5381   6042  -1167   1440    412       C  
ATOM   1844  CG  ASP F 323      19.315  23.810   4.131  1.00 58.91           C  
ANISOU 1844  CG  ASP F 323     9045   5879   7458  -1425   2150    390       C  
ATOM   1845  OD1 ASP F 323      20.210  24.077   4.967  1.00 62.20           O  
ANISOU 1845  OD1 ASP F 323     9032   6132   8466  -1932   2282   -105       O  
ATOM   1846  OD2 ASP F 323      19.520  23.926   2.893  1.00 64.16           O  
ANISOU 1846  OD2 ASP F 323    10116   6383   7877  -1044   2620    799       O  
ATOM   1847  N   SER F 324      15.807  21.715   6.341  1.00 41.35           N  
ANISOU 1847  N   SER F 324     6256   4869   4584  -1162    325     87       N  
ATOM   1848  CA  SER F 324      14.439  21.428   6.714  1.00 43.14           C  
ANISOU 1848  CA  SER F 324     6342   5274   4775  -1017     91     17       C  
ATOM   1849  C   SER F 324      14.238  21.506   8.235  1.00 42.12           C  
ANISOU 1849  C   SER F 324     6100   5094   4809  -1139    100    -13       C  
ATOM   1850  O   SER F 324      13.283  22.117   8.699  1.00 43.74           O  
ANISOU 1850  O   SER F 324     6322   5290   5005  -1011     81      3       O  
ATOM   1851  CB  SER F 324      14.032  20.035   6.210  1.00 45.27           C  
ANISOU 1851  CB  SER F 324     6329   5746   5123  -1033    -69   -219       C  
ATOM   1852  OG  SER F 324      12.617  19.889   6.251  1.00 54.72           O  
ANISOU 1852  OG  SER F 324     7247   7113   6429   -902   -213   -485       O  
ATOM   1853  N   LEU F 325      15.115  20.891   9.022  1.00 41.22           N  
ANISOU 1853  N   LEU F 325     5887   5035   4738  -1231    130    -57       N  
ATOM   1854  CA  LEU F 325      14.963  20.974  10.480  1.00 42.61           C  
ANISOU 1854  CA  LEU F 325     6019   5330   4839  -1065    139    -78       C  
ATOM   1855  C   LEU F 325      15.060  22.411  10.993  1.00 44.92           C  
ANISOU 1855  C   LEU F 325     6345   5590   5133  -1089    108   -303       C  
ATOM   1856  O   LEU F 325      14.264  22.809  11.840  1.00 42.96           O  
ANISOU 1856  O   LEU F 325     6128   5384   4808   -915    104   -296       O  
ATOM   1857  CB  LEU F 325      15.966  20.087  11.192  1.00 43.42           C  
ANISOU 1857  CB  LEU F 325     6043   5683   4770   -848    156    -91       C  
ATOM   1858  CG  LEU F 325      15.800  18.585  10.971  1.00 42.61           C  
ANISOU 1858  CG  LEU F 325     5975   5446   4766   -748    415    181       C  
ATOM   1859  CD1 LEU F 325      17.126  17.870  11.240  1.00 44.64           C  
ANISOU 1859  CD1 LEU F 325     6209   5966   4784   -461    420    190       C  
ATOM   1860  CD2 LEU F 325      14.721  18.029  11.870  1.00 43.51           C  
ANISOU 1860  CD2 LEU F 325     6176   5391   4965   -477    805    453       C  
ATOM   1861  N   GLU F 326      16.005  23.193  10.450  1.00 48.48           N  
ANISOU 1861  N   GLU F 326     6773   5868   5779  -1326    215   -536       N  
ATOM   1862  CA  GLU F 326      16.174  24.607  10.839  1.00 52.44           C  
ANISOU 1862  CA  GLU F 326     7253   6119   6550  -1460    406   -891       C  
ATOM   1863  C   GLU F 326      14.925  25.391  10.514  1.00 52.03           C  
ANISOU 1863  C   GLU F 326     7526   5759   6482  -1314    571   -560       C  
ATOM   1864  O   GLU F 326      14.539  26.282  11.262  1.00 53.81           O  
ANISOU 1864  O   GLU F 326     7765   5866   6813  -1276    651   -767       O  
ATOM   1865  CB  GLU F 326      17.355  25.262  10.116  1.00 55.08           C  
ANISOU 1865  CB  GLU F 326     7496   6071   7361  -1813    812  -1183       C  
ATOM   1866  CG  GLU F 326      18.688  24.694  10.558  1.00 59.26           C  
ANISOU 1866  CG  GLU F 326     7528   7007   7981  -1936    613  -1752       C  
ATOM   1867  CD  GLU F 326      19.890  25.455  10.034  1.00 63.79           C  
ANISOU 1867  CD  GLU F 326     7808   7153   9274  -2393   1136  -2285       C  
ATOM   1868  OE1 GLU F 326      19.732  26.314   9.140  1.00 67.07           O  
ANISOU 1868  OE1 GLU F 326     8577   6808  10097  -2571   1831  -1981       O  
ATOM   1869  OE2 GLU F 326      21.000  25.187  10.544  1.00 67.53           O  
ANISOU 1869  OE2 GLU F 326     7674   8066   9916  -2485    929  -3034       O  
ATOM   1870  N   LEU F 327      14.303  25.046   9.390  1.00 48.77           N  
ANISOU 1870  N   LEU F 327     7330   5314   5886  -1135    586   -134       N  
ATOM   1871  CA  LEU F 327      13.105  25.707   8.961  1.00 49.55           C  
ANISOU 1871  CA  LEU F 327     7677   5324   5824   -778    660    135       C  
ATOM   1872  C   LEU F 327      11.989  25.498   9.980  1.00 47.88           C  
ANISOU 1872  C   LEU F 327     7287   5364   5539   -666    398     67       C  
ATOM   1873  O   LEU F 327      11.289  26.457  10.335  1.00 48.48           O  
ANISOU 1873  O   LEU F 327     7503   5293   5622   -474    520    102       O  
ATOM   1874  CB  LEU F 327      12.695  25.217   7.580  1.00 51.13           C  
ANISOU 1874  CB  LEU F 327     7989   5745   5691   -418    564    380       C  
ATOM   1875  CG  LEU F 327      11.396  25.794   7.010  1.00 55.17           C  
ANISOU 1875  CG  LEU F 327     8663   6454   5845    227    506    557       C  
ATOM   1876  CD1 LEU F 327      11.511  27.298   6.821  1.00 60.76           C  
ANISOU 1876  CD1 LEU F 327     9902   6622   6560    554   1119    906       C  
ATOM   1877  CD2 LEU F 327      11.063  25.105   5.699  1.00 58.29           C  
ANISOU 1877  CD2 LEU F 327     8987   7367   5792    708    227    517       C  
ATOM   1878  N   SER F 328      11.835  24.263  10.464  1.00 45.36           N  
ANISOU 1878  N   SER F 328     6699   5329   5206   -748    192     11       N  
ATOM   1879  CA  SER F 328      10.826  23.963  11.479  1.00 46.65           C  
ANISOU 1879  CA  SER F 328     6716   5617   5390   -621    184     15       C  
ATOM   1880  C   SER F 328      11.063  24.690  12.806  1.00 47.69           C  
ANISOU 1880  C   SER F 328     6931   5755   5432   -533    240   -111       C  
ATOM   1881  O   SER F 328      10.126  24.837  13.593  1.00 47.47           O  
ANISOU 1881  O   SER F 328     6887   5784   5363   -326    312    -58       O  
ATOM   1882  CB  SER F 328      10.719  22.453  11.757  1.00 46.31           C  
ANISOU 1882  CB  SER F 328     6456   5656   5482   -676    284     62       C  
ATOM   1883  OG  SER F 328      10.006  21.814  10.728  1.00 48.12           O  
ANISOU 1883  OG  SER F 328     6423   5921   5938   -749    237    -80       O  
ATOM   1884  N   ASP F 329      12.314  25.081  13.074  1.00 46.48           N  
ANISOU 1884  N   ASP F 329     6773   5612   5274   -660    209   -406       N  
ATOM   1885  CA  ASP F 329      12.642  25.843  14.269  1.00 49.28           C  
ANISOU 1885  CA  ASP F 329     7058   6112   5552   -536    170   -843       C  
ATOM   1886  C   ASP F 329      12.323  27.321  14.165  1.00 50.11           C  
ANISOU 1886  C   ASP F 329     7291   5794   5952   -651    385  -1053       C  
ATOM   1887  O   ASP F 329      12.383  28.018  15.164  1.00 53.63           O  
ANISOU 1887  O   ASP F 329     7640   6335   6399   -552    366  -1531       O  
ATOM   1888  CB  ASP F 329      14.125  25.703  14.609  1.00 54.44           C  
ANISOU 1888  CB  ASP F 329     7433   7064   6186   -602     13  -1394       C  
ATOM   1889  CG  ASP F 329      14.478  24.335  15.142  1.00 56.81           C  
ANISOU 1889  CG  ASP F 329     7674   7884   6026   -192   -145  -1198       C  
ATOM   1890  OD1 ASP F 329      13.569  23.605  15.640  1.00 57.56           O  
ANISOU 1890  OD1 ASP F 329     7961   8047   5859    178      2   -698       O  
ATOM   1891  OD2 ASP F 329      15.680  24.003  15.056  1.00 56.69           O  
ANISOU 1891  OD2 ASP F 329     7415   8149   5974   -203   -299  -1543       O  
ATOM   1892  N   VAL F 330      12.001  27.813  12.975  1.00 50.11           N  
ANISOU 1892  N   VAL F 330     7536   5346   6155   -734    647   -718       N  
ATOM   1893  CA  VAL F 330      11.718  29.247  12.815  1.00 53.21           C  
ANISOU 1893  CA  VAL F 330     8186   5180   6852   -703   1085   -773       C  
ATOM   1894  C   VAL F 330      10.358  29.596  12.219  1.00 51.14           C  
ANISOU 1894  C   VAL F 330     8228   4837   6362   -247   1172   -226       C  
ATOM   1895  O   VAL F 330      10.025  30.758  12.175  1.00 54.70           O  
ANISOU 1895  O   VAL F 330     8968   4821   6993    -63   1598   -171       O  
ATOM   1896  CB  VAL F 330      12.836  29.954  12.026  1.00 57.43           C  
ANISOU 1896  CB  VAL F 330     8822   5082   7917  -1023   1658   -941       C  
ATOM   1897  CG1 VAL F 330      14.125  29.954  12.837  1.00 60.60           C  
ANISOU 1897  CG1 VAL F 330     8710   5606   8707  -1467   1581  -1849       C  
ATOM   1898  CG2 VAL F 330      13.057  29.304  10.664  1.00 55.93           C  
ANISOU 1898  CG2 VAL F 330     8830   4892   7527   -920   1723   -397       C  
ATOM   1899  N   VAL F 331       9.571  28.609  11.797  1.00 47.75           N  
ANISOU 1899  N   VAL F 331     7668   4873   5601    -26    810     60       N  
ATOM   1900  CA  VAL F 331       8.205  28.854  11.353  1.00 49.88           C  
ANISOU 1900  CA  VAL F 331     7988   5325   5638    490    743    315       C  
ATOM   1901  C   VAL F 331       7.266  28.613  12.531  1.00 49.88           C  
ANISOU 1901  C   VAL F 331     7715   5579   5658    513    582    168       C  
ATOM   1902  O   VAL F 331       7.345  27.563  13.161  1.00 46.66           O  
ANISOU 1902  O   VAL F 331     7025   5406   5298    286    448     64       O  
ATOM   1903  CB  VAL F 331       7.798  27.947  10.181  1.00 50.80           C  
ANISOU 1903  CB  VAL F 331     7908   5895   5498    739    439    403       C  
ATOM   1904  CG1 VAL F 331       6.365  28.248   9.739  1.00 53.73           C  
ANISOU 1904  CG1 VAL F 331     8144   6677   5594   1410    261    414       C  
ATOM   1905  CG2 VAL F 331       8.764  28.136   9.012  1.00 53.34           C  
ANISOU 1905  CG2 VAL F 331     8576   6006   5682    843    667    627       C  
ATOM   1906  N   PRO F 332       6.390  29.591  12.836  1.00 46.12           N  
ANISOU 1906  N   PRO F 332     6139   5530   5852   -969   1104    137       N  
ATOM   1907  CA  PRO F 332       5.468  29.475  13.945  1.00 45.43           C  
ANISOU 1907  CA  PRO F 332     6488   4969   5801   -890   1160     77       C  
ATOM   1908  C   PRO F 332       4.448  28.402  13.714  1.00 44.11           C  
ANISOU 1908  C   PRO F 332     6244   4722   5792   -501   1201     39       C  
ATOM   1909  O   PRO F 332       4.090  28.167  12.565  1.00 44.75           O  
ANISOU 1909  O   PRO F 332     6070   4941   5988   -272   1219     69       O  
ATOM   1910  CB  PRO F 332       4.776  30.846  13.981  1.00 46.90           C  
ANISOU 1910  CB  PRO F 332     7171   4681   5966  -1017   1437    119       C  
ATOM   1911  CG  PRO F 332       5.779  31.788  13.397  1.00 50.84           C  
ANISOU 1911  CG  PRO F 332     7746   5284   6286  -1500   1412    223       C  
ATOM   1912  CD  PRO F 332       6.428  30.975  12.311  1.00 50.10           C  
ANISOU 1912  CD  PRO F 332     6962   5827   6247  -1370   1313    264       C  
ATOM   1913  N   ALA F 333       3.968  27.790  14.799  1.00 41.33           N  
ANISOU 1913  N   ALA F 333     6196   4142   5364   -548   1223    -28       N  
ATOM   1914  CA  ALA F 333       3.040  26.683  14.694  1.00 43.44           C  
ANISOU 1914  CA  ALA F 333     6486   4329   5688   -455   1281    -73       C  
ATOM   1915  C   ALA F 333       1.804  27.042  13.858  1.00 42.90           C  
ANISOU 1915  C   ALA F 333     6080   4363   5856   -349   1519   -105       C  
ATOM   1916  O   ALA F 333       1.445  26.295  12.956  1.00 40.88           O  
ANISOU 1916  O   ALA F 333     5604   4252   5677   -264   1400   -130       O  
ATOM   1917  CB  ALA F 333       2.625  26.179  16.067  1.00 45.35           C  
ANISOU 1917  CB  ALA F 333     7248   4283   5700   -722   1398   -112       C  
ATOM   1918  N   SER F 334       1.185  28.187  14.130  1.00 43.93           N  
ANISOU 1918  N   SER F 334     6218   4424   6050   -275   1791   -132       N  
ATOM   1919  CA  SER F 334      -0.029  28.579  13.394  1.00 47.23           C  
ANISOU 1919  CA  SER F 334     6234   5048   6662     36   1923   -189       C  
ATOM   1920  C   SER F 334       0.251  28.722  11.891  1.00 46.16           C  
ANISOU 1920  C   SER F 334     5897   5055   6584    290   1638    -67       C  
ATOM   1921  O   SER F 334      -0.544  28.254  11.065  1.00 46.67           O  
ANISOU 1921  O   SER F 334     5572   5414   6747    431   1514   -119       O  
ATOM   1922  CB  SER F 334      -0.600  29.889  13.932  1.00 50.35           C  
ANISOU 1922  CB  SER F 334     6819   5268   7041    344   2218   -263       C  
ATOM   1923  OG  SER F 334       0.429  30.843  14.022  1.00 53.12           O  
ANISOU 1923  OG  SER F 334     7741   5214   7226    271   2133   -145       O  
ATOM   1924  N   ASP F 335       1.391  29.331  11.557  1.00 45.76           N  
ANISOU 1924  N   ASP F 335     6121   4860   6402    233   1543     78       N  
ATOM   1925  CA  ASP F 335       1.825  29.515  10.159  1.00 46.88           C  
ANISOU 1925  CA  ASP F 335     6203   5146   6460    357   1376    214       C  
ATOM   1926  C   ASP F 335       2.100  28.199   9.440  1.00 45.26           C  
ANISOU 1926  C   ASP F 335     5717   5245   6234    366   1186    146       C  
ATOM   1927  O   ASP F 335       1.666  27.992   8.313  1.00 45.19           O  
ANISOU 1927  O   ASP F 335     5593   5398   6179    563   1044    154       O  
ATOM   1928  CB  ASP F 335       3.070  30.404  10.092  1.00 50.02           C  
ANISOU 1928  CB  ASP F 335     6926   5435   6644     35   1430    358       C  
ATOM   1929  CG  ASP F 335       2.793  31.815  10.560  1.00 54.68           C  
ANISOU 1929  CG  ASP F 335     8124   5516   7133     11   1576    429       C  
ATOM   1930  OD1 ASP F 335       1.603  32.139  10.750  1.00 63.07           O  
ANISOU 1930  OD1 ASP F 335     9268   6388   8308    495   1633    361       O  
ATOM   1931  OD2 ASP F 335       3.745  32.588  10.753  1.00 56.75           O  
ANISOU 1931  OD2 ASP F 335     8790   5600   7171   -487   1633    515       O  
ATOM   1932  N   ALA F 336       2.805  27.305  10.101  1.00 44.91           N  
ANISOU 1932  N   ALA F 336     5688   5223   6152    225   1134     60       N  
ATOM   1933  CA  ALA F 336       3.041  25.988   9.544  1.00 45.63           C  
ANISOU 1933  CA  ALA F 336     5754   5428   6154    367    944    -53       C  
ATOM   1934  C   ALA F 336       1.732  25.305   9.167  1.00 46.01           C  
ANISOU 1934  C   ALA F 336     5788   5422   6269    309    863   -158       C  
ATOM   1935  O   ALA F 336       1.624  24.737   8.079  1.00 51.88           O  
ANISOU 1935  O   ALA F 336     6543   6274   6893    428    690   -232       O  
ATOM   1936  CB  ALA F 336       3.838  25.133  10.510  1.00 44.89           C  
ANISOU 1936  CB  ALA F 336     5868   5230   5958    389    823   -127       C  
ATOM   1937  N   GLU F 337       0.750  25.375  10.052  1.00 48.95           N  
ANISOU 1937  N   GLU F 337     6108   5711   6778     62   1008   -199       N  
ATOM   1938  CA  GLU F 337      -0.597  24.789   9.822  1.00 51.44           C  
ANISOU 1938  CA  GLU F 337     6190   6196   7159   -197    976   -341       C  
ATOM   1939  C   GLU F 337      -1.234  25.422   8.561  1.00 51.74           C  
ANISOU 1939  C   GLU F 337     5806   6599   7254    110    788   -332       C  
ATOM   1940  O   GLU F 337      -1.677  24.696   7.679  1.00 58.19           O  
ANISOU 1940  O   GLU F 337     6554   7584   7970    -14    518   -447       O  
ATOM   1941  CB  GLU F 337      -1.473  24.921  11.116  1.00 53.92           C  
ANISOU 1941  CB  GLU F 337     6373   6549   7562   -545   1321   -412       C  
ATOM   1942  CG  GLU F 337      -2.965  24.557  11.018  1.00 60.36           C  
ANISOU 1942  CG  GLU F 337     6626   7843   8464   -932   1410   -602       C  
ATOM   1943  CD  GLU F 337      -3.788  24.781  12.321  1.00 67.82           C  
ANISOU 1943  CD  GLU F 337     7330   9002   9434  -1265   1923   -713       C  
ATOM   1944  OE1 GLU F 337      -3.466  25.693  13.166  1.00 63.91           O  
ANISOU 1944  OE1 GLU F 337     7009   8327   8945   -943   2206   -659       O  
ATOM   1945  OE2 GLU F 337      -4.792  24.030  12.507  1.00 69.09           O  
ANISOU 1945  OE2 GLU F 337     7154   9554   9544  -1949   2085   -887       O  
ATOM   1946  N   LYS F 338      -1.224  26.749   8.452  1.00 49.89           N  
ANISOU 1946  N   LYS F 338     5473   6395   7086    514    867   -194       N  
ATOM   1947  CA  LYS F 338      -1.732  27.459   7.260  1.00 54.96           C  
ANISOU 1947  CA  LYS F 338     5953   7262   7666    952    607   -118       C  
ATOM   1948  C   LYS F 338      -1.160  26.950   5.932  1.00 51.64           C  
ANISOU 1948  C   LYS F 338     5774   6880   6966    968    329    -76       C  
ATOM   1949  O   LYS F 338      -1.878  26.733   4.963  1.00 54.29           O  
ANISOU 1949  O   LYS F 338     5939   7505   7184   1082    -17   -141       O  
ATOM   1950  CB  LYS F 338      -1.387  28.944   7.325  1.00 58.14           C  
ANISOU 1950  CB  LYS F 338     6704   7370   8013   1357    730     94       C  
ATOM   1951  CG  LYS F 338      -2.292  29.808   8.168  1.00 68.60           C  
ANISOU 1951  CG  LYS F 338     7871   8686   9507   1728    909     19       C  
ATOM   1952  CD  LYS F 338      -1.743  31.237   8.219  1.00 73.79           C  
ANISOU 1952  CD  LYS F 338     9280   8773   9983   2047   1007    232       C  
ATOM   1953  CE  LYS F 338      -2.095  31.937   9.524  1.00 80.39           C  
ANISOU 1953  CE  LYS F 338    10283   9351  10908   2231   1352     99       C  
ATOM   1954  NZ  LYS F 338      -1.238  33.136   9.767  1.00 84.58           N  
ANISOU 1954  NZ  LYS F 338    11814   9143  11179   2181   1468    278       N  
ATOM   1955  N   TYR F 339       0.155  26.843   5.889  1.00 48.23           N  
ANISOU 1955  N   TYR F 339     5701   6244   6377    889    485      7       N  
ATOM   1956  CA  TYR F 339       0.869  26.281   4.753  1.00 48.04           C  
ANISOU 1956  CA  TYR F 339     5909   6317   6026    946    376    -20       C  
ATOM   1957  C   TYR F 339       0.490  24.838   4.425  1.00 48.18           C  
ANISOU 1957  C   TYR F 339     6003   6354   5948    803    139   -288       C  
ATOM   1958  O   TYR F 339       0.387  24.484   3.254  1.00 48.79           O  
ANISOU 1958  O   TYR F 339     6270   6552   5715    897    -85   -368       O  
ATOM   1959  CB  TYR F 339       2.378  26.384   5.004  1.00 47.55           C  
ANISOU 1959  CB  TYR F 339     5965   6250   5849    905    664     38       C  
ATOM   1960  CG  TYR F 339       2.990  27.767   4.807  1.00 46.47           C  
ANISOU 1960  CG  TYR F 339     5966   6115   5575    815    887    299       C  
ATOM   1961  CD1 TYR F 339       2.946  28.405   3.577  1.00 49.12           C  
ANISOU 1961  CD1 TYR F 339     6610   6502   5552    891    862    473       C  
ATOM   1962  CD2 TYR F 339       3.657  28.397   5.843  1.00 45.99           C  
ANISOU 1962  CD2 TYR F 339     5881   5953   5637    549   1099    372       C  
ATOM   1963  CE1 TYR F 339       3.539  29.638   3.403  1.00 52.21           C  
ANISOU 1963  CE1 TYR F 339     7371   6763   5703    636   1096    740       C  
ATOM   1964  CE2 TYR F 339       4.253  29.626   5.676  1.00 47.77           C  
ANISOU 1964  CE2 TYR F 339     6393   6100   5657    247   1302    591       C  
ATOM   1965  CZ  TYR F 339       4.191  30.238   4.459  1.00 51.20           C  
ANISOU 1965  CZ  TYR F 339     7220   6508   5725    258   1326    787       C  
ATOM   1966  OH  TYR F 339       4.792  31.461   4.311  1.00 56.82           O  
ANISOU 1966  OH  TYR F 339     8444   7014   6130   -209   1557   1036       O  
ATOM   1967  N   ARG F 340       0.278  24.004   5.441  1.00 49.71           N  
ANISOU 1967  N   ARG F 340     6230   6349   6309    511    180   -427       N  
ATOM   1968  CA  ARG F 340      -0.189  22.623   5.204  1.00 57.31           C  
ANISOU 1968  CA  ARG F 340     7524   7149   7102    197    -55   -678       C  
ATOM   1969  C   ARG F 340      -1.653  22.573   4.734  1.00 64.16           C  
ANISOU 1969  C   ARG F 340     8004   8363   8010   -178   -340   -794       C  
ATOM   1970  O   ARG F 340      -1.987  21.781   3.849  1.00 71.38           O  
ANISOU 1970  O   ARG F 340     9198   9284   8637   -395   -668   -991       O  
ATOM   1971  CB  ARG F 340      -0.029  21.739   6.439  1.00 58.25           C  
ANISOU 1971  CB  ARG F 340     8032   6840   7261   -109     59   -747       C  
ATOM   1972  CG  ARG F 340       1.403  21.500   6.890  1.00 58.81           C  
ANISOU 1972  CG  ARG F 340     8471   6653   7219    355    159   -707       C  
ATOM   1973  CD  ARG F 340       1.394  20.828   8.254  1.00 61.46           C  
ANISOU 1973  CD  ARG F 340     9270   6534   7547     85    197   -699       C  
ATOM   1974  NE  ARG F 340       2.737  20.545   8.750  1.00 64.21           N  
ANISOU 1974  NE  ARG F 340     9926   6717   7752    657    145   -681       N  
ATOM   1975  CZ  ARG F 340       3.451  19.468   8.441  1.00 67.53           C  
ANISOU 1975  CZ  ARG F 340    11003   6810   7844   1168    -76   -848       C  
ATOM   1976  NH1 ARG F 340       2.962  18.549   7.626  1.00 73.64           N  
ANISOU 1976  NH1 ARG F 340    12392   7232   8354   1063   -240  -1048       N  
ATOM   1977  NH2 ARG F 340       4.661  19.303   8.956  1.00 69.84           N  
ANISOU 1977  NH2 ARG F 340    11362   7146   8025   1840   -177   -853       N  
ATOM   1978  N   GLN F 341      -2.522  23.396   5.324  1.00 66.30           N  
ANISOU 1978  N   GLN F 341     7614   8983   8594   -226   -239   -721       N  
ATOM   1979  CA  GLN F 341      -3.925  23.483   4.873  1.00 75.87           C  
ANISOU 1979  CA  GLN F 341     8148  10810   9866   -431   -548   -867       C  
ATOM   1980  C   GLN F 341      -3.979  23.831   3.375  1.00 77.61           C  
ANISOU 1980  C   GLN F 341     8428  11261   9798     -3  -1020   -832       C  
ATOM   1981  O   GLN F 341      -4.545  23.107   2.574  1.00 79.78           O  
ANISOU 1981  O   GLN F 341     8711  11771   9828   -355  -1449  -1042       O  
ATOM   1982  CB  GLN F 341      -4.697  24.576   5.627  1.00 79.03           C  
ANISOU 1982  CB  GLN F 341     7777  11641  10609   -133   -333   -809       C  
ATOM   1983  CG  GLN F 341      -4.875  24.439   7.135  1.00 80.65           C  
ANISOU 1983  CG  GLN F 341     7844  11769  11028   -537    184   -862       C  
ATOM   1984  CD  GLN F 341      -5.345  25.759   7.769  1.00 84.22           C  
ANISOU 1984  CD  GLN F 341     7770  12505  11723     79    458   -811       C  
ATOM   1985  OE1 GLN F 341      -4.902  26.141   8.856  1.00 82.05           O  
ANISOU 1985  OE1 GLN F 341     7781  11876  11518    111    894   -739       O  
ATOM   1986  NE2 GLN F 341      -6.234  26.470   7.072  1.00 87.82           N  
ANISOU 1986  NE2 GLN F 341     7558  13569  12240    665    143   -869       N  
ATOM   1987  N   LYS F 342      -3.351  24.957   3.044  1.00 76.72           N  
ANISOU 1987  N   LYS F 342     8494  11018   9634    664   -929   -557       N  
ATOM   1988  CA  LYS F 342      -3.299  25.548   1.703  1.00 79.34           C  
ANISOU 1988  CA  LYS F 342     9089  11467   9588   1132  -1293   -416       C  
ATOM   1989  C   LYS F 342      -2.971  24.566   0.570  1.00 83.02           C  
ANISOU 1989  C   LYS F 342    10094  11880   9567    907  -1570   -585       C  
ATOM   1990  O   LYS F 342      -3.588  24.617  -0.508  1.00 86.79           O  
ANISOU 1990  O   LYS F 342    10597  12677   9700   1026  -2103   -629       O  
ATOM   1991  CB  LYS F 342      -2.234  26.651   1.724  1.00 75.44           C  
ANISOU 1991  CB  LYS F 342     9076  10587   9001   1535   -930    -78       C  
ATOM   1992  CG  LYS F 342      -2.385  27.745   0.695  1.00 81.29           C  
ANISOU 1992  CG  LYS F 342    10185  11335   9367   2066  -1217    193       C  
ATOM   1993  CD  LYS F 342      -1.764  29.039   1.211  1.00 80.20           C  
ANISOU 1993  CD  LYS F 342    10450  10755   9266   2293   -835    510       C  
ATOM   1994  CE  LYS F 342      -1.514  30.036   0.090  1.00 86.91           C  
ANISOU 1994  CE  LYS F 342    12130  11360   9532   2626  -1003    856       C  
ATOM   1995  NZ  LYS F 342      -2.572  30.053  -0.962  1.00 93.49           N  
ANISOU 1995  NZ  LYS F 342    12967  12508  10046   3127  -1723    854       N  
ATOM   1996  N   PHE F 343      -1.989  23.695   0.813  1.00 79.76           N  
ANISOU 1996  N   PHE F 343    10175  11066   9063    690  -1246   -701       N  
ATOM   1997  CA  PHE F 343      -1.477  22.787  -0.217  1.00 82.69           C  
ANISOU 1997  CA  PHE F 343    11237  11281   8900    663  -1382   -909       C  
ATOM   1998  C   PHE F 343      -1.576  21.326   0.237  1.00 82.89           C  
ANISOU 1998  C   PHE F 343    11644  10945   8905    165  -1434  -1251       C  
ATOM   1999  O   PHE F 343      -2.663  20.732   0.222  1.00 83.03           O  
ANISOU 1999  O   PHE F 343    11535  11089   8922   -445  -1821  -1459       O  
ATOM   2000  CB  PHE F 343      -0.026  23.149  -0.586  1.00 79.96           C  
ANISOU 2000  CB  PHE F 343    11292  10807   8279   1102   -917   -768       C  
ATOM   2001  CG  PHE F 343       0.230  24.644  -0.717  1.00 79.30           C  
ANISOU 2001  CG  PHE F 343    11042  10876   8211   1363   -725   -372       C  
ATOM   2002  CD1 PHE F 343      -0.257  25.366  -1.812  1.00 84.07           C  
ANISOU 2002  CD1 PHE F 343    11893  11644   8403   1559  -1057   -193       C  
ATOM   2003  CD2 PHE F 343       0.978  25.326   0.252  1.00 74.58           C  
ANISOU 2003  CD2 PHE F 343    10219  10175   7943   1373   -266   -175       C  
ATOM   2004  CE1 PHE F 343      -0.013  26.731  -1.932  1.00 84.95           C  
ANISOU 2004  CE1 PHE F 343    12180  11683   8411   1770   -898    202       C  
ATOM   2005  CE2 PHE F 343       1.226  26.687   0.143  1.00 76.16           C  
ANISOU 2005  CE2 PHE F 343    10519  10351   8067   1461    -93    174       C  
ATOM   2006  CZ  PHE F 343       0.727  27.393  -0.952  1.00 82.87           C  
ANISOU 2006  CZ  PHE F 343    11772  11231   8482   1665   -390    379       C  
TER    2007      PHE F 343                                                      
ATOM   2008  N   GLU G 302      -3.302  12.063  -2.257  1.00133.16           N  
ANISOU 2008  N   GLU G 302    14425  14987  21179   6390 -11005  -5293       N  
ATOM   2009  CA  GLU G 302      -1.867  11.893  -2.609  1.00126.29           C  
ANISOU 2009  CA  GLU G 302    14701  13817  19464   6158 -10325  -4049       C  
ATOM   2010  C   GLU G 302      -1.420  10.451  -2.358  1.00119.74           C  
ANISOU 2010  C   GLU G 302    13699  13260  18536   5289  -9672  -4128       C  
ATOM   2011  O   GLU G 302      -1.988   9.749  -1.520  1.00118.70           O  
ANISOU 2011  O   GLU G 302    12627  13377  19097   4564  -9385  -4846       O  
ATOM   2012  CB  GLU G 302      -1.002  12.867  -1.802  1.00120.97           C  
ANISOU 2012  CB  GLU G 302    14315  12681  18965   5832  -9601  -3235       C  
ATOM   2013  CG  GLU G 302       0.397  13.066  -2.367  1.00118.33           C  
ANISOU 2013  CG  GLU G 302    15154  12007  17797   5816  -9074  -1973       C  
ATOM   2014  CD  GLU G 302       1.241  13.992  -1.523  1.00115.12           C  
ANISOU 2014  CD  GLU G 302    14879  11127  17733   5394  -8382  -1321       C  
ATOM   2015  OE1 GLU G 302       0.667  14.737  -0.703  1.00117.34           O  
ANISOU 2015  OE1 GLU G 302    14555  11237  18789   5411  -8543  -1791       O  
ATOM   2016  OE2 GLU G 302       2.485  13.963  -1.666  1.00111.88           O  
ANISOU 2016  OE2 GLU G 302    15101  10557  16850   5051  -7688   -436       O  
ATOM   2017  N   GLU G 303      -0.406  10.020  -3.100  1.00116.08           N  
ANISOU 2017  N   GLU G 303    14178  12734  17191   5385  -9430  -3382       N  
ATOM   2018  CA  GLU G 303       0.145   8.673  -2.985  1.00109.69           C  
ANISOU 2018  CA  GLU G 303    13397  12081  16198   4738  -8919  -3411       C  
ATOM   2019  C   GLU G 303       0.761   8.462  -1.572  1.00 99.85           C  
ANISOU 2019  C   GLU G 303    11785  10716  15436   3732  -7879  -3138       C  
ATOM   2020  O   GLU G 303       1.701   9.157  -1.169  1.00 94.42           O  
ANISOU 2020  O   GLU G 303    11470   9817  14586   3614  -7302  -2369       O  
ATOM   2021  CB  GLU G 303       1.160   8.464  -4.121  1.00110.76           C  
ANISOU 2021  CB  GLU G 303    14629  12251  15203   5240  -8900  -2684       C  
ATOM   2022  CG  GLU G 303       1.847   7.107  -4.166  1.00108.33           C  
ANISOU 2022  CG  GLU G 303    14492  12076  14591   4797  -8493  -2728       C  
ATOM   2023  CD  GLU G 303       1.117   6.050  -4.962  1.00114.41           C  
ANISOU 2023  CD  GLU G 303    15135  13071  15264   5103  -9280  -3629       C  
ATOM   2024  OE1 GLU G 303       0.341   6.405  -5.865  1.00123.64           O  
ANISOU 2024  OE1 GLU G 303    16370  14419  16188   5925 -10198  -4049       O  
ATOM   2025  OE2 GLU G 303       1.351   4.853  -4.689  1.00112.23           O  
ANISOU 2025  OE2 GLU G 303    14737  12748  15155   4562  -9033  -3938       O  
ATOM   2026  N   ILE G 304       0.187   7.520  -0.823  1.00 96.74           N  
ANISOU 2026  N   ILE G 304    10657  10453  15646   3013  -7672  -3798       N  
ATOM   2027  CA  ILE G 304       0.536   7.285   0.569  1.00 88.93           C  
ANISOU 2027  CA  ILE G 304     9301   9417  15072   2134  -6783  -3644       C  
ATOM   2028  C   ILE G 304       1.431   6.062   0.622  1.00 84.34           C  
ANISOU 2028  C   ILE G 304     9222   8719  14103   1691  -6322  -3316       C  
ATOM   2029  O   ILE G 304       1.205   5.100  -0.101  1.00 86.99           O  
ANISOU 2029  O   ILE G 304     9710   9048  14292   1761  -6719  -3674       O  
ATOM   2030  CB  ILE G 304      -0.712   7.014   1.433  1.00 92.53           C  
ANISOU 2030  CB  ILE G 304     8657  10101  16398   1562  -6738  -4522       C  
ATOM   2031  CG1 ILE G 304      -1.804   8.066   1.177  1.00 99.81           C  
ANISOU 2031  CG1 ILE G 304     8952  11221  17750   2180  -7444  -5155       C  
ATOM   2032  CG2 ILE G 304      -0.364   6.979   2.911  1.00 86.90           C  
ANISOU 2032  CG2 ILE G 304     7654   9416  15946    785  -5799  -4284       C  
ATOM   2033  CD1 ILE G 304      -1.374   9.497   1.451  1.00 97.90           C  
ANISOU 2033  CD1 ILE G 304     8957  10798  17439   2652  -7391  -4658       C  
ATOM   2034  N   PHE G 305       2.452   6.106   1.475  1.00 76.46           N  
ANISOU 2034  N   PHE G 305     8475   7617  12958   1311  -5569  -2718       N  
ATOM   2035  CA  PHE G 305       3.378   5.001   1.591  1.00 72.73           C  
ANISOU 2035  CA  PHE G 305     8511   7014  12107   1016  -5187  -2421       C  
ATOM   2036  C   PHE G 305       3.573   4.607   3.039  1.00 69.07           C  
ANISOU 2036  C   PHE G 305     7814   6482  11948    276  -4485  -2328       C  
ATOM   2037  O   PHE G 305       3.229   5.358   3.938  1.00 67.74           O  
ANISOU 2037  O   PHE G 305     7143   6444  12148     56  -4198  -2387       O  
ATOM   2038  CB  PHE G 305       4.709   5.390   0.982  1.00 69.62           C  
ANISOU 2038  CB  PHE G 305     8831   6633  10987   1498  -5026  -1728       C  
ATOM   2039  CG  PHE G 305       4.691   5.482  -0.507  1.00 74.17           C  
ANISOU 2039  CG  PHE G 305     9865   7326  10988   2231  -5612  -1711       C  
ATOM   2040  CD1 PHE G 305       4.860   4.347  -1.279  1.00 76.97           C  
ANISOU 2040  CD1 PHE G 305    10595   7726  10922   2430  -5903  -1962       C  
ATOM   2041  CD2 PHE G 305       4.524   6.704  -1.133  1.00 77.40           C  
ANISOU 2041  CD2 PHE G 305    10410   7774  11223   2776  -5897  -1439       C  
ATOM   2042  CE1 PHE G 305       4.853   4.421  -2.659  1.00 82.65           C  
ANISOU 2042  CE1 PHE G 305    11771   8663  10967   3197  -6450  -1992       C  
ATOM   2043  CE2 PHE G 305       4.523   6.794  -2.512  1.00 83.80           C  
ANISOU 2043  CE2 PHE G 305    11771   8736  11330   3520  -6418  -1340       C  
ATOM   2044  CZ  PHE G 305       4.684   5.645  -3.280  1.00 86.21           C  
ANISOU 2044  CZ  PHE G 305    12403   9223  11128   3748  -6685  -1642       C  
ATOM   2045  N   THR G 306       4.153   3.430   3.247  1.00 68.33           N  
ANISOU 2045  N   THR G 306     8152   6180  11629    -16  -4252  -2192       N  
ATOM   2046  CA  THR G 306       4.408   2.920   4.584  1.00 67.09           C  
ANISOU 2046  CA  THR G 306     7990   5910  11589   -636  -3626  -2010       C  
ATOM   2047  C   THR G 306       5.862   2.416   4.763  1.00 62.42           C  
ANISOU 2047  C   THR G 306     8120   5177  10418   -448  -3361  -1506       C  
ATOM   2048  O   THR G 306       6.425   1.800   3.867  1.00 62.45           O  
ANISOU 2048  O   THR G 306     8622   5064  10042    -73  -3660  -1480       O  
ATOM   2049  CB  THR G 306       3.396   1.800   4.926  1.00 73.65           C  
ANISOU 2049  CB  THR G 306     8583   6504  12894  -1342  -3599  -2434       C  
ATOM   2050  OG1 THR G 306       3.650   1.301   6.238  1.00 74.65           O  
ANISOU 2050  OG1 THR G 306     8864   6500  12997  -1928  -2940  -2123       O  
ATOM   2051  CG2 THR G 306       3.462   0.631   3.944  1.00 77.78           C  
ANISOU 2051  CG2 THR G 306     9589   6649  13313  -1229  -4092  -2652       C  
ATOM   2052  N   LEU G 307       6.441   2.674   5.933  1.00 58.78           N  
ANISOU 2052  N   LEU G 307     7662   4792   9878   -641  -2846  -1210       N  
ATOM   2053  CA  LEU G 307       7.788   2.182   6.303  1.00 56.53           C  
ANISOU 2053  CA  LEU G 307     7955   4425   9099   -435  -2631   -852       C  
ATOM   2054  C   LEU G 307       7.761   1.572   7.673  1.00 56.00           C  
ANISOU 2054  C   LEU G 307     8038   4219   9020   -894  -2218   -728       C  
ATOM   2055  O   LEU G 307       7.315   2.217   8.610  1.00 54.97           O  
ANISOU 2055  O   LEU G 307     7471   4332   9082  -1177  -1879   -758       O  
ATOM   2056  CB  LEU G 307       8.808   3.343   6.378  1.00 53.38           C  
ANISOU 2056  CB  LEU G 307     7429   4341   8511    -42  -2455   -603       C  
ATOM   2057  CG  LEU G 307       9.383   3.918   5.082  1.00 54.28           C  
ANISOU 2057  CG  LEU G 307     7646   4594   8381    468  -2679   -469       C  
ATOM   2058  CD1 LEU G 307      10.322   5.072   5.392  1.00 51.95           C  
ANISOU 2058  CD1 LEU G 307     7144   4505   8088    612  -2377   -217       C  
ATOM   2059  CD2 LEU G 307      10.090   2.794   4.313  1.00 55.88           C  
ANISOU 2059  CD2 LEU G 307     8408   4733   8091    798  -2868   -476       C  
ATOM   2060  N   GLN G 308       8.297   0.368   7.802  1.00 58.33           N  
ANISOU 2060  N   GLN G 308     9008   4133   9019   -881  -2263   -583       N  
ATOM   2061  CA  GLN G 308       8.509  -0.229   9.120  1.00 61.58           C  
ANISOU 2061  CA  GLN G 308     9810   4367   9218  -1169  -1890   -315       C  
ATOM   2062  C   GLN G 308       9.855   0.260   9.697  1.00 57.57           C  
ANISOU 2062  C   GLN G 308     9452   4173   8246   -617  -1787   -133       C  
ATOM   2063  O   GLN G 308      10.886   0.161   9.040  1.00 55.76           O  
ANISOU 2063  O   GLN G 308     9449   3984   7753    -54  -2050   -151       O  
ATOM   2064  CB  GLN G 308       8.501  -1.749   9.037  1.00 67.00           C  
ANISOU 2064  CB  GLN G 308    11278   4357   9821  -1345  -2067   -220       C  
ATOM   2065  CG  GLN G 308       7.298  -2.333   8.314  1.00 73.43           C  
ANISOU 2065  CG  GLN G 308    11917   4793  11191  -1872  -2281   -535       C  
ATOM   2066  CD  GLN G 308       6.014  -2.287   9.126  1.00 78.13           C  
ANISOU 2066  CD  GLN G 308    12032   5410  12243  -2777  -1792   -566       C  
ATOM   2067  OE1 GLN G 308       5.710  -3.219   9.872  1.00 85.35           O  
ANISOU 2067  OE1 GLN G 308    13411   5829  13188  -3379  -1471   -298       O  
ATOM   2068  NE2 GLN G 308       5.234  -1.234   8.942  1.00 76.10           N  
ANISOU 2068  NE2 GLN G 308    10860   5704  12350  -2874  -1734   -904       N  
ATOM   2069  N   VAL G 309       9.822   0.781  10.920  1.00 56.96           N  
ANISOU 2069  N   VAL G 309     9181   4384   8077   -769  -1408    -46       N  
ATOM   2070  CA  VAL G 309      10.979   1.358  11.562  1.00 54.05           C  
ANISOU 2070  CA  VAL G 309     8795   4368   7374   -276  -1361    -27       C  
ATOM   2071  C   VAL G 309      11.255   0.541  12.817  1.00 59.45           C  
ANISOU 2071  C   VAL G 309    10134   4915   7538   -270  -1190    218       C  
ATOM   2072  O   VAL G 309      10.354   0.341  13.630  1.00 65.36           O  
ANISOU 2072  O   VAL G 309    10933   5641   8257   -792   -816    361       O  
ATOM   2073  CB  VAL G 309      10.705   2.823  11.944  1.00 51.14           C  
ANISOU 2073  CB  VAL G 309     7623   4483   7324   -334  -1166   -244       C  
ATOM   2074  CG1 VAL G 309      11.908   3.441  12.622  1.00 49.51           C  
ANISOU 2074  CG1 VAL G 309     7312   4613   6886    135  -1168   -348       C  
ATOM   2075  CG2 VAL G 309      10.318   3.633  10.723  1.00 48.60           C  
ANISOU 2075  CG2 VAL G 309     6808   4180   7475   -322  -1365   -386       C  
ATOM   2076  N   ARG G 310      12.483   0.052  12.964  1.00 59.60           N  
ANISOU 2076  N   ARG G 310    10666   4871   7107    342  -1457    260       N  
ATOM   2077  CA  ARG G 310      12.885  -0.710  14.136  1.00 64.85           C  
ANISOU 2077  CA  ARG G 310    12098   5384   7158    552  -1426    512       C  
ATOM   2078  C   ARG G 310      13.378   0.231  15.224  1.00 64.20           C  
ANISOU 2078  C   ARG G 310    11639   5942   6809    863  -1287    325       C  
ATOM   2079  O   ARG G 310      14.243   1.045  14.968  1.00 62.72           O  
ANISOU 2079  O   ARG G 310    10898   6151   6780   1297  -1481    -40       O  
ATOM   2080  CB  ARG G 310      13.991  -1.686  13.758  1.00 67.20           C  
ANISOU 2080  CB  ARG G 310    13103   5320   7106   1232  -1927    510       C  
ATOM   2081  CG  ARG G 310      13.566  -2.647  12.676  1.00 70.00           C  
ANISOU 2081  CG  ARG G 310    13857   5020   7718   1026  -2161    572       C  
ATOM   2082  CD  ARG G 310      14.645  -3.657  12.338  1.00 74.22           C  
ANISOU 2082  CD  ARG G 310    15113   5185   7899   1799  -2711    473       C  
ATOM   2083  NE  ARG G 310      14.156  -4.575  11.322  1.00 77.71           N  
ANISOU 2083  NE  ARG G 310    15934   4966   8623   1604  -2981    437       N  
ATOM   2084  CZ  ARG G 310      13.639  -5.777  11.563  1.00 86.10           C  
ANISOU 2084  CZ  ARG G 310    17914   5115   9686   1299  -3102    733       C  
ATOM   2085  NH1 ARG G 310      13.555  -6.261  12.805  1.00 92.54           N  
ANISOU 2085  NH1 ARG G 310    19489   5553  10116   1159  -2920   1221       N  
ATOM   2086  NH2 ARG G 310      13.224  -6.520  10.548  1.00 88.54           N  
ANISOU 2086  NH2 ARG G 310    18437   4846  10357   1152  -3427    539       N  
ATOM   2087  N   GLY G 311      12.822   0.135  16.432  1.00 68.82           N  
ANISOU 2087  N   GLY G 311    12498   6653   6998    618   -928    541       N  
ATOM   2088  CA  GLY G 311      13.223   0.991  17.546  1.00 69.32           C  
ANISOU 2088  CA  GLY G 311    12239   7375   6723    982   -843    271       C  
ATOM   2089  C   GLY G 311      12.475   2.312  17.622  1.00 67.76           C  
ANISOU 2089  C   GLY G 311    11013   7677   7052    616   -542    -99       C  
ATOM   2090  O   GLY G 311      12.151   2.928  16.608  1.00 60.11           O  
ANISOU 2090  O   GLY G 311     9404   6641   6791    374   -599   -285       O  
ATOM   2091  N   ARG G 312      12.237   2.761  18.848  1.00 45.56           N  
ANISOU 2091  N   ARG G 312     4080   7244   5986    -23    928    573       N  
ATOM   2092  CA  ARG G 312      11.375   3.891  19.116  1.00 51.31           C  
ANISOU 2092  CA  ARG G 312     5072   7908   6515    282   1213    644       C  
ATOM   2093  C   ARG G 312      12.109   5.213  18.863  1.00 51.30           C  
ANISOU 2093  C   ARG G 312     5611   7854   6026    159    850    240       C  
ATOM   2094  O   ARG G 312      11.513   6.182  18.377  1.00 50.22           O  
ANISOU 2094  O   ARG G 312     5561   7647   5871    241    923    164       O  
ATOM   2095  CB  ARG G 312      10.866   3.841  20.557  1.00 59.26           C  
ANISOU 2095  CB  ARG G 312     6483   8875   7157    887   1793   1033       C  
ATOM   2096  CG  ARG G 312       9.949   4.996  20.942  1.00 65.50           C  
ANISOU 2096  CG  ARG G 312     7767   9530   7589   1495   2320   1243       C  
ATOM   2097  CD  ARG G 312       9.673   5.019  22.439  1.00 75.13           C  
ANISOU 2097  CD  ARG G 312     9831  10608   8104   2367   2986   1622       C  
ATOM   2098  NE  ARG G 312       8.427   4.341  22.796  1.00 82.48           N  
ANISOU 2098  NE  ARG G 312    10041  11620   9678   2926   3919   2577       N  
ATOM   2099  CZ  ARG G 312       8.318   3.062  23.166  1.00 86.25           C  
ANISOU 2099  CZ  ARG G 312     9864  12206  10699   2887   4115   3053       C  
ATOM   2100  NH1 ARG G 312       9.383   2.253  23.236  1.00 83.16           N  
ANISOU 2100  NH1 ARG G 312     9511  11890  10196   2365   3510   2586       N  
ATOM   2101  NH2 ARG G 312       7.119   2.580  23.467  1.00 92.93           N  
ANISOU 2101  NH2 ARG G 312     9918  13067  12324   3398   4950   4157       N  
ATOM   2102  N   GLU G 313      13.379   5.267  19.234  1.00 52.05           N  
ANISOU 2102  N   GLU G 313     6012   7935   5827    -57    400    104       N  
ATOM   2103  CA  GLU G 313      14.156   6.484  19.026  1.00 55.45           C  
ANISOU 2103  CA  GLU G 313     6842   8211   6016   -294   -146    -84       C  
ATOM   2104  C   GLU G 313      14.292   6.764  17.523  1.00 48.79           C  
ANISOU 2104  C   GLU G 313     5427   7487   5622   -550   -198   -158       C  
ATOM   2105  O   GLU G 313      14.166   7.909  17.088  1.00 50.15           O  
ANISOU 2105  O   GLU G 313     5802   7544   5706   -597   -348   -294       O  
ATOM   2106  CB  GLU G 313      15.514   6.417  19.749  1.00 59.97           C  
ANISOU 2106  CB  GLU G 313     7684   8656   6444   -579   -819     49       C  
ATOM   2107  CG  GLU G 313      16.560   7.445  19.292  1.00 67.18           C  
ANISOU 2107  CG  GLU G 313     8587   9380   7556  -1038  -1592    155       C  
ATOM   2108  CD  GLU G 313      16.205   8.928  19.519  1.00 73.12           C  
ANISOU 2108  CD  GLU G 313    10240   9701   7841   -995  -1999    -96       C  
ATOM   2109  OE1 GLU G 313      15.237   9.447  18.911  1.00 73.60           O  
ANISOU 2109  OE1 GLU G 313    10299   9831   7832   -740  -1485   -327       O  
ATOM   2110  OE2 GLU G 313      16.931   9.602  20.286  1.00 81.65           O  
ANISOU 2110  OE2 GLU G 313    12100  10280   8641  -1242  -2964    -20       O  
ATOM   2111  N   ARG G 314      14.478   5.712  16.734  1.00 43.27           N  
ANISOU 2111  N   ARG G 314     4189   6945   5306   -607    -43    -67       N  
ATOM   2112  CA  ARG G 314      14.680   5.859  15.312  1.00 40.01           C  
ANISOU 2112  CA  ARG G 314     3526   6553   5121   -643    -37   -102       C  
ATOM   2113  C   ARG G 314      13.394   6.310  14.665  1.00 40.42           C  
ANISOU 2113  C   ARG G 314     3620   6509   5227   -556     71   -307       C  
ATOM   2114  O   ARG G 314      13.413   7.159  13.774  1.00 39.76           O  
ANISOU 2114  O   ARG G 314     3572   6393   5140   -570      0   -409       O  
ATOM   2115  CB  ARG G 314      15.189   4.562  14.699  1.00 39.29           C  
ANISOU 2115  CB  ARG G 314     3246   6486   5194   -520    109     48       C  
ATOM   2116  CG  ARG G 314      15.378   4.615  13.197  1.00 39.70           C  
ANISOU 2116  CG  ARG G 314     3396   6437   5250   -294    211     40       C  
ATOM   2117  CD  ARG G 314      15.814   3.266  12.657  1.00 43.12           C  
ANISOU 2117  CD  ARG G 314     4032   6731   5618     41    402    177       C  
ATOM   2118  NE  ARG G 314      17.100   2.863  13.203  1.00 43.64           N  
ANISOU 2118  NE  ARG G 314     3781   7002   5796    119    617    662       N  
ATOM   2119  CZ  ARG G 314      17.639   1.654  13.075  1.00 45.12           C  
ANISOU 2119  CZ  ARG G 314     4105   7115   5923    464    892    900       C  
ATOM   2120  NH1 ARG G 314      17.025   0.709  12.384  1.00 46.24           N  
ANISOU 2120  NH1 ARG G 314     4892   6873   5802    762    876    615       N  
ATOM   2121  NH2 ARG G 314      18.832   1.412  13.602  1.00 45.54           N  
ANISOU 2121  NH2 ARG G 314     3706   7389   6205    519   1093   1503       N  
ATOM   2122  N   TYR G 315      12.277   5.744  15.106  1.00 41.65           N  
ANISOU 2122  N   TYR G 315     3674   6607   5542   -461    239   -222       N  
ATOM   2123  CA  TYR G 315      10.980   6.192  14.633  1.00 43.25           C  
ANISOU 2123  CA  TYR G 315     3734   6696   6000   -404    296   -161       C  
ATOM   2124  C   TYR G 315      10.769   7.676  14.932  1.00 43.44           C  
ANISOU 2124  C   TYR G 315     4055   6741   5708   -256    455   -246       C  
ATOM   2125  O   TYR G 315      10.310   8.408  14.074  1.00 42.53           O  
ANISOU 2125  O   TYR G 315     3889   6573   5695   -281    386   -327       O  
ATOM   2126  CB  TYR G 315       9.845   5.362  15.217  1.00 46.25           C  
ANISOU 2126  CB  TYR G 315     3731   6993   6849   -310    485    291       C  
ATOM   2127  CG  TYR G 315       8.475   5.948  14.944  1.00 50.15           C  
ANISOU 2127  CG  TYR G 315     3879   7381   7794   -209    607    672       C  
ATOM   2128  CD1 TYR G 315       7.833   5.729  13.735  1.00 51.80           C  
ANISOU 2128  CD1 TYR G 315     3819   7328   8532   -498     54    748       C  
ATOM   2129  CD2 TYR G 315       7.826   6.709  15.899  1.00 55.21           C  
ANISOU 2129  CD2 TYR G 315     4572   8105   8298    258   1258   1045       C  
ATOM   2130  CE1 TYR G 315       6.578   6.261  13.476  1.00 56.89           C  
ANISOU 2130  CE1 TYR G 315     3994   7859   9759   -463     72   1270       C  
ATOM   2131  CE2 TYR G 315       6.572   7.248  15.665  1.00 60.29           C  
ANISOU 2131  CE2 TYR G 315     4777   8675   9454    461   1521   1612       C  
ATOM   2132  CZ  TYR G 315       5.947   7.021  14.451  1.00 61.40           C  
ANISOU 2132  CZ  TYR G 315     4385   8619  10325     28    891   1769       C  
ATOM   2133  OH  TYR G 315       4.696   7.546  14.222  1.00 68.67           O  
ANISOU 2133  OH  TYR G 315     4715   9453  11923    175   1067   2503       O  
ATOM   2134  N   GLU G 316      11.115   8.110  16.137  1.00 46.77           N  
ANISOU 2134  N   GLU G 316     4953   7147   5670    -67    589   -240       N  
ATOM   2135  CA  GLU G 316      10.985   9.512  16.513  1.00 50.83           C  
ANISOU 2135  CA  GLU G 316     6106   7495   5710    148    624   -361       C  
ATOM   2136  C   GLU G 316      11.837  10.414  15.617  1.00 46.82           C  
ANISOU 2136  C   GLU G 316     5644   6942   5201   -211    136   -624       C  
ATOM   2137  O   GLU G 316      11.376  11.457  15.193  1.00 45.18           O  
ANISOU 2137  O   GLU G 316     5617   6637   4913   -123    181   -716       O  
ATOM   2138  CB  GLU G 316      11.386   9.732  17.977  1.00 58.48           C  
ANISOU 2138  CB  GLU G 316     7986   8240   5993    447    592   -363       C  
ATOM   2139  CG  GLU G 316      10.258   9.611  18.981  1.00 66.37           C  
ANISOU 2139  CG  GLU G 316     9365   9154   6697   1209   1375      9       C  
ATOM   2140  CD  GLU G 316      10.677  10.070  20.374  1.00 77.42           C  
ANISOU 2140  CD  GLU G 316    12186  10146   7084   1699   1276    -84       C  
ATOM   2141  OE1 GLU G 316      11.805   9.721  20.797  1.00 79.06           O  
ANISOU 2141  OE1 GLU G 316    12682  10254   7104   1307    571   -282       O  
ATOM   2142  OE2 GLU G 316       9.884  10.785  21.048  1.00 86.76           O  
ANISOU 2142  OE2 GLU G 316    14314  11033   7618   2547   1876    102       O  
ATOM   2143  N   ILE G 317      13.075  10.002  15.352  1.00 44.36           N  
ANISOU 2143  N   ILE G 317     5101   6702   5049   -551   -246   -597       N  
ATOM   2144  CA  ILE G 317      13.961  10.733  14.444  1.00 43.53           C  
ANISOU 2144  CA  ILE G 317     4811   6580   5149   -817   -576   -549       C  
ATOM   2145  C   ILE G 317      13.367  10.781  13.033  1.00 39.81           C  
ANISOU 2145  C   ILE G 317     4004   6223   4897   -704   -299   -635       C  
ATOM   2146  O   ILE G 317      13.267  11.836  12.425  1.00 38.30           O  
ANISOU 2146  O   ILE G 317     3883   5961   4706   -722   -361   -696       O  
ATOM   2147  CB  ILE G 317      15.367  10.105  14.390  1.00 44.69           C  
ANISOU 2147  CB  ILE G 317     4558   6815   5606  -1045   -826   -176       C  
ATOM   2148  CG1 ILE G 317      16.094  10.388  15.701  1.00 49.03           C  
ANISOU 2148  CG1 ILE G 317     5524   7106   5997  -1299  -1457    -26       C  
ATOM   2149  CG2 ILE G 317      16.164  10.669  13.217  1.00 48.09           C  
ANISOU 2149  CG2 ILE G 317     4558   7287   6425  -1117   -858    161       C  
ATOM   2150  CD1 ILE G 317      17.339   9.568  15.938  1.00 51.11           C  
ANISOU 2150  CD1 ILE G 317     5297   7464   6659  -1517  -1707    490       C  
ATOM   2151  N   LEU G 318      12.937   9.649  12.521  1.00 37.52           N  
ANISOU 2151  N   LEU G 318     3485   6012   4760   -587   -106   -640       N  
ATOM   2152  CA  LEU G 318      12.406   9.623  11.163  1.00 37.06           C  
ANISOU 2152  CA  LEU G 318     3394   5886   4800   -468    -88   -734       C  
ATOM   2153  C   LEU G 318      11.048  10.317  11.068  1.00 37.59           C  
ANISOU 2153  C   LEU G 318     3458   5871   4952   -444    -70   -814       C  
ATOM   2154  O   LEU G 318      10.712  10.889  10.022  1.00 35.46           O  
ANISOU 2154  O   LEU G 318     3239   5525   4707   -397   -159   -898       O  
ATOM   2155  CB  LEU G 318      12.325   8.202  10.603  1.00 37.47           C  
ANISOU 2155  CB  LEU G 318     3510   5812   4915   -351   -153   -720       C  
ATOM   2156  CG  LEU G 318      13.632   7.465  10.327  1.00 40.46           C  
ANISOU 2156  CG  LEU G 318     3970   6230   5171   -143      9   -529       C  
ATOM   2157  CD1 LEU G 318      13.317   6.063   9.814  1.00 43.41           C  
ANISOU 2157  CD1 LEU G 318     4734   6301   5457     55   -131   -602       C  
ATOM   2158  CD2 LEU G 318      14.524   8.190   9.305  1.00 43.69           C  
ANISOU 2158  CD2 LEU G 318     4445   6673   5481    145    239   -310       C  
ATOM   2159  N   LYS G 319      10.254  10.267  12.127  1.00 40.77           N  
ANISOU 2159  N   LYS G 319     3801   6278   5411   -375    123   -671       N  
ATOM   2160  CA  LYS G 319       8.978  10.965  12.090  1.00 43.94           C  
ANISOU 2160  CA  LYS G 319     4088   6616   5989   -213    318   -491       C  
ATOM   2161  C   LYS G 319       9.194  12.502  12.042  1.00 45.44           C  
ANISOU 2161  C   LYS G 319     4674   6775   5814   -113    401   -683       C  
ATOM   2162  O   LYS G 319       8.435  13.238  11.373  1.00 44.16           O  
ANISOU 2162  O   LYS G 319     4412   6571   5794    -31    460   -629       O  
ATOM   2163  CB  LYS G 319       8.120  10.625  13.285  1.00 47.49           C  
ANISOU 2163  CB  LYS G 319     4402   7067   6572     81    767    -51       C  
ATOM   2164  CG  LYS G 319       6.777  11.337  13.228  1.00 53.16           C  
ANISOU 2164  CG  LYS G 319     4858   7731   7610    394   1147    420       C  
ATOM   2165  CD  LYS G 319       5.944  11.041  14.453  1.00 61.69           C  
ANISOU 2165  CD  LYS G 319     5791   8812   8834    935   1867   1122       C  
ATOM   2166  CE  LYS G 319       4.473  11.367  14.251  1.00 68.20           C  
ANISOU 2166  CE  LYS G 319     5925   9594  10394   1253   2293   2008       C  
ATOM   2167  NZ  LYS G 319       3.672  10.581  15.242  1.00 77.70           N  
ANISOU 2167  NZ  LYS G 319     6585  10806  12128   1715   2961   3017       N  
ATOM   2168  N   LYS G 320      10.197  12.968  12.780  1.00 44.52           N  
ANISOU 2168  N   LYS G 320     5031   6599   5284   -156    285   -841       N  
ATOM   2169  CA  LYS G 320      10.563  14.378  12.780  1.00 48.23           C  
ANISOU 2169  CA  LYS G 320     5996   6877   5451   -167    109   -995       C  
ATOM   2170  C   LYS G 320      11.077  14.845  11.394  1.00 43.18           C  
ANISOU 2170  C   LYS G 320     5019   6311   5077   -402   -107  -1051       C  
ATOM   2171  O   LYS G 320      10.747  15.930  10.928  1.00 42.17           O  
ANISOU 2171  O   LYS G 320     5039   6084   4899   -342    -91  -1115       O  
ATOM   2172  CB  LYS G 320      11.600  14.650  13.878  1.00 53.47           C  
ANISOU 2172  CB  LYS G 320     7306   7277   5732   -298   -328  -1046       C  
ATOM   2173  CG  LYS G 320      12.088  16.090  13.965  1.00 61.00           C  
ANISOU 2173  CG  LYS G 320     8926   7820   6431   -432   -837  -1148       C  
ATOM   2174  CD  LYS G 320      10.956  17.122  13.969  1.00 65.64           C  
ANISOU 2174  CD  LYS G 320    10070   8216   6653     36   -426  -1262       C  
ATOM   2175  CE  LYS G 320      11.480  18.554  13.925  1.00 70.07           C  
ANISOU 2175  CE  LYS G 320    11358   8276   6989   -146  -1047  -1385       C  
ATOM   2176  NZ  LYS G 320      12.436  18.838  15.045  1.00 76.39           N  
ANISOU 2176  NZ  LYS G 320    13189   8458   7376   -371  -1975  -1424       N  
ATOM   2177  N   LEU G 321      11.849  14.006  10.729  1.00 39.52           N  
ANISOU 2177  N   LEU G 321     4176   5996   4844   -536   -200   -959       N  
ATOM   2178  CA  LEU G 321      12.354  14.333   9.407  1.00 39.04           C  
ANISOU 2178  CA  LEU G 321     3920   5981   4933   -507   -200   -870       C  
ATOM   2179  C   LEU G 321      11.214  14.425   8.446  1.00 39.61           C  
ANISOU 2179  C   LEU G 321     4010   6032   5005   -322    -97  -1027       C  
ATOM   2180  O   LEU G 321      11.111  15.381   7.679  1.00 39.22           O  
ANISOU 2180  O   LEU G 321     4009   5945   4944   -255    -78  -1044       O  
ATOM   2181  CB  LEU G 321      13.363  13.305   8.918  1.00 38.34           C  
ANISOU 2181  CB  LEU G 321     3613   5994   4959   -407   -109   -609       C  
ATOM   2182  CG  LEU G 321      14.699  13.287   9.643  1.00 41.47           C  
ANISOU 2182  CG  LEU G 321     3765   6409   5584   -629   -282   -190       C  
ATOM   2183  CD1 LEU G 321      15.503  12.094   9.142  1.00 41.90           C  
ANISOU 2183  CD1 LEU G 321     3594   6587   5736   -335     35    173       C  
ATOM   2184  CD2 LEU G 321      15.474  14.580   9.456  1.00 43.78           C  
ANISOU 2184  CD2 LEU G 321     3872   6572   6187   -841   -544    195       C  
ATOM   2185  N   ASN G 322      10.338  13.427   8.491  1.00 40.93           N  
ANISOU 2185  N   ASN G 322     4108   6167   5273   -286   -139  -1055       N  
ATOM   2186  CA  ASN G 322       9.160  13.426   7.644  1.00 40.37           C  
ANISOU 2186  CA  ASN G 322     4003   5955   5379   -233   -320  -1052       C  
ATOM   2187  C   ASN G 322       8.343  14.712   7.801  1.00 41.52           C  
ANISOU 2187  C   ASN G 322     4061   6119   5594   -179   -137   -987       C  
ATOM   2188  O   ASN G 322       7.958  15.336   6.825  1.00 42.54           O  
ANISOU 2188  O   ASN G 322     4233   6179   5751   -123   -254  -1017       O  
ATOM   2189  CB  ASN G 322       8.295  12.213   7.954  1.00 41.91           C  
ANISOU 2189  CB  ASN G 322     3985   6010   5927   -340   -567   -862       C  
ATOM   2190  CG  ASN G 322       7.110  12.077   7.015  1.00 46.02           C  
ANISOU 2190  CG  ASN G 322     4428   6228   6830   -428  -1100   -686       C  
ATOM   2191  OD1 ASN G 322       7.238  12.149   5.784  1.00 46.79           O  
ANISOU 2191  OD1 ASN G 322     4995   6092   6689   -345  -1490   -890       O  
ATOM   2192  ND2 ASN G 322       5.948  11.830   7.593  1.00 49.85           N  
ANISOU 2192  ND2 ASN G 322     4339   6649   7952   -551  -1159   -176       N  
ATOM   2193  N   ASP G 323       8.053  15.095   9.028  1.00 43.71           N  
ANISOU 2193  N   ASP G 323     4355   6437   5815    -86    189   -866       N  
ATOM   2194  CA  ASP G 323       7.236  16.273   9.254  1.00 45.89           C  
ANISOU 2194  CA  ASP G 323     4730   6657   6048    159    506   -729       C  
ATOM   2195  C   ASP G 323       7.985  17.524   8.800  1.00 45.05           C  
ANISOU 2195  C   ASP G 323     5001   6483   5631    111    409  -1010       C  
ATOM   2196  O   ASP G 323       7.386  18.444   8.285  1.00 47.15           O  
ANISOU 2196  O   ASP G 323     5284   6701   5930    245    521   -967       O  
ATOM   2197  CB  ASP G 323       6.838  16.379  10.721  1.00 49.90           C  
ANISOU 2197  CB  ASP G 323     5525   7103   6329    529    999   -495       C  
ATOM   2198  CG  ASP G 323       5.907  15.234  11.165  1.00 54.35           C  
ANISOU 2198  CG  ASP G 323     5505   7737   7408    655   1236     57       C  
ATOM   2199  OD1 ASP G 323       5.645  14.287  10.389  1.00 57.83           O  
ANISOU 2199  OD1 ASP G 323     5381   8190   8401    311    787    185       O  
ATOM   2200  OD2 ASP G 323       5.448  15.259  12.316  1.00 63.21           O  
ANISOU 2200  OD2 ASP G 323     6831   8817   8367   1152   1838    436       O  
ATOM   2201  N   SER G 324       9.296  17.542   8.993  1.00 44.53           N  
ANISOU 2201  N   SER G 324     5140   6388   5389   -103    165  -1162       N  
ATOM   2202  CA  SER G 324      10.120  18.673   8.579  1.00 45.09           C  
ANISOU 2202  CA  SER G 324     5399   6328   5404   -239    -44  -1203       C  
ATOM   2203  C   SER G 324      10.117  18.804   7.050  1.00 43.05           C  
ANISOU 2203  C   SER G 324     4820   6198   5339   -180      0  -1158       C  
ATOM   2204  O   SER G 324       9.861  19.892   6.508  1.00 41.06           O  
ANISOU 2204  O   SER G 324     4654   5868   5078   -113     40  -1167       O  
ATOM   2205  CB  SER G 324      11.556  18.516   9.087  1.00 45.74           C  
ANISOU 2205  CB  SER G 324     5513   6313   5551   -550   -432  -1066       C  
ATOM   2206  OG  SER G 324      11.656  18.955  10.422  1.00 48.90           O  
ANISOU 2206  OG  SER G 324     6592   6369   5618   -604   -724  -1154       O  
ATOM   2207  N   LEU G 325      10.411  17.697   6.371  1.00 39.68           N  
ANISOU 2207  N   LEU G 325     4201   5893   4980   -115     -5  -1107       N  
ATOM   2208  CA  LEU G 325      10.300  17.665   4.917  1.00 39.97           C  
ANISOU 2208  CA  LEU G 325     4300   5920   4965    139     21  -1089       C  
ATOM   2209  C   LEU G 325       8.892  18.064   4.405  1.00 41.37           C  
ANISOU 2209  C   LEU G 325     4520   6011   5186    199   -101  -1199       C  
ATOM   2210  O   LEU G 325       8.794  18.751   3.399  1.00 43.10           O  
ANISOU 2210  O   LEU G 325     4872   6182   5322    373    -93  -1195       O  
ATOM   2211  CB  LEU G 325      10.793  16.336   4.330  1.00 39.10           C  
ANISOU 2211  CB  LEU G 325     4375   5776   4704    377      7  -1037       C  
ATOM   2212  CG  LEU G 325      12.277  15.936   4.532  1.00 39.87           C  
ANISOU 2212  CG  LEU G 325     4318   5979   4851    483    276   -678       C  
ATOM   2213  CD1 LEU G 325      12.507  14.467   4.158  1.00 40.56           C  
ANISOU 2213  CD1 LEU G 325     4769   5966   4676    827    327   -671       C  
ATOM   2214  CD2 LEU G 325      13.237  16.825   3.730  1.00 42.70           C  
ANISOU 2214  CD2 LEU G 325     4523   6373   5327    760    617   -196       C  
ATOM   2215  N   GLU G 326       7.819  17.679   5.093  1.00 42.37           N  
ANISOU 2215  N   GLU G 326     4453   6114   5530     93   -178  -1143       N  
ATOM   2216  CA  GLU G 326       6.483  18.077   4.656  1.00 46.60           C  
ANISOU 2216  CA  GLU G 326     4802   6559   6344    133   -305   -963       C  
ATOM   2217  C   GLU G 326       6.348  19.602   4.627  1.00 46.35           C  
ANISOU 2217  C   GLU G 326     4833   6567   6209    272     28   -966       C  
ATOM   2218  O   GLU G 326       5.799  20.153   3.679  1.00 47.80           O  
ANISOU 2218  O   GLU G 326     4997   6691   6471    352   -103   -908       O  
ATOM   2219  CB  GLU G 326       5.377  17.486   5.540  1.00 51.48           C  
ANISOU 2219  CB  GLU G 326     4966   7158   7435     80   -269   -554       C  
ATOM   2220  CG  GLU G 326       4.944  16.079   5.149  1.00 58.10           C  
ANISOU 2220  CG  GLU G 326     5643   7777   8652   -149   -922   -377       C  
ATOM   2221  CD  GLU G 326       3.979  15.434   6.139  1.00 65.44           C  
ANISOU 2221  CD  GLU G 326     5918   8696  10248   -211   -818    258       C  
ATOM   2222  OE1 GLU G 326       3.558  16.109   7.103  1.00 67.48           O  
ANISOU 2222  OE1 GLU G 326     5929   9133  10574     95    -74    604       O  
ATOM   2223  OE2 GLU G 326       3.634  14.241   5.950  1.00 71.62           O  
ANISOU 2223  OE2 GLU G 326     6519   9216  11475   -490  -1470    497       O  
ATOM   2224  N   LEU G 327       6.839  20.264   5.671  1.00 43.13           N  
ANISOU 2224  N   LEU G 327     4639   6164   5584    306    348  -1033       N  
ATOM   2225  CA  LEU G 327       6.711  21.706   5.787  1.00 44.74           C  
ANISOU 2225  CA  LEU G 327     5131   6249   5617    460    574  -1052       C  
ATOM   2226  C   LEU G 327       7.533  22.442   4.710  1.00 44.60           C  
ANISOU 2226  C   LEU G 327     5172   6213   5559    366    407  -1161       C  
ATOM   2227  O   LEU G 327       7.057  23.400   4.110  1.00 43.78           O  
ANISOU 2227  O   LEU G 327     5103   6062   5469    503    507  -1123       O  
ATOM   2228  CB  LEU G 327       7.120  22.158   7.184  1.00 45.18           C  
ANISOU 2228  CB  LEU G 327     5775   6082   5306    540    701  -1132       C  
ATOM   2229  CG  LEU G 327       7.045  23.650   7.485  1.00 47.56           C  
ANISOU 2229  CG  LEU G 327     6751   6044   5274    750    799  -1195       C  
ATOM   2230  CD1 LEU G 327       5.614  24.127   7.314  1.00 49.91           C  
ANISOU 2230  CD1 LEU G 327     6927   6387   5648   1241   1366   -897       C  
ATOM   2231  CD2 LEU G 327       7.583  23.938   8.872  1.00 50.61           C  
ANISOU 2231  CD2 LEU G 327     8109   5991   5129    834    625  -1336       C  
ATOM   2232  N   SER G 328       8.747  21.968   4.470  1.00 44.77           N  
ANISOU 2232  N   SER G 328     5139   6280   5590    212    245  -1157       N  
ATOM   2233  CA  SER G 328       9.640  22.521   3.449  1.00 46.48           C  
ANISOU 2233  CA  SER G 328     5277   6498   5883    265    262   -981       C  
ATOM   2234  C   SER G 328       9.070  22.438   2.041  1.00 44.98           C  
ANISOU 2234  C   SER G 328     5133   6369   5587    595    338   -990       C  
ATOM   2235  O   SER G 328       9.368  23.250   1.192  1.00 45.50           O  
ANISOU 2235  O   SER G 328     5223   6412   5653    777    482   -832       O  
ATOM   2236  CB  SER G 328      10.954  21.752   3.433  1.00 47.28           C  
ANISOU 2236  CB  SER G 328     5182   6668   6113    222    257   -703       C  
ATOM   2237  OG  SER G 328      11.744  22.125   4.521  1.00 54.00           O  
ANISOU 2237  OG  SER G 328     5992   7353   7171   -157    -25   -546       O  
ATOM   2238  N   ASP G 329       8.295  21.407   1.793  1.00 44.30           N  
ANISOU 2238  N   ASP G 329     5133   6276   5421    665    133  -1117       N  
ATOM   2239  CA  ASP G 329       7.644  21.253   0.531  1.00 44.94           C  
ANISOU 2239  CA  ASP G 329     5503   6227   5343    924   -111  -1147       C  
ATOM   2240  C   ASP G 329       6.484  22.241   0.301  1.00 43.23           C  
ANISOU 2240  C   ASP G 329     5128   5978   5319    888   -186  -1095       C  
ATOM   2241  O   ASP G 329       6.143  22.497  -0.837  1.00 43.49           O  
ANISOU 2241  O   ASP G 329     5443   5882   5199   1111   -396  -1081       O  
ATOM   2242  CB  ASP G 329       7.110  19.840   0.407  1.00 50.13           C  
ANISOU 2242  CB  ASP G 329     6387   6691   5967    879   -632  -1224       C  
ATOM   2243  CG  ASP G 329       7.876  19.036  -0.569  1.00 57.38           C  
ANISOU 2243  CG  ASP G 329     8042   7397   6359   1328   -709  -1281       C  
ATOM   2244  OD1 ASP G 329       9.098  18.851  -0.330  1.00 61.02           O  
ANISOU 2244  OD1 ASP G 329     8466   8019   6697   1526   -196  -1146       O  
ATOM   2245  OD2 ASP G 329       7.250  18.574  -1.556  1.00 65.29           O  
ANISOU 2245  OD2 ASP G 329     9740   7996   7070   1530  -1326  -1375       O  
ATOM   2246  N   VAL G 330       5.871  22.744   1.359  1.00 40.34           N  
ANISOU 2246  N   VAL G 330     4425   5680   5221    722     17  -1005       N  
ATOM   2247  CA  VAL G 330       4.722  23.643   1.221  1.00 44.43           C  
ANISOU 2247  CA  VAL G 330     4743   6171   5969    814    105   -788       C  
ATOM   2248  C   VAL G 330       5.043  25.119   1.467  1.00 42.74           C  
ANISOU 2248  C   VAL G 330     4699   5942   5597    940    545   -838       C  
ATOM   2249  O   VAL G 330       4.227  25.959   1.131  1.00 46.28           O  
ANISOU 2249  O   VAL G 330     5064   6359   6158   1108    682   -661       O  
ATOM   2250  CB  VAL G 330       3.493  23.204   2.065  1.00 47.00           C  
ANISOU 2250  CB  VAL G 330     4598   6494   6764    787    152   -366       C  
ATOM   2251  CG1 VAL G 330       3.010  21.843   1.586  1.00 50.27           C  
ANISOU 2251  CG1 VAL G 330     4806   6768   7525    547   -578   -190       C  
ATOM   2252  CG2 VAL G 330       3.786  23.180   3.555  1.00 46.30           C  
ANISOU 2252  CG2 VAL G 330     4606   6453   6533    875    663   -371       C  
ATOM   2253  N   VAL G 331       6.213  25.420   2.026  1.00 40.84           N  
ANISOU 2253  N   VAL G 331     4703   5647   5168    825    643   -998       N  
ATOM   2254  CA  VAL G 331       6.670  26.804   2.237  1.00 43.09           C  
ANISOU 2254  CA  VAL G 331     5283   5726   5362    827    767  -1010       C  
ATOM   2255  C   VAL G 331       7.462  27.270   0.995  1.00 41.66           C  
ANISOU 2255  C   VAL G 331     4981   5581   5267    850    726   -887       C  
ATOM   2256  O   VAL G 331       8.525  26.713   0.692  1.00 42.25           O  
ANISOU 2256  O   VAL G 331     4912   5722   5416    794    671   -742       O  
ATOM   2257  CB  VAL G 331       7.578  26.903   3.499  1.00 44.31           C  
ANISOU 2257  CB  VAL G 331     5824   5617   5395    588    584  -1094       C  
ATOM   2258  CG1 VAL G 331       8.060  28.333   3.735  1.00 47.63           C  
ANISOU 2258  CG1 VAL G 331     6739   5595   5760    493    386  -1072       C  
ATOM   2259  CG2 VAL G 331       6.843  26.406   4.737  1.00 46.00           C  
ANISOU 2259  CG2 VAL G 331     6327   5769   5378    766    771  -1158       C  
ATOM   2260  N   PRO G 332       6.957  28.281   0.258  1.00 43.45           N  
ANISOU 2260  N   PRO G 332     4213   5438   6855   -175     77    -99       N  
ATOM   2261  CA  PRO G 332       7.769  28.838  -0.845  1.00 42.18           C  
ANISOU 2261  CA  PRO G 332     4301   5142   6583    -65    -44    -32       C  
ATOM   2262  C   PRO G 332       9.164  29.175  -0.370  1.00 40.03           C  
ANISOU 2262  C   PRO G 332     4166   4794   6248    -84    102     30       C  
ATOM   2263  O   PRO G 332       9.324  29.613   0.778  1.00 39.58           O  
ANISOU 2263  O   PRO G 332     4076   4751   6210    -96    172     29       O  
ATOM   2264  CB  PRO G 332       7.015  30.118  -1.208  1.00 45.47           C  
ANISOU 2264  CB  PRO G 332     4706   5569   6998    197   -211    -52       C  
ATOM   2265  CG  PRO G 332       5.594  29.821  -0.870  1.00 47.53           C  
ANISOU 2265  CG  PRO G 332     4496   6128   7435    252   -285   -147       C  
ATOM   2266  CD  PRO G 332       5.674  29.004   0.394  1.00 46.42           C  
ANISOU 2266  CD  PRO G 332     4234   6031   7370    -12     20   -179       C  
ATOM   2267  N   ALA G 333      10.177  28.943  -1.204  1.00 40.21           N  
ANISOU 2267  N   ALA G 333     4320   4776   6180   -116    162     70       N  
ATOM   2268  CA  ALA G 333      11.578  29.184  -0.770  1.00 40.67           C  
ANISOU 2268  CA  ALA G 333     4275   4953   6223   -182    289    102       C  
ATOM   2269  C   ALA G 333      11.780  30.628  -0.344  1.00 42.47           C  
ANISOU 2269  C   ALA G 333     4601   5149   6385   -355    279     91       C  
ATOM   2270  O   ALA G 333      12.572  30.925   0.564  1.00 43.09           O  
ANISOU 2270  O   ALA G 333     4552   5369   6449   -517    275     93       O  
ATOM   2271  CB  ALA G 333      12.572  28.810  -1.860  1.00 42.04           C  
ANISOU 2271  CB  ALA G 333     4478   5168   6324   -173    468    118       C  
ATOM   2272  N   SER G 334      11.075  31.539  -1.003  1.00 44.51           N  
ANISOU 2272  N   SER G 334     5192   5188   6529   -315    232     77       N  
ATOM   2273  CA  SER G 334      11.212  32.954  -0.656  1.00 50.01           C  
ANISOU 2273  CA  SER G 334     6269   5700   7030   -454    261     67       C  
ATOM   2274  C   SER G 334      10.629  33.280   0.751  1.00 50.74           C  
ANISOU 2274  C   SER G 334     6368   5760   7150   -350    230     55       C  
ATOM   2275  O   SER G 334      11.216  34.050   1.497  1.00 51.36           O  
ANISOU 2275  O   SER G 334     6708   5750   7054   -614    273     50       O  
ATOM   2276  CB  SER G 334      10.564  33.837  -1.710  1.00 51.98           C  
ANISOU 2276  CB  SER G 334     7077   5625   7049   -278    195     67       C  
ATOM   2277  OG  SER G 334      10.849  35.170  -1.390  1.00 55.86           O  
ANISOU 2277  OG  SER G 334     8165   5825   7231   -448    282     58       O  
ATOM   2278  N   ASP G 335       9.506  32.670   1.119  1.00 48.92           N  
ANISOU 2278  N   ASP G 335     5884   5605   7098    -51    194     35       N  
ATOM   2279  CA  ASP G 335       9.052  32.744   2.508  1.00 51.66           C  
ANISOU 2279  CA  ASP G 335     6233   5931   7462      3    294     10       C  
ATOM   2280  C   ASP G 335      10.054  32.155   3.486  1.00 51.16           C  
ANISOU 2280  C   ASP G 335     6108   5954   7375   -278    285     33       C  
ATOM   2281  O   ASP G 335      10.314  32.729   4.533  1.00 53.38           O  
ANISOU 2281  O   ASP G 335     6691   6104   7487   -410    306     31       O  
ATOM   2282  CB  ASP G 335       7.700  32.071   2.671  1.00 53.22           C  
ANISOU 2282  CB  ASP G 335     6067   6286   7866    248    355    -47       C  
ATOM   2283  CG  ASP G 335       6.593  32.846   1.986  1.00 57.41           C  
ANISOU 2283  CG  ASP G 335     6566   6834   8414    669    281    -83       C  
ATOM   2284  OD1 ASP G 335       6.908  33.893   1.369  1.00 61.51           O  
ANISOU 2284  OD1 ASP G 335     7556   7104   8709    810    185    -45       O  
ATOM   2285  OD2 ASP G 335       5.423  32.409   2.057  1.00 61.60           O  
ANISOU 2285  OD2 ASP G 335     6616   7642   9144    849    311   -159       O  
ATOM   2286  N   ALA G 336      10.658  31.037   3.122  1.00 49.84           N  
ANISOU 2286  N   ALA G 336     5641   5978   7314   -321    218     58       N  
ATOM   2287  CA  ALA G 336      11.592  30.374   4.001  1.00 50.15           C  
ANISOU 2287  CA  ALA G 336     5608   6139   7307   -402    120     87       C  
ATOM   2288  C   ALA G 336      12.836  31.188   4.275  1.00 54.99           C  
ANISOU 2288  C   ALA G 336     6206   6892   7793   -694    -19     97       C  
ATOM   2289  O   ALA G 336      13.395  31.080   5.363  1.00 59.57           O  
ANISOU 2289  O   ALA G 336     6833   7542   8259   -788   -202    108       O  
ATOM   2290  CB  ALA G 336      11.974  29.002   3.439  1.00 49.82           C  
ANISOU 2290  CB  ALA G 336     5352   6230   7345   -224    104    114       C  
ATOM   2291  N   GLU G 337      13.304  31.980   3.310  1.00 57.96           N  
ANISOU 2291  N   GLU G 337     6564   7318   8139   -913     47     82       N  
ATOM   2292  CA  GLU G 337      14.506  32.775   3.560  1.00 63.32           C  
ANISOU 2292  CA  GLU G 337     7191   8199   8667  -1398    -42     57       C  
ATOM   2293  C   GLU G 337      14.231  33.940   4.505  1.00 64.40           C  
ANISOU 2293  C   GLU G 337     7952   8012   8505  -1700    -90     35       C  
ATOM   2294  O   GLU G 337      15.118  34.344   5.257  1.00 69.39           O  
ANISOU 2294  O   GLU G 337     8595   8808   8959  -2153   -291     12       O  
ATOM   2295  CB  GLU G 337      15.183  33.256   2.274  1.00 66.06           C  
ANISOU 2295  CB  GLU G 337     7431   8673   8992  -1696    155     23       C  
ATOM   2296  CG  GLU G 337      16.700  33.309   2.408  1.00 74.33           C  
ANISOU 2296  CG  GLU G 337     7902  10284  10055  -2151     94    -25       C  
ATOM   2297  CD  GLU G 337      17.322  31.965   2.817  1.00 77.91           C  
ANISOU 2297  CD  GLU G 337     7626  11224  10750  -1699   -102      7       C  
ATOM   2298  OE1 GLU G 337      16.717  30.908   2.508  1.00 76.45           O  
ANISOU 2298  OE1 GLU G 337     7472  10881  10695  -1115    -37     62       O  
ATOM   2299  OE2 GLU G 337      18.410  31.960   3.453  1.00 81.99           O  
ANISOU 2299  OE2 GLU G 337     7596  12278  11277  -1919   -356    -26       O  
ATOM   2300  N   LYS G 338      13.006  34.449   4.487  1.00 61.24           N  
ANISOU 2300  N   LYS G 338     8068   7177   8021  -1421     75     36       N  
ATOM   2301  CA  LYS G 338      12.572  35.469   5.459  1.00 65.67           C  
ANISOU 2301  CA  LYS G 338     9372   7327   8250  -1520    125     19       C  
ATOM   2302  C   LYS G 338      12.466  34.928   6.911  1.00 62.89           C  
ANISOU 2302  C   LYS G 338     9084   6956   7853  -1471     22     26       C  
ATOM   2303  O   LYS G 338      12.991  35.543   7.847  1.00 66.81           O  
ANISOU 2303  O   LYS G 338    10068   7302   8013  -1870   -115     14       O  
ATOM   2304  CB  LYS G 338      11.251  36.104   4.993  1.00 68.16           C  
ANISOU 2304  CB  LYS G 338    10129   7259   8509  -1019    359     13       C  
ATOM   2305  CG  LYS G 338      11.401  36.831   3.651  1.00 72.31           C  
ANISOU 2305  CG  LYS G 338    10943   7637   8893  -1078    403     12       C  
ATOM   2306  CD  LYS G 338      10.103  37.457   3.156  1.00 74.93           C  
ANISOU 2306  CD  LYS G 338    11715   7626   9129   -412    504     14       C  
ATOM   2307  CE  LYS G 338      10.371  38.491   2.072  1.00 78.60           C  
ANISOU 2307  CE  LYS G 338    12949   7712   9203   -523    529     19       C  
ATOM   2308  NZ  LYS G 338       9.607  39.745   2.305  1.00 83.50           N  
ANISOU 2308  NZ  LYS G 338    14618   7739   9366    -63    642     20       N  
ATOM   2309  N   TYR G 339      11.816  33.776   7.101  1.00 56.38           N  
ANISOU 2309  N   TYR G 339     7901   6235   7286  -1071     85     39       N  
ATOM   2310  CA  TYR G 339      11.787  33.144   8.423  1.00 55.54           C  
ANISOU 2310  CA  TYR G 339     7996   6045   7059  -1058     15     45       C  
ATOM   2311  C   TYR G 339      13.208  32.934   8.966  1.00 59.04           C  
ANISOU 2311  C   TYR G 339     8324   6754   7353  -1396   -443     73       C  
ATOM   2312  O   TYR G 339      13.455  33.187  10.143  1.00 61.06           O  
ANISOU 2312  O   TYR G 339     9095   6820   7282  -1603   -625     73       O  
ATOM   2313  CB  TYR G 339      11.028  31.801   8.407  1.00 52.34           C  
ANISOU 2313  CB  TYR G 339     7294   5706   6884   -720    174     42       C  
ATOM   2314  CG  TYR G 339       9.516  31.915   8.268  1.00 50.32           C  
ANISOU 2314  CG  TYR G 339     7049   5309   6759   -461    599    -19       C  
ATOM   2315  CD1 TYR G 339       8.747  32.436   9.299  1.00 52.74           C  
ANISOU 2315  CD1 TYR G 339     7849   5315   6872   -397    920    -69       C  
ATOM   2316  CD2 TYR G 339       8.856  31.471   7.121  1.00 46.88           C  
ANISOU 2316  CD2 TYR G 339     6097   5092   6621   -276    676    -41       C  
ATOM   2317  CE1 TYR G 339       7.368  32.541   9.187  1.00 53.77           C  
ANISOU 2317  CE1 TYR G 339     7784   5474   7170    -97   1346   -150       C  
ATOM   2318  CE2 TYR G 339       7.477  31.565   7.008  1.00 48.70           C  
ANISOU 2318  CE2 TYR G 339     6139   5363   7000    -48    981   -120       C  
ATOM   2319  CZ  TYR G 339       6.740  32.095   8.049  1.00 51.88           C  
ANISOU 2319  CZ  TYR G 339     6860   5576   7274     66   1335   -180       C  
ATOM   2320  OH  TYR G 339       5.377  32.209   7.966  1.00 55.60           O  
ANISOU 2320  OH  TYR G 339     6961   6228   7933    355   1682   -280       O  
ATOM   2321  N   ARG G 340      14.135  32.463   8.127  1.00 59.25           N  
ANISOU 2321  N   ARG G 340     7664   7250   7596  -1419   -638     90       N  
ATOM   2322  CA  ARG G 340      15.539  32.316   8.549  1.00 63.78           C  
ANISOU 2322  CA  ARG G 340     7869   8277   8087  -1675  -1107     96       C  
ATOM   2323  C   ARG G 340      16.168  33.636   9.048  1.00 66.76           C  
ANISOU 2323  C   ARG G 340     8597   8639   8128  -2395  -1307     45       C  
ATOM   2324  O   ARG G 340      16.911  33.634  10.017  1.00 70.92           O  
ANISOU 2324  O   ARG G 340     9174   9347   8422  -2656  -1771     41       O  
ATOM   2325  CB  ARG G 340      16.399  31.688   7.440  1.00 64.83           C  
ANISOU 2325  CB  ARG G 340     7120   8978   8532  -1519  -1135     98       C  
ATOM   2326  CG  ARG G 340      16.167  30.191   7.227  1.00 63.33           C  
ANISOU 2326  CG  ARG G 340     6725   8820   8518   -840  -1097    154       C  
ATOM   2327  CD  ARG G 340      16.950  29.672   6.029  1.00 65.59           C  
ANISOU 2327  CD  ARG G 340     6290   9571   9057   -624   -995    152       C  
ATOM   2328  NE  ARG G 340      16.160  28.727   5.247  1.00 63.77           N  
ANISOU 2328  NE  ARG G 340     6224   9062   8942   -183   -684    183       N  
ATOM   2329  CZ  ARG G 340      16.036  27.421   5.503  1.00 64.80           C  
ANISOU 2329  CZ  ARG G 340     6541   9069   9009    342   -734    232       C  
ATOM   2330  NH1 ARG G 340      16.649  26.852   6.534  1.00 68.18           N  
ANISOU 2330  NH1 ARG G 340     7033   9611   9261    646  -1110    271       N  
ATOM   2331  NH2 ARG G 340      15.270  26.673   4.721  1.00 62.77           N  
ANISOU 2331  NH2 ARG G 340     6539   8522   8789    543   -438    240       N  
ATOM   2332  N   GLN G 341      15.845  34.754   8.407  1.00 67.21           N  
ANISOU 2332  N   GLN G 341     9033   8424   8078  -2726   -992      4       N  
TER    2333      GLN G 341                                                      
ATOM   2334  N   GLU H 303      11.070  -2.865  19.417  1.00 65.98           N  
ANISOU 2334  N   GLU H 303     8931   9040   7097  -1379    184   1198       N  
ATOM   2335  CA  GLU H 303       9.683  -2.843  18.878  1.00 65.91           C  
ANISOU 2335  CA  GLU H 303     8812   8748   7480  -1430    543    947       C  
ATOM   2336  C   GLU H 303       9.634  -2.202  17.503  1.00 61.84           C  
ANISOU 2336  C   GLU H 303     7884   8311   7300  -1320    416    793       C  
ATOM   2337  O   GLU H 303      10.509  -1.414  17.133  1.00 58.21           O  
ANISOU 2337  O   GLU H 303     7200   8156   6762  -1303    169    893       O  
ATOM   2338  CB  GLU H 303       8.706  -2.121  19.821  1.00 69.73           C  
ANISOU 2338  CB  GLU H 303     9517   9174   7803  -1497   1006    885       C  
ATOM   2339  CG  GLU H 303       7.886  -3.052  20.728  1.00 76.54           C  
ANISOU 2339  CG  GLU H 303    10465  10022   8593  -1549   1449   1249       C  
ATOM   2340  CD  GLU H 303       6.933  -4.012  19.993  1.00 78.79           C  
ANISOU 2340  CD  GLU H 303    10235  10215   9485  -1916   1377   1626       C  
ATOM   2341  OE1 GLU H 303       6.639  -3.837  18.777  1.00 74.46           O  
ANISOU 2341  OE1 GLU H 303     9346   9564   9379  -2013   1076   1500       O  
ATOM   2342  OE2 GLU H 303       6.469  -4.969  20.657  1.00 82.65           O  
ANISOU 2342  OE2 GLU H 303    10779  10657   9969  -2225   1467   2153       O  
ATOM   2343  N   ILE H 304       8.589  -2.563  16.762  1.00 60.05           N  
ANISOU 2343  N   ILE H 304     7542   7821   7452  -1368    469    714       N  
ATOM   2344  CA  ILE H 304       8.418  -2.152  15.387  1.00 57.52           C  
ANISOU 2344  CA  ILE H 304     7005   7453   7394  -1213    287    555       C  
ATOM   2345  C   ILE H 304       7.299  -1.114  15.279  1.00 56.71           C  
ANISOU 2345  C   ILE H 304     6510   7404   7634  -1405    532    453       C  
ATOM   2346  O   ILE H 304       6.250  -1.219  15.924  1.00 59.07           O  
ANISOU 2346  O   ILE H 304     6589   7764   8090  -1573    848    699       O  
ATOM   2347  CB  ILE H 304       8.179  -3.377  14.482  1.00 61.38           C  
ANISOU 2347  CB  ILE H 304     8013   7421   7886  -1055   -150    586       C  
ATOM   2348  CG1 ILE H 304       9.416  -4.297  14.516  1.00 64.00           C  
ANISOU 2348  CG1 ILE H 304     8953   7747   7616   -354   -255    709       C  
ATOM   2349  CG2 ILE H 304       7.910  -2.951  13.046  1.00 59.65           C  
ANISOU 2349  CG2 ILE H 304     7804   7045   7812   -830   -402    400       C  
ATOM   2350  CD1 ILE H 304       9.602  -5.075  15.806  1.00 66.79           C  
ANISOU 2350  CD1 ILE H 304     9583   8025   7766   -554   -201    901       C  
ATOM   2351  N   PHE H 305       7.560  -0.094  14.465  1.00 54.71           N  
ANISOU 2351  N   PHE H 305     6114   7242   7430  -1258    443    257       N  
ATOM   2352  CA  PHE H 305       6.681   1.034  14.300  1.00 54.22           C  
ANISOU 2352  CA  PHE H 305     5867   7196   7537  -1202    651    132       C  
ATOM   2353  C   PHE H 305       6.367   1.182  12.814  1.00 53.60           C  
ANISOU 2353  C   PHE H 305     5540   7020   7805  -1139    363     35       C  
ATOM   2354  O   PHE H 305       7.113   0.717  11.948  1.00 51.28           O  
ANISOU 2354  O   PHE H 305     5408   6666   7408   -982     62     17       O  
ATOM   2355  CB  PHE H 305       7.335   2.297  14.870  1.00 55.90           C  
ANISOU 2355  CB  PHE H 305     6573   7360   7304  -1167    596    -14       C  
ATOM   2356  CG  PHE H 305       7.439   2.309  16.389  1.00 61.45           C  
ANISOU 2356  CG  PHE H 305     7914   7962   7471  -1115    781     22       C  
ATOM   2357  CD1 PHE H 305       8.420   1.566  17.051  1.00 61.98           C  
ANISOU 2357  CD1 PHE H 305     8124   8103   7321  -1389    533    200       C  
ATOM   2358  CD2 PHE H 305       6.564   3.082  17.160  1.00 67.31           C  
ANISOU 2358  CD2 PHE H 305     9259   8546   7766   -565   1238    -64       C  
ATOM   2359  CE1 PHE H 305       8.504   1.566  18.441  1.00 66.75           C  
ANISOU 2359  CE1 PHE H 305     9478   8536   7347  -1328    621    222       C  
ATOM   2360  CE2 PHE H 305       6.656   3.105  18.552  1.00 72.76           C  
ANISOU 2360  CE2 PHE H 305    10872   9056   7715   -275   1434    -40       C  
ATOM   2361  CZ  PHE H 305       7.623   2.338  19.195  1.00 72.62           C  
ANISOU 2361  CZ  PHE H 305    11012   9024   7556   -766   1065     69       C  
ATOM   2362  N   THR H 306       5.228   1.791  12.508  1.00 53.88           N  
ANISOU 2362  N   THR H 306     5234   7091   8145  -1074    500     70       N  
ATOM   2363  CA  THR H 306       4.865   2.014  11.117  1.00 52.80           C  
ANISOU 2363  CA  THR H 306     4943   6810   8305  -1041    130    -16       C  
ATOM   2364  C   THR H 306       4.792   3.525  10.867  1.00 51.32           C  
ANISOU 2364  C   THR H 306     4808   6673   8018   -732    304   -228       C  
ATOM   2365  O   THR H 306       4.154   4.256  11.632  1.00 53.56           O  
ANISOU 2365  O   THR H 306     5122   7068   8158   -402    730   -174       O  
ATOM   2366  CB  THR H 306       3.548   1.319  10.817  1.00 59.41           C  
ANISOU 2366  CB  THR H 306     5292   7623   9657  -1388   -158    424       C  
ATOM   2367  OG1 THR H 306       3.686  -0.090  11.099  1.00 61.91           O  
ANISOU 2367  OG1 THR H 306     5929   7637   9955  -1826   -561    656       O  
ATOM   2368  CG2 THR H 306       3.150   1.546   9.380  1.00 60.24           C  
ANISOU 2368  CG2 THR H 306     5427   7461   9999  -1403   -741    336       C  
ATOM   2369  N   LEU H 307       5.482   3.997   9.829  1.00 47.51           N  
ANISOU 2369  N   LEU H 307     4510   6084   7456   -689      1   -387       N  
ATOM   2370  CA  LEU H 307       5.578   5.437   9.577  1.00 48.75           C  
ANISOU 2370  CA  LEU H 307     4936   6131   7455   -565    -30   -519       C  
ATOM   2371  C   LEU H 307       4.912   5.675   8.262  1.00 47.68           C  
ANISOU 2371  C   LEU H 307     4582   5918   7616   -379   -230   -579       C  
ATOM   2372  O   LEU H 307       5.293   5.082   7.273  1.00 43.00           O  
ANISOU 2372  O   LEU H 307     3997   5302   7038   -361   -501   -548       O  
ATOM   2373  CB  LEU H 307       7.044   5.896   9.522  1.00 48.93           C  
ANISOU 2373  CB  LEU H 307     5214   6224   7151   -892   -327   -318       C  
ATOM   2374  CG  LEU H 307       7.305   7.365   9.208  1.00 52.69           C  
ANISOU 2374  CG  LEU H 307     6168   6418   7434  -1093   -692   -266       C  
ATOM   2375  CD1 LEU H 307       6.699   8.305  10.246  1.00 56.42           C  
ANISOU 2375  CD1 LEU H 307     7617   6311   7507   -913   -714   -565       C  
ATOM   2376  CD2 LEU H 307       8.796   7.613   9.061  1.00 54.84           C  
ANISOU 2376  CD2 LEU H 307     6275   7018   7542  -1713  -1150    413       C  
ATOM   2377  N   GLN H 308       3.891   6.524   8.249  1.00 51.22           N  
ANISOU 2377  N   GLN H 308     4971   6317   8172    -48    -85   -618       N  
ATOM   2378  CA  GLN H 308       3.205   6.808   7.006  1.00 53.10           C  
ANISOU 2378  CA  GLN H 308     4972   6495   8707    108   -371   -614       C  
ATOM   2379  C   GLN H 308       3.867   8.011   6.374  1.00 48.73           C  
ANISOU 2379  C   GLN H 308     4994   5673   7847    189   -548   -794       C  
ATOM   2380  O   GLN H 308       4.176   8.966   7.061  1.00 50.04           O  
ANISOU 2380  O   GLN H 308     5785   5596   7630    247   -489   -872       O  
ATOM   2381  CB  GLN H 308       1.699   7.068   7.225  1.00 62.35           C  
ANISOU 2381  CB  GLN H 308     5518   7973  10199    529   -124   -281       C  
ATOM   2382  CG  GLN H 308       0.887   6.832   5.952  1.00 67.15           C  
ANISOU 2382  CG  GLN H 308     5628   8590  11294    381   -712    -49       C  
ATOM   2383  CD  GLN H 308      -0.566   6.449   6.206  1.00 78.99           C  
ANISOU 2383  CD  GLN H 308     5950  10704  13356    374   -710    803       C  
ATOM   2384  OE1 GLN H 308      -1.010   5.340   5.850  1.00 83.53           O  
ANISOU 2384  OE1 GLN H 308     6076  11265  14396   -417  -1445   1290       O  
ATOM   2385  NE2 GLN H 308      -1.315   7.358   6.824  1.00 83.96           N  
ANISOU 2385  NE2 GLN H 308     6157  11883  13860   1297     36   1166       N  
ATOM   2386  N   VAL H 309       4.094   7.942   5.067  1.00 46.51           N  
ANISOU 2386  N   VAL H 309     4706   5336   7628    175   -877   -786       N  
ATOM   2387  CA  VAL H 309       4.704   9.034   4.325  1.00 48.72           C  
ANISOU 2387  CA  VAL H 309     5394   5462   7655    163  -1065   -734       C  
ATOM   2388  C   VAL H 309       3.816   9.394   3.127  1.00 52.00           C  
ANISOU 2388  C   VAL H 309     5802   5705   8250    520  -1311   -841       C  
ATOM   2389  O   VAL H 309       3.344   8.506   2.424  1.00 54.86           O  
ANISOU 2389  O   VAL H 309     5982   6067   8795    611  -1563   -852       O  
ATOM   2390  CB  VAL H 309       6.110   8.629   3.830  1.00 46.11           C  
ANISOU 2390  CB  VAL H 309     4994   5480   7045    -21  -1083   -325       C  
ATOM   2391  CG1 VAL H 309       6.760   9.749   3.065  1.00 49.45           C  
ANISOU 2391  CG1 VAL H 309     5601   5930   7256   -199  -1292     83       C  
ATOM   2392  CG2 VAL H 309       6.982   8.211   4.993  1.00 45.78           C  
ANISOU 2392  CG2 VAL H 309     4805   5709   6879   -400   -952    -75       C  
ATOM   2393  N   ARG H 310       3.604  10.686   2.898  1.00 53.83           N  
ANISOU 2393  N   ARG H 310     6458   5651   8345    687  -1410   -891       N  
ATOM   2394  CA  ARG H 310       2.920  11.164   1.691  1.00 58.11           C  
ANISOU 2394  CA  ARG H 310     7062   6028   8987   1035  -1692   -938       C  
ATOM   2395  C   ARG H 310       3.889  11.554   0.562  1.00 56.29           C  
ANISOU 2395  C   ARG H 310     7197   5752   8438    886  -1898   -714       C  
ATOM   2396  O   ARG H 310       4.808  12.338   0.747  1.00 58.56           O  
ANISOU 2396  O   ARG H 310     7816   5983   8450    480  -1955   -397       O  
ATOM   2397  CB  ARG H 310       1.997  12.348   2.026  1.00 66.99           C  
ANISOU 2397  CB  ARG H 310     8532   6877  10042   1594  -1628  -1044       C  
ATOM   2398  CG  ARG H 310       1.048  12.090   3.195  1.00 73.98           C  
ANISOU 2398  CG  ARG H 310     8981   8074  11053   2110  -1154   -971       C  
ATOM   2399  CD  ARG H 310       0.420  13.375   3.716  1.00 86.38           C  
ANISOU 2399  CD  ARG H 310    11361   9334  12125   3121   -890  -1026       C  
ATOM   2400  NE  ARG H 310       0.324  13.341   5.180  1.00 95.05           N  
ANISOU 2400  NE  ARG H 310    12829  10491  12794   3624   -334  -1013       N  
ATOM   2401  CZ  ARG H 310       0.334  14.408   5.987  1.00104.01           C  
ANISOU 2401  CZ  ARG H 310    15543  10961  13014   4477   -203  -1223       C  
ATOM   2402  NH1 ARG H 310       0.442  15.645   5.507  1.00108.33           N  
ANISOU 2402  NH1 ARG H 310    17496  10646  13019   4806   -679  -1450       N  
ATOM   2403  NH2 ARG H 310       0.245  14.232   7.304  1.00109.78           N  
ANISOU 2403  NH2 ARG H 310    16737  11749  13223   5061    323  -1197       N  
ATOM   2404  N   GLY H 311       3.693  10.978  -0.619  1.00 57.55           N  
ANISOU 2404  N   GLY H 311     7364   5938   8561   1188  -2100   -719       N  
ATOM   2405  CA  GLY H 311       4.444  11.379  -1.800  1.00 58.65           C  
ANISOU 2405  CA  GLY H 311     7872   6147   8263   1372  -2136   -387       C  
ATOM   2406  C   GLY H 311       5.627  10.473  -2.051  1.00 61.56           C  
ANISOU 2406  C   GLY H 311     8178   7040   8170   1609  -1774     57       C  
ATOM   2407  O   GLY H 311       6.249   9.943  -1.108  1.00 60.36           O  
ANISOU 2407  O   GLY H 311     7644   7233   8055   1353  -1493    232       O  
ATOM   2408  N   ARG H 312       5.941  10.304  -3.329  1.00 69.19           N  
ANISOU 2408  N   ARG H 312     9744   8199   8344   2647  -4069  -1170       N  
ATOM   2409  CA  ARG H 312       7.025   9.445  -3.734  1.00 70.94           C  
ANISOU 2409  CA  ARG H 312    10283   8604   8067   2939  -4181  -1491       C  
ATOM   2410  C   ARG H 312       8.372  10.047  -3.262  1.00 63.30           C  
ANISOU 2410  C   ARG H 312     9479   7963   6609   2656  -3094   -920       C  
ATOM   2411  O   ARG H 312       9.175   9.324  -2.711  1.00 57.98           O  
ANISOU 2411  O   ARG H 312     8699   7257   6072   2350  -2922   -965       O  
ATOM   2412  CB  ARG H 312       6.968   9.196  -5.257  1.00 80.16           C  
ANISOU 2412  CB  ARG H 312    12029  10100   8326   4129  -4961  -2052       C  
ATOM   2413  CG  ARG H 312       8.091   8.338  -5.829  1.00 85.42           C  
ANISOU 2413  CG  ARG H 312    13154  11120   8179   4844  -5074  -2418       C  
ATOM   2414  CD  ARG H 312       7.870   6.828  -5.743  1.00 90.63           C  
ANISOU 2414  CD  ARG H 312    13657  11149   9628   4853  -6283  -3335       C  
ATOM   2415  NE  ARG H 312       9.127   6.138  -6.065  1.00 95.44           N  
ANISOU 2415  NE  ARG H 312    14715  12156   9390   5484  -6094  -3549       N  
ATOM   2416  CZ  ARG H 312       9.427   4.870  -5.782  1.00 98.65           C  
ANISOU 2416  CZ  ARG H 312    15008  12055  10416   5387  -6758  -4134       C  
ATOM   2417  NH1 ARG H 312       8.556   4.079  -5.166  1.00101.98           N  
ANISOU 2417  NH1 ARG H 312    14763  11452  12532   4628  -7700  -4464       N  
ATOM   2418  NH2 ARG H 312      10.621   4.391  -6.119  1.00 99.70           N  
ANISOU 2418  NH2 ARG H 312    15600  12695   9586   6105  -6424  -4232       N  
ATOM   2419  N   GLU H 313       8.591  11.354  -3.436  1.00 62.75           N  
ANISOU 2419  N   GLU H 313     9556   8074   6212   2719  -2473   -345       N  
ATOM   2420  CA  GLU H 313       9.925  11.966  -3.187  1.00 63.37           C  
ANISOU 2420  CA  GLU H 313     9632   8275   6169   2501  -1677    288       C  
ATOM   2421  C   GLU H 313      10.409  11.661  -1.765  1.00 55.38           C  
ANISOU 2421  C   GLU H 313     8322   6947   5774   1687  -1509    183       C  
ATOM   2422  O   GLU H 313      11.540  11.202  -1.519  1.00 56.16           O  
ANISOU 2422  O   GLU H 313     8351   7151   5833   1531  -1256    304       O  
ATOM   2423  CB  GLU H 313       9.935  13.501  -3.365  1.00 68.86           C  
ANISOU 2423  CB  GLU H 313    10305   8840   7017   2499  -1222    997       C  
ATOM   2424  CG  GLU H 313       8.805  14.163  -4.164  1.00 77.84           C  
ANISOU 2424  CG  GLU H 313    11620  10062   7893   3039  -1449   1051       C  
ATOM   2425  CD  GLU H 313       8.747  13.776  -5.647  1.00 88.63           C  
ANISOU 2425  CD  GLU H 313    13355  12107   8213   4207  -1645   1072       C  
ATOM   2426  OE1 GLU H 313       9.599  12.984  -6.120  1.00 95.82           O  
ANISOU 2426  OE1 GLU H 313    14432  13471   8503   4732  -1566   1045       O  
ATOM   2427  OE2 GLU H 313       7.840  14.273  -6.357  1.00 95.22           O  
ANISOU 2427  OE2 GLU H 313    14363  13088   8728   4786  -1918   1083       O  
ATOM   2428  N   ARG H 314       9.500  11.890  -0.838  1.00 49.13           N  
ANISOU 2428  N   ARG H 314     7345   5863   5457   1345  -1644     -2       N  
ATOM   2429  CA  ARG H 314       9.774  11.807   0.559  1.00 47.95           C  
ANISOU 2429  CA  ARG H 314     6996   5566   5656    914  -1474    -67       C  
ATOM   2430  C   ARG H 314       9.945  10.363   1.024  1.00 46.46           C  
ANISOU 2430  C   ARG H 314     6561   5475   5614    770  -1591   -253       C  
ATOM   2431  O   ARG H 314      10.793  10.071   1.875  1.00 42.52           O  
ANISOU 2431  O   ARG H 314     5984   5027   5142    538  -1376   -234       O  
ATOM   2432  CB  ARG H 314       8.627  12.448   1.311  1.00 47.79           C  
ANISOU 2432  CB  ARG H 314     6875   5413   5869    988  -1494    -93       C  
ATOM   2433  CG  ARG H 314       9.039  13.452   2.324  1.00 48.34           C  
ANISOU 2433  CG  ARG H 314     7095   5282   5990    968  -1369   -163       C  
ATOM   2434  CD  ARG H 314       7.806  14.101   2.879  1.00 50.72           C  
ANISOU 2434  CD  ARG H 314     7392   5576   6301   1363  -1369   -198       C  
ATOM   2435  NE  ARG H 314       7.524  15.246   2.089  1.00 54.80           N  
ANISOU 2435  NE  ARG H 314     8129   5781   6911   1459  -1474   -107       N  
ATOM   2436  CZ  ARG H 314       6.331  15.607   1.643  1.00 55.13           C  
ANISOU 2436  CZ  ARG H 314     8118   5864   6965   1749  -1509     24       C  
ATOM   2437  NH1 ARG H 314       5.238  14.904   1.898  1.00 57.55           N  
ANISOU 2437  NH1 ARG H 314     8043   6460   7362   1934  -1484    143       N  
ATOM   2438  NH2 ARG H 314       6.259  16.683   0.920  1.00 54.77           N  
ANISOU 2438  NH2 ARG H 314     8285   5516   7006   1852  -1572    180       N  
ATOM   2439  N   TYR H 315       9.076   9.496   0.521  1.00 46.50           N  
ANISOU 2439  N   TYR H 315     6379   5401   5887    926  -2052   -426       N  
ATOM   2440  CA  TYR H 315       9.190   8.069   0.731  1.00 47.79           C  
ANISOU 2440  CA  TYR H 315     6234   5431   6490    816  -2355   -568       C  
ATOM   2441  C   TYR H 315      10.552   7.538   0.336  1.00 46.71           C  
ANISOU 2441  C   TYR H 315     6399   5478   5868    903  -2265   -738       C  
ATOM   2442  O   TYR H 315      11.119   6.762   1.085  1.00 46.86           O  
ANISOU 2442  O   TYR H 315     6196   5476   6130    654  -2123   -675       O  
ATOM   2443  CB  TYR H 315       8.135   7.301  -0.072  1.00 52.10           C  
ANISOU 2443  CB  TYR H 315     6543   5600   7652   1042  -3246   -874       C  
ATOM   2444  CG  TYR H 315       8.323   5.810  -0.020  1.00 54.95           C  
ANISOU 2444  CG  TYR H 315     6579   5564   8735    965  -3814  -1102       C  
ATOM   2445  CD1 TYR H 315       8.090   5.111   1.155  1.00 55.14           C  
ANISOU 2445  CD1 TYR H 315     5870   5354   9723    545  -3572   -549       C  
ATOM   2446  CD2 TYR H 315       8.720   5.093  -1.139  1.00 60.24           C  
ANISOU 2446  CD2 TYR H 315     7671   6100   9118   1487  -4610  -1823       C  
ATOM   2447  CE1 TYR H 315       8.254   3.740   1.222  1.00 60.04           C  
ANISOU 2447  CE1 TYR H 315     6083   5452  11275    435  -4122   -628       C  
ATOM   2448  CE2 TYR H 315       8.879   3.706  -1.091  1.00 65.17           C  
ANISOU 2448  CE2 TYR H 315     8016   6169  10574   1472  -5323  -2152       C  
ATOM   2449  CZ  TYR H 315       8.646   3.034   0.100  1.00 64.87           C  
ANISOU 2449  CZ  TYR H 315     7142   5736  11770    835  -5081  -1509       C  
ATOM   2450  OH  TYR H 315       8.810   1.660   0.192  1.00 70.25           O  
ANISOU 2450  OH  TYR H 315     7429   5723  13538    767  -5784  -1682       O  
ATOM   2451  N   GLU H 316      11.043   7.915  -0.846  1.00 49.05           N  
ANISOU 2451  N   GLU H 316     7146   6036   5454   1398  -2285   -826       N  
ATOM   2452  CA  GLU H 316      12.344   7.438  -1.321  1.00 51.75           C  
ANISOU 2452  CA  GLU H 316     7717   6703   5240   1721  -2066   -799       C  
ATOM   2453  C   GLU H 316      13.487   7.893  -0.386  1.00 47.95           C  
ANISOU 2453  C   GLU H 316     7031   6309   4877   1185  -1383   -313       C  
ATOM   2454  O   GLU H 316      14.389   7.129  -0.088  1.00 47.05           O  
ANISOU 2454  O   GLU H 316     6830   6298   4749   1118  -1260   -312       O  
ATOM   2455  CB  GLU H 316      12.611   7.855  -2.776  1.00 59.97           C  
ANISOU 2455  CB  GLU H 316     9213   8225   5347   2676  -2020   -695       C  
ATOM   2456  CG  GLU H 316      11.915   6.968  -3.822  1.00 70.38           C  
ANISOU 2456  CG  GLU H 316    10905   9541   6293   3591  -3005  -1506       C  
ATOM   2457  CD  GLU H 316      12.199   7.361  -5.281  1.00 81.21           C  
ANISOU 2457  CD  GLU H 316    12850  11655   6351   4976  -2923  -1393       C  
ATOM   2458  OE1 GLU H 316      11.590   8.330  -5.788  1.00 87.12           O  
ANISOU 2458  OE1 GLU H 316    13701  12580   6820   5262  -2823  -1091       O  
ATOM   2459  OE2 GLU H 316      13.002   6.677  -5.953  1.00 88.72           O  
ANISOU 2459  OE2 GLU H 316    14169  13095   6443   5980  -2947  -1568       O  
ATOM   2460  N   ILE H 317      13.432   9.119   0.095  1.00 45.07           N  
ANISOU 2460  N   ILE H 317     6581   5811   4731    854  -1104     12       N  
ATOM   2461  CA  ILE H 317      14.508   9.662   0.915  1.00 44.25           C  
ANISOU 2461  CA  ILE H 317     6272   5604   4937    429   -803    321       C  
ATOM   2462  C   ILE H 317      14.508   8.959   2.250  1.00 39.23           C  
ANISOU 2462  C   ILE H 317     5476   4912   4518    116   -917      0       C  
ATOM   2463  O   ILE H 317      15.561   8.492   2.711  1.00 34.36           O  
ANISOU 2463  O   ILE H 317     4712   4388   3955    -42   -808     70       O  
ATOM   2464  CB  ILE H 317      14.406  11.200   1.090  1.00 47.72           C  
ANISOU 2464  CB  ILE H 317     6674   5673   5782    250   -780    594       C  
ATOM   2465  CG1 ILE H 317      14.597  11.894  -0.250  1.00 54.74           C  
ANISOU 2465  CG1 ILE H 317     7575   6681   6543    636   -484   1267       C  
ATOM   2466  CG2 ILE H 317      15.494  11.710   2.002  1.00 51.58           C  
ANISOU 2466  CG2 ILE H 317     6901   5819   6878   -161   -863    704       C  
ATOM   2467  CD1 ILE H 317      14.047  13.319  -0.313  1.00 59.43           C  
ANISOU 2467  CD1 ILE H 317     8155   6815   7607    565   -556   1528       C  
ATOM   2468  N   LEU H 318      13.313   8.819   2.831  1.00 36.46           N  
ANISOU 2468  N   LEU H 318     5078   4491   4284    148  -1071   -205       N  
ATOM   2469  CA  LEU H 318      13.187   8.180   4.152  1.00 35.57           C  
ANISOU 2469  CA  LEU H 318     4729   4488   4294    108  -1005   -227       C  
ATOM   2470  C   LEU H 318      13.486   6.675   4.141  1.00 34.67           C  
ANISOU 2470  C   LEU H 318     4370   4433   4369     57  -1025   -173       C  
ATOM   2471  O   LEU H 318      14.070   6.138   5.106  1.00 33.44           O  
ANISOU 2471  O   LEU H 318     4041   4450   4212     23   -855    -59       O  
ATOM   2472  CB  LEU H 318      11.827   8.457   4.798  1.00 36.27           C  
ANISOU 2472  CB  LEU H 318     4670   4612   4499    360   -965   -120       C  
ATOM   2473  CG  LEU H 318      11.530   9.928   5.085  1.00 38.59           C  
ANISOU 2473  CG  LEU H 318     5264   4820   4579    569  -1008   -285       C  
ATOM   2474  CD1 LEU H 318      10.049  10.196   5.392  1.00 41.70           C  
ANISOU 2474  CD1 LEU H 318     5497   5319   5026    969   -899    -82       C  
ATOM   2475  CD2 LEU H 318      12.403  10.430   6.221  1.00 41.07           C  
ANISOU 2475  CD2 LEU H 318     5769   5189   4646    743  -1112   -567       C  
ATOM   2476  N   LYS H 319      13.058   6.005   3.080  1.00 37.16           N  
ANISOU 2476  N   LYS H 319     4691   4560   4867    165  -1355   -317       N  
ATOM   2477  CA  LYS H 319      13.398   4.611   2.867  1.00 39.33           C  
ANISOU 2477  CA  LYS H 319     4812   4686   5442    211  -1614   -434       C  
ATOM   2478  C   LYS H 319      14.925   4.445   2.787  1.00 37.89           C  
ANISOU 2478  C   LYS H 319     4830   4796   4769    237  -1328   -439       C  
ATOM   2479  O   LYS H 319      15.475   3.552   3.396  1.00 37.13           O  
ANISOU 2479  O   LYS H 319     4521   4708   4877    146  -1256   -354       O  
ATOM   2480  CB  LYS H 319      12.771   4.109   1.593  1.00 43.20           C  
ANISOU 2480  CB  LYS H 319     5456   4855   6103    564  -2322   -876       C  
ATOM   2481  CG  LYS H 319      12.945   2.634   1.316  1.00 49.53           C  
ANISOU 2481  CG  LYS H 319     6127   5244   7446    736  -2933  -1209       C  
ATOM   2482  CD  LYS H 319      12.230   2.265   0.016  1.00 58.40           C  
ANISOU 2482  CD  LYS H 319     7519   5961   8709   1312  -3990  -1926       C  
ATOM   2483  CE  LYS H 319      12.178   0.759  -0.212  1.00 66.74           C  
ANISOU 2483  CE  LYS H 319     8386   6265  10705   1524  -4999  -2442       C  
ATOM   2484  NZ  LYS H 319      13.511   0.103  -0.133  1.00 65.69           N  
ANISOU 2484  NZ  LYS H 319     8525   6403  10029   1763  -4677  -2535       N  
ATOM   2485  N   LYS H 320      15.573   5.284   1.994  1.00 38.79           N  
ANISOU 2485  N   LYS H 320     5241   5143   4352    418  -1131   -375       N  
ATOM   2486  CA  LYS H 320      17.014   5.251   1.832  1.00 40.96           C  
ANISOU 2486  CA  LYS H 320     5510   5712   4339    492   -776   -106       C  
ATOM   2487  C   LYS H 320      17.695   5.348   3.194  1.00 37.76           C  
ANISOU 2487  C   LYS H 320     4807   5306   4233     18   -607     53       C  
ATOM   2488  O   LYS H 320      18.587   4.554   3.496  1.00 36.02           O  
ANISOU 2488  O   LYS H 320     4441   5230   4015     16   -502    125       O  
ATOM   2489  CB  LYS H 320      17.444   6.419   0.952  1.00 46.26           C  
ANISOU 2489  CB  LYS H 320     6267   6576   4731    716   -457    351       C  
ATOM   2490  CG  LYS H 320      18.825   6.332   0.353  1.00 52.40           C  
ANISOU 2490  CG  LYS H 320     6898   7753   5258   1074     13    941       C  
ATOM   2491  CD  LYS H 320      18.981   7.411  -0.711  1.00 60.88           C  
ANISOU 2491  CD  LYS H 320     7936   9062   6130   1525    425   1692       C  
ATOM   2492  CE  LYS H 320      20.431   7.788  -0.912  1.00 67.63           C  
ANISOU 2492  CE  LYS H 320     8225  10164   7304   1601   1055   2786       C  
ATOM   2493  NZ  LYS H 320      21.194   6.662  -1.497  1.00 72.36           N  
ANISOU 2493  NZ  LYS H 320     8935  11403   7155   2435   1371   2888       N  
ATOM   2494  N   LEU H 321      17.232   6.291   4.019  1.00 35.11           N  
ANISOU 2494  N   LEU H 321     4438   4829   4070   -217   -676     18       N  
ATOM   2495  CA  LEU H 321      17.785   6.510   5.329  1.00 35.69           C  
ANISOU 2495  CA  LEU H 321     4371   4941   4247   -368   -743    -35       C  
ATOM   2496  C   LEU H 321      17.528   5.321   6.240  1.00 36.09           C  
ANISOU 2496  C   LEU H 321     4267   5211   4232   -229   -660    -32       C  
ATOM   2497  O   LEU H 321      18.421   4.876   6.965  1.00 34.82           O  
ANISOU 2497  O   LEU H 321     3967   5242   4020   -224   -634     14       O  
ATOM   2498  CB  LEU H 321      17.204   7.774   6.014  1.00 37.21           C  
ANISOU 2498  CB  LEU H 321     4714   4939   4482   -310  -1007   -270       C  
ATOM   2499  CG  LEU H 321      17.384   9.155   5.370  1.00 38.64           C  
ANISOU 2499  CG  LEU H 321     4946   4695   5040   -478  -1198   -191       C  
ATOM   2500  CD1 LEU H 321      16.753  10.196   6.260  1.00 40.68           C  
ANISOU 2500  CD1 LEU H 321     5434   4698   5324   -254  -1628   -637       C  
ATOM   2501  CD2 LEU H 321      18.844   9.510   5.088  1.00 42.85           C  
ANISOU 2501  CD2 LEU H 321     5123   4994   6164   -783  -1275    188       C  
ATOM   2502  N   ASN H 322      16.303   4.820   6.229  1.00 34.43           N  
ANISOU 2502  N   ASN H 322     3964   4940   4177    -93   -628     55       N  
ATOM   2503  CA  ASN H 322      15.944   3.728   7.123  1.00 36.15           C  
ANISOU 2503  CA  ASN H 322     3808   5293   4635     73   -454    410       C  
ATOM   2504  C   ASN H 322      16.694   2.446   6.739  1.00 36.54           C  
ANISOU 2504  C   ASN H 322     3701   5205   4977    -40   -505    458       C  
ATOM   2505  O   ASN H 322      17.227   1.793   7.631  1.00 37.27           O  
ANISOU 2505  O   ASN H 322     3565   5528   5067     60   -305    738       O  
ATOM   2506  CB  ASN H 322      14.429   3.531   7.142  1.00 38.73           C  
ANISOU 2506  CB  ASN H 322     3806   5444   5463    204   -429    759       C  
ATOM   2507  CG  ASN H 322      13.961   2.541   8.187  1.00 43.09           C  
ANISOU 2507  CG  ASN H 322     3724   6154   6491    474    -82   1549       C  
ATOM   2508  OD1 ASN H 322      14.094   2.746   9.379  1.00 46.31           O  
ANISOU 2508  OD1 ASN H 322     4088   7150   6355    973    323   1885       O  
ATOM   2509  ND2 ASN H 322      13.357   1.476   7.726  1.00 47.02           N  
ANISOU 2509  ND2 ASN H 322     3682   6089   8094    273   -314   1904       N  
ATOM   2510  N   ASP H 323      16.768   2.112   5.442  1.00 35.67           N  
ANISOU 2510  N   ASP H 323     3775   4786   4989    -65   -800    150       N  
ATOM   2511  CA  ASP H 323      17.493   0.915   4.987  1.00 37.71           C  
ANISOU 2511  CA  ASP H 323     4013   4895   5418     58   -960     34       C  
ATOM   2512  C   ASP H 323      18.971   1.039   5.390  1.00 37.18           C  
ANISOU 2512  C   ASP H 323     3984   5267   4873     29   -605    159       C  
ATOM   2513  O   ASP H 323      19.608   0.053   5.712  1.00 37.41           O  
ANISOU 2513  O   ASP H 323     3842   5312   5058    101   -557    273       O  
ATOM   2514  CB  ASP H 323      17.436   0.713   3.465  1.00 40.33           C  
ANISOU 2514  CB  ASP H 323     4740   5013   5569    442  -1408   -479       C  
ATOM   2515  CG  ASP H 323      16.040   0.245   2.939  1.00 47.58           C  
ANISOU 2515  CG  ASP H 323     5557   5277   7242    542  -2149   -789       C  
ATOM   2516  OD1 ASP H 323      15.175  -0.183   3.736  1.00 48.18           O  
ANISOU 2516  OD1 ASP H 323     5056   4963   8287    232  -2240   -388       O  
ATOM   2517  OD2 ASP H 323      15.831   0.287   1.684  1.00 52.39           O  
ANISOU 2517  OD2 ASP H 323     6612   5780   7512   1061  -2685  -1368       O  
ATOM   2518  N   SER H 324      19.502   2.253   5.314  1.00 36.59           N  
ANISOU 2518  N   SER H 324     4046   5436   4420    -83   -449    185       N  
ATOM   2519  CA  SER H 324      20.881   2.515   5.640  1.00 38.49           C  
ANISOU 2519  CA  SER H 324     4139   5936   4548   -180   -281    383       C  
ATOM   2520  C   SER H 324      21.114   2.258   7.117  1.00 38.71           C  
ANISOU 2520  C   SER H 324     3960   6137   4609   -232   -316    430       C  
ATOM   2521  O   SER H 324      22.071   1.605   7.481  1.00 40.18           O  
ANISOU 2521  O   SER H 324     3955   6507   4802   -192   -239    576       O  
ATOM   2522  CB  SER H 324      21.240   3.963   5.279  1.00 40.13           C  
ANISOU 2522  CB  SER H 324     4336   6091   4819   -356   -291    525       C  
ATOM   2523  OG  SER H 324      22.632   4.163   5.340  1.00 43.74           O  
ANISOU 2523  OG  SER H 324     4436   6653   5531   -472   -204    900       O  
ATOM   2524  N   LEU H 325      20.233   2.777   7.961  1.00 38.23           N  
ANISOU 2524  N   LEU H 325     3961   6116   4447   -136   -407    342       N  
ATOM   2525  CA  LEU H 325      20.355   2.602   9.389  1.00 40.92           C  
ANISOU 2525  CA  LEU H 325     4203   6831   4513    201   -412    412       C  
ATOM   2526  C   LEU H 325      20.350   1.124   9.762  1.00 42.91           C  
ANISOU 2526  C   LEU H 325     4141   7224   4936    373    -92    880       C  
ATOM   2527  O   LEU H 325      21.178   0.675  10.565  1.00 43.58           O  
ANISOU 2527  O   LEU H 325     4093   7650   4812    592    -55   1015       O  
ATOM   2528  CB  LEU H 325      19.285   3.372  10.116  1.00 43.32           C  
ANISOU 2528  CB  LEU H 325     4678   7297   4485    616   -457    319       C  
ATOM   2529  CG  LEU H 325      19.449   4.890  10.029  1.00 45.21           C  
ANISOU 2529  CG  LEU H 325     5235   7289   4651    549   -969   -239       C  
ATOM   2530  CD1 LEU H 325      18.181   5.632  10.439  1.00 45.79           C  
ANISOU 2530  CD1 LEU H 325     5553   7459   4386   1038   -970   -366       C  
ATOM   2531  CD2 LEU H 325      20.606   5.340  10.915  1.00 48.66           C  
ANISOU 2531  CD2 LEU H 325     5716   7807   4964    751  -1568   -655       C  
ATOM   2532  N   GLU H 326      19.493   0.362   9.087  1.00 44.38           N  
ANISOU 2532  N   GLU H 326     4167   7024   5669    264      0   1101       N  
ATOM   2533  CA  GLU H 326      19.324  -1.052   9.372  1.00 47.88           C  
ANISOU 2533  CA  GLU H 326     4175   7296   6721    372    156   1631       C  
ATOM   2534  C   GLU H 326      20.523  -1.855   8.910  1.00 47.26           C  
ANISOU 2534  C   GLU H 326     4135   7111   6711    287     62   1459       C  
ATOM   2535  O   GLU H 326      20.872  -2.847   9.535  1.00 51.91           O  
ANISOU 2535  O   GLU H 326     4396   7746   7579    449    226   1899       O  
ATOM   2536  CB  GLU H 326      18.021  -1.590   8.761  1.00 50.40           C  
ANISOU 2536  CB  GLU H 326     4189   6953   8007    254    -37   1847       C  
ATOM   2537  CG  GLU H 326      16.795  -1.089   9.535  1.00 55.57           C  
ANISOU 2537  CG  GLU H 326     4519   7839   8755    502    282   2450       C  
ATOM   2538  CD  GLU H 326      15.467  -1.679   9.093  1.00 61.09           C  
ANISOU 2538  CD  GLU H 326     4612   7807  10791    349     56   2935       C  
ATOM   2539  OE1 GLU H 326      15.392  -2.314   8.015  1.00 62.18           O  
ANISOU 2539  OE1 GLU H 326     4759   7128  11735     46   -626   2461       O  
ATOM   2540  OE2 GLU H 326      14.480  -1.488   9.835  1.00 65.40           O  
ANISOU 2540  OE2 GLU H 326     4639   8600  11609    661    493   3800       O  
ATOM   2541  N   LEU H 327      21.143  -1.438   7.823  1.00 42.82           N  
ANISOU 2541  N   LEU H 327     3920   6469   5880    165   -115    967       N  
ATOM   2542  CA  LEU H 327      22.293  -2.127   7.329  1.00 43.74           C  
ANISOU 2542  CA  LEU H 327     4069   6626   5924    296    -97    892       C  
ATOM   2543  C   LEU H 327      23.404  -2.001   8.388  1.00 46.27           C  
ANISOU 2543  C   LEU H 327     4171   7459   5949    283    110   1162       C  
ATOM   2544  O   LEU H 327      24.003  -3.014   8.791  1.00 46.52           O  
ANISOU 2544  O   LEU H 327     3988   7556   6130    449    216   1407       O  
ATOM   2545  CB  LEU H 327      22.742  -1.554   6.006  1.00 41.26           C  
ANISOU 2545  CB  LEU H 327     4087   6371   5218    438   -126    596       C  
ATOM   2546  CG  LEU H 327      24.060  -2.168   5.475  1.00 43.44           C  
ANISOU 2546  CG  LEU H 327     4353   6903   5247    821     63    691       C  
ATOM   2547  CD1 LEU H 327      23.888  -3.632   5.106  1.00 45.32           C  
ANISOU 2547  CD1 LEU H 327     4714   6722   5784   1265   -249    398       C  
ATOM   2548  CD2 LEU H 327      24.592  -1.366   4.293  1.00 44.57           C  
ANISOU 2548  CD2 LEU H 327     4662   7378   4894   1160    309    809       C  
ATOM   2549  N   SER H 328      23.628  -0.786   8.888  1.00 44.09           N  
ANISOU 2549  N   SER H 328     3936   7455   5360    148     20   1062       N  
ATOM   2550  CA  SER H 328      24.699  -0.587   9.849  1.00 48.23           C  
ANISOU 2550  CA  SER H 328     4261   8354   5707    213   -107   1123       C  
ATOM   2551  C   SER H 328      24.423  -1.244  11.249  1.00 49.41           C  
ANISOU 2551  C   SER H 328     4296   8894   5583    673    -14   1380       C  
ATOM   2552  O   SER H 328      25.340  -1.392  12.067  1.00 50.18           O  
ANISOU 2552  O   SER H 328     4248   9369   5447    914   -164   1422       O  
ATOM   2553  CB  SER H 328      25.090   0.900   9.914  1.00 50.29           C  
ANISOU 2553  CB  SER H 328     4545   8544   6018    -10   -548    829       C  
ATOM   2554  OG  SER H 328      24.219   1.580  10.764  1.00 59.63           O  
ANISOU 2554  OG  SER H 328     5982   9802   6872    245   -823    512       O  
ATOM   2555  N   ASP H 329      23.183  -1.668  11.494  1.00 47.99           N  
ANISOU 2555  N   ASP H 329     4081   8652   5501    885    259   1703       N  
ATOM   2556  CA  ASP H 329      22.850  -2.504  12.640  1.00 53.21           C  
ANISOU 2556  CA  ASP H 329     4437   9711   6067   1460    617   2391       C  
ATOM   2557  C   ASP H 329      23.234  -3.982  12.454  1.00 52.49           C  
ANISOU 2557  C   ASP H 329     3967   9327   6650   1397    846   2909       C  
ATOM   2558  O   ASP H 329      23.274  -4.730  13.409  1.00 55.28           O  
ANISOU 2558  O   ASP H 329     3973  10031   6998   1885   1181   3632       O  
ATOM   2559  CB  ASP H 329      21.349  -2.432  12.949  1.00 59.26           C  
ANISOU 2559  CB  ASP H 329     5040  10480   6995   1756    940   2911       C  
ATOM   2560  CG  ASP H 329      20.947  -1.134  13.616  1.00 63.53           C  
ANISOU 2560  CG  ASP H 329     5958  11553   6626   2272    801   2545       C  
ATOM   2561  OD1 ASP H 329      21.818  -0.374  14.092  1.00 70.07           O  
ANISOU 2561  OD1 ASP H 329     7145  12719   6756   2513    317   1881       O  
ATOM   2562  OD2 ASP H 329      19.745  -0.864  13.652  1.00 65.74           O  
ANISOU 2562  OD2 ASP H 329     6145  11827   7004   2485   1061   2887       O  
ATOM   2563  N   VAL H 330      23.503  -4.413  11.234  1.00 49.38           N  
ANISOU 2563  N   VAL H 330     3655   8313   6794    972    648   2566       N  
ATOM   2564  CA  VAL H 330      23.863  -5.818  11.020  1.00 52.35           C  
ANISOU 2564  CA  VAL H 330     3754   8269   7865   1040    681   2879       C  
ATOM   2565  C   VAL H 330      25.273  -6.058  10.491  1.00 49.87           C  
ANISOU 2565  C   VAL H 330     3604   8083   7258   1054    599   2519       C  
ATOM   2566  O   VAL H 330      25.681  -7.203  10.397  1.00 54.57           O  
ANISOU 2566  O   VAL H 330     4026   8384   8321   1240    604   2718       O  
ATOM   2567  CB  VAL H 330      22.843  -6.523  10.100  1.00 55.06           C  
ANISOU 2567  CB  VAL H 330     3994   7620   9306    877    344   2811       C  
ATOM   2568  CG1 VAL H 330      21.468  -6.573  10.775  1.00 58.38           C  
ANISOU 2568  CG1 VAL H 330     3895   7854  10433    895    534   3606       C  
ATOM   2569  CG2 VAL H 330      22.780  -5.844   8.732  1.00 51.21           C  
ANISOU 2569  CG2 VAL H 330     4060   6896   8500    730    -53   1908       C  
ATOM   2570  N   VAL H 331      26.011  -5.000  10.149  1.00 47.03           N  
ANISOU 2570  N   VAL H 331     3468   8103   6296    904    528   2122       N  
ATOM   2571  CA  VAL H 331      27.404  -5.117   9.691  1.00 46.49           C  
ANISOU 2571  CA  VAL H 331     3338   8270   6054    984    583   2083       C  
ATOM   2572  C   VAL H 331      28.322  -4.916  10.892  1.00 48.00           C  
ANISOU 2572  C   VAL H 331     3220   9021   5995   1043    542   2331       C  
ATOM   2573  O   VAL H 331      28.248  -3.890  11.564  1.00 45.10           O  
ANISOU 2573  O   VAL H 331     2870   8904   5359    954    256   2154       O  
ATOM   2574  CB  VAL H 331      27.749  -4.112   8.577  1.00 46.35           C  
ANISOU 2574  CB  VAL H 331     3477   8297   5836    854    579   1856       C  
ATOM   2575  CG1 VAL H 331      29.198  -4.248   8.135  1.00 49.51           C  
ANISOU 2575  CG1 VAL H 331     3590   9038   6182   1070    810   2172       C  
ATOM   2576  CG2 VAL H 331      26.833  -4.319   7.376  1.00 46.23           C  
ANISOU 2576  CG2 VAL H 331     3874   7845   5843   1047    504   1498       C  
ATOM   2577  N   PRO H 332      29.173  -5.926  11.187  1.00 41.26           N  
ANISOU 2577  N   PRO H 332     4691   5030   5955    234    -85    152       N  
ATOM   2578  CA  PRO H 332      30.106  -5.774  12.294  1.00 39.91           C  
ANISOU 2578  CA  PRO H 332     4907   4627   5630    619    -28    112       C  
ATOM   2579  C   PRO H 332      30.992  -4.557  12.105  1.00 36.95           C  
ANISOU 2579  C   PRO H 332     4332   4455   5249    817   -212     75       C  
ATOM   2580  O   PRO H 332      31.368  -4.245  10.963  1.00 35.45           O  
ANISOU 2580  O   PRO H 332     3877   4474   5117    786   -391     49       O  
ATOM   2581  CB  PRO H 332      30.896  -7.064  12.251  1.00 41.15           C  
ANISOU 2581  CB  PRO H 332     5604   4503   5527    774    -69     38       C  
ATOM   2582  CG  PRO H 332      29.928  -8.068  11.764  1.00 44.79           C  
ANISOU 2582  CG  PRO H 332     6343   4704   5969    246     91     -6       C  
ATOM   2583  CD  PRO H 332      29.125  -7.319  10.722  1.00 44.02           C  
ANISOU 2583  CD  PRO H 332     5519   5109   6094   -145    -90     12       C  
ATOM   2584  N   ALA H 333      31.299  -3.875  13.214  1.00 36.39           N  
ANISOU 2584  N   ALA H 333     4513   4297   5015    885   -136     57       N  
ATOM   2585  CA  ALA H 333      32.267  -2.777  13.209  1.00 37.32           C  
ANISOU 2585  CA  ALA H 333     4646   4560   4971    769   -312    -31       C  
ATOM   2586  C   ALA H 333      33.502  -3.103  12.382  1.00 37.96           C  
ANISOU 2586  C   ALA H 333     4365   5082   4976    774   -645    -47       C  
ATOM   2587  O   ALA H 333      33.925  -2.279  11.576  1.00 38.75           O  
ANISOU 2587  O   ALA H 333     4258   5348   5115    561   -707    -66       O  
ATOM   2588  CB  ALA H 333      32.674  -2.377  14.621  1.00 39.78           C  
ANISOU 2588  CB  ALA H 333     5455   4785   4872    629   -307   -119       C  
ATOM   2589  N   SER H 334      34.063  -4.297  12.563  1.00 39.47           N  
ANISOU 2589  N   SER H 334     4543   5432   5022   1104   -753     14       N  
ATOM   2590  CA  SER H 334      35.303  -4.632  11.862  1.00 43.58           C  
ANISOU 2590  CA  SER H 334     4649   6482   5426   1351   -925     81       C  
ATOM   2591  C   SER H 334      35.054  -4.679  10.355  1.00 40.81           C  
ANISOU 2591  C   SER H 334     4167   6054   5282   1322   -794     11       C  
ATOM   2592  O   SER H 334      35.811  -4.092   9.603  1.00 39.38           O  
ANISOU 2592  O   SER H 334     3596   6296   5071   1201   -846     26       O  
ATOM   2593  CB  SER H 334      35.899  -5.962  12.367  1.00 46.76           C  
ANISOU 2593  CB  SER H 334     5211   6977   5578   2034   -925    271       C  
ATOM   2594  OG  SER H 334      34.921  -6.991  12.241  1.00 47.24           O  
ANISOU 2594  OG  SER H 334     5928   6290   5729   2168   -618    222       O  
ATOM   2595  N   ASP H 335      33.983  -5.356   9.936  1.00 40.86           N  
ANISOU 2595  N   ASP H 335     4518   5594   5412   1292   -637    -53       N  
ATOM   2596  CA  ASP H 335      33.655  -5.463   8.521  1.00 42.07           C  
ANISOU 2596  CA  ASP H 335     4656   5733   5594   1137   -603   -132       C  
ATOM   2597  C   ASP H 335      33.345  -4.095   7.927  1.00 40.74           C  
ANISOU 2597  C   ASP H 335     4145   5765   5566    829   -700    -61       C  
ATOM   2598  O   ASP H 335      33.788  -3.800   6.837  1.00 40.99           O  
ANISOU 2598  O   ASP H 335     4057   6017   5499    783   -713    -56       O  
ATOM   2599  CB  ASP H 335      32.463  -6.393   8.274  1.00 46.27           C  
ANISOU 2599  CB  ASP H 335     5602   5868   6107    843   -522   -218       C  
ATOM   2600  CG  ASP H 335      32.732  -7.809   8.693  1.00 51.70           C  
ANISOU 2600  CG  ASP H 335     7007   6076   6560   1107   -291   -288       C  
ATOM   2601  OD1 ASP H 335      33.728  -8.054   9.369  1.00 59.61           O  
ANISOU 2601  OD1 ASP H 335     8066   7130   7453   1719   -225   -170       O  
ATOM   2602  OD2 ASP H 335      31.943  -8.702   8.359  1.00 60.52           O  
ANISOU 2602  OD2 ASP H 335     8695   6772   7526    674   -170   -421       O  
ATOM   2603  N   ALA H 336      32.600  -3.262   8.650  1.00 38.80           N  
ANISOU 2603  N   ALA H 336     3878   5377   5486    714   -668     31       N  
ATOM   2604  CA  ALA H 336      32.311  -1.924   8.190  1.00 38.45           C  
ANISOU 2604  CA  ALA H 336     3764   5329   5514    627   -628    178       C  
ATOM   2605  C   ALA H 336      33.563  -1.131   7.817  1.00 41.53           C  
ANISOU 2605  C   ALA H 336     4156   5879   5741    423   -645    149       C  
ATOM   2606  O   ALA H 336      33.590  -0.553   6.723  1.00 42.93           O  
ANISOU 2606  O   ALA H 336     4322   6123   5866    343   -623    271       O  
ATOM   2607  CB  ALA H 336      31.476  -1.146   9.205  1.00 38.87           C  
ANISOU 2607  CB  ALA H 336     4014   5067   5686    744   -393    286       C  
ATOM   2608  N   GLU H 337      34.576  -1.094   8.692  1.00 43.65           N  
ANISOU 2608  N   GLU H 337     4401   6322   5859    254   -705     39       N  
ATOM   2609  CA  GLU H 337      35.812  -0.336   8.389  1.00 48.95           C  
ANISOU 2609  CA  GLU H 337     4899   7377   6320   -203   -739     40       C  
ATOM   2610  C   GLU H 337      36.602  -0.980   7.247  1.00 48.61           C  
ANISOU 2610  C   GLU H 337     4376   7880   6214    -26   -720     96       C  
ATOM   2611  O   GLU H 337      37.295  -0.287   6.527  1.00 49.05           O  
ANISOU 2611  O   GLU H 337     4273   8224   6136   -411   -619    168       O  
ATOM   2612  CB  GLU H 337      36.720  -0.063   9.635  1.00 54.87           C  
ANISOU 2612  CB  GLU H 337     5592   8464   6790   -644   -926    -48       C  
ATOM   2613  CG  GLU H 337      36.479   1.313  10.347  1.00 60.46           C  
ANISOU 2613  CG  GLU H 337     7076   8602   7291  -1304   -796   -172       C  
ATOM   2614  CD  GLU H 337      36.980   2.574   9.588  1.00 66.15           C  
ANISOU 2614  CD  GLU H 337     8116   9176   7840  -2049   -611   -151       C  
ATOM   2615  OE1 GLU H 337      37.693   2.392   8.572  1.00 73.25           O  
ANISOU 2615  OE1 GLU H 337     8408  10663   8761  -2152   -641    -24       O  
ATOM   2616  OE2 GLU H 337      36.685   3.756   9.990  1.00 64.41           O  
ANISOU 2616  OE2 GLU H 337     8904   8171   7394  -2534   -334   -250       O  
ATOM   2617  N   LYS H 338      36.488  -2.292   7.062  1.00 46.28           N  
ANISOU 2617  N   LYS H 338     4007   7632   5943    534   -705     63       N  
ATOM   2618  CA  LYS H 338      37.157  -2.923   5.931  1.00 48.96           C  
ANISOU 2618  CA  LYS H 338     4152   8320   6128    836   -514     83       C  
ATOM   2619  C   LYS H 338      36.512  -2.452   4.603  1.00 47.53           C  
ANISOU 2619  C   LYS H 338     4262   7903   5894    605   -435     87       C  
ATOM   2620  O   LYS H 338      37.219  -2.072   3.696  1.00 49.06           O  
ANISOU 2620  O   LYS H 338     4296   8442   5900    477   -248    163       O  
ATOM   2621  CB  LYS H 338      37.119  -4.430   6.087  1.00 53.39           C  
ANISOU 2621  CB  LYS H 338     4971   8701   6614   1508   -393     17       C  
ATOM   2622  CG  LYS H 338      37.772  -5.188   4.951  1.00 62.53           C  
ANISOU 2622  CG  LYS H 338     6223  10028   7508   1989    -18     -3       C  
ATOM   2623  CD  LYS H 338      38.580  -6.394   5.450  1.00 70.89           C  
ANISOU 2623  CD  LYS H 338     7306  11223   8405   2937    250    117       C  
ATOM   2624  CE  LYS H 338      38.885  -7.364   4.315  1.00 78.01           C  
ANISOU 2624  CE  LYS H 338     8810  11865   8963   3566    820     14       C  
ATOM   2625  NZ  LYS H 338      39.902  -8.401   4.673  1.00 89.15           N  
ANISOU 2625  NZ  LYS H 338    10205  13503  10165   4823   1274    275       N  
ATOM   2626  N   TYR H 339      35.175  -2.445   4.508  1.00 40.53           N  
ANISOU 2626  N   TYR H 339     3716   6567   5114    540   -583     78       N  
ATOM   2627  CA  TYR H 339      34.507  -1.898   3.347  1.00 41.63           C  
ANISOU 2627  CA  TYR H 339     4026   6672   5117    370   -639    213       C  
ATOM   2628  C   TYR H 339      34.858  -0.430   3.087  1.00 43.55           C  
ANISOU 2628  C   TYR H 339     4305   6907   5332    113   -530    445       C  
ATOM   2629  O   TYR H 339      34.999  -0.056   1.930  1.00 44.86           O  
ANISOU 2629  O   TYR H 339     4620   7196   5228     14   -450    588       O  
ATOM   2630  CB  TYR H 339      32.977  -2.009   3.491  1.00 39.72           C  
ANISOU 2630  CB  TYR H 339     3836   6255   5000    360   -879    310       C  
ATOM   2631  CG  TYR H 339      32.432  -3.384   3.298  1.00 39.34           C  
ANISOU 2631  CG  TYR H 339     3962   6181   4801    254   -990     93       C  
ATOM   2632  CD1 TYR H 339      32.394  -3.954   2.038  1.00 42.39           C  
ANISOU 2632  CD1 TYR H 339     4672   6693   4739     43  -1055    -25       C  
ATOM   2633  CD2 TYR H 339      31.927  -4.109   4.361  1.00 38.27           C  
ANISOU 2633  CD2 TYR H 339     3859   5819   4862    242   -982     -8       C  
ATOM   2634  CE1 TYR H 339      31.860  -5.205   1.841  1.00 45.68           C  
ANISOU 2634  CE1 TYR H 339     5537   6939   4880   -286  -1120   -293       C  
ATOM   2635  CE2 TYR H 339      31.382  -5.370   4.164  1.00 41.53           C  
ANISOU 2635  CE2 TYR H 339     4654   6070   5055    -72  -1019   -217       C  
ATOM   2636  CZ  TYR H 339      31.342  -5.897   2.899  1.00 45.22           C  
ANISOU 2636  CZ  TYR H 339     5530   6599   5049   -394  -1098   -382       C  
ATOM   2637  OH  TYR H 339      30.794  -7.131   2.671  1.00 50.58           O  
ANISOU 2637  OH  TYR H 339     6856   6993   5369   -939  -1105   -661       O  
ATOM   2638  N   ARG H 340      34.976   0.393   4.144  1.00 45.74           N  
ANISOU 2638  N   ARG H 340     4652   6945   5782    -60   -478    473       N  
ATOM   2639  CA  ARG H 340      35.312   1.804   3.966  1.00 52.86           C  
ANISOU 2639  CA  ARG H 340     5934   7591   6558   -457   -270    651       C  
ATOM   2640  C   ARG H 340      36.721   1.953   3.452  1.00 59.64           C  
ANISOU 2640  C   ARG H 340     6527   8953   7178   -967   -106    619       C  
ATOM   2641  O   ARG H 340      36.989   2.825   2.625  1.00 65.92           O  
ANISOU 2641  O   ARG H 340     7660   9640   7747  -1322    124    817       O  
ATOM   2642  CB  ARG H 340      35.143   2.620   5.244  1.00 55.69           C  
ANISOU 2642  CB  ARG H 340     6725   7434   6997   -664   -170    593       C  
ATOM   2643  CG  ARG H 340      33.697   2.823   5.651  1.00 56.53           C  
ANISOU 2643  CG  ARG H 340     7135   7041   7302    -59   -108    761       C  
ATOM   2644  CD  ARG H 340      33.556   3.743   6.852  1.00 61.38           C  
ANISOU 2644  CD  ARG H 340     8478   6977   7867   -186    190    683       C  
ATOM   2645  NE  ARG H 340      32.603   3.173   7.801  1.00 62.43           N  
ANISOU 2645  NE  ARG H 340     8450   7047   8221    324    199    644       N  
ATOM   2646  CZ  ARG H 340      31.378   3.625   8.059  1.00 66.69           C  
ANISOU 2646  CZ  ARG H 340     9241   7210   8887   1005    521    921       C  
ATOM   2647  NH1 ARG H 340      30.884   4.715   7.473  1.00 69.74           N  
ANISOU 2647  NH1 ARG H 340    10173   7134   9188   1458    867   1313       N  
ATOM   2648  NH2 ARG H 340      30.643   2.969   8.947  1.00 68.39           N  
ANISOU 2648  NH2 ARG H 340     9164   7541   9280   1318    569    871       N  
ATOM   2649  N   GLN H 341      37.629   1.105   3.930  1.00 63.33           N  
ANISOU 2649  N   GLN H 341     6359  10045   7659   -950   -173    451       N  
ATOM   2650  CA  GLN H 341      39.004   1.139   3.435  1.00 72.55           C  
ANISOU 2650  CA  GLN H 341     6951  12012   8602  -1311     38    518       C  
ATOM   2651  C   GLN H 341      39.092   0.577   2.014  1.00 75.04           C  
ANISOU 2651  C   GLN H 341     7254  12532   8724   -903    309    587       C  
ATOM   2652  O   GLN H 341      39.877   1.051   1.219  1.00 76.90           O  
ANISOU 2652  O   GLN H 341     7326  13181   8709  -1289    640    735       O  
ATOM   2653  CB  GLN H 341      39.956   0.439   4.401  1.00 76.48           C  
ANISOU 2653  CB  GLN H 341     6628  13318   9111  -1208   -112    471       C  
ATOM   2654  CG  GLN H 341      40.530   1.418   5.420  1.00 85.07           C  
ANISOU 2654  CG  GLN H 341     7611  14651  10061  -2205   -307    453       C  
ATOM   2655  CD  GLN H 341      41.018   0.760   6.694  1.00 89.72           C  
ANISOU 2655  CD  GLN H 341     7592  15890  10604  -2030   -682    433       C  
ATOM   2656  OE1 GLN H 341      42.161   0.964   7.110  1.00 96.78           O  
ANISOU 2656  OE1 GLN H 341     7651  17887  11233  -2638   -852    563       O  
ATOM   2657  NE2 GLN H 341      40.151  -0.023   7.328  1.00 84.16           N  
ANISOU 2657  NE2 GLN H 341     7265  14617  10092  -1266   -833    328       N  
ATOM   2658  N   LYS H 342      38.261  -0.415   1.706  1.00 75.87           N  
ANISOU 2658  N   LYS H 342     7641  12326   8858   -259    200    460       N  
ATOM   2659  CA  LYS H 342      38.106  -0.941   0.340  1.00 81.79           C  
ANISOU 2659  CA  LYS H 342     8727  13091   9258      2    405    442       C  
ATOM   2660  C   LYS H 342      37.077  -0.122  -0.470  1.00 81.35           C  
ANISOU 2660  C   LYS H 342     9259  12620   9029   -241    225    635       C  
ATOM   2661  O   LYS H 342      37.400   0.910  -1.068  1.00 81.48           O  
ANISOU 2661  O   LYS H 342     9464  12651   8844   -611    428    889       O  
ATOM   2662  CB  LYS H 342      37.695  -2.422   0.413  1.00 81.11           C  
ANISOU 2662  CB  LYS H 342     8885  12805   9126    584    364    174       C  
ATOM   2663  CG  LYS H 342      37.070  -3.000  -0.848  1.00 84.33           C  
ANISOU 2663  CG  LYS H 342     9999  12984   9059    615    401     37       C  
ATOM   2664  CD  LYS H 342      37.805  -4.243  -1.308  1.00 90.45           C  
ANISOU 2664  CD  LYS H 342    11103  13791   9469   1172    924   -198       C  
ATOM   2665  CE  LYS H 342      39.170  -3.877  -1.880  1.00 96.40           C  
ANISOU 2665  CE  LYS H 342    11387  15210  10031   1388   1531    -12       C  
ATOM   2666  NZ  LYS H 342      39.839  -5.033  -2.531  1.00102.83           N  
ANISOU 2666  NZ  LYS H 342    12663  16029  10378   2154   2238   -187       N  
TER    2667      LYS H 342                                                      
ATOM   2668  N   GLU I 303      -0.167   9.142 -15.784  1.00 78.45           N  
ANISOU 2668  N   GLU I 303     9387   9725  10695   1482    126  -2272       N  
ATOM   2669  CA  GLU I 303       1.130   9.592 -15.194  1.00 75.47           C  
ANISOU 2669  CA  GLU I 303     9648   8651  10375   1287    111  -2022       C  
ATOM   2670  C   GLU I 303       2.343   9.082 -16.023  1.00 71.15           C  
ANISOU 2670  C   GLU I 303     9284   8137   9610   1096   -145  -1603       C  
ATOM   2671  O   GLU I 303       2.656   7.889 -16.030  1.00 65.13           O  
ANISOU 2671  O   GLU I 303     8570   7595   8578    724   -100  -1691       O  
ATOM   2672  CB  GLU I 303       1.231   9.140 -13.735  1.00 76.68           C  
ANISOU 2672  CB  GLU I 303    10128   8637  10367    894    404  -2431       C  
ATOM   2673  CG  GLU I 303       2.355   9.834 -12.966  1.00 80.28           C  
ANISOU 2673  CG  GLU I 303    11007   8671  10822    769    360  -2462       C  
ATOM   2674  CD  GLU I 303       2.590   9.269 -11.568  1.00 82.44           C  
ANISOU 2674  CD  GLU I 303    11546   9144  10631    517    573  -2785       C  
ATOM   2675  OE1 GLU I 303       2.383   8.045 -11.358  1.00 84.09           O  
ANISOU 2675  OE1 GLU I 303    11815   9638  10495    394    788  -2666       O  
ATOM   2676  OE2 GLU I 303       3.005  10.054 -10.686  1.00 84.44           O  
ANISOU 2676  OE2 GLU I 303    11925   9299  10859    470    604  -3170       O  
ATOM   2677  N   ILE I 304       3.026  10.010 -16.695  1.00 71.40           N  
ANISOU 2677  N   ILE I 304     9433   7850   9845   1368   -282  -1134       N  
ATOM   2678  CA  ILE I 304       3.990   9.687 -17.745  1.00 68.74           C  
ANISOU 2678  CA  ILE I 304     9153   7639   9324   1313   -497   -686       C  
ATOM   2679  C   ILE I 304       5.407   9.934 -17.241  1.00 65.54           C  
ANISOU 2679  C   ILE I 304     9179   6672   9051    955   -480   -639       C  
ATOM   2680  O   ILE I 304       5.664  10.928 -16.552  1.00 66.11           O  
ANISOU 2680  O   ILE I 304     9421   6181   9514    938   -294   -817       O  
ATOM   2681  CB  ILE I 304       3.717  10.519 -19.033  1.00 75.04           C  
ANISOU 2681  CB  ILE I 304     9706   8624  10181   1979   -565    -74       C  
ATOM   2682  CG1 ILE I 304       2.316  10.219 -19.586  1.00 79.99           C  
ANISOU 2682  CG1 ILE I 304     9695  10190  10508   2414   -690   -233       C  
ATOM   2683  CG2 ILE I 304       4.749  10.232 -20.117  1.00 73.91           C  
ANISOU 2683  CG2 ILE I 304     9641   8647   9793   1929   -722    402       C  
ATOM   2684  CD1 ILE I 304       1.674  11.389 -20.318  1.00 88.88           C  
ANISOU 2684  CD1 ILE I 304    10554  11491  11723   3384   -645    387       C  
ATOM   2685  N   PHE I 305       6.299   8.987 -17.541  1.00 58.78           N  
ANISOU 2685  N   PHE I 305     8411   6027   7893    645   -628   -538       N  
ATOM   2686  CA  PHE I 305       7.720   9.115 -17.244  1.00 57.18           C  
ANISOU 2686  CA  PHE I 305     8457   5529   7738    355   -680   -507       C  
ATOM   2687  C   PHE I 305       8.551   8.836 -18.490  1.00 56.34           C  
ANISOU 2687  C   PHE I 305     8320   5524   7561    340   -802    -51       C  
ATOM   2688  O   PHE I 305       8.086   8.228 -19.455  1.00 55.69           O  
ANISOU 2688  O   PHE I 305     8033   5892   7233    480   -877    140       O  
ATOM   2689  CB  PHE I 305       8.176   8.117 -16.201  1.00 55.08           C  
ANISOU 2689  CB  PHE I 305     8325   5515   7088     86   -697   -779       C  
ATOM   2690  CG  PHE I 305       7.525   8.253 -14.862  1.00 57.27           C  
ANISOU 2690  CG  PHE I 305     8665   5844   7252     97   -539  -1212       C  
ATOM   2691  CD1 PHE I 305       6.332   7.596 -14.589  1.00 56.19           C  
ANISOU 2691  CD1 PHE I 305     8463   5897   6990    171   -319  -1316       C  
ATOM   2692  CD2 PHE I 305       8.167   8.948 -13.833  1.00 61.89           C  
ANISOU 2692  CD2 PHE I 305     9307   6399   7806    -18   -560  -1628       C  
ATOM   2693  CE1 PHE I 305       5.759   7.663 -13.338  1.00 58.89           C  
ANISOU 2693  CE1 PHE I 305     8884   6320   7168    192    -97  -1671       C  
ATOM   2694  CE2 PHE I 305       7.586   9.044 -12.575  1.00 64.73           C  
ANISOU 2694  CE2 PHE I 305     9699   6974   7920     16   -404  -2076       C  
ATOM   2695  CZ  PHE I 305       6.378   8.400 -12.330  1.00 64.08           C  
ANISOU 2695  CZ  PHE I 305     9641   7011   7693    152   -161  -2017       C  
ATOM   2696  N   THR I 306       9.814   9.228 -18.407  1.00 57.52           N  
ANISOU 2696  N   THR I 306     8597   5363   7894    114   -800    -22       N  
ATOM   2697  CA  THR I 306      10.732   9.220 -19.518  1.00 58.23           C  
ANISOU 2697  CA  THR I 306     8677   5424   8022     79   -815    399       C  
ATOM   2698  C   THR I 306      12.056   8.559 -19.130  1.00 55.71           C  
ANISOU 2698  C   THR I 306     8377   5233   7556   -282   -945    214       C  
ATOM   2699  O   THR I 306      12.546   8.723 -18.012  1.00 54.18           O  
ANISOU 2699  O   THR I 306     8177   5037   7370   -472   -987   -232       O  
ATOM   2700  CB  THR I 306      10.987  10.673 -19.958  1.00 64.29           C  
ANISOU 2700  CB  THR I 306     9515   5521   9388    225   -476    680       C  
ATOM   2701  OG1 THR I 306       9.981  11.047 -20.900  1.00 67.75           O  
ANISOU 2701  OG1 THR I 306     9885   6091   9766    810   -376   1241       O  
ATOM   2702  CG2 THR I 306      12.379  10.860 -20.582  1.00 65.54           C  
ANISOU 2702  CG2 THR I 306     9704   5432   9766    -37   -338    887       C  
ATOM   2703  N   LEU I 307      12.648   7.854 -20.089  1.00 53.77           N  
ANISOU 2703  N   LEU I 307     8083   5220   7127   -320  -1004    528       N  
ATOM   2704  CA  LEU I 307      13.871   7.115 -19.855  1.00 53.28           C  
ANISOU 2704  CA  LEU I 307     7980   5343   6919   -541  -1105    441       C  
ATOM   2705  C   LEU I 307      14.792   7.305 -21.033  1.00 52.96           C  
ANISOU 2705  C   LEU I 307     7873   5216   7032   -635  -1027    765       C  
ATOM   2706  O   LEU I 307      14.354   7.139 -22.167  1.00 53.85           O  
ANISOU 2706  O   LEU I 307     7969   5486   7006   -470   -965   1115       O  
ATOM   2707  CB  LEU I 307      13.506   5.637 -19.708  1.00 51.56           C  
ANISOU 2707  CB  LEU I 307     7783   5482   6323   -470  -1099    454       C  
ATOM   2708  CG  LEU I 307      14.115   4.817 -18.601  1.00 51.16           C  
ANISOU 2708  CG  LEU I 307     7776   5646   6015   -416  -1105    361       C  
ATOM   2709  CD1 LEU I 307      14.259   5.614 -17.335  1.00 53.26           C  
ANISOU 2709  CD1 LEU I 307     8017   6017   6199   -397  -1247     10       C  
ATOM   2710  CD2 LEU I 307      13.216   3.613 -18.367  1.00 51.52           C  
ANISOU 2710  CD2 LEU I 307     7937   5730   5907   -298   -799    417       C  
ATOM   2711  N   GLN I 308      16.053   7.657 -20.778  1.00 53.80           N  
ANISOU 2711  N   GLN I 308     7865   5206   7371   -891  -1012    581       N  
ATOM   2712  CA  GLN I 308      17.037   7.777 -21.844  1.00 55.86           C  
ANISOU 2712  CA  GLN I 308     8040   5373   7810  -1031   -852    858       C  
ATOM   2713  C   GLN I 308      17.682   6.432 -22.012  1.00 52.78           C  
ANISOU 2713  C   GLN I 308     7540   5451   7060  -1031  -1013    888       C  
ATOM   2714  O   GLN I 308      18.227   5.874 -21.072  1.00 54.75           O  
ANISOU 2714  O   GLN I 308     7664   5986   7150  -1025  -1186    617       O  
ATOM   2715  CB  GLN I 308      18.092   8.851 -21.558  1.00 62.63           C  
ANISOU 2715  CB  GLN I 308     8722   5825   9249  -1395   -618    515       C  
ATOM   2716  CG  GLN I 308      17.528  10.270 -21.468  1.00 69.32           C  
ANISOU 2716  CG  GLN I 308     9703   5931  10704  -1415   -193    485       C  
ATOM   2717  CD  GLN I 308      16.909  10.761 -22.779  1.00 73.66           C  
ANISOU 2717  CD  GLN I 308    10511   6126  11348  -1026    187   1350       C  
ATOM   2718  OE1 GLN I 308      15.672  10.813 -22.936  1.00 72.81           O  
ANISOU 2718  OE1 GLN I 308    10554   6114  10995   -574    120   1683       O  
ATOM   2719  NE2 GLN I 308      17.767  11.131 -23.729  1.00 76.56           N  
ANISOU 2719  NE2 GLN I 308    10876   6202  12010  -1132    614   1735       N  
ATOM   2720  N   VAL I 309      17.611   5.917 -23.230  1.00 51.62           N  
ANISOU 2720  N   VAL I 309     7411   5450   6751   -963   -903   1231       N  
ATOM   2721  CA  VAL I 309      18.091   4.600 -23.542  1.00 48.30           C  
ANISOU 2721  CA  VAL I 309     6897   5347   6106   -965   -900   1223       C  
ATOM   2722  C   VAL I 309      19.075   4.702 -24.662  1.00 49.29           C  
ANISOU 2722  C   VAL I 309     6894   5514   6317  -1103   -734   1423       C  
ATOM   2723  O   VAL I 309      18.809   5.315 -25.676  1.00 51.02           O  
ANISOU 2723  O   VAL I 309     7163   5731   6489  -1054   -572   1730       O  
ATOM   2724  CB  VAL I 309      16.960   3.683 -24.019  1.00 45.83           C  
ANISOU 2724  CB  VAL I 309     6621   5276   5513   -852   -817   1184       C  
ATOM   2725  CG1 VAL I 309      17.537   2.346 -24.451  1.00 45.05           C  
ANISOU 2725  CG1 VAL I 309     6416   5325   5375   -918   -606   1092       C  
ATOM   2726  CG2 VAL I 309      15.918   3.532 -22.921  1.00 45.23           C  
ANISOU 2726  CG2 VAL I 309     6667   5119   5398   -742   -865    985       C  
ATOM   2727  N   ARG I 310      20.179   4.010 -24.482  1.00 51.04           N  
ANISOU 2727  N   ARG I 310     6935   5861   6595  -1176   -734   1308       N  
ATOM   2728  CA  ARG I 310      21.326   4.090 -25.346  1.00 52.76           C  
ANISOU 2728  CA  ARG I 310     6962   6119   6963  -1351   -551   1404       C  
ATOM   2729  C   ARG I 310      21.297   2.934 -26.333  1.00 49.85           C  
ANISOU 2729  C   ARG I 310     6564   6023   6352  -1295   -369   1463       C  
ATOM   2730  O   ARG I 310      21.405   1.754 -25.931  1.00 48.57           O  
ANISOU 2730  O   ARG I 310     6357   5927   6171  -1172   -318   1318       O  
ATOM   2731  CB  ARG I 310      22.576   4.033 -24.462  1.00 57.01           C  
ANISOU 2731  CB  ARG I 310     7173   6781   7707  -1420   -685   1113       C  
ATOM   2732  CG  ARG I 310      23.881   3.989 -25.214  1.00 63.84           C  
ANISOU 2732  CG  ARG I 310     7728   7740   8789  -1618   -481   1102       C  
ATOM   2733  CD  ARG I 310      25.068   4.186 -24.277  1.00 68.67           C  
ANISOU 2733  CD  ARG I 310     7833   8663   9593  -1693   -669    655       C  
ATOM   2734  NE  ARG I 310      26.197   4.767 -24.996  1.00 71.96           N  
ANISOU 2734  NE  ARG I 310     7906   9000  10434  -2089   -364    503       N  
ATOM   2735  CZ  ARG I 310      26.600   6.038 -24.914  1.00 77.63           C  
ANISOU 2735  CZ  ARG I 310     8422   9399  11674  -2554   -119    148       C  
ATOM   2736  NH1 ARG I 310      25.986   6.924 -24.122  1.00 77.75           N  
ANISOU 2736  NH1 ARG I 310     8527   9148  11864  -2684   -174   -150       N  
ATOM   2737  NH2 ARG I 310      27.657   6.425 -25.621  1.00 82.42           N  
ANISOU 2737  NH2 ARG I 310     8702   9885  12728  -2934    304     22       N  
ATOM   2738  N   GLY I 311      21.127   3.271 -27.612  1.00 48.57           N  
ANISOU 2738  N   GLY I 311     6417   6034   6001  -1338   -177   1677       N  
ATOM   2739  CA  GLY I 311      21.236   2.306 -28.721  1.00 48.85           C  
ANISOU 2739  CA  GLY I 311     6315   6485   5759  -1369     44   1564       C  
ATOM   2740  C   GLY I 311      19.873   1.815 -29.183  1.00 48.59           C  
ANISOU 2740  C   GLY I 311     6269   6889   5303  -1272     28   1325       C  
ATOM   2741  O   GLY I 311      18.987   1.610 -28.363  1.00 47.09           O  
ANISOU 2741  O   GLY I 311     6166   6553   5172  -1212   -104   1138       O  
ATOM   2742  N   ARG I 312      19.725   1.601 -30.492  1.00 45.77           N  
ANISOU 2742  N   ARG I 312     6901   5852   4635   -633    405    499       N  
ATOM   2743  CA  ARG I 312      18.448   1.238 -31.103  1.00 48.52           C  
ANISOU 2743  CA  ARG I 312     7261   6363   4810   -840    306    694       C  
ATOM   2744  C   ARG I 312      17.923  -0.149 -30.665  1.00 47.06           C  
ANISOU 2744  C   ARG I 312     7223   6111   4544   -733    489    363       C  
ATOM   2745  O   ARG I 312      16.746  -0.254 -30.321  1.00 43.91           O  
ANISOU 2745  O   ARG I 312     6830   5652   4201   -669    370    486       O  
ATOM   2746  CB  ARG I 312      18.507   1.319 -32.633  1.00 53.99           C  
ANISOU 2746  CB  ARG I 312     7856   7610   5046  -1407    263    913       C  
ATOM   2747  CG  ARG I 312      17.136   1.426 -33.303  1.00 60.92           C  
ANISOU 2747  CG  ARG I 312     8545   8909   5691  -1755     23   1414       C  
ATOM   2748  CD  ARG I 312      17.216   1.606 -34.830  1.00 70.38           C  
ANISOU 2748  CD  ARG I 312     9493  11011   6235  -2521    -81   1778       C  
ATOM   2749  NE  ARG I 312      17.791   2.895 -35.274  1.00 76.22           N  
ANISOU 2749  NE  ARG I 312     9946  11820   7191  -2569   -288   2458       N  
ATOM   2750  CZ  ARG I 312      18.797   3.060 -36.155  1.00 85.49           C  
ANISOU 2750  CZ  ARG I 312    11058  13478   7945  -3008   -221   2422       C  
ATOM   2751  NH1 ARG I 312      19.393   2.019 -36.742  1.00 88.55           N  
ANISOU 2751  NH1 ARG I 312    11631  14324   7686  -3490    122   1633       N  
ATOM   2752  NH2 ARG I 312      19.212   4.296 -36.476  1.00 87.26           N  
ANISOU 2752  NH2 ARG I 312    10975  13681   8498  -3004   -415   3164       N  
ATOM   2753  N   GLU I 313      18.779  -1.177 -30.675  1.00 48.18           N  
ANISOU 2753  N   GLU I 313     7414   6186   4703   -701    834      2       N  
ATOM   2754  CA  GLU I 313      18.391  -2.528 -30.265  1.00 51.33           C  
ANISOU 2754  CA  GLU I 313     7850   6360   5290   -576   1140   -237       C  
ATOM   2755  C   GLU I 313      17.900  -2.564 -28.807  1.00 46.96           C  
ANISOU 2755  C   GLU I 313     7258   5606   4979   -129    958    -16       C  
ATOM   2756  O   GLU I 313      16.848  -3.154 -28.515  1.00 43.59           O  
ANISOU 2756  O   GLU I 313     6888   5091   4581    -96    972    -30       O  
ATOM   2757  CB  GLU I 313      19.518  -3.554 -30.512  1.00 60.93           C  
ANISOU 2757  CB  GLU I 313     8959   7351   6840   -567   1690   -550       C  
ATOM   2758  CG  GLU I 313      20.795  -3.376 -29.680  1.00 68.93           C  
ANISOU 2758  CG  GLU I 313     9757   8236   8195   -153   1680   -287       C  
ATOM   2759  CD  GLU I 313      21.954  -4.300 -30.119  1.00 81.18           C  
ANISOU 2759  CD  GLU I 313    11077   9499  10267   -147   2295   -492       C  
ATOM   2760  OE1 GLU I 313      21.790  -5.556 -30.061  1.00 89.78           O  
ANISOU 2760  OE1 GLU I 313    12011  10137  11963    -65   2841   -628       O  
ATOM   2761  OE2 GLU I 313      23.040  -3.777 -30.503  1.00 79.58           O  
ANISOU 2761  OE2 GLU I 313    10792   9436  10009   -217   2312   -516       O  
ATOM   2762  N   ARG I 314      18.614  -1.865 -27.924  1.00 43.33           N  
ANISOU 2762  N   ARG I 314     6669   5199   4594     90    793    141       N  
ATOM   2763  CA  ARG I 314      18.233  -1.785 -26.523  1.00 41.66           C  
ANISOU 2763  CA  ARG I 314     6339   5061   4428    299    647    269       C  
ATOM   2764  C   ARG I 314      16.907  -1.048 -26.342  1.00 40.99           C  
ANISOU 2764  C   ARG I 314     6351   4907   4314    225    457    220       C  
ATOM   2765  O   ARG I 314      16.071  -1.474 -25.540  1.00 38.30           O  
ANISOU 2765  O   ARG I 314     5993   4570   3989    320    432    231       O  
ATOM   2766  CB  ARG I 314      19.326  -1.108 -25.691  1.00 42.39           C  
ANISOU 2766  CB  ARG I 314     6196   5462   4446    309    568    325       C  
ATOM   2767  CG  ARG I 314      18.967  -1.036 -24.218  1.00 43.38           C  
ANISOU 2767  CG  ARG I 314     6108   5953   4419    290    460    374       C  
ATOM   2768  CD  ARG I 314      20.101  -0.509 -23.361  1.00 46.14           C  
ANISOU 2768  CD  ARG I 314     6116   6900   4514     99    414    404       C  
ATOM   2769  NE  ARG I 314      21.328  -1.291 -23.500  1.00 47.82           N  
ANISOU 2769  NE  ARG I 314     6055   7290   4824    265    471    857       N  
ATOM   2770  CZ  ARG I 314      22.536  -0.860 -23.144  1.00 50.53           C  
ANISOU 2770  CZ  ARG I 314     6077   8156   4964     99    425    974       C  
ATOM   2771  NH1 ARG I 314      22.705   0.345 -22.618  1.00 52.04           N  
ANISOU 2771  NH1 ARG I 314     6216   8767   4789   -315    368    537       N  
ATOM   2772  NH2 ARG I 314      23.587  -1.642 -23.305  1.00 53.82           N  
ANISOU 2772  NH2 ARG I 314     6157   8653   5638    311    516   1504       N  
ATOM   2773  N   TYR I 315      16.711   0.048 -27.089  1.00 40.83           N  
ANISOU 2773  N   TYR I 315     6349   4805   4357     62    356    261       N  
ATOM   2774  CA  TYR I 315      15.427   0.767 -27.058  1.00 40.32           C  
ANISOU 2774  CA  TYR I 315     6228   4557   4534     31    254    387       C  
ATOM   2775  C   TYR I 315      14.270  -0.122 -27.458  1.00 39.16           C  
ANISOU 2775  C   TYR I 315     6177   4464   4238     -6    198    501       C  
ATOM   2776  O   TYR I 315      13.275  -0.175 -26.774  1.00 39.83           O  
ANISOU 2776  O   TYR I 315     6231   4436   4467     94    174    486       O  
ATOM   2777  CB  TYR I 315      15.450   2.049 -27.918  1.00 43.28           C  
ANISOU 2777  CB  TYR I 315     6432   4791   5218   -113    193    703       C  
ATOM   2778  CG  TYR I 315      14.098   2.696 -28.107  1.00 44.93           C  
ANISOU 2778  CG  TYR I 315     6412   4764   5893   -113    126   1106       C  
ATOM   2779  CD1 TYR I 315      13.513   3.437 -27.095  1.00 46.35           C  
ANISOU 2779  CD1 TYR I 315     6404   4501   6704     15    333    914       C  
ATOM   2780  CD2 TYR I 315      13.393   2.560 -29.311  1.00 48.37           C  
ANISOU 2780  CD2 TYR I 315     6719   5507   6150   -329    -93   1698       C  
ATOM   2781  CE1 TYR I 315      12.257   4.035 -27.271  1.00 50.84           C  
ANISOU 2781  CE1 TYR I 315     6649   4729   7940     68    358   1366       C  
ATOM   2782  CE2 TYR I 315      12.152   3.161 -29.504  1.00 51.88           C  
ANISOU 2782  CE2 TYR I 315     6798   5808   7106   -316   -186   2306       C  
ATOM   2783  CZ  TYR I 315      11.577   3.893 -28.479  1.00 53.65           C  
ANISOU 2783  CZ  TYR I 315     6824   5383   8176    -46     56   2173       C  
ATOM   2784  OH  TYR I 315      10.325   4.482 -28.651  1.00 59.70           O  
ANISOU 2784  OH  TYR I 315     7120   5881   9680     21     51   2843       O  
ATOM   2785  N   GLU I 316      14.408  -0.843 -28.551  1.00 42.54           N  
ANISOU 2785  N   GLU I 316     6696   5115   4350   -242    243    515       N  
ATOM   2786  CA  GLU I 316      13.309  -1.693 -29.034  1.00 44.90           C  
ANISOU 2786  CA  GLU I 316     7050   5584   4425   -453    259    509       C  
ATOM   2787  C   GLU I 316      12.986  -2.825 -28.065  1.00 42.77           C  
ANISOU 2787  C   GLU I 316     6892   5089   4267   -211    445    253       C  
ATOM   2788  O   GLU I 316      11.848  -3.250 -27.973  1.00 44.60           O  
ANISOU 2788  O   GLU I 316     7146   5344   4454   -267    414    267       O  
ATOM   2789  CB  GLU I 316      13.627  -2.279 -30.417  1.00 46.98           C  
ANISOU 2789  CB  GLU I 316     7337   6269   4245   -983    427    345       C  
ATOM   2790  CG  GLU I 316      13.760  -1.247 -31.546  1.00 52.55           C  
ANISOU 2790  CG  GLU I 316     7828   7457   4679  -1382    180    789       C  
ATOM   2791  CD  GLU I 316      13.834  -1.898 -32.911  1.00 55.53           C  
ANISOU 2791  CD  GLU I 316     8157   8557   4384  -2156    363    547       C  
ATOM   2792  OE1 GLU I 316      13.575  -3.113 -32.960  1.00 55.88           O  
ANISOU 2792  OE1 GLU I 316     8338   8600   4293  -2378    745    -48       O  
ATOM   2793  OE2 GLU I 316      14.106  -1.222 -33.950  1.00 73.39           O  
ANISOU 2793  OE2 GLU I 316    10186  11447   6249  -2643    187    924       O  
ATOM   2794  N   ILE I 317      13.991  -3.328 -27.361  1.00 42.69           N  
ANISOU 2794  N   ILE I 317     6870   4916   4431     37    632    141       N  
ATOM   2795  CA  ILE I 317      13.766  -4.370 -26.336  1.00 41.41           C  
ANISOU 2795  CA  ILE I 317     6661   4592   4477    287    787    166       C  
ATOM   2796  C   ILE I 317      13.003  -3.814 -25.152  1.00 39.84           C  
ANISOU 2796  C   ILE I 317     6398   4490   4249    431    537    280       C  
ATOM   2797  O   ILE I 317      11.969  -4.371 -24.731  1.00 40.35           O  
ANISOU 2797  O   ILE I 317     6490   4506   4332    465    542    292       O  
ATOM   2798  CB  ILE I 317      15.081  -4.981 -25.843  1.00 42.72           C  
ANISOU 2798  CB  ILE I 317     6624   4678   4928    508   1015    318       C  
ATOM   2799  CG1 ILE I 317      15.584  -6.000 -26.866  1.00 45.71           C  
ANISOU 2799  CG1 ILE I 317     7001   4744   5620    369   1528     71       C  
ATOM   2800  CG2 ILE I 317      14.872  -5.666 -24.507  1.00 45.60           C  
ANISOU 2800  CG2 ILE I 317     6756   5093   5476    760   1010    679       C  
ATOM   2801  CD1 ILE I 317      17.078  -6.218 -26.830  1.00 49.29           C  
ANISOU 2801  CD1 ILE I 317     7197   5081   6451    538   1777    231       C  
ATOM   2802  N   LEU I 318      13.506  -2.719 -24.607  1.00 38.41           N  
ANISOU 2802  N   LEU I 318     6104   4452   4037    438    400    265       N  
ATOM   2803  CA  LEU I 318      12.813  -2.075 -23.508  1.00 38.12           C  
ANISOU 2803  CA  LEU I 318     5952   4525   4007    410    327    146       C  
ATOM   2804  C   LEU I 318      11.393  -1.638 -23.889  1.00 37.82           C  
ANISOU 2804  C   LEU I 318     5970   4231   4169    372    273    124       C  
ATOM   2805  O   LEU I 318      10.494  -1.634 -23.040  1.00 41.77           O  
ANISOU 2805  O   LEU I 318     6398   4744   4727    372    299      6       O  
ATOM   2806  CB  LEU I 318      13.619  -0.905 -22.951  1.00 38.98           C  
ANISOU 2806  CB  LEU I 318     5883   4811   4115    257    361    -75       C  
ATOM   2807  CG  LEU I 318      14.945  -1.270 -22.256  1.00 42.10           C  
ANISOU 2807  CG  LEU I 318     6069   5716   4210    207    360     40       C  
ATOM   2808  CD1 LEU I 318      15.570  -0.067 -21.572  1.00 43.43           C  
ANISOU 2808  CD1 LEU I 318     6022   6221   4258   -131    448   -347       C  
ATOM   2809  CD2 LEU I 318      14.770  -2.400 -21.239  1.00 43.64           C  
ANISOU 2809  CD2 LEU I 318     6057   6333   4190    252    320    371       C  
ATOM   2810  N   LYS I 319      11.187  -1.287 -25.148  1.00 38.04           N  
ANISOU 2810  N   LYS I 319     6038   4132   4280    290    196    316       N  
ATOM   2811  CA  LYS I 319       9.875  -0.832 -25.616  1.00 40.21           C  
ANISOU 2811  CA  LYS I 319     6196   4291   4791    230     97    563       C  
ATOM   2812  C   LYS I 319       8.892  -1.979 -25.716  1.00 38.61           C  
ANISOU 2812  C   LYS I 319     6113   4224   4333    180     66    574       C  
ATOM   2813  O   LYS I 319       7.741  -1.833 -25.372  1.00 39.41           O  
ANISOU 2813  O   LYS I 319     6103   4244   4626    216     26    658       O  
ATOM   2814  CB  LYS I 319       9.971  -0.129 -26.978  1.00 42.66           C  
ANISOU 2814  CB  LYS I 319     6352   4690   5166     40    -42   1015       C  
ATOM   2815  CG  LYS I 319       8.626   0.409 -27.460  1.00 48.75           C  
ANISOU 2815  CG  LYS I 319     6793   5455   6272    -30   -188   1575       C  
ATOM   2816  CD  LYS I 319       8.681   0.991 -28.863  1.00 55.86           C  
ANISOU 2816  CD  LYS I 319     7387   6723   7114   -328   -404   2300       C  
ATOM   2817  CE  LYS I 319       7.440   1.834 -29.117  1.00 62.73           C  
ANISOU 2817  CE  LYS I 319     7688   7495   8648   -300   -527   3143       C  
ATOM   2818  NZ  LYS I 319       7.372   2.283 -30.526  1.00 70.06           N  
ANISOU 2818  NZ  LYS I 319     8157   9069   9391   -698   -830   4136       N  
ATOM   2819  N   LYS I 320       9.358  -3.089 -26.259  1.00 39.57           N  
ANISOU 2819  N   LYS I 320     6415   4497   4122     57    171    448       N  
ATOM   2820  CA  LYS I 320       8.618  -4.330 -26.260  1.00 41.86           C  
ANISOU 2820  CA  LYS I 320     6816   4819   4269    -33    306    307       C  
ATOM   2821  C   LYS I 320       8.286  -4.784 -24.817  1.00 39.93           C  
ANISOU 2821  C   LYS I 320     6568   4414   4190    256    359    252       C  
ATOM   2822  O   LYS I 320       7.155  -5.194 -24.520  1.00 40.35           O  
ANISOU 2822  O   LYS I 320     6629   4464   4239    236    344    249       O  
ATOM   2823  CB  LYS I 320       9.451  -5.377 -27.045  1.00 46.68           C  
ANISOU 2823  CB  LYS I 320     7537   5437   4761   -253    647     29       C  
ATOM   2824  CG  LYS I 320       9.024  -6.820 -26.864  1.00 51.60           C  
ANISOU 2824  CG  LYS I 320     8225   5852   5525   -311   1027   -231       C  
ATOM   2825  CD  LYS I 320       7.711  -7.117 -27.566  1.00 56.65           C  
ANISOU 2825  CD  LYS I 320     8883   6803   5836   -759   1011   -367       C  
ATOM   2826  CE  LYS I 320       7.406  -8.610 -27.579  1.00 59.64           C  
ANISOU 2826  CE  LYS I 320     9318   6905   6437   -949   1564   -801       C  
ATOM   2827  NZ  LYS I 320       6.075  -8.849 -28.179  1.00 63.75           N  
ANISOU 2827  NZ  LYS I 320     9824   7870   6526  -1472   1522   -966       N  
ATOM   2828  N   LEU I 321       9.242  -4.692 -23.893  1.00 39.10           N  
ANISOU 2828  N   LEU I 321     6384   4319   4152    446    397    264       N  
ATOM   2829  CA  LEU I 321       8.932  -5.056 -22.492  1.00 38.65           C  
ANISOU 2829  CA  LEU I 321     6201   4402   4080    559    400    321       C  
ATOM   2830  C   LEU I 321       7.870  -4.122 -21.933  1.00 40.94           C  
ANISOU 2830  C   LEU I 321     6419   4730   4406    486    302    142       C  
ATOM   2831  O   LEU I 321       6.905  -4.562 -21.284  1.00 40.55           O  
ANISOU 2831  O   LEU I 321     6342   4737   4326    479    315    120       O  
ATOM   2832  CB  LEU I 321      10.166  -5.044 -21.589  1.00 38.15           C  
ANISOU 2832  CB  LEU I 321     5911   4657   3925    609    407    489       C  
ATOM   2833  CG  LEU I 321      11.228  -6.093 -21.940  1.00 40.80           C  
ANISOU 2833  CG  LEU I 321     6156   4859   4487    762    601    815       C  
ATOM   2834  CD1 LEU I 321      12.436  -5.986 -21.019  1.00 42.55           C  
ANISOU 2834  CD1 LEU I 321     6002   5569   4596    782    530   1193       C  
ATOM   2835  CD2 LEU I 321      10.619  -7.488 -21.915  1.00 43.69           C  
ANISOU 2835  CD2 LEU I 321     6500   4921   5179    867    850   1010       C  
ATOM   2836  N   ASN I 322       8.058  -2.824 -22.148  1.00 42.45           N  
ANISOU 2836  N   ASN I 322     6519   4819   4791    424    289      7       N  
ATOM   2837  CA  ASN I 322       7.084  -1.863 -21.679  1.00 45.06           C  
ANISOU 2837  CA  ASN I 322     6666   4974   5479    360    384   -198       C  
ATOM   2838  C   ASN I 322       5.698  -2.217 -22.198  1.00 43.71           C  
ANISOU 2838  C   ASN I 322     6509   4645   5453    411    295     28       C  
ATOM   2839  O   ASN I 322       4.756  -2.245 -21.455  1.00 45.33           O  
ANISOU 2839  O   ASN I 322     6616   4829   5778    394    385   -129       O  
ATOM   2840  CB  ASN I 322       7.459  -0.465 -22.135  1.00 48.55           C  
ANISOU 2840  CB  ASN I 322     6926   5096   6422    323    497   -242       C  
ATOM   2841  CG  ASN I 322       6.418   0.566 -21.748  1.00 54.85           C  
ANISOU 2841  CG  ASN I 322     7402   5466   7971    289    778   -419       C  
ATOM   2842  OD1 ASN I 322       6.323   0.954 -20.591  1.00 55.07           O  
ANISOU 2842  OD1 ASN I 322     7276   5537   8110     84   1111  -1015       O  
ATOM   2843  ND2 ASN I 322       5.610   0.995 -22.721  1.00 57.90           N  
ANISOU 2843  ND2 ASN I 322     7589   5506   8904    417    692    131       N  
ATOM   2844  N   ASP I 323       5.590  -2.498 -23.486  1.00 44.49           N  
ANISOU 2844  N   ASP I 323     6683   4759   5459    376    134    376       N  
ATOM   2845  CA  ASP I 323       4.299  -2.762 -24.105  1.00 45.67           C  
ANISOU 2845  CA  ASP I 323     6745   4975   5630    284     13    662       C  
ATOM   2846  C   ASP I 323       3.679  -4.087 -23.596  1.00 42.43           C  
ANISOU 2846  C   ASP I 323     6534   4689   4898    260     68    464       C  
ATOM   2847  O   ASP I 323       2.471  -4.215 -23.491  1.00 41.06           O  
ANISOU 2847  O   ASP I 323     6256   4539   4804    223     28    550       O  
ATOM   2848  CB  ASP I 323       4.422  -2.739 -25.641  1.00 48.31           C  
ANISOU 2848  CB  ASP I 323     7017   5614   5722     19   -166   1067       C  
ATOM   2849  CG  ASP I 323       4.769  -1.323 -26.199  1.00 54.45           C  
ANISOU 2849  CG  ASP I 323     7452   6263   6969     46   -251   1531       C  
ATOM   2850  OD1 ASP I 323       4.788  -0.305 -25.444  1.00 58.61           O  
ANISOU 2850  OD1 ASP I 323     7770   6305   8193    279    -73   1464       O  
ATOM   2851  OD2 ASP I 323       5.006  -1.222 -27.420  1.00 60.61           O  
ANISOU 2851  OD2 ASP I 323     8110   7456   7461   -246   -430   1954       O  
ATOM   2852  N   SER I 324       4.503  -5.047 -23.236  1.00 39.93           N  
ANISOU 2852  N   SER I 324     6420   4404   4344    301    197    282       N  
ATOM   2853  CA  SER I 324       3.977  -6.300 -22.690  1.00 42.74           C  
ANISOU 2853  CA  SER I 324     6873   4764   4601    308    326    212       C  
ATOM   2854  C   SER I 324       3.482  -6.165 -21.271  1.00 41.17           C  
ANISOU 2854  C   SER I 324     6551   4646   4443    412    324    155       C  
ATOM   2855  O   SER I 324       2.473  -6.761 -20.897  1.00 42.85           O  
ANISOU 2855  O   SER I 324     6769   4880   4632    380    353    148       O  
ATOM   2856  CB  SER I 324       5.041  -7.384 -22.732  1.00 41.99           C  
ANISOU 2856  CB  SER I 324     6863   4560   4532    357    569    219       C  
ATOM   2857  OG  SER I 324       5.355  -7.622 -24.065  1.00 47.72           O  
ANISOU 2857  OG  SER I 324     7687   5250   5190    115    700     75       O  
ATOM   2858  N   LEU I 325       4.257  -5.457 -20.462  1.00 41.98           N  
ANISOU 2858  N   LEU I 325     6520   4901   4528    434    332     61       N  
ATOM   2859  CA  LEU I 325       3.849  -5.134 -19.119  1.00 42.19           C  
ANISOU 2859  CA  LEU I 325     6351   5214   4462    311    398   -152       C  
ATOM   2860  C   LEU I 325       2.506  -4.372 -19.102  1.00 42.39           C  
ANISOU 2860  C   LEU I 325     6269   5000   4837    265    476   -397       C  
ATOM   2861  O   LEU I 325       1.681  -4.622 -18.231  1.00 43.39           O  
ANISOU 2861  O   LEU I 325     6300   5301   4885    154    562   -561       O  
ATOM   2862  CB  LEU I 325       4.942  -4.342 -18.419  1.00 44.67           C  
ANISOU 2862  CB  LEU I 325     6477   5871   4621    138    466   -362       C  
ATOM   2863  CG  LEU I 325       6.243  -5.138 -18.189  1.00 47.74           C  
ANISOU 2863  CG  LEU I 325     6802   6637   4698    175    379     55       C  
ATOM   2864  CD1 LEU I 325       7.354  -4.172 -17.785  1.00 49.44           C  
ANISOU 2864  CD1 LEU I 325     6822   7237   4725    -61    416   -176       C  
ATOM   2865  CD2 LEU I 325       6.085  -6.273 -17.165  1.00 47.92           C  
ANISOU 2865  CD2 LEU I 325     6610   7156   4439    108    346    489       C  
ATOM   2866  N   GLU I 326       2.273  -3.471 -20.058  1.00 41.94           N  
ANISOU 2866  N   GLU I 326     6137   4564   5233    342    461   -310       N  
ATOM   2867  CA  GLU I 326       0.984  -2.744 -20.120  1.00 44.91           C  
ANISOU 2867  CA  GLU I 326     6240   4626   6197    361    575   -306       C  
ATOM   2868  C   GLU I 326      -0.173  -3.705 -20.387  1.00 42.25           C  
ANISOU 2868  C   GLU I 326     5982   4406   5663    371    417    -63       C  
ATOM   2869  O   GLU I 326      -1.213  -3.596 -19.793  1.00 44.12           O  
ANISOU 2869  O   GLU I 326     6043   4573   6146    349    548   -203       O  
ATOM   2870  CB  GLU I 326       0.935  -1.706 -21.240  1.00 48.42           C  
ANISOU 2870  CB  GLU I 326     6424   4704   7267    460    536    118       C  
ATOM   2871  CG  GLU I 326       1.797  -0.474 -21.112  1.00 54.29           C  
ANISOU 2871  CG  GLU I 326     6965   5112   8548    456    802    -89       C  
ATOM   2872  CD  GLU I 326       1.549   0.508 -22.265  1.00 61.68           C  
ANISOU 2872  CD  GLU I 326     7501   5653  10280    582    760    614       C  
ATOM   2873  OE1 GLU I 326       0.613   0.244 -23.075  1.00 65.08           O  
ANISOU 2873  OE1 GLU I 326     7746   6230  10752    612    489   1296       O  
ATOM   2874  OE2 GLU I 326       2.257   1.552 -22.347  1.00 64.79           O  
ANISOU 2874  OE2 GLU I 326     7683   5660  11274    598   1009    564       O  
ATOM   2875  N   LEU I 327       0.026  -4.634 -21.301  1.00 40.66           N  
ANISOU 2875  N   LEU I 327     6018   4384   5046    331    214    209       N  
ATOM   2876  CA  LEU I 327      -0.978  -5.613 -21.638  1.00 42.57           C  
ANISOU 2876  CA  LEU I 327     6336   4788   5051    213    141    325       C  
ATOM   2877  C   LEU I 327      -1.367  -6.465 -20.438  1.00 42.68           C  
ANISOU 2877  C   LEU I 327     6456   4862   4898    231    274     76       C  
ATOM   2878  O   LEU I 327      -2.555  -6.643 -20.165  1.00 45.29           O  
ANISOU 2878  O   LEU I 327     6686   5223   5299    184    283     66       O  
ATOM   2879  CB  LEU I 327      -0.478  -6.502 -22.786  1.00 43.65           C  
ANISOU 2879  CB  LEU I 327     6689   5114   4782     -1    102    398       C  
ATOM   2880  CG  LEU I 327      -1.464  -7.531 -23.344  1.00 45.38           C  
ANISOU 2880  CG  LEU I 327     6956   5575   4710   -317    134    370       C  
ATOM   2881  CD1 LEU I 327      -2.739  -6.855 -23.812  1.00 48.23           C  
ANISOU 2881  CD1 LEU I 327     6952   6211   5160   -454   -101    762       C  
ATOM   2882  CD2 LEU I 327      -0.788  -8.282 -24.481  1.00 48.46           C  
ANISOU 2882  CD2 LEU I 327     7503   6153   4755   -696    293    187       C  
ATOM   2883  N   SER I 328      -0.373  -6.938 -19.695  1.00 42.37           N  
ANISOU 2883  N   SER I 328     6525   4915   4655    277    360    -10       N  
ATOM   2884  CA  SER I 328      -0.616  -7.686 -18.449  1.00 43.55           C  
ANISOU 2884  CA  SER I 328     6634   5298   4613    236    449    -32       C  
ATOM   2885  C   SER I 328      -1.339  -6.849 -17.388  1.00 46.94           C  
ANISOU 2885  C   SER I 328     6824   5915   5094    101    540   -367       C  
ATOM   2886  O   SER I 328      -1.912  -7.389 -16.448  1.00 48.17           O  
ANISOU 2886  O   SER I 328     6900   6364   5038    -33    600   -405       O  
ATOM   2887  CB  SER I 328       0.706  -8.186 -17.870  1.00 44.00           C  
ANISOU 2887  CB  SER I 328     6647   5585   4485    268    479    201       C  
ATOM   2888  OG  SER I 328       1.167  -9.311 -18.612  1.00 45.51           O  
ANISOU 2888  OG  SER I 328     6975   5476   4838    378    592    473       O  
ATOM   2889  N   ASP I 329      -1.315  -5.530 -17.528  1.00 48.34           N  
ANISOU 2889  N   ASP I 329     6831   5892   5643     87    641   -640       N  
ATOM   2890  CA  ASP I 329      -2.038  -4.675 -16.597  1.00 50.70           C  
ANISOU 2890  CA  ASP I 329     6829   6203   6231   -110    946  -1146       C  
ATOM   2891  C   ASP I 329      -3.507  -4.508 -16.976  1.00 48.60           C  
ANISOU 2891  C   ASP I 329     6407   5573   6483      0    996  -1062       C  
ATOM   2892  O   ASP I 329      -4.266  -3.926 -16.220  1.00 50.75           O  
ANISOU 2892  O   ASP I 329     6389   5755   7139   -152   1341  -1501       O  
ATOM   2893  CB  ASP I 329      -1.342  -3.321 -16.497  1.00 58.48           C  
ANISOU 2893  CB  ASP I 329     7594   6980   7643   -217   1232  -1556       C  
ATOM   2894  CG  ASP I 329      -1.533  -2.669 -15.159  1.00 68.09           C  
ANISOU 2894  CG  ASP I 329     8498   8482   8888   -688   1722  -2371       C  
ATOM   2895  OD1 ASP I 329      -2.318  -3.190 -14.333  1.00 76.84           O  
ANISOU 2895  OD1 ASP I 329     9537   9970   9686   -914   1802  -2568       O  
ATOM   2896  OD2 ASP I 329      -0.907  -1.617 -14.928  1.00 75.23           O  
ANISOU 2896  OD2 ASP I 329     9192   9267  10123   -922   2097  -2899       O  
ATOM   2897  N   VAL I 330      -3.922  -5.052 -18.125  1.00 47.04           N  
ANISOU 2897  N   VAL I 330     6339   5259   6274    171    703   -533       N  
ATOM   2898  CA  VAL I 330      -5.304  -4.856 -18.610  1.00 48.59           C  
ANISOU 2898  CA  VAL I 330     6267   5275   6919    225    678   -266       C  
ATOM   2899  C   VAL I 330      -6.066  -6.114 -19.071  1.00 46.62           C  
ANISOU 2899  C   VAL I 330     6215   5313   6184    135    445     -5       C  
ATOM   2900  O   VAL I 330      -7.280  -6.070 -19.266  1.00 47.40           O  
ANISOU 2900  O   VAL I 330     6059   5421   6529    107    418    192       O  
ATOM   2901  CB  VAL I 330      -5.337  -3.778 -19.715  1.00 51.23           C  
ANISOU 2901  CB  VAL I 330     6236   5292   7935    364    612    245       C  
ATOM   2902  CG1 VAL I 330      -4.825  -2.456 -19.162  1.00 53.32           C  
ANISOU 2902  CG1 VAL I 330     6202   5072   8983    430   1032   -113       C  
ATOM   2903  CG2 VAL I 330      -4.497  -4.187 -20.916  1.00 48.95           C  
ANISOU 2903  CG2 VAL I 330     6191   5272   7133    310    270    647       C  
ATOM   2904  N   VAL I 331      -5.376  -7.235 -19.235  1.00 43.55           N  
ANISOU 2904  N   VAL I 331     6208   5116   5220     58    361    -15       N  
ATOM   2905  CA  VAL I 331      -6.047  -8.498 -19.489  1.00 43.55           C  
ANISOU 2905  CA  VAL I 331     6378   5279   4887   -107    339     33       C  
ATOM   2906  C   VAL I 331      -6.442  -9.073 -18.097  1.00 44.69           C  
ANISOU 2906  C   VAL I 331     6551   5497   4931   -108    495   -174       C  
ATOM   2907  O   VAL I 331      -5.604  -9.160 -17.230  1.00 45.75           O  
ANISOU 2907  O   VAL I 331     6722   5733   4927    -75    573   -244       O  
ATOM   2908  CB  VAL I 331      -5.111  -9.450 -20.263  1.00 40.79           C  
ANISOU 2908  CB  VAL I 331     6321   4927   4247   -226    391     41       C  
ATOM   2909  CG1 VAL I 331      -5.739 -10.824 -20.435  1.00 40.78           C  
ANISOU 2909  CG1 VAL I 331     6463   4953   4078   -472    577    -72       C  
ATOM   2910  CG2 VAL I 331      -4.756  -8.838 -21.596  1.00 42.70           C  
ANISOU 2910  CG2 VAL I 331     6484   5301   4436   -365    234    216       C  
ATOM   2911  N   PRO I 332      -7.730  -9.408 -17.867  1.00 43.16           N  
ANISOU 2911  N   PRO I 332     5371   5624   5403    -26    920   1010       N  
ATOM   2912  CA  PRO I 332      -8.112 -10.032 -16.587  1.00 45.40           C  
ANISOU 2912  CA  PRO I 332     5681   6013   5555    -52    970    878       C  
ATOM   2913  C   PRO I 332      -7.422 -11.383 -16.302  1.00 44.75           C  
ANISOU 2913  C   PRO I 332     5786   6019   5195   -107    817    858       C  
ATOM   2914  O   PRO I 332      -7.109 -12.123 -17.225  1.00 41.59           O  
ANISOU 2914  O   PRO I 332     5360   5635   4806   -177    675    921       O  
ATOM   2915  CB  PRO I 332      -9.619 -10.236 -16.734  1.00 45.77           C  
ANISOU 2915  CB  PRO I 332     5481   6080   5828    -40   1062   1013       C  
ATOM   2916  CG  PRO I 332     -10.040  -9.171 -17.694  1.00 47.04           C  
ANISOU 2916  CG  PRO I 332     5479   6147   6245    136    933   1134       C  
ATOM   2917  CD  PRO I 332      -8.908  -9.024 -18.651  1.00 46.48           C  
ANISOU 2917  CD  PRO I 332     5681   6037   5940    135    824   1243       C  
ATOM   2918  N   ALA I 333      -7.219 -11.699 -15.025  1.00 45.32           N  
ANISOU 2918  N   ALA I 333     6135   6120   4961      0    846    774       N  
ATOM   2919  CA  ALA I 333      -6.501 -12.908 -14.670  1.00 46.22           C  
ANISOU 2919  CA  ALA I 333     6519   6232   4808     92    637    829       C  
ATOM   2920  C   ALA I 333      -7.079 -14.134 -15.374  1.00 46.48           C  
ANISOU 2920  C   ALA I 333     6494   6147   5018    -73    756   1078       C  
ATOM   2921  O   ALA I 333      -6.336 -15.005 -15.822  1.00 47.74           O  
ANISOU 2921  O   ALA I 333     6681   6229   5226    -52    547   1063       O  
ATOM   2922  CB  ALA I 333      -6.522 -13.110 -13.167  1.00 49.29           C  
ANISOU 2922  CB  ALA I 333     7449   6654   4625    358    686    850       C  
ATOM   2923  N   SER I 334      -8.402 -14.217 -15.451  1.00 47.37           N  
ANISOU 2923  N   SER I 334     6437   6190   5368   -237   1094   1201       N  
ATOM   2924  CA  SER I 334      -9.039 -15.423 -15.963  1.00 50.06           C  
ANISOU 2924  CA  SER I 334     6629   6329   6062   -446   1207   1277       C  
ATOM   2925  C   SER I 334      -8.855 -15.484 -17.465  1.00 47.65           C  
ANISOU 2925  C   SER I 334     6034   6134   5934   -526    791   1067       C  
ATOM   2926  O   SER I 334      -8.599 -16.541 -18.015  1.00 48.32           O  
ANISOU 2926  O   SER I 334     6139   6082   6138   -615    680    972       O  
ATOM   2927  CB  SER I 334     -10.518 -15.391 -15.647  1.00 53.73           C  
ANISOU 2927  CB  SER I 334     6775   6651   6989   -626   1683   1304       C  
ATOM   2928  OG  SER I 334     -11.005 -14.127 -16.061  1.00 55.78           O  
ANISOU 2928  OG  SER I 334     6664   7119   7409   -550   1522   1154       O  
ATOM   2929  N   ASP I 335      -8.998 -14.328 -18.116  1.00 49.35           N  
ANISOU 2929  N   ASP I 335     6084   6553   6114   -440    612   1007       N  
ATOM   2930  CA  ASP I 335      -8.814 -14.215 -19.559  1.00 48.00           C  
ANISOU 2930  CA  ASP I 335     5893   6513   5831   -391    276    895       C  
ATOM   2931  C   ASP I 335      -7.430 -14.651 -19.938  1.00 47.97           C  
ANISOU 2931  C   ASP I 335     6150   6486   5589   -371    288    825       C  
ATOM   2932  O   ASP I 335      -7.284 -15.415 -20.895  1.00 45.54           O  
ANISOU 2932  O   ASP I 335     5915   6188   5198   -401    149    644       O  
ATOM   2933  CB  ASP I 335      -9.019 -12.786 -20.034  1.00 51.19           C  
ANISOU 2933  CB  ASP I 335     6298   7015   6135   -190    209   1021       C  
ATOM   2934  CG  ASP I 335     -10.468 -12.370 -20.048  1.00 56.53           C  
ANISOU 2934  CG  ASP I 335     6590   7715   7172    -99     44   1006       C  
ATOM   2935  OD1 ASP I 335     -11.362 -13.224 -19.868  1.00 63.39           O  
ANISOU 2935  OD1 ASP I 335     7085   8539   8460   -260    -10    810       O  
ATOM   2936  OD2 ASP I 335     -10.717 -11.166 -20.266  1.00 60.21           O  
ANISOU 2936  OD2 ASP I 335     7062   8164   7647    144      2   1163       O  
ATOM   2937  N   ALA I 336      -6.432 -14.165 -19.176  1.00 45.61           N  
ANISOU 2937  N   ALA I 336     5927   6141   5261   -303    429    855       N  
ATOM   2938  CA  ALA I 336      -5.018 -14.472 -19.396  1.00 44.89           C  
ANISOU 2938  CA  ALA I 336     5866   5979   5210   -258    456    690       C  
ATOM   2939  C   ALA I 336      -4.796 -15.943 -19.359  1.00 46.93           C  
ANISOU 2939  C   ALA I 336     6183   6101   5547   -254    356    608       C  
ATOM   2940  O   ALA I 336      -4.117 -16.488 -20.232  1.00 49.07           O  
ANISOU 2940  O   ALA I 336     6453   6310   5879   -250    414    408       O  
ATOM   2941  CB  ALA I 336      -4.122 -13.820 -18.332  1.00 44.88           C  
ANISOU 2941  CB  ALA I 336     5764   5936   5352   -155    412    562       C  
ATOM   2942  N   GLU I 337      -5.318 -16.588 -18.322  1.00 47.11           N  
ANISOU 2942  N   GLU I 337     6319   5995   5583   -228    326    775       N  
ATOM   2943  CA  GLU I 337      -5.154 -18.034 -18.209  1.00 49.32           C  
ANISOU 2943  CA  GLU I 337     6731   5971   6038   -197    318    791       C  
ATOM   2944  C   GLU I 337      -5.805 -18.755 -19.382  1.00 47.95           C  
ANISOU 2944  C   GLU I 337     6436   5705   6078   -431    349    563       C  
ATOM   2945  O   GLU I 337      -5.232 -19.715 -19.889  1.00 50.20           O  
ANISOU 2945  O   GLU I 337     6754   5766   6551   -402    334    348       O  
ATOM   2946  CB  GLU I 337      -5.691 -18.586 -16.883  1.00 51.45           C  
ANISOU 2946  CB  GLU I 337     7325   5995   6228   -108    484   1152       C  
ATOM   2947  CG  GLU I 337      -5.253 -20.031 -16.610  1.00 58.71           C  
ANISOU 2947  CG  GLU I 337     8521   6442   7343     52    507   1297       C  
ATOM   2948  CD  GLU I 337      -3.734 -20.192 -16.414  1.00 64.06           C  
ANISOU 2948  CD  GLU I 337     9238   7119   7983    486     73   1176       C  
ATOM   2949  OE1 GLU I 337      -3.042 -19.200 -16.077  1.00 66.29           O  
ANISOU 2949  OE1 GLU I 337     9387   7737   8063    667   -234   1009       O  
ATOM   2950  OE2 GLU I 337      -3.219 -21.321 -16.579  1.00 69.71           O  
ANISOU 2950  OE2 GLU I 337    10032   7432   9021    659     23   1174       O  
ATOM   2951  N   LYS I 338      -6.989 -18.308 -19.797  1.00 48.54           N  
ANISOU 2951  N   LYS I 338     6331   5933   6176   -609    318    515       N  
ATOM   2952  CA  LYS I 338      -7.689 -18.895 -20.957  1.00 53.98           C  
ANISOU 2952  CA  LYS I 338     6859   6613   7035   -770    106    120       C  
ATOM   2953  C   LYS I 338      -6.859 -18.809 -22.253  1.00 56.42           C  
ANISOU 2953  C   LYS I 338     7389   7131   6917   -631    -32   -174       C  
ATOM   2954  O   LYS I 338      -6.738 -19.809 -22.978  1.00 62.25           O  
ANISOU 2954  O   LYS I 338     8186   7716   7750   -685   -108   -590       O  
ATOM   2955  CB  LYS I 338      -9.069 -18.243 -21.188  1.00 56.36           C  
ANISOU 2955  CB  LYS I 338     6822   7107   7483   -851   -108     46       C  
ATOM   2956  CG  LYS I 338      -9.915 -18.928 -22.268  1.00 62.96           C  
ANISOU 2956  CG  LYS I 338     7383   7938   8599   -972   -558   -534       C  
ATOM   2957  CD  LYS I 338     -11.240 -18.211 -22.563  1.00 67.44           C  
ANISOU 2957  CD  LYS I 338     7477   8730   9414   -921   -990   -702       C  
ATOM   2958  CE  LYS I 338     -11.850 -18.661 -23.900  1.00 75.83           C  
ANISOU 2958  CE  LYS I 338     8373   9968  10468   -848  -1788  -1421       C  
ATOM   2959  NZ  LYS I 338     -13.310 -18.370 -24.069  1.00 81.54           N  
ANISOU 2959  NZ  LYS I 338     8336  10772  11873   -825  -2367  -1812       N  
ATOM   2960  N   TYR I 339      -6.292 -17.632 -22.551  1.00 52.90           N  
ANISOU 2960  N   TYR I 339     7106   6953   6038   -463     58     11       N  
ATOM   2961  CA  TYR I 339      -5.343 -17.500 -23.669  1.00 53.27           C  
ANISOU 2961  CA  TYR I 339     7466   7097   5678   -333    259   -164       C  
ATOM   2962  C   TYR I 339      -4.136 -18.455 -23.564  1.00 53.50           C  
ANISOU 2962  C   TYR I 339     7443   6848   6034   -323    538   -400       C  
ATOM   2963  O   TYR I 339      -3.671 -18.988 -24.577  1.00 53.13           O  
ANISOU 2963  O   TYR I 339     7613   6778   5793   -270    719   -765       O  
ATOM   2964  CB  TYR I 339      -4.833 -16.054 -23.804  1.00 51.66           C  
ANISOU 2964  CB  TYR I 339     7407   7011   5209   -216    574    162       C  
ATOM   2965  CG  TYR I 339      -5.890 -15.082 -24.284  1.00 52.66           C  
ANISOU 2965  CG  TYR I 339     7727   7353   4929    -71    313    401       C  
ATOM   2966  CD1 TYR I 339      -6.504 -15.244 -25.529  1.00 58.55           C  
ANISOU 2966  CD1 TYR I 339     8875   8320   5051    135    -34    237       C  
ATOM   2967  CD2 TYR I 339      -6.269 -14.002 -23.504  1.00 49.51           C  
ANISOU 2967  CD2 TYR I 339     7135   6922   4751    -54    333    731       C  
ATOM   2968  CE1 TYR I 339      -7.483 -14.363 -25.968  1.00 61.94           C  
ANISOU 2968  CE1 TYR I 339     9477   8937   5118    421   -457    465       C  
ATOM   2969  CE2 TYR I 339      -7.236 -13.109 -23.939  1.00 53.22           C  
ANISOU 2969  CE2 TYR I 339     7733   7510   4976    172     62    960       C  
ATOM   2970  CZ  TYR I 339      -7.836 -13.294 -25.163  1.00 58.97           C  
ANISOU 2970  CZ  TYR I 339     8831   8458   5117    442   -376    863       C  
ATOM   2971  OH  TYR I 339      -8.790 -12.405 -25.565  1.00 64.09           O  
ANISOU 2971  OH  TYR I 339     9596   9209   5547    805   -804   1103       O  
ATOM   2972  N   ARG I 340      -3.615 -18.637 -22.352  1.00 51.81           N  
ANISOU 2972  N   ARG I 340     6988   6426   6271   -291    547   -223       N  
ATOM   2973  CA  ARG I 340      -2.423 -19.466 -22.138  1.00 56.48           C  
ANISOU 2973  CA  ARG I 340     7442   6722   7295   -142    666   -425       C  
ATOM   2974  C   ARG I 340      -2.596 -20.930 -22.588  1.00 61.97           C  
ANISOU 2974  C   ARG I 340     8229   7087   8230   -163    645   -744       C  
ATOM   2975  O   ARG I 340      -1.614 -21.639 -22.709  1.00 61.27           O  
ANISOU 2975  O   ARG I 340     8032   6714   8531      8    794   -995       O  
ATOM   2976  CB  ARG I 340      -1.916 -19.385 -20.688  1.00 55.81           C  
ANISOU 2976  CB  ARG I 340     7185   6512   7506     54    431   -178       C  
ATOM   2977  CG  ARG I 340      -1.096 -18.132 -20.447  1.00 58.21           C  
ANISOU 2977  CG  ARG I 340     7219   6999   7899    109    492   -228       C  
ATOM   2978  CD  ARG I 340      -0.572 -17.982 -19.021  1.00 59.34           C  
ANISOU 2978  CD  ARG I 340     7218   7106   8222    387     40   -171       C  
ATOM   2979  NE  ARG I 340       0.595 -17.109 -19.030  1.00 63.13           N  
ANISOU 2979  NE  ARG I 340     7183   7608   9195    429     75   -547       N  
ATOM   2980  CZ  ARG I 340       0.635 -15.819 -18.671  1.00 62.84           C  
ANISOU 2980  CZ  ARG I 340     6975   7701   9200    312     87   -619       C  
ATOM   2981  NH1 ARG I 340      -0.439 -15.172 -18.204  1.00 61.50           N  
ANISOU 2981  NH1 ARG I 340     7151   7706   8510    212     36   -309       N  
ATOM   2982  NH2 ARG I 340       1.788 -15.168 -18.762  1.00 63.64           N  
ANISOU 2982  NH2 ARG I 340     6461   7673  10046    284    208  -1088       N  
ATOM   2983  N   GLN I 341      -3.824 -21.375 -22.848  1.00 67.94           N  
ANISOU 2983  N   GLN I 341     9083   7813   8917   -372    462   -829       N  
ATOM   2984  CA  GLN I 341      -4.029 -22.559 -23.706  1.00 77.40           C  
ANISOU 2984  CA  GLN I 341    10357   8733  10318   -462    454  -1389       C  
ATOM   2985  C   GLN I 341      -5.409 -22.556 -24.357  1.00 80.28           C  
ANISOU 2985  C   GLN I 341    10715   9283  10505   -692     97  -1704       C  
ATOM   2986  O   GLN I 341      -5.526 -22.439 -25.580  1.00 86.72           O  
ANISOU 2986  O   GLN I 341    11775  10403  10772   -630    -71  -2185       O  
ATOM   2987  CB  GLN I 341      -3.783 -23.869 -22.948  1.00 82.43           C  
ANISOU 2987  CB  GLN I 341    10920   8683  11716   -421    546  -1347       C  
ATOM   2988  CG  GLN I 341      -4.920 -24.336 -22.045  1.00 87.50           C  
ANISOU 2988  CG  GLN I 341    11512   8949  12785   -651    528  -1023       C  
ATOM   2989  CD  GLN I 341      -5.309 -23.312 -20.999  1.00 83.39           C  
ANISOU 2989  CD  GLN I 341    11003   8732  11947   -624    516   -393       C  
ATOM   2990  OE1 GLN I 341      -4.663 -23.192 -19.955  1.00 84.88           O  
ANISOU 2990  OE1 GLN I 341    11367   8829  12054   -336    555     78       O  
ATOM   2991  NE2 GLN I 341      -6.367 -22.569 -21.271  1.00 81.30           N  
ANISOU 2991  NE2 GLN I 341    10561   8829  11499   -856    392   -454       N  
TER    2992      GLN I 341                                                      
ATOM   2993  N   GLU J 303      23.385   5.902 -30.844  1.00 73.21           N  
ANISOU 2993  N   GLU J 303     8899   8658  10257    444    708   2072       N  
ATOM   2994  CA  GLU J 303      22.196   6.791 -30.827  1.00 69.81           C  
ANISOU 2994  CA  GLU J 303     8751   8058   9714     58    239   1695       C  
ATOM   2995  C   GLU J 303      21.431   6.599 -29.522  1.00 66.65           C  
ANISOU 2995  C   GLU J 303     8299   7736   9288    156      1   1624       C  
ATOM   2996  O   GLU J 303      21.409   5.511 -28.938  1.00 63.28           O  
ANISOU 2996  O   GLU J 303     7830   7323   8890    533    270   1849       O  
ATOM   2997  CB  GLU J 303      21.279   6.546 -32.043  1.00 72.80           C  
ANISOU 2997  CB  GLU J 303     9563   8216   9882   -165    385   1488       C  
ATOM   2998  CG  GLU J 303      20.314   7.702 -32.341  1.00 75.80           C  
ANISOU 2998  CG  GLU J 303     9943   8693  10162   -357      9   1573       C  
ATOM   2999  CD  GLU J 303      19.662   7.630 -33.723  1.00 81.19           C  
ANISOU 2999  CD  GLU J 303    10675   9840  10331   -632     72   1661       C  
ATOM   3000  OE1 GLU J 303      19.502   6.505 -34.259  1.00 85.60           O  
ANISOU 3000  OE1 GLU J 303    11424  10593  10505   -954    403   1243       O  
ATOM   3001  OE2 GLU J 303      19.306   8.705 -34.273  1.00 82.30           O  
ANISOU 3001  OE2 GLU J 303    10607  10242  10419   -579    -61   2180       O  
ATOM   3002  N   ILE J 304      20.806   7.680 -29.078  1.00 61.67           N  
ANISOU 3002  N   ILE J 304     7687   7060   8684   -147   -315   1375       N  
ATOM   3003  CA  ILE J 304      20.134   7.732 -27.799  1.00 58.68           C  
ANISOU 3003  CA  ILE J 304     7241   6810   8244   -193   -505   1194       C  
ATOM   3004  C   ILE J 304      18.633   7.972 -28.045  1.00 53.11           C  
ANISOU 3004  C   ILE J 304     6906   5620   7650   -192   -562   1068       C  
ATOM   3005  O   ILE J 304      18.270   8.932 -28.706  1.00 50.74           O  
ANISOU 3005  O   ILE J 304     6683   5048   7545   -282   -487   1154       O  
ATOM   3006  CB  ILE J 304      20.771   8.857 -26.960  1.00 61.05           C  
ANISOU 3006  CB  ILE J 304     7179   7530   8486   -738   -549    853       C  
ATOM   3007  CG1 ILE J 304      22.223   8.475 -26.617  1.00 68.37           C  
ANISOU 3007  CG1 ILE J 304     7430   9494   9051   -776   -594   1122       C  
ATOM   3008  CG2 ILE J 304      19.959   9.114 -25.699  1.00 61.58           C  
ANISOU 3008  CG2 ILE J 304     7244   7715   8436   -992   -621    469       C  
ATOM   3009  CD1 ILE J 304      23.201   9.637 -26.495  1.00 74.37           C  
ANISOU 3009  CD1 ILE J 304     7794  10765   9695  -1596   -489    670       C  
ATOM   3010  N   PHE J 305      17.770   7.109 -27.501  1.00 49.80           N  
ANISOU 3010  N   PHE J 305     6614   5179   7126    -30   -599   1019       N  
ATOM   3011  CA  PHE J 305      16.306   7.210 -27.694  1.00 46.23           C  
ANISOU 3011  CA  PHE J 305     6339   4552   6675    -59   -673    956       C  
ATOM   3012  C   PHE J 305      15.598   7.557 -26.389  1.00 47.24           C  
ANISOU 3012  C   PHE J 305     6440   4597   6911    -64   -755    770       C  
ATOM   3013  O   PHE J 305      16.116   7.287 -25.306  1.00 50.93           O  
ANISOU 3013  O   PHE J 305     6771   5326   7253    -89   -785    655       O  
ATOM   3014  CB  PHE J 305      15.768   5.900 -28.282  1.00 46.64           C  
ANISOU 3014  CB  PHE J 305     6587   4661   6473   -124   -475    842       C  
ATOM   3015  CG  PHE J 305      16.424   5.518 -29.588  1.00 49.96           C  
ANISOU 3015  CG  PHE J 305     7083   5188   6710   -311   -203    821       C  
ATOM   3016  CD1 PHE J 305      17.705   4.953 -29.603  1.00 51.73           C  
ANISOU 3016  CD1 PHE J 305     7340   5200   7113   -108    171    912       C  
ATOM   3017  CD2 PHE J 305      15.797   5.787 -30.810  1.00 54.21           C  
ANISOU 3017  CD2 PHE J 305     7523   6254   6820   -680   -279    828       C  
ATOM   3018  CE1 PHE J 305      18.334   4.632 -30.801  1.00 55.08           C  
ANISOU 3018  CE1 PHE J 305     7874   5634   7420   -308    564    824       C  
ATOM   3019  CE2 PHE J 305      16.412   5.461 -32.023  1.00 58.30           C  
ANISOU 3019  CE2 PHE J 305     8093   7041   7017  -1008     17    704       C  
ATOM   3020  CZ  PHE J 305      17.686   4.890 -32.017  1.00 59.09           C  
ANISOU 3020  CZ  PHE J 305     8398   6623   7430   -838    483    614       C  
ATOM   3021  N   THR J 306      14.418   8.167 -26.484  1.00 48.07           N  
ANISOU 3021  N   THR J 306     6562   4520   7183    -25   -734    846       N  
ATOM   3022  CA  THR J 306      13.591   8.498 -25.320  1.00 49.24           C  
ANISOU 3022  CA  THR J 306     6730   4484   7495    -34   -658    631       C  
ATOM   3023  C   THR J 306      12.404   7.512 -25.257  1.00 49.12           C  
ANISOU 3023  C   THR J 306     6741   4667   7255     62   -795    663       C  
ATOM   3024  O   THR J 306      11.623   7.414 -26.191  1.00 49.10           O  
ANISOU 3024  O   THR J 306     6588   4960   7106     73   -850    931       O  
ATOM   3025  CB  THR J 306      13.084   9.960 -25.408  1.00 55.67           C  
ANISOU 3025  CB  THR J 306     7507   4767   8876     42   -205    805       C  
ATOM   3026  OG1 THR J 306      14.209  10.826 -25.547  1.00 60.49           O  
ANISOU 3026  OG1 THR J 306     8160   5078   9745   -226    133    632       O  
ATOM   3027  CG2 THR J 306      12.290  10.394 -24.163  1.00 57.08           C  
ANISOU 3027  CG2 THR J 306     7768   4592   9328    -43    135    444       C  
ATOM   3028  N   LEU J 307      12.287   6.777 -24.155  1.00 48.31           N  
ANISOU 3028  N   LEU J 307     6729   4600   7025     48   -803    421       N  
ATOM   3029  CA  LEU J 307      11.187   5.846 -23.959  1.00 48.53           C  
ANISOU 3029  CA  LEU J 307     6830   4686   6922     42   -764    354       C  
ATOM   3030  C   LEU J 307      10.153   6.469 -23.031  1.00 48.24           C  
ANISOU 3030  C   LEU J 307     6721   4546   7058     89   -738    267       C  
ATOM   3031  O   LEU J 307      10.470   6.900 -21.935  1.00 46.14           O  
ANISOU 3031  O   LEU J 307     6483   4216   6833     31   -658     44       O  
ATOM   3032  CB  LEU J 307      11.702   4.514 -23.388  1.00 48.88           C  
ANISOU 3032  CB  LEU J 307     7040   4684   6847    137   -518    352       C  
ATOM   3033  CG  LEU J 307      10.679   3.405 -23.138  1.00 52.36           C  
ANISOU 3033  CG  LEU J 307     7666   4959   7269     36   -179    198       C  
ATOM   3034  CD1 LEU J 307      10.066   2.917 -24.449  1.00 54.26           C  
ANISOU 3034  CD1 LEU J 307     7972   5299   7343   -466     26   -126       C  
ATOM   3035  CD2 LEU J 307      11.321   2.231 -22.376  1.00 54.26           C  
ANISOU 3035  CD2 LEU J 307     8040   4958   7615    388    369    522       C  
ATOM   3036  N   GLN J 308       8.906   6.475 -23.475  1.00 50.96           N  
ANISOU 3036  N   GLN J 308     6884   5072   7405    102   -745    424       N  
ATOM   3037  CA  GLN J 308       7.805   6.951 -22.666  1.00 53.46           C  
ANISOU 3037  CA  GLN J 308     7082   5275   7956    234   -598    440       C  
ATOM   3038  C   GLN J 308       7.274   5.749 -21.896  1.00 50.28           C  
ANISOU 3038  C   GLN J 308     6834   4966   7302     65   -590    130       C  
ATOM   3039  O   GLN J 308       7.081   4.701 -22.479  1.00 52.30           O  
ANISOU 3039  O   GLN J 308     7129   5456   7286   -197   -562     23       O  
ATOM   3040  CB  GLN J 308       6.727   7.537 -23.573  1.00 60.29           C  
ANISOU 3040  CB  GLN J 308     7427   6579   8901    453   -569   1060       C  
ATOM   3041  CG  GLN J 308       5.776   8.502 -22.874  1.00 68.59           C  
ANISOU 3041  CG  GLN J 308     8275   7271  10513    855   -125   1364       C  
ATOM   3042  CD  GLN J 308       5.441   9.713 -23.735  1.00 76.46           C  
ANISOU 3042  CD  GLN J 308     8766   8300  11983   1442    282   2383       C  
ATOM   3043  OE1 GLN J 308       4.272  10.046 -23.947  1.00 80.93           O  
ANISOU 3043  OE1 GLN J 308     8694   9361  12693   1893    497   3201       O  
ATOM   3044  NE2 GLN J 308       6.476  10.375 -24.236  1.00 77.53           N  
ANISOU 3044  NE2 GLN J 308     9093   7978  12385   1511    489   2502       N  
ATOM   3045  N   VAL J 309       7.072   5.905 -20.592  1.00 47.41           N  
ANISOU 3045  N   VAL J 309     6583   4402   7027    114   -449    -76       N  
ATOM   3046  CA  VAL J 309       6.556   4.854 -19.729  1.00 47.31           C  
ANISOU 3046  CA  VAL J 309     6700   4448   6827     48   -333   -219       C  
ATOM   3047  C   VAL J 309       5.378   5.423 -18.934  1.00 49.68           C  
ANISOU 3047  C   VAL J 309     6875   4686   7313     89   -170   -321       C  
ATOM   3048  O   VAL J 309       5.448   6.552 -18.457  1.00 52.02           O  
ANISOU 3048  O   VAL J 309     7156   4745   7864    131     36   -451       O  
ATOM   3049  CB  VAL J 309       7.654   4.353 -18.754  1.00 46.63           C  
ANISOU 3049  CB  VAL J 309     6742   4503   6471    123   -282   -171       C  
ATOM   3050  CG1 VAL J 309       7.118   3.240 -17.857  1.00 47.82           C  
ANISOU 3050  CG1 VAL J 309     6992   4684   6493    215     11    -44       C  
ATOM   3051  CG2 VAL J 309       8.877   3.889 -19.532  1.00 47.33           C  
ANISOU 3051  CG2 VAL J 309     6864   4615   6504    229   -301     84       C  
ATOM   3052  N   ARG J 310       4.309   4.642 -18.798  1.00 50.64           N  
ANISOU 3052  N   ARG J 310     6930   4949   7361     -7    -78   -345       N  
ATOM   3053  CA  ARG J 310       3.074   5.070 -18.133  1.00 54.70           C  
ANISOU 3053  CA  ARG J 310     7242   5470   8070     70    121   -363       C  
ATOM   3054  C   ARG J 310       2.980   4.383 -16.763  1.00 54.43           C  
ANISOU 3054  C   ARG J 310     7480   5361   7837    -13    322   -611       C  
ATOM   3055  O   ARG J 310       2.775   3.180 -16.689  1.00 50.54           O  
ANISOU 3055  O   ARG J 310     7121   4898   7183   -147    454   -604       O  
ATOM   3056  CB  ARG J 310       1.862   4.718 -19.030  1.00 61.06           C  
ANISOU 3056  CB  ARG J 310     7554   6856   8787    -83     55   -144       C  
ATOM   3057  CG  ARG J 310       0.488   5.103 -18.492  1.00 68.85           C  
ANISOU 3057  CG  ARG J 310     8130   8043   9987     80    284     33       C  
ATOM   3058  CD  ARG J 310      -0.584   5.199 -19.595  1.00 77.08           C  
ANISOU 3058  CD  ARG J 310     8274  10191  10820     14    131    577       C  
ATOM   3059  NE  ARG J 310      -0.909   3.905 -20.212  1.00 81.41           N  
ANISOU 3059  NE  ARG J 310     8696  11523  10712   -849     -7    120       N  
ATOM   3060  CZ  ARG J 310      -1.762   2.996 -19.718  1.00 84.22           C  
ANISOU 3060  CZ  ARG J 310     9033  12080  10884  -1379    234   -329       C  
ATOM   3061  NH1 ARG J 310      -2.416   3.201 -18.579  1.00 85.41           N  
ANISOU 3061  NH1 ARG J 310     9235  11824  11390  -1035    477   -275       N  
ATOM   3062  NH2 ARG J 310      -1.966   1.861 -20.369  1.00 87.59           N  
ANISOU 3062  NH2 ARG J 310     9426  13074  10777  -2388    400   -950       N  
ATOM   3063  N   GLY J 311       3.177   5.136 -15.674  1.00 55.46           N  
ANISOU 3063  N   GLY J 311     7694   5426   7950    -20    506   -852       N  
ATOM   3064  CA  GLY J 311       2.961   4.590 -14.324  1.00 57.02           C  
ANISOU 3064  CA  GLY J 311     8001   5875   7787   -130    696   -991       C  
ATOM   3065  C   GLY J 311       4.264   4.343 -13.598  1.00 59.95           C  
ANISOU 3065  C   GLY J 311     8389   6849   7541   -233    576   -915       C  
ATOM   3066  O   GLY J 311       5.277   4.061 -14.228  1.00 58.56           O  
ANISOU 3066  O   GLY J 311     8186   6786   7275   -113    349   -621       O  
ATOM   3067  N   ARG J 312       4.238   4.443 -12.271  1.00 64.98           N  
ANISOU 3067  N   ARG J 312     8466   6964   9260    921    559  -1820       N  
ATOM   3068  CA  ARG J 312       5.461   4.345 -11.460  1.00 68.27           C  
ANISOU 3068  CA  ARG J 312     9002   7673   9261    762    606  -1991       C  
ATOM   3069  C   ARG J 312       6.120   2.965 -11.528  1.00 63.84           C  
ANISOU 3069  C   ARG J 312     8609   7410   8236    574    597  -1469       C  
ATOM   3070  O   ARG J 312       7.319   2.883 -11.738  1.00 61.13           O  
ANISOU 3070  O   ARG J 312     8467   6992   7766    457    483  -1346       O  
ATOM   3071  CB  ARG J 312       5.198   4.699  -9.978  1.00 74.92           C  
ANISOU 3071  CB  ARG J 312     9544   9130   9790    819    840  -2626       C  
ATOM   3072  CG  ARG J 312       6.446   4.732  -9.094  1.00 80.81           C  
ANISOU 3072  CG  ARG J 312    10299  10374  10031    686    846  -2909       C  
ATOM   3073  CD  ARG J 312       7.261   6.011  -9.303  1.00 88.42           C  
ANISOU 3073  CD  ARG J 312    11285  10764  11546    667    697  -3472       C  
ATOM   3074  NE  ARG J 312       8.694   5.845  -9.028  1.00 93.45           N  
ANISOU 3074  NE  ARG J 312    12037  11653  11817    474    591  -3481       N  
ATOM   3075  CZ  ARG J 312       9.595   6.836  -9.055  1.00102.45           C  
ANISOU 3075  CZ  ARG J 312    13125  12389  13413    382    476  -3991       C  
ATOM   3076  NH1 ARG J 312       9.220   8.084  -9.330  1.00105.89           N  
ANISOU 3076  NH1 ARG J 312    13378  12045  14808    474    469  -4500       N  
ATOM   3077  NH2 ARG J 312      10.882   6.587  -8.785  1.00103.95           N  
ANISOU 3077  NH2 ARG J 312    13373  12907  13213    200    373  -3983       N  
ATOM   3078  N   GLU J 313       5.352   1.899 -11.307  1.00 64.09           N  
ANISOU 3078  N   GLU J 313     8489   7729   8133    545    737  -1167       N  
ATOM   3079  CA  GLU J 313       5.941   0.566 -11.133  1.00 64.00           C  
ANISOU 3079  CA  GLU J 313     8505   7920   7890    387    788   -666       C  
ATOM   3080  C   GLU J 313       6.734   0.150 -12.371  1.00 57.36           C  
ANISOU 3080  C   GLU J 313     7910   6620   7264    304    557   -462       C  
ATOM   3081  O   GLU J 313       7.881  -0.324 -12.283  1.00 58.45           O  
ANISOU 3081  O   GLU J 313     8168   6807   7230    213    516   -264       O  
ATOM   3082  CB  GLU J 313       4.857  -0.483 -10.847  1.00 68.97           C  
ANISOU 3082  CB  GLU J 313     8830   8720   8653    349    994   -321       C  
ATOM   3083  CG  GLU J 313       5.397  -1.729 -10.158  1.00 73.89           C  
ANISOU 3083  CG  GLU J 313     9311   9631   9130    226   1156    291       C  
ATOM   3084  CD  GLU J 313       4.737  -3.025 -10.612  1.00 78.91           C  
ANISOU 3084  CD  GLU J 313     9705   9893  10381    105   1242    719       C  
ATOM   3085  OE1 GLU J 313       3.579  -2.996 -11.097  1.00 80.16           O  
ANISOU 3085  OE1 GLU J 313     9698   9849  10906    108   1250    516       O  
ATOM   3086  OE2 GLU J 313       5.394  -4.091 -10.475  1.00 83.14           O  
ANISOU 3086  OE2 GLU J 313    10150  10300  11137      7   1298   1239       O  
ATOM   3087  N   ARG J 314       6.101   0.328 -13.519  1.00 53.25           N  
ANISOU 3087  N   ARG J 314     7390   5776   7067    362    408   -526       N  
ATOM   3088  CA  ARG J 314       6.700   0.022 -14.820  1.00 50.38           C  
ANISOU 3088  CA  ARG J 314     7150   5201   6791    322    191   -433       C  
ATOM   3089  C   ARG J 314       7.981   0.834 -15.034  1.00 46.78           C  
ANISOU 3089  C   ARG J 314     6936   4663   6173    309     80   -424       C  
ATOM   3090  O   ARG J 314       8.996   0.311 -15.487  1.00 40.22           O  
ANISOU 3090  O   ARG J 314     6209   3840   5233    221      7   -304       O  
ATOM   3091  CB  ARG J 314       5.703   0.380 -15.909  1.00 51.96           C  
ANISOU 3091  CB  ARG J 314     7204   5341   7196    445     35   -512       C  
ATOM   3092  CG  ARG J 314       5.408  -0.681 -16.932  1.00 54.36           C  
ANISOU 3092  CG  ARG J 314     7318   5722   7612    385    -87   -577       C  
ATOM   3093  CD  ARG J 314       4.236  -0.203 -17.773  1.00 60.22           C  
ANISOU 3093  CD  ARG J 314     7813   6620   8446    543   -246   -667       C  
ATOM   3094  NE  ARG J 314       2.966  -0.612 -17.191  1.00 63.40           N  
ANISOU 3094  NE  ARG J 314     7940   7009   9137    529   -108   -794       N  
ATOM   3095  CZ  ARG J 314       1.818   0.050 -17.264  1.00 67.05           C  
ANISOU 3095  CZ  ARG J 314     8189   7552   9732    699   -139   -840       C  
ATOM   3096  NH1 ARG J 314       1.715   1.216 -17.891  1.00 72.17           N  
ANISOU 3096  NH1 ARG J 314     8849   8240  10331    931   -313   -695       N  
ATOM   3097  NH2 ARG J 314       0.749  -0.474 -16.686  1.00 71.10           N  
ANISOU 3097  NH2 ARG J 314     8409   8090  10512    644     25   -953       N  
ATOM   3098  N   TYR J 315       7.921   2.119 -14.708  1.00 46.44           N  
ANISOU 3098  N   TYR J 315     6916   4495   6233    394     84   -595       N  
ATOM   3099  CA  TYR J 315       9.087   2.978 -14.836  1.00 47.82           C  
ANISOU 3099  CA  TYR J 315     7229   4490   6448    341      5   -606       C  
ATOM   3100  C   TYR J 315      10.227   2.456 -13.997  1.00 46.70           C  
ANISOU 3100  C   TYR J 315     7174   4606   5963    194     61   -658       C  
ATOM   3101  O   TYR J 315      11.390   2.481 -14.405  1.00 46.25           O  
ANISOU 3101  O   TYR J 315     7229   4500   5841     96    -26   -533       O  
ATOM   3102  CB  TYR J 315       8.757   4.394 -14.391  1.00 51.15           C  
ANISOU 3102  CB  TYR J 315     7539   4609   7285    441     42   -921       C  
ATOM   3103  CG  TYR J 315       9.970   5.296 -14.197  1.00 54.25           C  
ANISOU 3103  CG  TYR J 315     7969   4746   7897    327      6  -1080       C  
ATOM   3104  CD1 TYR J 315      10.579   5.907 -15.277  1.00 56.33           C  
ANISOU 3104  CD1 TYR J 315     8258   4637   8506    302   -106   -670       C  
ATOM   3105  CD2 TYR J 315      10.470   5.580 -12.918  1.00 56.69           C  
ANISOU 3105  CD2 TYR J 315     8190   5272   8074    242     93  -1654       C  
ATOM   3106  CE1 TYR J 315      11.657   6.776 -15.100  1.00 60.19           C  
ANISOU 3106  CE1 TYR J 315     8700   4795   9374    159   -115   -799       C  
ATOM   3107  CE2 TYR J 315      11.542   6.442 -12.729  1.00 60.18           C  
ANISOU 3107  CE2 TYR J 315     8573   5458   8833    107     44  -1944       C  
ATOM   3108  CZ  TYR J 315      12.139   7.039 -13.825  1.00 61.64           C  
ANISOU 3108  CZ  TYR J 315     8799   5089   9530     47    -51  -1503       C  
ATOM   3109  OH  TYR J 315      13.214   7.894 -13.669  1.00 63.18           O  
ANISOU 3109  OH  TYR J 315     8869   4940  10195   -129    -78  -1746       O  
ATOM   3110  N   GLU J 316       9.891   1.990 -12.807  1.00 48.05           N  
ANISOU 3110  N   GLU J 316     7227   5154   5875    194    216   -779       N  
ATOM   3111  CA  GLU J 316      10.891   1.518 -11.883  1.00 49.93           C  
ANISOU 3111  CA  GLU J 316     7444   5819   5705    105    261   -733       C  
ATOM   3112  C   GLU J 316      11.482   0.245 -12.438  1.00 46.63           C  
ANISOU 3112  C   GLU J 316     7093   5345   5278     45    221   -267       C  
ATOM   3113  O   GLU J 316      12.695   0.086 -12.461  1.00 48.77           O  
ANISOU 3113  O   GLU J 316     7430   5685   5414    -21    144   -174       O  
ATOM   3114  CB  GLU J 316      10.274   1.255 -10.506  1.00 54.75           C  
ANISOU 3114  CB  GLU J 316     7797   7067   5936    159    461   -812       C  
ATOM   3115  CG  GLU J 316       9.628   2.467  -9.872  1.00 60.66           C  
ANISOU 3115  CG  GLU J 316     8377   7957   6712    249    531  -1478       C  
ATOM   3116  CD  GLU J 316      10.410   2.981  -8.696  1.00 69.92           C  
ANISOU 3116  CD  GLU J 316     9350   9800   7416    218    548  -1980       C  
ATOM   3117  OE1 GLU J 316      10.178   2.478  -7.558  1.00 74.02           O  
ANISOU 3117  OE1 GLU J 316     9580  11245   7296    269    711  -1920       O  
ATOM   3118  OE2 GLU J 316      11.231   3.910  -8.915  1.00 74.76           O  
ANISOU 3118  OE2 GLU J 316    10017  10078   8309    142    403  -2430       O  
ATOM   3119  N   ILE J 317      10.623  -0.655 -12.900  1.00 45.76           N  
ANISOU 3119  N   ILE J 317     6899   5078   5410     71    273    -56       N  
ATOM   3120  CA  ILE J 317      11.097  -1.897 -13.502  1.00 46.43           C  
ANISOU 3120  CA  ILE J 317     6943   4981   5715     24    245    210       C  
ATOM   3121  C   ILE J 317      12.060  -1.576 -14.632  1.00 43.05           C  
ANISOU 3121  C   ILE J 317     6681   4394   5280      0     65     78       C  
ATOM   3122  O   ILE J 317      13.180  -2.091 -14.664  1.00 39.94           O  
ANISOU 3122  O   ILE J 317     6296   4030   4847    -33     37    201       O  
ATOM   3123  CB  ILE J 317       9.949  -2.778 -14.044  1.00 48.67           C  
ANISOU 3123  CB  ILE J 317     7024   5018   6447     23    296    227       C  
ATOM   3124  CG1 ILE J 317       9.161  -3.393 -12.875  1.00 53.26           C  
ANISOU 3124  CG1 ILE J 317     7345   5771   7119     13    538    568       C  
ATOM   3125  CG2 ILE J 317      10.526  -3.910 -14.891  1.00 51.88           C  
ANISOU 3125  CG2 ILE J 317     7324   5144   7242    -19    233    220       C  
ATOM   3126  CD1 ILE J 317       7.778  -3.932 -13.217  1.00 54.28           C  
ANISOU 3126  CD1 ILE J 317     7214   5676   7733    -16    619    516       C  
ATOM   3127  N   LEU J 318      11.635  -0.702 -15.542  1.00 42.20           N  
ANISOU 3127  N   LEU J 318     6643   4185   5204     40    -43    -90       N  
ATOM   3128  CA  LEU J 318      12.423  -0.444 -16.755  1.00 41.08           C  
ANISOU 3128  CA  LEU J 318     6556   4058   4994     31   -180    -80       C  
ATOM   3129  C   LEU J 318      13.692   0.352 -16.469  1.00 40.92           C  
ANISOU 3129  C   LEU J 318     6662   4049   4835    -48   -202    -10       C  
ATOM   3130  O   LEU J 318      14.718   0.140 -17.114  1.00 37.82           O  
ANISOU 3130  O   LEU J 318     6270   3756   4343    -92   -252     65       O  
ATOM   3131  CB  LEU J 318      11.576   0.204 -17.857  1.00 42.26           C  
ANISOU 3131  CB  LEU J 318     6628   4252   5175    130   -288    -77       C  
ATOM   3132  CG  LEU J 318      10.397  -0.631 -18.360  1.00 43.23           C  
ANISOU 3132  CG  LEU J 318     6533   4469   5420    190   -320   -263       C  
ATOM   3133  CD1 LEU J 318       9.447   0.210 -19.181  1.00 45.42           C  
ANISOU 3133  CD1 LEU J 318     6685   4905   5667    331   -443   -184       C  
ATOM   3134  CD2 LEU J 318      10.846  -1.834 -19.190  1.00 44.43           C  
ANISOU 3134  CD2 LEU J 318     6505   4797   5578    154   -374   -512       C  
ATOM   3135  N   LYS J 319      13.644   1.243 -15.488  1.00 45.39           N  
ANISOU 3135  N   LYS J 319     7264   4555   5425    -74   -157   -130       N  
ATOM   3136  CA  LYS J 319      14.832   2.027 -15.105  1.00 47.96           C  
ANISOU 3136  CA  LYS J 319     7616   4872   5732   -191   -188   -213       C  
ATOM   3137  C   LYS J 319      15.910   1.147 -14.442  1.00 48.24           C  
ANISOU 3137  C   LYS J 319     7626   5226   5476   -252   -183   -161       C  
ATOM   3138  O   LYS J 319      17.107   1.316 -14.699  1.00 47.91           O  
ANISOU 3138  O   LYS J 319     7579   5224   5400   -346   -242   -118       O  
ATOM   3139  CB  LYS J 319      14.432   3.159 -14.147  1.00 53.59           C  
ANISOU 3139  CB  LYS J 319     8254   5479   6629   -198   -147   -600       C  
ATOM   3140  CG  LYS J 319      15.583   4.042 -13.696  1.00 57.07           C  
ANISOU 3140  CG  LYS J 319     8612   5866   7204   -356   -191   -880       C  
ATOM   3141  CD  LYS J 319      15.131   5.082 -12.674  1.00 64.60           C  
ANISOU 3141  CD  LYS J 319     9375   6753   8415   -354   -146  -1529       C  
ATOM   3142  CE  LYS J 319      16.264   5.491 -11.736  1.00 68.86           C  
ANISOU 3142  CE  LYS J 319     9720   7600   8841   -519   -200  -2054       C  
ATOM   3143  NZ  LYS J 319      15.864   5.296 -10.315  1.00 74.12           N  
ANISOU 3143  NZ  LYS J 319    10175   9016   8969   -445   -143  -2594       N  
ATOM   3144  N   LYS J 320      15.497   0.225 -13.577  1.00 46.59           N  
ANISOU 3144  N   LYS J 320     7336   5267   5098   -187   -101    -72       N  
ATOM   3145  CA  LYS J 320      16.442  -0.752 -13.030  1.00 46.89           C  
ANISOU 3145  CA  LYS J 320     7267   5595   4954   -182    -96    186       C  
ATOM   3146  C   LYS J 320      17.102  -1.610 -14.139  1.00 43.68           C  
ANISOU 3146  C   LYS J 320     6863   4957   4775   -165   -137    348       C  
ATOM   3147  O   LYS J 320      18.315  -1.839 -14.134  1.00 45.16           O  
ANISOU 3147  O   LYS J 320     6991   5274   4891   -187   -188    432       O  
ATOM   3148  CB  LYS J 320      15.743  -1.629 -12.001  1.00 50.28           C  
ANISOU 3148  CB  LYS J 320     7514   6312   5276    -91     38    485       C  
ATOM   3149  CG  LYS J 320      16.638  -2.692 -11.409  1.00 55.69           C  
ANISOU 3149  CG  LYS J 320     7995   7278   5886    -32     55    972       C  
ATOM   3150  CD  LYS J 320      16.096  -3.212 -10.084  1.00 63.78           C  
ANISOU 3150  CD  LYS J 320     8735   8866   6629     56    204   1425       C  
ATOM   3151  CE  LYS J 320      14.662  -3.692 -10.223  1.00 66.07           C  
ANISOU 3151  CE  LYS J 320     8969   8848   7286     75    375   1580       C  
ATOM   3152  NZ  LYS J 320      14.176  -4.433  -9.023  1.00 73.53           N  
ANISOU 3152  NZ  LYS J 320     9539  10336   8061    159    580   2272       N  
ATOM   3153  N   LEU J 321      16.337  -2.044 -15.127  1.00 41.23           N  
ANISOU 3153  N   LEU J 321     6554   4384   4724   -120   -124    287       N  
ATOM   3154  CA  LEU J 321      16.953  -2.834 -16.224  1.00 40.31           C  
ANISOU 3154  CA  LEU J 321     6339   4185   4790    -89   -159    214       C  
ATOM   3155  C   LEU J 321      17.981  -1.982 -16.977  1.00 39.78           C  
ANISOU 3155  C   LEU J 321     6340   4292   4479   -158   -236    155       C  
ATOM   3156  O   LEU J 321      19.134  -2.395 -17.201  1.00 39.34           O  
ANISOU 3156  O   LEU J 321     6186   4350   4409   -158   -244    169       O  
ATOM   3157  CB  LEU J 321      15.894  -3.413 -17.178  1.00 38.38           C  
ANISOU 3157  CB  LEU J 321     5974   3796   4811    -36   -159    -30       C  
ATOM   3158  CG  LEU J 321      14.889  -4.405 -16.571  1.00 38.78           C  
ANISOU 3158  CG  LEU J 321     5851   3569   5312     -9    -52     43       C  
ATOM   3159  CD1 LEU J 321      13.880  -4.804 -17.619  1.00 39.20           C  
ANISOU 3159  CD1 LEU J 321     5725   3537   5631      5    -96   -368       C  
ATOM   3160  CD2 LEU J 321      15.529  -5.649 -15.962  1.00 40.94           C  
ANISOU 3160  CD2 LEU J 321     5895   3612   6047     32     43    317       C  
ATOM   3161  N   ASN J 322      17.549  -0.781 -17.331  1.00 39.93           N  
ANISOU 3161  N   ASN J 322     6469   4303   4399   -208   -270    158       N  
ATOM   3162  CA  ASN J 322      18.343   0.159 -18.101  1.00 41.72           C  
ANISOU 3162  CA  ASN J 322     6686   4638   4526   -291   -303    280       C  
ATOM   3163  C   ASN J 322      19.641   0.538 -17.417  1.00 41.91           C  
ANISOU 3163  C   ASN J 322     6696   4692   4534   -425   -308    308       C  
ATOM   3164  O   ASN J 322      20.699   0.450 -18.021  1.00 42.88           O  
ANISOU 3164  O   ASN J 322     6711   5005   4574   -473   -303    392       O  
ATOM   3165  CB  ASN J 322      17.511   1.419 -18.353  1.00 42.65           C  
ANISOU 3165  CB  ASN J 322     6847   4571   4784   -299   -318    416       C  
ATOM   3166  CG  ASN J 322      18.119   2.321 -19.395  1.00 44.35           C  
ANISOU 3166  CG  ASN J 322     6946   4892   5012   -359   -318    779       C  
ATOM   3167  OD1 ASN J 322      18.594   1.865 -20.434  1.00 45.05           O  
ANISOU 3167  OD1 ASN J 322     6891   5423   4801   -320   -313    900       O  
ATOM   3168  ND2 ASN J 322      18.084   3.618 -19.135  1.00 47.58           N  
ANISOU 3168  ND2 ASN J 322     7335   4915   5827   -446   -303    957       N  
ATOM   3169  N   ASP J 323      19.537   0.981 -16.168  1.00 44.44           N  
ANISOU 3169  N   ASP J 323     7059   4932   4893   -482   -320    171       N  
ATOM   3170  CA  ASP J 323      20.702   1.248 -15.303  1.00 50.02           C  
ANISOU 3170  CA  ASP J 323     7664   5820   5521   -605   -366     60       C  
ATOM   3171  C   ASP J 323      21.637   0.059 -15.229  1.00 47.56           C  
ANISOU 3171  C   ASP J 323     7242   5784   5045   -529   -380    208       C  
ATOM   3172  O   ASP J 323      22.853   0.193 -15.360  1.00 47.79           O  
ANISOU 3172  O   ASP J 323     7143   5967   5046   -618   -418    224       O  
ATOM   3173  CB  ASP J 323      20.264   1.611 -13.875  1.00 53.90           C  
ANISOU 3173  CB  ASP J 323     8110   6469   5897   -614   -383   -236       C  
ATOM   3174  CG  ASP J 323      19.749   3.059 -13.759  1.00 61.56           C  
ANISOU 3174  CG  ASP J 323     9063   7101   7222   -720   -378   -586       C  
ATOM   3175  OD1 ASP J 323      19.698   3.773 -14.803  1.00 62.77           O  
ANISOU 3175  OD1 ASP J 323     9246   6826   7776   -778   -358   -399       O  
ATOM   3176  OD2 ASP J 323      19.398   3.477 -12.622  1.00 65.15           O  
ANISOU 3176  OD2 ASP J 323     9401   7764   7588   -724   -383  -1033       O  
ATOM   3177  N   SER J 324      21.059  -1.108 -15.032  1.00 44.11           N  
ANISOU 3177  N   SER J 324     6789   5345   4622   -361   -336    339       N  
ATOM   3178  CA  SER J 324      21.839  -2.315 -15.012  1.00 47.11           C  
ANISOU 3178  CA  SER J 324     6989   5816   5093   -240   -329    523       C  
ATOM   3179  C   SER J 324      22.579  -2.511 -16.345  1.00 45.88           C  
ANISOU 3179  C   SER J 324     6757   5636   5039   -238   -314    405       C  
ATOM   3180  O   SER J 324      23.796  -2.727 -16.373  1.00 46.91           O  
ANISOU 3180  O   SER J 324     6719   5950   5155   -234   -336    445       O  
ATOM   3181  CB  SER J 324      20.933  -3.501 -14.724  1.00 47.46           C  
ANISOU 3181  CB  SER J 324     6953   5658   5418    -80   -247    715       C  
ATOM   3182  OG  SER J 324      21.731  -4.623 -14.580  1.00 56.31           O  
ANISOU 3182  OG  SER J 324     7820   6748   6827     58   -231    958       O  
ATOM   3183  N   LEU J 325      21.850  -2.419 -17.449  1.00 43.37           N  
ANISOU 3183  N   LEU J 325     6495   5229   4752   -224   -276    248       N  
ATOM   3184  CA  LEU J 325      22.456  -2.616 -18.765  1.00 44.20           C  
ANISOU 3184  CA  LEU J 325     6432   5573   4787   -194   -242     89       C  
ATOM   3185  C   LEU J 325      23.592  -1.607 -19.019  1.00 45.76           C  
ANISOU 3185  C   LEU J 325     6587   6029   4769   -358   -240    258       C  
ATOM   3186  O   LEU J 325      24.605  -1.940 -19.643  1.00 46.35           O  
ANISOU 3186  O   LEU J 325     6437   6400   4771   -332   -192    197       O  
ATOM   3187  CB  LEU J 325      21.390  -2.555 -19.862  1.00 44.17           C  
ANISOU 3187  CB  LEU J 325     6415   5686   4681   -143   -233    -91       C  
ATOM   3188  CG  LEU J 325      20.534  -3.811 -20.028  1.00 45.07           C  
ANISOU 3188  CG  LEU J 325     6384   5607   5132      1   -221   -458       C  
ATOM   3189  CD1 LEU J 325      19.346  -3.522 -20.928  1.00 44.27           C  
ANISOU 3189  CD1 LEU J 325     6252   5725   4841     26   -264   -647       C  
ATOM   3190  CD2 LEU J 325      21.313  -5.008 -20.591  1.00 47.54           C  
ANISOU 3190  CD2 LEU J 325     6344   5993   5726    131   -172   -876       C  
ATOM   3191  N   GLU J 326      23.441  -0.395 -18.488  1.00 47.22           N  
ANISOU 3191  N   GLU J 326     6918   6064   4960   -531   -276    421       N  
ATOM   3192  CA  GLU J 326      24.450   0.633 -18.652  1.00 51.38           C  
ANISOU 3192  CA  GLU J 326     7331   6675   5516   -739   -260    584       C  
ATOM   3193  C   GLU J 326      25.674   0.376 -17.778  1.00 54.78           C  
ANISOU 3193  C   GLU J 326     7616   7237   5960   -802   -320    488       C  
ATOM   3194  O   GLU J 326      26.778   0.799 -18.113  1.00 58.81           O  
ANISOU 3194  O   GLU J 326     7921   7922   6501   -948   -289    575       O  
ATOM   3195  CB  GLU J 326      23.864   2.010 -18.372  1.00 53.87           C  
ANISOU 3195  CB  GLU J 326     7741   6629   6097   -903   -272    683       C  
ATOM   3196  CG  GLU J 326      22.904   2.458 -19.460  1.00 57.41           C  
ANISOU 3196  CG  GLU J 326     8214   7049   6550   -833   -216    982       C  
ATOM   3197  CD  GLU J 326      22.501   3.913 -19.353  1.00 63.17           C  
ANISOU 3197  CD  GLU J 326     8920   7304   7777   -975   -199   1212       C  
ATOM   3198  OE1 GLU J 326      22.813   4.552 -18.321  1.00 64.86           O  
ANISOU 3198  OE1 GLU J 326     9115   7157   8371  -1139   -238    919       O  
ATOM   3199  OE2 GLU J 326      21.861   4.419 -20.311  1.00 67.35           O  
ANISOU 3199  OE2 GLU J 326     9374   7854   8362   -904   -152   1664       O  
ATOM   3200  N   LEU J 327      25.499  -0.322 -16.664  1.00 51.44           N  
ANISOU 3200  N   LEU J 327     7228   6818   5498   -684   -400    388       N  
ATOM   3201  CA  LEU J 327      26.628  -0.637 -15.848  1.00 49.83           C  
ANISOU 3201  CA  LEU J 327     6806   6898   5226   -687   -487    385       C  
ATOM   3202  C   LEU J 327      27.516  -1.665 -16.533  1.00 50.15           C  
ANISOU 3202  C   LEU J 327     6627   7097   5331   -525   -433    461       C  
ATOM   3203  O   LEU J 327      28.738  -1.496 -16.571  1.00 50.99           O  
ANISOU 3203  O   LEU J 327     6491   7460   5420   -605   -456    466       O  
ATOM   3204  CB  LEU J 327      26.176  -1.135 -14.478  1.00 51.27           C  
ANISOU 3204  CB  LEU J 327     6984   7234   5260   -558   -575    431       C  
ATOM   3205  CG  LEU J 327      27.316  -1.407 -13.512  1.00 53.19           C  
ANISOU 3205  CG  LEU J 327     6914   7982   5313   -526   -709    509       C  
ATOM   3206  CD1 LEU J 327      28.084  -0.133 -13.204  1.00 55.48           C  
ANISOU 3206  CD1 LEU J 327     7060   8482   5537   -824   -812    142       C  
ATOM   3207  CD2 LEU J 327      26.734  -2.036 -12.264  1.00 55.59           C  
ANISOU 3207  CD2 LEU J 327     7138   8617   5367   -338   -758    763       C  
ATOM   3208  N   SER J 328      26.935  -2.729 -17.077  1.00 49.76           N  
ANISOU 3208  N   SER J 328     6584   6883   5437   -300   -356    431       N  
ATOM   3209  CA  SER J 328      27.762  -3.759 -17.719  1.00 54.42           C  
ANISOU 3209  CA  SER J 328     6871   7571   6234   -110   -290    325       C  
ATOM   3210  C   SER J 328      28.546  -3.233 -18.936  1.00 57.15           C  
ANISOU 3210  C   SER J 328     7056   8283   6374   -221   -188    181       C  
ATOM   3211  O   SER J 328      29.626  -3.745 -19.208  1.00 61.02           O  
ANISOU 3211  O   SER J 328     7227   9005   6952   -123   -145     90       O  
ATOM   3212  CB  SER J 328      26.942  -4.999 -18.080  1.00 56.09           C  
ANISOU 3212  CB  SER J 328     7015   7443   6851    130   -220    141       C  
ATOM   3213  OG  SER J 328      25.634  -4.621 -18.448  1.00 57.69           O  
ANISOU 3213  OG  SER J 328     7472   7507   6937     56   -202     28       O  
ATOM   3214  N   ASP J 329      28.028  -2.199 -19.611  1.00 56.28           N  
ANISOU 3214  N   ASP J 329     7101   8265   6016   -407   -138    256       N  
ATOM   3215  CA  ASP J 329      28.756  -1.464 -20.686  1.00 60.31           C  
ANISOU 3215  CA  ASP J 329     7399   9229   6287   -555    -10    387       C  
ATOM   3216  C   ASP J 329      30.103  -0.890 -20.247  1.00 61.95           C  
ANISOU 3216  C   ASP J 329     7397   9562   6578   -757    -20    554       C  
ATOM   3217  O   ASP J 329      31.031  -0.778 -21.045  1.00 61.64           O  
ANISOU 3217  O   ASP J 329     7035   9972   6411   -809    115    628       O  
ATOM   3218  CB  ASP J 329      27.954  -0.245 -21.181  1.00 59.93           C  
ANISOU 3218  CB  ASP J 329     7511   9136   6124   -736     26    722       C  
ATOM   3219  CG  ASP J 329      26.791  -0.614 -22.063  1.00 61.64           C  
ANISOU 3219  CG  ASP J 329     7779   9542   6099   -558     56    609       C  
ATOM   3220  OD1 ASP J 329      26.900  -1.631 -22.775  1.00 66.96           O  
ANISOU 3220  OD1 ASP J 329     8222  10621   6597   -353    111    208       O  
ATOM   3221  OD2 ASP J 329      25.782   0.137 -22.061  1.00 59.26           O  
ANISOU 3221  OD2 ASP J 329     7679   9009   5827   -618     18    852       O  
ATOM   3222  N   VAL J 330      30.182  -0.497 -18.981  1.00 61.14           N  
ANISOU 3222  N   VAL J 330     7412   9167   6652   -880   -179    569       N  
ATOM   3223  CA  VAL J 330      31.257   0.368 -18.508  1.00 62.84           C  
ANISOU 3223  CA  VAL J 330     7402   9468   7003  -1161   -226    629       C  
ATOM   3224  C   VAL J 330      32.264  -0.366 -17.609  1.00 63.89           C  
ANISOU 3224  C   VAL J 330     7287   9856   7133  -1043   -369    495       C  
ATOM   3225  O   VAL J 330      33.378   0.128 -17.365  1.00 68.61           O  
ANISOU 3225  O   VAL J 330     7571  10681   7817  -1244   -413    471       O  
ATOM   3226  CB  VAL J 330      30.626   1.604 -17.846  1.00 63.54           C  
ANISOU 3226  CB  VAL J 330     7665   9149   7327  -1425   -307    598       C  
ATOM   3227  CG1 VAL J 330      31.672   2.500 -17.236  1.00 70.54           C  
ANISOU 3227  CG1 VAL J 330     8238  10055   8509  -1749   -386    456       C  
ATOM   3228  CG2 VAL J 330      29.857   2.400 -18.882  1.00 63.78           C  
ANISOU 3228  CG2 VAL J 330     7804   8947   7481  -1520   -150    920       C  
ATOM   3229  N   VAL J 331      31.906  -1.566 -17.162  1.00 61.79           N  
ANISOU 3229  N   VAL J 331     7078   9558   6841   -711   -433    473       N  
ATOM   3230  CA  VAL J 331      32.821  -2.402 -16.398  1.00 63.70           C  
ANISOU 3230  CA  VAL J 331     7003  10061   7137   -509   -557    538       C  
ATOM   3231  C   VAL J 331      33.592  -3.307 -17.364  1.00 65.92           C  
ANISOU 3231  C   VAL J 331     6973  10466   7606   -282   -408    471       C  
ATOM   3232  O   VAL J 331      32.977  -4.096 -18.076  1.00 65.94           O  
ANISOU 3232  O   VAL J 331     7035  10251   7767    -63   -281    328       O  
ATOM   3233  CB  VAL J 331      32.065  -3.289 -15.375  1.00 61.54           C  
ANISOU 3233  CB  VAL J 331     6827   9660   6894   -233   -669    742       C  
ATOM   3234  CG1 VAL J 331      33.047  -4.081 -14.516  1.00 64.46           C  
ANISOU 3234  CG1 VAL J 331     6775  10390   7326      7   -815   1023       C  
ATOM   3235  CG2 VAL J 331      31.145  -2.449 -14.493  1.00 59.91           C  
ANISOU 3235  CG2 VAL J 331     6893   9447   6420   -417   -771    696       C  
ATOM   3236  N   PRO J 332      34.932  -3.199 -17.393  1.00 61.00           N  
ANISOU 3236  N   PRO J 332     7099   9181   6894    853   1439     36       N  
ATOM   3237  CA  PRO J 332      35.763  -4.172 -18.120  1.00 64.93           C  
ANISOU 3237  CA  PRO J 332     7626   9633   7409    910   1909   -216       C  
ATOM   3238  C   PRO J 332      35.472  -5.621 -17.691  1.00 67.50           C  
ANISOU 3238  C   PRO J 332     7946   9720   7979   1110   1871   -404       C  
ATOM   3239  O   PRO J 332      35.116  -5.877 -16.514  1.00 66.02           O  
ANISOU 3239  O   PRO J 332     7495   9474   8113   1222   1571   -258       O  
ATOM   3240  CB  PRO J 332      37.189  -3.793 -17.711  1.00 66.35           C  
ANISOU 3240  CB  PRO J 332     7278   9930   8002    963   2207    -64       C  
ATOM   3241  CG  PRO J 332      37.127  -2.361 -17.325  1.00 64.27           C  
ANISOU 3241  CG  PRO J 332     7026   9737   7656    699   1883    200       C  
ATOM   3242  CD  PRO J 332      35.727  -2.076 -16.858  1.00 60.88           C  
ANISOU 3242  CD  PRO J 332     6923   9202   7007    764   1426    232       C  
ATOM   3243  N   ALA J 333      35.635  -6.562 -18.619  1.00 71.20           N  
ANISOU 3243  N   ALA J 333     8846   9973   8232   1148   2214   -722       N  
ATOM   3244  CA  ALA J 333      35.223  -7.952 -18.379  1.00 73.30           C  
ANISOU 3244  CA  ALA J 333     9357   9844   8648   1242   2126   -926       C  
ATOM   3245  C   ALA J 333      35.990  -8.651 -17.255  1.00 71.61           C  
ANISOU 3245  C   ALA J 333     8649   9468   9091   1662   2259   -811       C  
ATOM   3246  O   ALA J 333      35.425  -9.494 -16.563  1.00 72.37           O  
ANISOU 3246  O   ALA J 333     8815   9284   9397   1673   1979   -771       O  
ATOM   3247  CB  ALA J 333      35.320  -8.769 -19.658  1.00 79.53           C  
ANISOU 3247  CB  ALA J 333    10995  10279   8944   1200   2498  -1366       C  
ATOM   3248  N   SER J 334      37.256  -8.305 -17.061  1.00 71.47           N  
ANISOU 3248  N   SER J 334     8095   9630   9428   1958   2623   -670       N  
ATOM   3249  CA  SER J 334      38.046  -8.957 -16.025  1.00 74.90           C  
ANISOU 3249  CA  SER J 334     7998   9939  10520   2370   2603   -454       C  
ATOM   3250  C   SER J 334      37.506  -8.460 -14.704  1.00 69.10           C  
ANISOU 3250  C   SER J 334     7053   9348   9850   2174   1926   -140       C  
ATOM   3251  O   SER J 334      37.321  -9.235 -13.761  1.00 69.58           O  
ANISOU 3251  O   SER J 334     7121   9168  10146   2336   1668      3       O  
ATOM   3252  CB  SER J 334      39.547  -8.642 -16.139  1.00 79.11           C  
ANISOU 3252  CB  SER J 334     7791  10722  11544   2671   3050   -238       C  
ATOM   3253  OG  SER J 334      39.886  -7.501 -15.360  1.00 75.73           O  
ANISOU 3253  OG  SER J 334     6810  10684  11278   2364   2556    135       O  
ATOM   3254  N   ASP J 335      37.247  -7.158 -14.654  1.00 66.10           N  
ANISOU 3254  N   ASP J 335     6627   9291   9195   1850   1702    -30       N  
ATOM   3255  CA  ASP J 335      36.652  -6.549 -13.481  1.00 61.70           C  
ANISOU 3255  CA  ASP J 335     6112   8799   8532   1718   1211    196       C  
ATOM   3256  C   ASP J 335      35.330  -7.238 -13.178  1.00 59.93           C  
ANISOU 3256  C   ASP J 335     6216   8390   8166   1696   1101    177       C  
ATOM   3257  O   ASP J 335      35.128  -7.686 -12.047  1.00 62.93           O  
ANISOU 3257  O   ASP J 335     6617   8642   8649   1801    911    378       O  
ATOM   3258  CB  ASP J 335      36.504  -5.033 -13.658  1.00 60.88           C  
ANISOU 3258  CB  ASP J 335     6111   8909   8113   1438   1094    259       C  
ATOM   3259  CG  ASP J 335      37.861  -4.292 -13.645  1.00 63.56           C  
ANISOU 3259  CG  ASP J 335     6057   9406   8687   1285   1068    416       C  
ATOM   3260  OD1 ASP J 335      38.915  -4.952 -13.813  1.00 64.84           O  
ANISOU 3260  OD1 ASP J 335     5704   9621   9309   1455   1282    483       O  
ATOM   3261  OD2 ASP J 335      37.867  -3.046 -13.460  1.00 61.82           O  
ANISOU 3261  OD2 ASP J 335     6021   9218   8248    992    839    518       O  
ATOM   3262  N   ALA J 336      34.456  -7.386 -14.177  1.00 58.81           N  
ANISOU 3262  N   ALA J 336     6326   8228   7790   1504   1182      1       N  
ATOM   3263  CA  ALA J 336      33.171  -8.097 -13.981  1.00 58.77           C  
ANISOU 3263  CA  ALA J 336     6466   8078   7784   1338   1009     79       C  
ATOM   3264  C   ALA J 336      33.295  -9.513 -13.380  1.00 63.88           C  
ANISOU 3264  C   ALA J 336     7214   8320   8735   1441   1027    104       C  
ATOM   3265  O   ALA J 336      32.540  -9.872 -12.464  1.00 64.84           O  
ANISOU 3265  O   ALA J 336     7304   8374   8957   1369    909    388       O  
ATOM   3266  CB  ALA J 336      32.397  -8.172 -15.278  1.00 59.67           C  
ANISOU 3266  CB  ALA J 336     6842   8200   7628    999    902    -90       C  
ATOM   3267  N   GLU J 337      34.223 -10.326 -13.899  1.00 68.31           N  
ANISOU 3267  N   GLU J 337     7940   8566   9448   1654   1259   -146       N  
ATOM   3268  CA  GLU J 337      34.349 -11.703 -13.434  1.00 71.59           C  
ANISOU 3268  CA  GLU J 337     8582   8445  10171   1818   1282   -115       C  
ATOM   3269  C   GLU J 337      34.834 -11.650 -11.989  1.00 71.01           C  
ANISOU 3269  C   GLU J 337     8194   8439  10347   2100   1111    293       C  
ATOM   3270  O   GLU J 337      34.308 -12.355 -11.129  1.00 75.24           O  
ANISOU 3270  O   GLU J 337     8905   8711  10970   2041    964    559       O  
ATOM   3271  CB  GLU J 337      35.285 -12.546 -14.340  1.00 78.81           C  
ANISOU 3271  CB  GLU J 337     9823   8914  11206   2167   1706   -482       C  
ATOM   3272  CG  GLU J 337      35.019 -14.061 -14.324  1.00 85.38           C  
ANISOU 3272  CG  GLU J 337    11283   8950  12206   2200   1729   -597       C  
ATOM   3273  CD  GLU J 337      35.582 -14.807 -15.545  1.00 95.12           C  
ANISOU 3273  CD  GLU J 337    13217   9617  13305   2471   2247  -1124       C  
ATOM   3274  OE1 GLU J 337      35.382 -14.326 -16.682  1.00 98.58           O  
ANISOU 3274  OE1 GLU J 337    14014  10222  13220   2196   2390  -1480       O  
ATOM   3275  OE2 GLU J 337      36.221 -15.879 -15.387  1.00 97.96           O  
ANISOU 3275  OE2 GLU J 337    13889   9305  14025   3005   2553  -1177       O  
ATOM   3276  N   LYS J 338      35.806 -10.784 -11.718  1.00 67.82           N  
ANISOU 3276  N   LYS J 338     7388   8378  10001   2309   1071    390       N  
ATOM   3277  CA  LYS J 338      36.341 -10.628 -10.376  1.00 68.73           C  
ANISOU 3277  CA  LYS J 338     7324   8562  10225   2471    718    780       C  
ATOM   3278  C   LYS J 338      35.226 -10.372  -9.357  1.00 67.78           C  
ANISOU 3278  C   LYS J 338     7535   8492   9726   2235    544   1016       C  
ATOM   3279  O   LYS J 338      35.221 -10.976  -8.262  1.00 68.33           O  
ANISOU 3279  O   LYS J 338     7824   8346   9793   2337    353   1345       O  
ATOM   3280  CB  LYS J 338      37.351  -9.479 -10.350  1.00 69.35           C  
ANISOU 3280  CB  LYS J 338     6967   9040  10339   2463    555    846       C  
ATOM   3281  CG  LYS J 338      37.760  -9.010  -8.956  1.00 71.85           C  
ANISOU 3281  CG  LYS J 338     7303   9454  10541   2411    -26   1220       C  
ATOM   3282  CD  LYS J 338      39.047  -8.185  -9.005  1.00 75.48           C  
ANISOU 3282  CD  LYS J 338     7205  10207  11267   2320   -330   1361       C  
ATOM   3283  CE  LYS J 338      39.646  -7.953  -7.620  1.00 79.66           C  
ANISOU 3283  CE  LYS J 338     7811  10747  11709   2204  -1140   1775       C  
ATOM   3284  NZ  LYS J 338      41.125  -7.815  -7.674  1.00 86.41           N  
ANISOU 3284  NZ  LYS J 338     7782  11827  13223   2205  -1545   2109       N  
ATOM   3285  N   TYR J 339      34.296  -9.484  -9.729  1.00 62.62           N  
ANISOU 3285  N   TYR J 339     6927   8109   8757   1981    670    905       N  
ATOM   3286  CA  TYR J 339      33.182  -9.093  -8.864  1.00 62.96           C  
ANISOU 3286  CA  TYR J 339     7185   8250   8487   1881    734   1152       C  
ATOM   3287  C   TYR J 339      32.194 -10.224  -8.610  1.00 68.36           C  
ANISOU 3287  C   TYR J 339     7958   8692   9321   1729    884   1375       C  
ATOM   3288  O   TYR J 339      31.671 -10.351  -7.498  1.00 68.90           O  
ANISOU 3288  O   TYR J 339     8244   8727   9206   1751   1005   1729       O  
ATOM   3289  CB  TYR J 339      32.406  -7.906  -9.451  1.00 59.82           C  
ANISOU 3289  CB  TYR J 339     6693   8161   7874   1778    883   1052       C  
ATOM   3290  CG  TYR J 339      32.975  -6.546  -9.146  1.00 57.31           C  
ANISOU 3290  CG  TYR J 339     6543   7985   7246   1866    776    991       C  
ATOM   3291  CD1 TYR J 339      33.162  -6.120  -7.832  1.00 59.29           C  
ANISOU 3291  CD1 TYR J 339     7248   8147   7132   1975    675   1154       C  
ATOM   3292  CD2 TYR J 339      33.308  -5.669 -10.173  1.00 55.63           C  
ANISOU 3292  CD2 TYR J 339     6199   7921   7018   1769    751    780       C  
ATOM   3293  CE1 TYR J 339      33.690  -4.867  -7.547  1.00 58.89           C  
ANISOU 3293  CE1 TYR J 339     7547   8089   6739   1937    474   1059       C  
ATOM   3294  CE2 TYR J 339      33.816  -4.412  -9.900  1.00 55.57           C  
ANISOU 3294  CE2 TYR J 339     6434   7931   6748   1740    612    752       C  
ATOM   3295  CZ  TYR J 339      34.008  -4.019  -8.587  1.00 57.48           C  
ANISOU 3295  CZ  TYR J 339     7158   8019   6660   1800    439    867       C  
ATOM   3296  OH  TYR J 339      34.505  -2.772  -8.333  1.00 58.82           O  
ANISOU 3296  OH  TYR J 339     7749   8079   6521   1661    212    799       O  
ATOM   3297  N   ARG J 340      31.908 -11.014  -9.640  1.00 72.25           N  
ANISOU 3297  N   ARG J 340     8382   8983  10085   1509    893   1185       N  
ATOM   3298  CA  ARG J 340      31.031 -12.179  -9.488  1.00 81.85           C  
ANISOU 3298  CA  ARG J 340     9724   9860  11516   1193    923   1409       C  
ATOM   3299  C   ARG J 340      31.588 -13.196  -8.493  1.00 90.03           C  
ANISOU 3299  C   ARG J 340    11102  10437  12668   1386    884   1671       C  
ATOM   3300  O   ARG J 340      30.845 -13.804  -7.719  1.00 90.89           O  
ANISOU 3300  O   ARG J 340    11361  10368  12804   1171    989   2088       O  
ATOM   3301  CB  ARG J 340      30.817 -12.863 -10.844  1.00 84.19           C  
ANISOU 3301  CB  ARG J 340    10150   9865  11970    849    794   1058       C  
ATOM   3302  CG  ARG J 340      29.979 -12.017 -11.793  1.00 81.30           C  
ANISOU 3302  CG  ARG J 340     9497   9928  11465    526    678    963       C  
ATOM   3303  CD  ARG J 340      30.100 -12.456 -13.240  1.00 82.78           C  
ANISOU 3303  CD  ARG J 340    10066   9845  11538    235    477    503       C  
ATOM   3304  NE  ARG J 340      29.437 -11.487 -14.114  1.00 82.01           N  
ANISOU 3304  NE  ARG J 340     9730  10209  11218    -14    255    486       N  
ATOM   3305  CZ  ARG J 340      28.124 -11.432 -14.353  1.00 81.88           C  
ANISOU 3305  CZ  ARG J 340     9369  10403  11337   -526   -101    817       C  
ATOM   3306  NH1 ARG J 340      27.281 -12.304 -13.808  1.00 86.52           N  
ANISOU 3306  NH1 ARG J 340     9773  10800  12299   -953   -223   1190       N  
ATOM   3307  NH2 ARG J 340      27.652 -10.495 -15.153  1.00 79.15           N  
ANISOU 3307  NH2 ARG J 340     8801  10466  10803   -634   -366    862       N  
ATOM   3308  N   GLN J 341      32.907 -13.338  -8.501  1.00 59.02           N  
ATOM   3309  CA  GLN J 341      33.574 -14.479  -7.878  1.00 69.27           C  
ATOM   3310  C   GLN J 341      33.745 -14.341  -6.366  1.00 66.40           C  
ATOM   3311  O   GLN J 341      33.499 -13.273  -5.802  1.00 81.56           O  
ATOM   3312  CB  GLN J 341      34.921 -14.701  -8.571  1.00 71.87           C  
ATOM   3313  CG  GLN J 341      34.775 -15.251  -9.984  1.00 74.32           C  
ATOM   3314  CD  GLN J 341      34.436 -16.726  -9.996  1.00 77.55           C  
ATOM   3315  OE1 GLN J 341      34.394 -17.368  -8.946  1.00 80.38           O  
ATOM   3316  NE2 GLN J 341      34.202 -17.275 -11.183  1.00 77.62           N  
TER    3317      GLN J 341                                                      
ATOM   3318  N   GLU K 302      23.239 -19.481  -2.480  1.00 92.68           N  
ANISOU 3318  N   GLU K 302    12409  12612  10190    175  -1581   -232       N  
ATOM   3319  CA  GLU K 302      21.869 -18.892  -2.520  1.00 89.96           C  
ANISOU 3319  CA  GLU K 302    12488  11737   9953     17  -1295   -200       C  
ATOM   3320  C   GLU K 302      20.913 -19.873  -3.192  1.00 83.59           C  
ANISOU 3320  C   GLU K 302    11709  10800   9249    226   -948   -147       C  
ATOM   3321  O   GLU K 302      21.366 -20.859  -3.780  1.00 84.53           O  
ANISOU 3321  O   GLU K 302    11660  11087   9371    465   -974   -135       O  
ATOM   3322  CB  GLU K 302      21.893 -17.545  -3.256  1.00 92.06           C  
ANISOU 3322  CB  GLU K 302    12692  11978  10308   -456  -1361   -171       C  
ATOM   3323  CG  GLU K 302      20.644 -16.692  -3.055  1.00 91.73           C  
ANISOU 3323  CG  GLU K 302    13212  11445  10195   -386  -1239   -231       C  
ATOM   3324  CD  GLU K 302      20.959 -15.253  -2.699  1.00 96.02           C  
ANISOU 3324  CD  GLU K 302    14314  11666  10503   -719  -1645   -271       C  
ATOM   3325  OE1 GLU K 302      21.626 -15.044  -1.663  1.00 97.67           O  
ANISOU 3325  OE1 GLU K 302    14774  11829  10505   -832  -1977   -298       O  
ATOM   3326  OE2 GLU K 302      20.542 -14.337  -3.447  1.00 98.08           O  
ANISOU 3326  OE2 GLU K 302    14901  11646  10717   -869  -1703   -279       O  
ATOM   3327  N   GLU K 303      19.605 -19.633  -3.059  1.00 78.91           N  
ANISOU 3327  N   GLU K 303    11360   9981   8638    179   -676   -127       N  
ATOM   3328  CA  GLU K 303      18.599 -20.415  -3.785  1.00 76.09           C  
ANISOU 3328  CA  GLU K 303    10958   9612   8339    156   -383    -40       C  
ATOM   3329  C   GLU K 303      18.679 -20.134  -5.290  1.00 71.15           C  
ANISOU 3329  C   GLU K 303     9958   9081   7995     76   -320    -35       C  
ATOM   3330  O   GLU K 303      18.435 -19.017  -5.751  1.00 65.66           O  
ANISOU 3330  O   GLU K 303     9175   8377   7393    -27   -296    -83       O  
ATOM   3331  CB  GLU K 303      17.176 -20.133  -3.271  1.00 80.04           C  
ANISOU 3331  CB  GLU K 303    11574  10193   8645    110   -101    -26       C  
ATOM   3332  CG  GLU K 303      16.630 -21.171  -2.288  1.00 87.25           C  
ANISOU 3332  CG  GLU K 303    12808  11141   9200    -17      8    102       C  
ATOM   3333  CD  GLU K 303      15.720 -22.222  -2.927  1.00 90.81           C  
ANISOU 3333  CD  GLU K 303    13248  11691   9562   -393    191    289       C  
ATOM   3334  OE1 GLU K 303      14.839 -21.846  -3.733  1.00 92.51           O  
ANISOU 3334  OE1 GLU K 303    13052  12216   9879   -491    402    285       O  
ATOM   3335  OE2 GLU K 303      15.862 -23.427  -2.597  1.00 94.22           O  
ANISOU 3335  OE2 GLU K 303    14195  11861   9741   -615     60    442       O  
ATOM   3336  N   ILE K 304      19.037 -21.169  -6.040  1.00 68.75           N  
ANISOU 3336  N   ILE K 304     9585   8807   7731    190   -344     10       N  
ATOM   3337  CA  ILE K 304      19.043 -21.133  -7.492  1.00 66.09           C  
ANISOU 3337  CA  ILE K 304     8952   8570   7590    171   -258     24       C  
ATOM   3338  C   ILE K 304      17.643 -21.478  -8.020  1.00 61.80           C  
ANISOU 3338  C   ILE K 304     8523   7873   7085     12    -37     93       C  
ATOM   3339  O   ILE K 304      17.058 -22.459  -7.586  1.00 64.01           O  
ANISOU 3339  O   ILE K 304     9144   8012   7166    -88    -28    183       O  
ATOM   3340  CB  ILE K 304      20.106 -22.130  -8.021  1.00 70.24           C  
ANISOU 3340  CB  ILE K 304     9412   9275   7998    557   -436     -5       C  
ATOM   3341  CG1 ILE K 304      21.506 -21.677  -7.546  1.00 72.50           C  
ANISOU 3341  CG1 ILE K 304     9312  10055   8178    676   -655    -79       C  
ATOM   3342  CG2 ILE K 304      20.001 -22.292  -9.540  1.00 69.52           C  
ANISOU 3342  CG2 ILE K 304     9118   9273   8023    619   -326      8       C  
ATOM   3343  CD1 ILE K 304      22.677 -22.416  -8.173  1.00 76.56           C  
ANISOU 3343  CD1 ILE K 304     9483  11140   8463   1229   -817   -167       C  
ATOM   3344  N   PHE K 305      17.088 -20.658  -8.916  1.00 56.37           N  
ANISOU 3344  N   PHE K 305     7597   7249   6572    -80     92     67       N  
ATOM   3345  CA  PHE K 305      15.826 -20.995  -9.582  1.00 53.98           C  
ANISOU 3345  CA  PHE K 305     7254   6972   6281   -210    254    115       C  
ATOM   3346  C   PHE K 305      16.078 -21.273 -11.046  1.00 52.61           C  
ANISOU 3346  C   PHE K 305     6993   6725   6271   -162    228    128       C  
ATOM   3347  O   PHE K 305      17.155 -21.013 -11.566  1.00 51.23           O  
ANISOU 3347  O   PHE K 305     6691   6603   6171    -24    152     97       O  
ATOM   3348  CB  PHE K 305      14.807 -19.865  -9.510  1.00 55.51           C  
ANISOU 3348  CB  PHE K 305     7280   7369   6439   -150    382     19       C  
ATOM   3349  CG  PHE K 305      14.422 -19.488  -8.131  1.00 57.36           C  
ANISOU 3349  CG  PHE K 305     7600   7782   6411    -50    432    -31       C  
ATOM   3350  CD1 PHE K 305      15.234 -18.647  -7.384  1.00 59.46           C  
ANISOU 3350  CD1 PHE K 305     8107   7852   6632    103    263   -123       C  
ATOM   3351  CD2 PHE K 305      13.248 -19.964  -7.574  1.00 61.03           C  
ANISOU 3351  CD2 PHE K 305     7901   8699   6587   -173    630     27       C  
ATOM   3352  CE1 PHE K 305      14.875 -18.284  -6.088  1.00 63.93           C  
ANISOU 3352  CE1 PHE K 305     8852   8547   6890    292    284   -195       C  
ATOM   3353  CE2 PHE K 305      12.885 -19.609  -6.282  1.00 65.56           C  
ANISOU 3353  CE2 PHE K 305     8517   9576   6817     -9    721    -25       C  
ATOM   3354  CZ  PHE K 305      13.700 -18.771  -5.536  1.00 65.44           C  
ANISOU 3354  CZ  PHE K 305     8844   9237   6780    302    544   -157       C  
ATOM   3355  N   THR K 306      15.054 -21.795 -11.704  1.00 52.65           N  
ANISOU 3355  N   THR K 306     7021   6721   6259   -325    290    186       N  
ATOM   3356  CA  THR K 306      15.131 -22.138 -13.102  1.00 53.04           C  
ANISOU 3356  CA  THR K 306     7092   6649   6411   -259    244    194       C  
ATOM   3357  C   THR K 306      13.902 -21.587 -13.834  1.00 51.09           C  
ANISOU 3357  C   THR K 306     6606   6565   6238   -386    345    168       C  
ATOM   3358  O   THR K 306      12.786 -21.911 -13.489  1.00 53.39           O  
ANISOU 3358  O   THR K 306     6803   7104   6378   -660    392    225       O  
ATOM   3359  CB  THR K 306      15.281 -23.676 -13.268  1.00 56.50           C  
ANISOU 3359  CB  THR K 306     8062   6778   6627   -272     40    285       C  
ATOM   3360  OG1 THR K 306      16.576 -24.084 -12.791  1.00 55.79           O  
ANISOU 3360  OG1 THR K 306     8172   6624   6402    139   -110    228       O  
ATOM   3361  CG2 THR K 306      15.153 -24.087 -14.710  1.00 57.69           C  
ANISOU 3361  CG2 THR K 306     8356   6762   6799   -173    -42    281       C  
ATOM   3362  N   LEU K 307      14.118 -20.741 -14.843  1.00 49.96           N  
ANISOU 3362  N   LEU K 307     6350   6383   6247   -207    359     89       N  
ATOM   3363  CA  LEU K 307      13.013 -20.237 -15.664  1.00 50.87           C  
ANISOU 3363  CA  LEU K 307     6320   6624   6383   -174    380     24       C  
ATOM   3364  C   LEU K 307      12.898 -21.000 -16.979  1.00 47.25           C  
ANISOU 3364  C   LEU K 307     5982   5996   5973   -233    301     79       C  
ATOM   3365  O   LEU K 307      13.900 -21.148 -17.649  1.00 46.80           O  
ANISOU 3365  O   LEU K 307     6078   5739   5963    -86    277     94       O  
ATOM   3366  CB  LEU K 307      13.269 -18.765 -16.004  1.00 52.26           C  
ANISOU 3366  CB  LEU K 307     6573   6698   6583     65    349    -95       C  
ATOM   3367  CG  LEU K 307      12.454 -17.710 -15.296  1.00 56.51           C  
ANISOU 3367  CG  LEU K 307     7129   7412   6928    359    316   -258       C  
ATOM   3368  CD1 LEU K 307      12.724 -16.379 -15.987  1.00 58.12           C  
ANISOU 3368  CD1 LEU K 307     7784   7248   7048    561    134   -357       C  
ATOM   3369  CD2 LEU K 307      10.972 -18.066 -15.301  1.00 59.09           C  
ANISOU 3369  CD2 LEU K 307     7053   8299   7097    479    379   -324       C  
ATOM   3370  N   GLN K 308      11.694 -21.441 -17.351  1.00 48.66           N  
ANISOU 3370  N   GLN K 308     6054   6364   6068   -445    246    104       N  
ATOM   3371  CA  GLN K 308      11.405 -21.954 -18.710  1.00 49.47           C  
ANISOU 3371  CA  GLN K 308     6332   6275   6187   -490    105    126       C  
ATOM   3372  C   GLN K 308      11.116 -20.794 -19.679  1.00 46.56           C  
ANISOU 3372  C   GLN K 308     5823   5951   5914   -154    120    -18       C  
ATOM   3373  O   GLN K 308      10.118 -20.080 -19.523  1.00 48.87           O  
ANISOU 3373  O   GLN K 308     5804   6642   6121    -19    117   -134       O  
ATOM   3374  CB  GLN K 308      10.195 -22.890 -18.712  1.00 54.55           C  
ANISOU 3374  CB  GLN K 308     6935   7165   6624  -1036    -45    245       C  
ATOM   3375  CG  GLN K 308      10.384 -24.224 -17.988  1.00 61.71           C  
ANISOU 3375  CG  GLN K 308     8343   7813   7289  -1531   -199    443       C  
ATOM   3376  CD  GLN K 308      10.530 -25.402 -18.944  1.00 65.91           C  
ANISOU 3376  CD  GLN K 308     9653   7743   7646  -1697   -550    534       C  
ATOM   3377  OE1 GLN K 308       9.601 -25.756 -19.689  1.00 68.67           O  
ANISOU 3377  OE1 GLN K 308    10044   8176   7872  -2130   -755    603       O  
ATOM   3378  NE2 GLN K 308      11.700 -26.012 -18.930  1.00 67.17           N  
ANISOU 3378  NE2 GLN K 308    10466   7340   7713  -1276   -674    510       N  
ATOM   3379  N   VAL K 309      11.979 -20.623 -20.676  1.00 43.91           N  
ANISOU 3379  N   VAL K 309     5754   5278   5650     38    116    -19       N  
ATOM   3380  CA  VAL K 309      11.853 -19.542 -21.677  1.00 43.46           C  
ANISOU 3380  CA  VAL K 309     5790   5121   5599    277     89   -114       C  
ATOM   3381  C   VAL K 309      11.638 -20.093 -23.101  1.00 43.56           C  
ANISOU 3381  C   VAL K 309     6016   4944   5590    325    -23   -100       C  
ATOM   3382  O   VAL K 309      12.355 -20.983 -23.523  1.00 42.38           O  
ANISOU 3382  O   VAL K 309     6083   4623   5396    333    -24    -21       O  
ATOM   3383  CB  VAL K 309      13.114 -18.666 -21.685  1.00 42.45           C  
ANISOU 3383  CB  VAL K 309     5835   4845   5448    288    185    -74       C  
ATOM   3384  CG1 VAL K 309      12.996 -17.555 -22.707  1.00 42.44           C  
ANISOU 3384  CG1 VAL K 309     6175   4619   5331    387     96   -121       C  
ATOM   3385  CG2 VAL K 309      13.380 -18.102 -20.281  1.00 43.55           C  
ANISOU 3385  CG2 VAL K 309     5893   5082   5572    217    217    -92       C  
ATOM   3386  N   ARG K 310      10.650 -19.548 -23.815  1.00 45.16           N  
ANISOU 3386  N   ARG K 310     6207   5202   5748    478   -161   -211       N  
ATOM   3387  CA  ARG K 310      10.311 -19.947 -25.191  1.00 46.47           C  
ANISOU 3387  CA  ARG K 310     6611   5176   5867    542   -320   -220       C  
ATOM   3388  C   ARG K 310      11.064 -19.096 -26.197  1.00 46.15           C  
ANISOU 3388  C   ARG K 310     6954   4825   5755    764   -260   -224       C  
ATOM   3389  O   ARG K 310      10.929 -17.883 -26.188  1.00 47.73           O  
ANISOU 3389  O   ARG K 310     7310   4954   5868    919   -299   -304       O  
ATOM   3390  CB  ARG K 310       8.808 -19.771 -25.434  1.00 50.97           C  
ANISOU 3390  CB  ARG K 310     6895   6116   6354    604   -545   -351       C  
ATOM   3391  CG  ARG K 310       7.954 -20.655 -24.554  1.00 55.99           C  
ANISOU 3391  CG  ARG K 310     7064   7282   6926    151   -607   -282       C  
ATOM   3392  CD  ARG K 310       6.465 -20.500 -24.833  1.00 63.13           C  
ANISOU 3392  CD  ARG K 310     7440   8907   7637    158   -826   -402       C  
ATOM   3393  NE  ARG K 310       5.759 -21.761 -24.588  1.00 70.76           N  
ANISOU 3393  NE  ARG K 310     8160  10273   8450   -654   -990   -212       N  
ATOM   3394  CZ  ARG K 310       5.563 -22.309 -23.389  1.00 74.67           C  
ANISOU 3394  CZ  ARG K 310     8341  11210   8820  -1205   -884    -59       C  
ATOM   3395  NH1 ARG K 310       5.997 -21.714 -22.281  1.00 76.00           N  
ANISOU 3395  NH1 ARG K 310     8320  11512   9042   -910   -592   -110       N  
ATOM   3396  NH2 ARG K 310       4.916 -23.461 -23.293  1.00 80.83           N  
ANISOU 3396  NH2 ARG K 310     9094  12270   9347  -2145  -1115    170       N  
ATOM   3397  N   GLY K 311      11.858 -19.721 -27.053  1.00 45.18           N  
ANISOU 3397  N   GLY K 311     7078   4531   5556    790   -197   -134       N  
ATOM   3398  CA  GLY K 311      12.601 -19.012 -28.070  1.00 46.33           C  
ANISOU 3398  CA  GLY K 311     7526   4554   5523    872    -92    -83       C  
ATOM   3399  C   GLY K 311      14.020 -18.661 -27.653  1.00 47.48           C  
ANISOU 3399  C   GLY K 311     7527   4961   5551    674    179     59       C  
ATOM   3400  O   GLY K 311      14.248 -18.124 -26.572  1.00 46.88           O  
ANISOU 3400  O   GLY K 311     7275   4985   5550    460    221     79       O  
ATOM   3401  N   ARG K 312      14.972 -18.975 -28.524  1.00 53.22           N  
ANISOU 3401  N   ARG K 312     8853   6151   5214   2553    958   -921       N  
ATOM   3402  CA  ARG K 312      16.377 -18.717 -28.277  1.00 57.96           C  
ANISOU 3402  CA  ARG K 312     9051   7211   5758   2551   1022  -1439       C  
ATOM   3403  C   ARG K 312      16.608 -17.229 -27.986  1.00 56.13           C  
ANISOU 3403  C   ARG K 312     9080   7213   5033   2028   1398   -921       C  
ATOM   3404  O   ARG K 312      17.293 -16.873 -27.034  1.00 53.11           O  
ANISOU 3404  O   ARG K 312     8672   6751   4756   2102   1378   -882       O  
ATOM   3405  CB  ARG K 312      17.197 -19.174 -29.468  1.00 65.18           C  
ANISOU 3405  CB  ARG K 312     9222   9047   6494   2495   1123  -2530       C  
ATOM   3406  CG  ARG K 312      18.694 -18.886 -29.392  1.00 74.76           C  
ANISOU 3406  CG  ARG K 312     9741  11134   7531   2366   1281  -3428       C  
ATOM   3407  CD  ARG K 312      19.427 -19.606 -28.252  1.00 78.80           C  
ANISOU 3407  CD  ARG K 312    10051  11050   8841   3174    611  -3917       C  
ATOM   3408  NE  ARG K 312      20.729 -20.153 -28.683  1.00 91.10           N  
ANISOU 3408  NE  ARG K 312    10484  13528  10602   3513    390  -5625       N  
ATOM   3409  CZ  ARG K 312      21.763 -20.436 -27.880  1.00 97.60           C  
ANISOU 3409  CZ  ARG K 312    10892  14226  11964   4097   -167  -6418       C  
ATOM   3410  NH1 ARG K 312      21.707 -20.235 -26.565  1.00 94.03           N  
ANISOU 3410  NH1 ARG K 312    11166  12739  11819   4311   -536  -5498       N  
ATOM   3411  NH2 ARG K 312      22.878 -20.934 -28.408  1.00110.29           N  
ANISOU 3411  NH2 ARG K 312    11246  16867  13790   4470   -413  -8326       N  
ATOM   3412  N   GLU K 313      16.015 -16.382 -28.817  1.00 56.84           N  
ANISOU 3412  N   GLU K 313     9502   7470   4622   1502   1565   -521       N  
ATOM   3413  CA  GLU K 313      16.227 -14.951 -28.782  1.00 57.44           C  
ANISOU 3413  CA  GLU K 313     9988   7611   4224    899   1614    -41       C  
ATOM   3414  C   GLU K 313      15.825 -14.376 -27.434  1.00 52.06           C  
ANISOU 3414  C   GLU K 313     9594   6247   3939   1268   1433    406       C  
ATOM   3415  O   GLU K 313      16.582 -13.636 -26.798  1.00 48.01           O  
ANISOU 3415  O   GLU K 313     9110   5796   3336   1092   1476    485       O  
ATOM   3416  CB  GLU K 313      15.482 -14.276 -29.943  1.00 64.30           C  
ANISOU 3416  CB  GLU K 313    11397   8460   4573    301   1416    367       C  
ATOM   3417  CG  GLU K 313      13.945 -14.222 -29.844  1.00 65.53           C  
ANISOU 3417  CG  GLU K 313    11948   7805   5146    798   1009    731       C  
ATOM   3418  CD  GLU K 313      13.217 -15.574 -29.914  1.00 63.48           C  
ANISOU 3418  CD  GLU K 313    11321   7472   5324   1378   1119    414       C  
ATOM   3419  OE1 GLU K 313      13.386 -16.354 -30.922  1.00 69.34           O  
ANISOU 3419  OE1 GLU K 313    11799   8671   5874   1251   1259     42       O  
ATOM   3420  OE2 GLU K 313      12.441 -15.823 -28.959  1.00 57.96           O  
ANISOU 3420  OE2 GLU K 313    10594   6333   5092   1844   1029    491       O  
ATOM   3421  N   ARG K 314      14.658 -14.798 -26.973  1.00 48.16           N  
ANISOU 3421  N   ARG K 314     9195   5266   3835   1715   1270    560       N  
ATOM   3422  CA  ARG K 314      14.121 -14.348 -25.748  1.00 44.86           C  
ANISOU 3422  CA  ARG K 314     8859   4514   3670   1948   1160    742       C  
ATOM   3423  C   ARG K 314      15.016 -14.877 -24.633  1.00 42.75           C  
ANISOU 3423  C   ARG K 314     8381   4303   3557   2082   1267    656       C  
ATOM   3424  O   ARG K 314      15.254 -14.180 -23.636  1.00 40.76           O  
ANISOU 3424  O   ARG K 314     8154   4005   3324   2083   1266    763       O  
ATOM   3425  CB  ARG K 314      12.660 -14.806 -25.569  1.00 44.15           C  
ANISOU 3425  CB  ARG K 314     8731   4253   3788   2164   1053    695       C  
ATOM   3426  CG  ARG K 314      12.068 -14.446 -24.196  1.00 43.35           C  
ANISOU 3426  CG  ARG K 314     8467   4203   3799   2235   1042    600       C  
ATOM   3427  CD  ARG K 314      10.633 -14.912 -24.073  1.00 45.84           C  
ANISOU 3427  CD  ARG K 314     8554   4701   4159   2225   1032    322       C  
ATOM   3428  NE  ARG K 314       9.832 -14.404 -25.185  1.00 47.72           N  
ANISOU 3428  NE  ARG K 314     8856   4758   4516   2457    722    114       N  
ATOM   3429  CZ  ARG K 314       8.598 -14.793 -25.491  1.00 49.40           C  
ANISOU 3429  CZ  ARG K 314     8833   5126   4808   2527    656   -249       C  
ATOM   3430  NH1 ARG K 314       7.958 -15.720 -24.777  1.00 51.13           N  
ANISOU 3430  NH1 ARG K 314     8730   5805   4893   2196    961   -420       N  
ATOM   3431  NH2 ARG K 314       7.989 -14.223 -26.518  1.00 49.13           N  
ANISOU 3431  NH2 ARG K 314     8947   4792   4925   2808    184   -437       N  
ATOM   3432  N   TYR K 315      15.523 -16.084 -24.797  1.00 43.39           N  
ANISOU 3432  N   TYR K 315     8275   4411   3799   2242   1197    390       N  
ATOM   3433  CA  TYR K 315      16.458 -16.629 -23.826  1.00 45.26           C  
ANISOU 3433  CA  TYR K 315     8417   4519   4259   2436    978    241       C  
ATOM   3434  C   TYR K 315      17.720 -15.762 -23.741  1.00 46.00           C  
ANISOU 3434  C   TYR K 315     8273   5003   4200   2343   1177     -4       C  
ATOM   3435  O   TYR K 315      18.120 -15.374 -22.650  1.00 47.21           O  
ANISOU 3435  O   TYR K 315     8492   5037   4406   2382   1124    147       O  
ATOM   3436  CB  TYR K 315      16.816 -18.092 -24.136  1.00 49.00           C  
ANISOU 3436  CB  TYR K 315     8759   4753   5103   2769    490   -203       C  
ATOM   3437  CG  TYR K 315      18.038 -18.570 -23.416  1.00 53.33           C  
ANISOU 3437  CG  TYR K 315     9163   5113   5985   3109    -17   -627       C  
ATOM   3438  CD1 TYR K 315      17.981 -18.935 -22.070  1.00 55.51           C  
ANISOU 3438  CD1 TYR K 315     9923   4787   6379   3060   -542   -163       C  
ATOM   3439  CD2 TYR K 315      19.262 -18.664 -24.065  1.00 58.55           C  
ANISOU 3439  CD2 TYR K 315     9160   6300   6783   3397    -49  -1609       C  
ATOM   3440  CE1 TYR K 315      19.112 -19.409 -21.400  1.00 59.81           C  
ANISOU 3440  CE1 TYR K 315    10443   4982   7299   3440  -1272   -566       C  
ATOM   3441  CE2 TYR K 315      20.396 -19.124 -23.402  1.00 64.05           C  
ANISOU 3441  CE2 TYR K 315     9609   6808   7917   3870   -690  -2252       C  
ATOM   3442  CZ  TYR K 315      20.315 -19.474 -22.061  1.00 64.72           C  
ANISOU 3442  CZ  TYR K 315    10332   6026   8231   3955  -1373  -1663       C  
ATOM   3443  OH  TYR K 315      21.441 -19.929 -21.392  1.00 72.50           O  
ANISOU 3443  OH  TYR K 315    11180   6664   9701   4479  -2241  -2299       O  
ATOM   3444  N   GLU K 316      18.337 -15.448 -24.873  1.00 49.08           N  
ANISOU 3444  N   GLU K 316     8374   5981   4289   2064   1424   -403       N  
ATOM   3445  CA  GLU K 316      19.568 -14.642 -24.855  1.00 52.59           C  
ANISOU 3445  CA  GLU K 316     8545   7007   4429   1704   1660   -708       C  
ATOM   3446  C   GLU K 316      19.302 -13.259 -24.208  1.00 50.22           C  
ANISOU 3446  C   GLU K 316     8725   6410   3946   1396   1704    -27       C  
ATOM   3447  O   GLU K 316      20.132 -12.750 -23.461  1.00 50.36           O  
ANISOU 3447  O   GLU K 316     8631   6534   3966   1353   1750   -105       O  
ATOM   3448  CB  GLU K 316      20.186 -14.560 -26.254  1.00 60.62           C  
ANISOU 3448  CB  GLU K 316     9144   9008   4879   1076   1973  -1305       C  
ATOM   3449  CG  GLU K 316      21.108 -15.751 -26.597  1.00 68.62           C  
ANISOU 3449  CG  GLU K 316     9247  10658   6166   1499   1878  -2588       C  
ATOM   3450  CD  GLU K 316      21.199 -16.058 -28.083  1.00 78.72           C  
ANISOU 3450  CD  GLU K 316    10024  12962   6922    980   2163  -3303       C  
ATOM   3451  OE1 GLU K 316      20.417 -15.478 -28.861  1.00 80.47           O  
ANISOU 3451  OE1 GLU K 316    10795  13207   6573    293   2360  -2587       O  
ATOM   3452  OE2 GLU K 316      22.046 -16.902 -28.497  1.00 89.59           O  
ANISOU 3452  OE2 GLU K 316    10407  15163   8470   1278   2085  -4724       O  
ATOM   3453  N   ILE K 317      18.103 -12.707 -24.399  1.00 47.47           N  
ANISOU 3453  N   ILE K 317     8853   5617   3564   1324   1550    498       N  
ATOM   3454  CA  ILE K 317      17.785 -11.377 -23.857  1.00 48.26           C  
ANISOU 3454  CA  ILE K 317     9348   5336   3651   1190   1311    888       C  
ATOM   3455  C   ILE K 317      17.606 -11.395 -22.358  1.00 45.47           C  
ANISOU 3455  C   ILE K 317     8848   4760   3665   1667   1284    873       C  
ATOM   3456  O   ILE K 317      18.178 -10.581 -21.635  1.00 47.30           O  
ANISOU 3456  O   ILE K 317     9097   4969   3906   1608   1239    899       O  
ATOM   3457  CB  ILE K 317      16.561 -10.754 -24.583  1.00 49.17           C  
ANISOU 3457  CB  ILE K 317     9944   4995   3739   1103    865   1172       C  
ATOM   3458  CG1 ILE K 317      17.001 -10.343 -25.985  1.00 53.22           C  
ANISOU 3458  CG1 ILE K 317    10838   5756   3624    241    760   1371       C  
ATOM   3459  CG2 ILE K 317      16.001  -9.582 -23.793  1.00 49.12           C  
ANISOU 3459  CG2 ILE K 317    10184   4442   4035   1346    335   1239       C  
ATOM   3460  CD1 ILE K 317      15.874 -10.053 -26.952  1.00 55.86           C  
ANISOU 3460  CD1 ILE K 317    11716   5625   3882    124    194   1640       C  
ATOM   3461  N   LEU K 318      16.831 -12.353 -21.886  1.00 44.83           N  
ANISOU 3461  N   LEU K 318     8646   4599   3788   1985   1299    833       N  
ATOM   3462  CA  LEU K 318      16.636 -12.538 -20.491  1.00 42.95           C  
ANISOU 3462  CA  LEU K 318     8304   4367   3648   2118   1291    838       C  
ATOM   3463  C   LEU K 318      17.928 -12.982 -19.790  1.00 44.00           C  
ANISOU 3463  C   LEU K 318     8349   4548   3818   2172   1279    784       C  
ATOM   3464  O   LEU K 318      18.141 -12.634 -18.619  1.00 43.86           O  
ANISOU 3464  O   LEU K 318     8311   4577   3775   2161   1250    830       O  
ATOM   3465  CB  LEU K 318      15.530 -13.559 -20.256  1.00 44.10           C  
ANISOU 3465  CB  LEU K 318     8446   4532   3777   2071   1262    874       C  
ATOM   3466  CG  LEU K 318      14.101 -13.192 -20.611  1.00 45.14           C  
ANISOU 3466  CG  LEU K 318     8472   4766   3913   2081   1244    686       C  
ATOM   3467  CD1 LEU K 318      13.218 -14.307 -20.093  1.00 46.84           C  
ANISOU 3467  CD1 LEU K 318     8626   5229   3940   1754   1307    699       C  
ATOM   3468  CD2 LEU K 318      13.651 -11.882 -19.981  1.00 47.31           C  
ANISOU 3468  CD2 LEU K 318     8517   5184   4271   2224   1108    315       C  
ATOM   3469  N   LYS K 319      18.766 -13.760 -20.467  1.00 44.46           N  
ANISOU 3469  N   LYS K 319     8275   4652   3964   2275   1215    524       N  
ATOM   3470  CA  LYS K 319      20.110 -14.077 -19.940  1.00 47.16           C  
ANISOU 3470  CA  LYS K 319     8396   5061   4461   2473   1032    166       C  
ATOM   3471  C   LYS K 319      20.981 -12.832 -19.778  1.00 49.00           C  
ANISOU 3471  C   LYS K 319     8457   5639   4519   2264   1311     57       C  
ATOM   3472  O   LYS K 319      21.649 -12.684 -18.767  1.00 50.32           O  
ANISOU 3472  O   LYS K 319     8562   5769   4785   2402   1187     -9       O  
ATOM   3473  CB  LYS K 319      20.865 -15.078 -20.820  1.00 51.49           C  
ANISOU 3473  CB  LYS K 319     8567   5768   5227   2739    808   -529       C  
ATOM   3474  CG  LYS K 319      21.963 -15.819 -20.065  1.00 57.10           C  
ANISOU 3474  CG  LYS K 319     9082   6267   6345   3213    185  -1072       C  
ATOM   3475  CD  LYS K 319      22.760 -16.745 -20.968  1.00 65.43           C  
ANISOU 3475  CD  LYS K 319     9510   7593   7755   3651   -191  -2201       C  
ATOM   3476  CE  LYS K 319      24.058 -16.106 -21.431  1.00 69.96           C  
ANISOU 3476  CE  LYS K 319     9230   9205   8144   3523    231  -3198       C  
ATOM   3477  NZ  LYS K 319      24.576 -16.850 -22.605  1.00 79.19           N  
ANISOU 3477  NZ  LYS K 319     9547  11098   9442   3733    131  -4517       N  
ATOM   3478  N   LYS K 320      21.005 -11.955 -20.784  1.00 50.22           N  
ANISOU 3478  N   LYS K 320     8626   6096   4358   1812   1581     82       N  
ATOM   3479  CA  LYS K 320      21.768 -10.716 -20.678  1.00 51.95           C  
ANISOU 3479  CA  LYS K 320     8861   6555   4321   1368   1711    106       C  
ATOM   3480  C   LYS K 320      21.263  -9.847 -19.507  1.00 49.04           C  
ANISOU 3480  C   LYS K 320     8767   5731   4132   1552   1529    479       C  
ATOM   3481  O   LYS K 320      22.052  -9.221 -18.830  1.00 48.21           O  
ANISOU 3481  O   LYS K 320     8569   5721   4024   1485   1544    393       O  
ATOM   3482  CB  LYS K 320      21.714  -9.937 -21.995  1.00 57.08           C  
ANISOU 3482  CB  LYS K 320     9778   7462   4445    551   1783    281       C  
ATOM   3483  CG  LYS K 320      22.690  -8.768 -22.114  1.00 64.17           C  
ANISOU 3483  CG  LYS K 320    10787   8715   4879   -293   1834    319       C  
ATOM   3484  CD  LYS K 320      24.126  -9.212 -22.367  1.00 70.52           C  
ANISOU 3484  CD  LYS K 320    10818  10601   5374   -649   2273   -527       C  
ATOM   3485  CE  LYS K 320      25.026  -8.081 -22.880  1.00 79.07           C  
ANISOU 3485  CE  LYS K 320    12027  12364   5651  -2003   2425   -496       C  
ATOM   3486  NZ  LYS K 320      25.474  -8.221 -24.306  1.00 86.69           N  
ANISOU 3486  NZ  LYS K 320    12728  14526   5682  -3233   2782   -913       N  
ATOM   3487  N   LEU K 321      19.952  -9.806 -19.283  1.00 45.67           N  
ANISOU 3487  N   LEU K 321     8550   4951   3852   1778   1357    710       N  
ATOM   3488  CA  LEU K 321      19.384  -9.003 -18.226  1.00 44.52           C  
ANISOU 3488  CA  LEU K 321     8418   4629   3865   1971   1170    708       C  
ATOM   3489  C   LEU K 321      19.779  -9.503 -16.866  1.00 44.64           C  
ANISOU 3489  C   LEU K 321     8204   4854   3902   2146   1282    617       C  
ATOM   3490  O   LEU K 321      20.027  -8.695 -15.967  1.00 44.04           O  
ANISOU 3490  O   LEU K 321     8030   4833   3870   2194   1220    502       O  
ATOM   3491  CB  LEU K 321      17.858  -8.946 -18.307  1.00 44.53           C  
ANISOU 3491  CB  LEU K 321     8427   4496   3993   2167    966    609       C  
ATOM   3492  CG  LEU K 321      17.367  -8.151 -19.517  1.00 48.00           C  
ANISOU 3492  CG  LEU K 321     9249   4501   4486   2052    518    700       C  
ATOM   3493  CD1 LEU K 321      15.843  -8.103 -19.585  1.00 50.14           C  
ANISOU 3493  CD1 LEU K 321     9387   4658   5004   2411    186    342       C  
ATOM   3494  CD2 LEU K 321      17.929  -6.736 -19.502  1.00 51.87           C  
ANISOU 3494  CD2 LEU K 321    10086   4584   5035   1846      4    779       C  
ATOM   3495  N   ASN K 322      19.800 -10.828 -16.724  1.00 44.28           N  
ANISOU 3495  N   ASN K 322     8161   4842   3819   2194   1290    682       N  
ATOM   3496  CA  ASN K 322      20.122 -11.500 -15.483  1.00 44.78           C  
ANISOU 3496  CA  ASN K 322     8266   4941   3807   2185   1121    752       C  
ATOM   3497  C   ASN K 322      21.591 -11.334 -15.143  1.00 47.01           C  
ANISOU 3497  C   ASN K 322     8425   5213   4224   2361   1018    547       C  
ATOM   3498  O   ASN K 322      21.930 -11.034 -14.010  1.00 47.40           O  
ANISOU 3498  O   ASN K 322     8469   5342   4195   2340    929    566       O  
ATOM   3499  CB  ASN K 322      19.848 -12.995 -15.623  1.00 47.17           C  
ANISOU 3499  CB  ASN K 322     8834   4989   4099   2126    795    931       C  
ATOM   3500  CG  ASN K 322      20.114 -13.754 -14.342  1.00 50.04           C  
ANISOU 3500  CG  ASN K 322     9542   5191   4278   1889    298   1185       C  
ATOM   3501  OD1 ASN K 322      19.487 -13.502 -13.324  1.00 51.46           O  
ANISOU 3501  OD1 ASN K 322     9790   5741   4019   1399    402   1372       O  
ATOM   3502  ND2 ASN K 322      21.046 -14.689 -14.390  1.00 54.20           N  
ANISOU 3502  ND2 ASN K 322    10274   5206   5110   2186   -367   1083       N  
ATOM   3503  N   ASP K 323      22.460 -11.608 -16.118  1.00 47.75           N  
ANISOU 3503  N   ASP K 323     8318   5351   4471   2492   1025    208       N  
ATOM   3504  CA  ASP K 323      23.896 -11.337 -15.985  1.00 51.99           C  
ANISOU 3504  CA  ASP K 323     8504   6137   5110   2604   1008   -282       C  
ATOM   3505  C   ASP K 323      24.155  -9.850 -15.593  1.00 52.58           C  
ANISOU 3505  C   ASP K 323     8548   6400   5028   2323   1299   -172       C  
ATOM   3506  O   ASP K 323      25.037  -9.548 -14.795  1.00 52.94           O  
ANISOU 3506  O   ASP K 323     8421   6555   5137   2424   1229   -389       O  
ATOM   3507  CB  ASP K 323      24.643 -11.703 -17.276  1.00 55.82           C  
ANISOU 3507  CB  ASP K 323     8536   7059   5613   2568   1130   -945       C  
ATOM   3508  CG  ASP K 323      24.604 -13.242 -17.597  1.00 61.55           C  
ANISOU 3508  CG  ASP K 323     9181   7510   6693   3055    587  -1343       C  
ATOM   3509  OD1 ASP K 323      23.872 -14.019 -16.918  1.00 61.37           O  
ANISOU 3509  OD1 ASP K 323     9673   6828   6815   3235     85   -850       O  
ATOM   3510  OD2 ASP K 323      25.319 -13.679 -18.539  1.00 66.68           O  
ANISOU 3510  OD2 ASP K 323     9231   8668   7435   3164    587  -2241       O  
ATOM   3511  N   SER K 324      23.342  -8.940 -16.105  1.00 50.37           N  
ANISOU 3511  N   SER K 324     8495   6030   4612   2025   1438    135       N  
ATOM   3512  CA  SER K 324      23.491  -7.518 -15.821  1.00 52.91           C  
ANISOU 3512  CA  SER K 324     8926   6279   4896   1783   1397    221       C  
ATOM   3513  C   SER K 324      22.941  -7.120 -14.421  1.00 51.82           C  
ANISOU 3513  C   SER K 324     8751   6027   4909   2106   1245    222       C  
ATOM   3514  O   SER K 324      23.560  -6.354 -13.681  1.00 51.24           O  
ANISOU 3514  O   SER K 324     8577   5999   4891   2112   1189     89       O  
ATOM   3515  CB  SER K 324      22.868  -6.732 -16.981  1.00 55.09           C  
ANISOU 3515  CB  SER K 324     9597   6299   5034   1346   1227    485       C  
ATOM   3516  OG  SER K 324      22.789  -5.354 -16.710  1.00 62.09           O  
ANISOU 3516  OG  SER K 324    10780   6797   6011   1170    811    596       O  
ATOM   3517  N   LEU K 325      21.793  -7.673 -14.045  1.00 50.82           N  
ANISOU 3517  N   LEU K 325     8624   5922   4762   2264   1215    271       N  
ATOM   3518  CA  LEU K 325      21.304  -7.538 -12.694  1.00 50.38           C  
ANISOU 3518  CA  LEU K 325     8369   6158   4612   2331   1188     97       C  
ATOM   3519  C   LEU K 325      22.245  -8.164 -11.633  1.00 49.79           C  
ANISOU 3519  C   LEU K 325     8299   6249   4371   2292   1163    179       C  
ATOM   3520  O   LEU K 325      22.380  -7.598 -10.560  1.00 49.02           O  
ANISOU 3520  O   LEU K 325     8024   6424   4177   2274   1147     -7       O  
ATOM   3521  CB  LEU K 325      19.873  -8.069 -12.561  1.00 51.00           C  
ANISOU 3521  CB  LEU K 325     8349   6532   4497   2214   1234      7       C  
ATOM   3522  CG  LEU K 325      18.794  -7.250 -13.302  1.00 50.67           C  
ANISOU 3522  CG  LEU K 325     8175   6350   4725   2421   1041   -354       C  
ATOM   3523  CD1 LEU K 325      17.570  -8.132 -13.457  1.00 51.52           C  
ANISOU 3523  CD1 LEU K 325     8153   6819   4603   2240   1184   -446       C  
ATOM   3524  CD2 LEU K 325      18.412  -5.940 -12.600  1.00 53.97           C  
ANISOU 3524  CD2 LEU K 325     8192   6912   5403   2706    716  -1065       C  
ATOM   3525  N   GLU K 326      22.892  -9.288 -11.936  1.00 50.50           N  
ANISOU 3525  N   GLU K 326     8578   6127   4481   2337   1005    343       N  
ATOM   3526  CA  GLU K 326      23.933  -9.856 -11.059  1.00 54.78           C  
ANISOU 3526  CA  GLU K 326     9206   6583   5023   2440    645    317       C  
ATOM   3527  C   GLU K 326      25.090  -8.859 -10.833  1.00 54.50           C  
ANISOU 3527  C   GLU K 326     8849   6681   5175   2622    766    -37       C  
ATOM   3528  O   GLU K 326      25.507  -8.623  -9.681  1.00 52.84           O  
ANISOU 3528  O   GLU K 326     8624   6585   4868   2632    612    -75       O  
ATOM   3529  CB  GLU K 326      24.491 -11.187 -11.601  1.00 58.28           C  
ANISOU 3529  CB  GLU K 326     9828   6616   5698   2681    143    249       C  
ATOM   3530  CG  GLU K 326      23.587 -12.396 -11.378  1.00 63.70           C  
ANISOU 3530  CG  GLU K 326    11058   6985   6159   2383   -319    719       C  
ATOM   3531  CD  GLU K 326      24.189 -13.731 -11.848  1.00 71.16           C  
ANISOU 3531  CD  GLU K 326    12245   7281   7510   2764  -1176    529       C  
ATOM   3532  OE1 GLU K 326      25.362 -13.745 -12.287  1.00 75.34           O  
ANISOU 3532  OE1 GLU K 326    12332   7784   8510   3343  -1374   -190       O  
ATOM   3533  OE2 GLU K 326      23.494 -14.780 -11.774  1.00 73.38           O  
ANISOU 3533  OE2 GLU K 326    13111   7118   7651   2456  -1749    967       O  
ATOM   3534  N   LEU K 327      25.597  -8.282 -11.926  1.00 53.04           N  
ANISOU 3534  N   LEU K 327     8445   6561   5146   2596   1026   -278       N  
ATOM   3535  CA  LEU K 327      26.690  -7.307 -11.853  1.00 53.16           C  
ANISOU 3535  CA  LEU K 327     8185   6794   5219   2502   1162   -602       C  
ATOM   3536  C   LEU K 327      26.347  -6.148 -10.969  1.00 50.27           C  
ANISOU 3536  C   LEU K 327     7865   6396   4841   2449   1163   -495       C  
ATOM   3537  O   LEU K 327      27.145  -5.779 -10.108  1.00 50.62           O  
ANISOU 3537  O   LEU K 327     7734   6571   4929   2544   1102   -708       O  
ATOM   3538  CB  LEU K 327      27.113  -6.788 -13.245  1.00 55.52           C  
ANISOU 3538  CB  LEU K 327     8370   7328   5396   2026   1438   -762       C  
ATOM   3539  CG  LEU K 327      28.438  -6.005 -13.260  1.00 57.72           C  
ANISOU 3539  CG  LEU K 327     8312   8048   5568   1643   1594  -1192       C  
ATOM   3540  CD1 LEU K 327      29.598  -6.829 -12.717  1.00 60.01           C  
ANISOU 3540  CD1 LEU K 327     8052   8687   6063   2107   1465  -1928       C  
ATOM   3541  CD2 LEU K 327      28.726  -5.499 -14.656  1.00 61.63           C  
ANISOU 3541  CD2 LEU K 327     8818   8959   5636    733   1859  -1240       C  
ATOM   3542  N   SER K 328      25.149  -5.595 -11.149  1.00 49.85           N  
ANISOU 3542  N   SER K 328     7968   6183   4790   2386   1134   -328       N  
ATOM   3543  CA  SER K 328      24.679  -4.474 -10.338  1.00 48.75           C  
ANISOU 3543  CA  SER K 328     7720   6034   4768   2487    957   -539       C  
ATOM   3544  C   SER K 328      24.586  -4.792  -8.864  1.00 48.94           C  
ANISOU 3544  C   SER K 328     7500   6503   4590   2607    989   -718       C  
ATOM   3545  O   SER K 328      24.662  -3.896  -8.015  1.00 48.94           O  
ANISOU 3545  O   SER K 328     7250   6674   4670   2711    883  -1075       O  
ATOM   3546  CB  SER K 328      23.290  -3.995 -10.802  1.00 50.89           C  
ANISOU 3546  CB  SER K 328     8049   6097   5188   2575    713   -652       C  
ATOM   3547  OG  SER K 328      23.352  -3.544 -12.138  1.00 53.94           O  
ANISOU 3547  OG  SER K 328     8841   5971   5681   2320    488   -387       O  
ATOM   3548  N   ASP K 329      24.332  -6.052  -8.563  1.00 48.79           N  
ANISOU 3548  N   ASP K 329     7617   6669   4250   2481   1030   -468       N  
ATOM   3549  CA  ASP K 329      24.205  -6.467  -7.205  1.00 53.38           C  
ANISOU 3549  CA  ASP K 329     8173   7716   4392   2247    954   -469       C  
ATOM   3550  C   ASP K 329      25.561  -6.753  -6.510  1.00 52.77           C  
ANISOU 3550  C   ASP K 329     8226   7498   4324   2356    685   -397       C  
ATOM   3551  O   ASP K 329      25.635  -6.706  -5.294  1.00 55.33           O  
ANISOU 3551  O   ASP K 329     8534   8207   4278   2131    565   -438       O  
ATOM   3552  CB  ASP K 329      23.201  -7.629  -7.085  1.00 57.83           C  
ANISOU 3552  CB  ASP K 329     9004   8522   4447   1760    917   -143       C  
ATOM   3553  CG  ASP K 329      21.882  -7.190  -6.439  1.00 64.99           C  
ANISOU 3553  CG  ASP K 329     9451  10333   4907   1354   1179   -612       C  
ATOM   3554  OD1 ASP K 329      21.241  -6.230  -6.964  1.00 66.38           O  
ANISOU 3554  OD1 ASP K 329     9170  10559   5491   1737   1286  -1189       O  
ATOM   3555  OD2 ASP K 329      21.503  -7.780  -5.384  1.00 71.47           O  
ANISOU 3555  OD2 ASP K 329    10349  11874   4931    579   1167   -512       O  
ATOM   3556  N   VAL K 330      26.620  -6.995  -7.264  1.00 51.47           N  
ANISOU 3556  N   VAL K 330     8091   6922   4542   2665    571   -449       N  
ATOM   3557  CA  VAL K 330      27.938  -7.231  -6.650  1.00 54.13           C  
ANISOU 3557  CA  VAL K 330     8393   7165   5009   2909    208   -662       C  
ATOM   3558  C   VAL K 330      28.875  -6.034  -6.729  1.00 54.04           C  
ANISOU 3558  C   VAL K 330     7945   7315   5273   3043    476  -1106       C  
ATOM   3559  O   VAL K 330      29.875  -5.999  -6.012  1.00 55.62           O  
ANISOU 3559  O   VAL K 330     8002   7574   5554   3237    232  -1390       O  
ATOM   3560  CB  VAL K 330      28.633  -8.494  -7.192  1.00 56.43           C  
ANISOU 3560  CB  VAL K 330     8838   7039   5564   3218   -336   -787       C  
ATOM   3561  CG1 VAL K 330      27.910  -9.729  -6.671  1.00 59.50           C  
ANISOU 3561  CG1 VAL K 330     9909   7070   5626   2959   -981   -227       C  
ATOM   3562  CG2 VAL K 330      28.717  -8.509  -8.727  1.00 55.52           C  
ANISOU 3562  CG2 VAL K 330     8418   6959   5714   3300     20  -1080       C  
ATOM   3563  N   VAL K 331      28.538  -5.039  -7.561  1.00 52.01           N  
ANISOU 3563  N   VAL K 331     7569   7063   5127   2857    836  -1135       N  
ATOM   3564  CA  VAL K 331      29.300  -3.798  -7.601  1.00 51.80           C  
ANISOU 3564  CA  VAL K 331     7322   7098   5258   2719    944  -1411       C  
ATOM   3565  C   VAL K 331      28.753  -2.801  -6.589  1.00 52.63           C  
ANISOU 3565  C   VAL K 331     7368   7231   5398   2799    833  -1498       C  
ATOM   3566  O   VAL K 331      27.592  -2.455  -6.618  1.00 55.48           O  
ANISOU 3566  O   VAL K 331     7778   7527   5772   2819    765  -1479       O  
ATOM   3567  CB  VAL K 331      29.337  -3.182  -9.015  1.00 51.39           C  
ANISOU 3567  CB  VAL K 331     7385   6925   5216   2232   1099  -1329       C  
ATOM   3568  CG1 VAL K 331      30.235  -1.957  -9.040  1.00 54.18           C  
ANISOU 3568  CG1 VAL K 331     7668   7324   5591   1788   1076  -1514       C  
ATOM   3569  CG2 VAL K 331      29.828  -4.200 -10.035  1.00 51.64           C  
ANISOU 3569  CG2 VAL K 331     7268   7214   5138   2114   1281  -1493       C  
ATOM   3570  N   PRO K 332      29.590  -2.336  -5.658  1.00 44.42           N  
ANISOU 3570  N   PRO K 332     3776   5210   7889    586  -1579    -99       N  
ATOM   3571  CA  PRO K 332      29.123  -1.297  -4.747  1.00 45.08           C  
ANISOU 3571  CA  PRO K 332     3874   5401   7852    512  -1982   -288       C  
ATOM   3572  C   PRO K 332      28.790   0.027  -5.441  1.00 45.89           C  
ANISOU 3572  C   PRO K 332     4088   5354   7994    435  -1994   -387       C  
ATOM   3573  O   PRO K 332      29.472   0.406  -6.397  1.00 45.97           O  
ANISOU 3573  O   PRO K 332     4047   5218   8202    365  -1851   -277       O  
ATOM   3574  CB  PRO K 332      30.306  -1.061  -3.821  1.00 47.65           C  
ANISOU 3574  CB  PRO K 332     3900   5867   8335    411  -2277   -144       C  
ATOM   3575  CG  PRO K 332      31.422  -1.909  -4.309  1.00 50.93           C  
ANISOU 3575  CG  PRO K 332     3960   6303   9087    571  -2045    237       C  
ATOM   3576  CD  PRO K 332      30.889  -2.902  -5.269  1.00 48.05           C  
ANISOU 3576  CD  PRO K 332     3887   5691   8675    742  -1508    236       C  
ATOM   3577  N   ALA K 333      27.794   0.744  -4.920  1.00 44.68           N  
ANISOU 3577  N   ALA K 333     4110   5179   7685    493  -2070   -543       N  
ATOM   3578  CA  ALA K 333      27.292   1.937  -5.575  1.00 45.64           C  
ANISOU 3578  CA  ALA K 333     4366   5108   7865    588  -1954   -502       C  
ATOM   3579  C   ALA K 333      28.450   2.884  -5.854  1.00 48.26           C  
ANISOU 3579  C   ALA K 333     4754   5153   8430    383  -1908   -503       C  
ATOM   3580  O   ALA K 333      28.535   3.514  -6.898  1.00 50.20           O  
ANISOU 3580  O   ALA K 333     5088   5211   8772    428  -1735   -358       O  
ATOM   3581  CB  ALA K 333      26.229   2.634  -4.716  1.00 46.03           C  
ANISOU 3581  CB  ALA K 333     4599   5056   7834    767  -1872   -614       C  
ATOM   3582  N   SER K 334      29.349   2.972  -4.901  1.00 50.30           N  
ANISOU 3582  N   SER K 334     4952   5433   8725     84  -2080   -642       N  
ATOM   3583  CA  SER K 334      30.476   3.871  -5.005  1.00 54.17           C  
ANISOU 3583  CA  SER K 334     5438   5747   9397   -294  -2061   -687       C  
ATOM   3584  C   SER K 334      31.411   3.522  -6.179  1.00 54.14           C  
ANISOU 3584  C   SER K 334     5118   5766   9685   -303  -1931   -448       C  
ATOM   3585  O   SER K 334      31.919   4.424  -6.867  1.00 55.39           O  
ANISOU 3585  O   SER K 334     5396   5638  10008   -485  -1715   -447       O  
ATOM   3586  CB  SER K 334      31.250   3.853  -3.704  1.00 56.51           C  
ANISOU 3586  CB  SER K 334     5608   6302   9558   -757  -2402   -818       C  
ATOM   3587  OG  SER K 334      32.122   4.931  -3.731  1.00 64.65           O  
ANISOU 3587  OG  SER K 334     6726   7168  10669  -1292  -2353   -951       O  
ATOM   3588  N   ASP K 335      31.644   2.223  -6.384  1.00 51.96           N  
ANISOU 3588  N   ASP K 335     4527   5741   9474   -114  -1934   -249       N  
ATOM   3589  CA  ASP K 335      32.424   1.754  -7.534  1.00 52.88           C  
ANISOU 3589  CA  ASP K 335     4459   5769   9864    -71  -1602    -25       C  
ATOM   3590  C   ASP K 335      31.646   2.000  -8.834  1.00 51.20           C  
ANISOU 3590  C   ASP K 335     4669   5313   9472     27  -1318    -26       C  
ATOM   3591  O   ASP K 335      32.227   2.434  -9.826  1.00 53.40           O  
ANISOU 3591  O   ASP K 335     5032   5357   9898    -87  -1030     60       O  
ATOM   3592  CB  ASP K 335      32.771   0.263  -7.415  1.00 52.09           C  
ANISOU 3592  CB  ASP K 335     4083   5840   9868    162  -1456    207       C  
ATOM   3593  CG  ASP K 335      33.897  -0.012  -6.436  1.00 57.05           C  
ANISOU 3593  CG  ASP K 335     4099   6805  10769    124  -1705    471       C  
ATOM   3594  OD1 ASP K 335      34.370   0.928  -5.786  1.00 60.42           O  
ANISOU 3594  OD1 ASP K 335     4335   7423  11199   -250  -2082    388       O  
ATOM   3595  OD2 ASP K 335      34.331  -1.185  -6.332  1.00 60.04           O  
ANISOU 3595  OD2 ASP K 335     4196   7274  11339    442  -1485    816       O  
ATOM   3596  N   ALA K 336      30.347   1.727  -8.808  1.00 47.19           N  
ANISOU 3596  N   ALA K 336     4383   4930   8615    194  -1419    -78       N  
ATOM   3597  CA  ALA K 336      29.475   1.919  -9.970  1.00 48.88           C  
ANISOU 3597  CA  ALA K 336     4884   5147   8540    231  -1308     36       C  
ATOM   3598  C   ALA K 336      29.566   3.311 -10.524  1.00 51.71           C  
ANISOU 3598  C   ALA K 336     5440   5225   8981    257  -1230    147       C  
ATOM   3599  O   ALA K 336      29.595   3.487 -11.731  1.00 53.29           O  
ANISOU 3599  O   ALA K 336     5861   5345   9042    190  -1044    332       O  
ATOM   3600  CB  ALA K 336      28.014   1.621  -9.639  1.00 46.06           C  
ANISOU 3600  CB  ALA K 336     4533   5124   7842    374  -1524     33       C  
ATOM   3601  N   GLU K 337      29.584   4.308  -9.658  1.00 52.99           N  
ANISOU 3601  N   GLU K 337     5643   5185   9306    310  -1293     36       N  
ATOM   3602  CA  GLU K 337      29.587   5.647 -10.165  1.00 57.50           C  
ANISOU 3602  CA  GLU K 337     6540   5355   9951    370  -1059    158       C  
ATOM   3603  C   GLU K 337      30.976   6.016 -10.689  1.00 59.42           C  
ANISOU 3603  C   GLU K 337     6822   5302  10451      6   -809    103       C  
ATOM   3604  O   GLU K 337      31.099   6.840 -11.601  1.00 61.31           O  
ANISOU 3604  O   GLU K 337     7395   5202  10698     15   -514    274       O  
ATOM   3605  CB  GLU K 337      29.062   6.648  -9.134  1.00 61.35           C  
ANISOU 3605  CB  GLU K 337     7259   5557  10494    510   -977     32       C  
ATOM   3606  CG  GLU K 337      28.945   8.094  -9.659  1.00 68.23           C  
ANISOU 3606  CG  GLU K 337     8615   5847  11460    679   -534    224       C  
ATOM   3607  CD  GLU K 337      28.080   8.294 -10.931  1.00 70.98           C  
ANISOU 3607  CD  GLU K 337     9015   6304  11649   1158   -472    798       C  
ATOM   3608  OE1 GLU K 337      27.198   7.447 -11.256  1.00 67.93           O  
ANISOU 3608  OE1 GLU K 337     8285   6513  11011   1359   -805   1038       O  
ATOM   3609  OE2 GLU K 337      28.266   9.347 -11.602  1.00 76.48           O  
ANISOU 3609  OE2 GLU K 337    10124   6513  12419   1281    -83   1048       O  
ATOM   3610  N   LYS K 338      32.016   5.411 -10.128  1.00 58.34           N  
ANISOU 3610  N   LYS K 338     6300   5327  10539   -289   -901    -57       N  
ATOM   3611  CA  LYS K 338      33.364   5.654 -10.636  1.00 62.30           C  
ANISOU 3611  CA  LYS K 338     6645   5662  11362   -639   -636    -40       C  
ATOM   3612  C   LYS K 338      33.516   5.080 -12.059  1.00 61.11           C  
ANISOU 3612  C   LYS K 338     6619   5420  11179   -546   -279    176       C  
ATOM   3613  O   LYS K 338      34.107   5.721 -12.939  1.00 66.28           O  
ANISOU 3613  O   LYS K 338     7497   5737  11948   -727     98    244       O  
ATOM   3614  CB  LYS K 338      34.425   5.090  -9.696  1.00 64.00           C  
ANISOU 3614  CB  LYS K 338     6225   6235  11857   -914   -858    -88       C  
ATOM   3615  CG  LYS K 338      34.697   5.980  -8.498  1.00 69.11           C  
ANISOU 3615  CG  LYS K 338     6869   6930  12458  -1368  -1126   -345       C  
ATOM   3616  CD  LYS K 338      35.894   5.498  -7.687  1.00 73.48           C  
ANISOU 3616  CD  LYS K 338     6657   8030  13230  -1759  -1452   -249       C  
ATOM   3617  CE  LYS K 338      35.949   6.226  -6.357  1.00 78.51           C  
ANISOU 3617  CE  LYS K 338     7417   8842  13569  -2358  -1830   -551       C  
ATOM   3618  NZ  LYS K 338      37.107   5.769  -5.546  1.00 85.60           N  
ANISOU 3618  NZ  LYS K 338     7460  10487  14576  -2819  -2303   -335       N  
ATOM   3619  N   TYR K 339      32.950   3.906 -12.289  1.00 56.42           N  
ANISOU 3619  N   TYR K 339     6004   5073  10357   -353   -323    247       N  
ATOM   3620  CA  TYR K 339      32.924   3.325 -13.620  1.00 57.05           C  
ANISOU 3620  CA  TYR K 339     6414   5047  10214   -413     65    379       C  
ATOM   3621  C   TYR K 339      32.101   4.174 -14.580  1.00 60.09           C  
ANISOU 3621  C   TYR K 339     7321   5339  10171   -395     47    552       C  
ATOM   3622  O   TYR K 339      32.614   4.571 -15.627  1.00 62.56           O  
ANISOU 3622  O   TYR K 339     7971   5351  10446   -571    432    665       O  
ATOM   3623  CB  TYR K 339      32.372   1.918 -13.592  1.00 54.42           C  
ANISOU 3623  CB  TYR K 339     6103   4964   9608   -361     79    349       C  
ATOM   3624  CG  TYR K 339      33.363   0.904 -13.094  1.00 55.59           C  
ANISOU 3624  CG  TYR K 339     5858   5070  10193   -290    382    363       C  
ATOM   3625  CD1 TYR K 339      34.626   0.764 -13.692  1.00 58.83           C  
ANISOU 3625  CD1 TYR K 339     6135   5174  11041   -358    983    496       C  
ATOM   3626  CD2 TYR K 339      33.036   0.067 -12.036  1.00 53.00           C  
ANISOU 3626  CD2 TYR K 339     5267   4998   9869    -95    141    330       C  
ATOM   3627  CE1 TYR K 339      35.526  -0.185 -13.235  1.00 61.03           C  
ANISOU 3627  CE1 TYR K 339     5930   5447  11810   -142   1331    685       C  
ATOM   3628  CE2 TYR K 339      33.927  -0.870 -11.572  1.00 55.54           C  
ANISOU 3628  CE2 TYR K 339     5203   5294  10604     95    445    505       C  
ATOM   3629  CZ  TYR K 339      35.166  -0.989 -12.168  1.00 59.14           C  
ANISOU 3629  CZ  TYR K 339     5434   5486  11550    115   1034    726       C  
ATOM   3630  OH  TYR K 339      36.017  -1.924 -11.671  1.00 63.71           O  
ANISOU 3630  OH  TYR K 339     5510   6082  12613    448   1375   1061       O  
ATOM   3631  N   ARG K 340      30.847   4.466 -14.223  1.00 57.97           N  
ANISOU 3631  N   ARG K 340     7084   5343   9599   -146   -361    650       N  
ATOM   3632  CA  ARG K 340      30.005   5.282 -15.079  1.00 62.04           C  
ANISOU 3632  CA  ARG K 340     7945   5887   9740      3   -424   1014       C  
ATOM   3633  C   ARG K 340      30.692   6.605 -15.382  1.00 65.11           C  
ANISOU 3633  C   ARG K 340     8631   5705  10400     29    -82   1107       C  
ATOM   3634  O   ARG K 340      30.525   7.163 -16.457  1.00 69.75           O  
ANISOU 3634  O   ARG K 340     9630   6164  10706     54     80   1451       O  
ATOM   3635  CB  ARG K 340      28.613   5.493 -14.463  1.00 62.75           C  
ANISOU 3635  CB  ARG K 340     7825   6364   9653    393   -837   1206       C  
ATOM   3636  CG  ARG K 340      27.769   4.201 -14.409  1.00 62.15           C  
ANISOU 3636  CG  ARG K 340     7519   6915   9177    241  -1147   1157       C  
ATOM   3637  CD  ARG K 340      26.446   4.424 -13.691  1.00 63.16           C  
ANISOU 3637  CD  ARG K 340     7302   7448   9247    627  -1491   1352       C  
ATOM   3638  NE  ARG K 340      25.379   3.557 -14.193  1.00 65.64           N  
ANISOU 3638  NE  ARG K 340     7436   8510   8995    389  -1815   1538       N  
ATOM   3639  CZ  ARG K 340      24.801   2.570 -13.519  1.00 64.75           C  
ANISOU 3639  CZ  ARG K 340     7061   8770   8768    233  -1973   1295       C  
ATOM   3640  NH1 ARG K 340      25.170   2.257 -12.286  1.00 65.02           N  
ANISOU 3640  NH1 ARG K 340     6994   8513   9196    366  -1868    898       N  
ATOM   3641  NH2 ARG K 340      23.849   1.876 -14.079  1.00 69.53           N  
ANISOU 3641  NH2 ARG K 340     7532  10089   8797   -143  -2243   1460       N  
ATOM   3642  N   GLN K 341      31.472   7.098 -14.433  1.00 64.27           N  
ANISOU 3642  N   GLN K 341     8363   5284  10773    -63     32    808       N  
ATOM   3643  CA  GLN K 341      32.178   8.352 -14.601  1.00 68.52           C  
ANISOU 3643  CA  GLN K 341     9237   5236  11561   -206    438    793       C  
ATOM   3644  C   GLN K 341      33.397   8.124 -15.485  1.00 70.88           C  
ANISOU 3644  C   GLN K 341     9575   5334  12019   -613    845    742       C  
ATOM   3645  O   GLN K 341      33.905   9.052 -16.105  1.00 73.78           O  
ANISOU 3645  O   GLN K 341    10349   5218  12466   -772   1278    819       O  
ATOM   3646  CB  GLN K 341      32.606   8.867 -13.229  1.00 69.01           C  
ANISOU 3646  CB  GLN K 341     9132   5136  11954   -412    399    418       C  
ATOM   3647  CG  GLN K 341      33.207  10.241 -13.211  1.00 74.91           C  
ANISOU 3647  CG  GLN K 341    10344   5229  12889   -706    880    305       C  
ATOM   3648  CD  GLN K 341      32.276  11.313 -13.757  1.00 78.61           C  
ANISOU 3648  CD  GLN K 341    11487   5204  13177   -206   1230    690       C  
ATOM   3649  OE1 GLN K 341      32.732  12.249 -14.411  1.00 83.54           O  
ANISOU 3649  OE1 GLN K 341    12638   5242  13861   -339   1761    792       O  
ATOM   3650  NE2 GLN K 341      30.974  11.191 -13.484  1.00 76.95           N  
ANISOU 3650  NE2 GLN K 341    11229   5229  12779    402    988    973       N  
TER    3651      GLN K 341                                                      
ATOM   3652  N   GLU L 303      10.523 -23.660 -29.204  1.00 60.24           N  
ANISOU 3652  N   GLU L 303     8894   6772   7219   1470   -234  -1263       N  
ATOM   3653  CA  GLU L 303      11.807 -24.174 -28.628  1.00 58.75           C  
ANISOU 3653  CA  GLU L 303     8705   6411   7206   1057    353   -709       C  
ATOM   3654  C   GLU L 303      12.051 -23.650 -27.208  1.00 56.59           C  
ANISOU 3654  C   GLU L 303     8145   6295   7061   1059    385   -606       C  
ATOM   3655  O   GLU L 303      12.079 -22.439 -26.982  1.00 55.68           O  
ANISOU 3655  O   GLU L 303     8282   6070   6802   1306     19   -628       O  
ATOM   3656  CB  GLU L 303      12.987 -23.804 -29.531  1.00 62.49           C  
ANISOU 3656  CB  GLU L 303     9726   6592   7422    861    492   -421       C  
ATOM   3657  CG  GLU L 303      14.275 -24.555 -29.202  1.00 63.80           C  
ANISOU 3657  CG  GLU L 303     9542   6976   7722    711    988   -304       C  
ATOM   3658  CD  GLU L 303      15.264 -24.612 -30.364  1.00 71.78           C  
ANISOU 3658  CD  GLU L 303    10680   8225   8366    388   1293   -455       C  
ATOM   3659  OE1 GLU L 303      15.510 -23.555 -30.999  1.00 79.08           O  
ANISOU 3659  OE1 GLU L 303    12197   9107   8742   -192   1268   -396       O  
ATOM   3660  OE2 GLU L 303      15.807 -25.718 -30.646  1.00 75.57           O  
ANISOU 3660  OE2 GLU L 303    10820   8940   8951    654   1504   -732       O  
ATOM   3661  N   ILE L 304      12.239 -24.568 -26.263  1.00 53.41           N  
ANISOU 3661  N   ILE L 304     7501   5989   6800    765    715   -486       N  
ATOM   3662  CA  ILE L 304      12.272 -24.220 -24.854  1.00 53.62           C  
ANISOU 3662  CA  ILE L 304     7295   6204   6871    655    749   -441       C  
ATOM   3663  C   ILE L 304      13.717 -24.190 -24.343  1.00 50.10           C  
ANISOU 3663  C   ILE L 304     7008   5500   6526    744    857    -22       C  
ATOM   3664  O   ILE L 304      14.503 -25.073 -24.637  1.00 47.88           O  
ANISOU 3664  O   ILE L 304     6905   5026   6261    863    930     58       O  
ATOM   3665  CB  ILE L 304      11.404 -25.169 -24.019  1.00 59.67           C  
ANISOU 3665  CB  ILE L 304     7949   7282   7438      0    963   -684       C  
ATOM   3666  CG1 ILE L 304       9.924 -25.008 -24.385  1.00 66.67           C  
ANISOU 3666  CG1 ILE L 304     8199   9001   8131   -164    892  -1484       C  
ATOM   3667  CG2 ILE L 304      11.550 -24.856 -22.534  1.00 63.28           C  
ANISOU 3667  CG2 ILE L 304     8318   7905   7820   -262   1044   -608       C  
ATOM   3668  CD1 ILE L 304       9.549 -25.436 -25.795  1.00 69.73           C  
ANISOU 3668  CD1 ILE L 304     8692   9300   8500    -24    777  -1652       C  
ATOM   3669  N   PHE L 305      14.067 -23.117 -23.635  1.00 47.23           N  
ANISOU 3669  N   PHE L 305     6541   5235   6169    802    763     71       N  
ATOM   3670  CA  PHE L 305      15.350 -23.007 -22.954  1.00 46.99           C  
ANISOU 3670  CA  PHE L 305     6441   5234   6179    814    843    290       C  
ATOM   3671  C   PHE L 305      15.145 -22.865 -21.454  1.00 46.56           C  
ANISOU 3671  C   PHE L 305     6318   5214   6156    728    788    376       C  
ATOM   3672  O   PHE L 305      14.028 -22.627 -20.963  1.00 46.43           O  
ANISOU 3672  O   PHE L 305     6192   5376   6072    569    763    169       O  
ATOM   3673  CB  PHE L 305      16.161 -21.839 -23.494  1.00 46.40           C  
ANISOU 3673  CB  PHE L 305     6470   5288   5869    597    858    327       C  
ATOM   3674  CG  PHE L 305      16.603 -22.050 -24.894  1.00 49.21           C  
ANISOU 3674  CG  PHE L 305     6940   5758   5996    391   1033    187       C  
ATOM   3675  CD1 PHE L 305      15.721 -21.839 -25.936  1.00 49.33           C  
ANISOU 3675  CD1 PHE L 305     7472   5431   5840    375    852    159       C  
ATOM   3676  CD2 PHE L 305      17.866 -22.531 -25.164  1.00 52.60           C  
ANISOU 3676  CD2 PHE L 305     6869   6788   6327    306   1320   -101       C  
ATOM   3677  CE1 PHE L 305      16.105 -22.065 -27.231  1.00 52.40           C  
ANISOU 3677  CE1 PHE L 305     8077   5907   5926     64   1042     38       C  
ATOM   3678  CE2 PHE L 305      18.265 -22.756 -26.455  1.00 56.86           C  
ANISOU 3678  CE2 PHE L 305     7380   7669   6555      9   1576   -406       C  
ATOM   3679  CZ  PHE L 305      17.380 -22.527 -27.491  1.00 56.35           C  
ANISOU 3679  CZ  PHE L 305     8030   7088   6290   -209   1482   -238       C  
ATOM   3680  N   THR L 306      16.250 -22.989 -20.740  1.00 46.60           N  
ANISOU 3680  N   THR L 306     6279   5237   6188    847    746    509       N  
ATOM   3681  CA  THR L 306      16.224 -23.015 -19.304  1.00 48.61           C  
ANISOU 3681  CA  THR L 306     6661   5417   6390    739    647    638       C  
ATOM   3682  C   THR L 306      17.187 -21.951 -18.726  1.00 47.85           C  
ANISOU 3682  C   THR L 306     6273   5594   6312    777    596    704       C  
ATOM   3683  O   THR L 306      18.381 -21.972 -18.963  1.00 45.87           O  
ANISOU 3683  O   THR L 306     5716   5665   6048    955    564    561       O  
ATOM   3684  CB  THR L 306      16.516 -24.454 -18.878  1.00 54.58           C  
ANISOU 3684  CB  THR L 306     8060   5698   6976    896    390    688       C  
ATOM   3685  OG1 THR L 306      15.927 -24.700 -17.601  1.00 63.32           O  
ANISOU 3685  OG1 THR L 306     9734   6566   7757    345    350    835       O  
ATOM   3686  CG2 THR L 306      17.975 -24.734 -18.895  1.00 53.62           C  
ANISOU 3686  CG2 THR L 306     7780   5675   6918   1659     35    496       C  
ATOM   3687  N   LEU L 307      16.629 -20.961 -18.041  1.00 45.46           N  
ANISOU 3687  N   LEU L 307     5988   5332   5954    571    584    746       N  
ATOM   3688  CA  LEU L 307      17.425 -19.883 -17.480  1.00 46.55           C  
ANISOU 3688  CA  LEU L 307     6074   5614   5996    442    510    832       C  
ATOM   3689  C   LEU L 307      17.560 -20.090 -15.975  1.00 45.74           C  
ANISOU 3689  C   LEU L 307     5988   5502   5888    439    416    941       C  
ATOM   3690  O   LEU L 307      16.572 -20.119 -15.246  1.00 43.57           O  
ANISOU 3690  O   LEU L 307     5833   5193   5527    280    454    879       O  
ATOM   3691  CB  LEU L 307      16.784 -18.516 -17.759  1.00 48.70           C  
ANISOU 3691  CB  LEU L 307     6740   5703   6059    369    324    753       C  
ATOM   3692  CG  LEU L 307      17.518 -17.304 -17.179  1.00 52.64           C  
ANISOU 3692  CG  LEU L 307     7586   6146   6265     36    176    872       C  
ATOM   3693  CD1 LEU L 307      18.908 -17.170 -17.776  1.00 56.38           C  
ANISOU 3693  CD1 LEU L 307     7979   6987   6454   -625    414    905       C  
ATOM   3694  CD2 LEU L 307      16.705 -16.039 -17.429  1.00 55.84           C  
ANISOU 3694  CD2 LEU L 307     8884   6018   6311    245   -341    708       C  
ATOM   3695  N   GLN L 308      18.809 -20.178 -15.553  1.00 47.44           N  
ANISOU 3695  N   GLN L 308     6007   5928   6087    555    284    946       N  
ATOM   3696  CA  GLN L 308      19.215 -20.251 -14.184  1.00 51.50           C  
ANISOU 3696  CA  GLN L 308     6647   6401   6521    619     49   1041       C  
ATOM   3697  C   GLN L 308      19.316 -18.863 -13.527  1.00 49.55           C  
ANISOU 3697  C   GLN L 308     6341   6320   6165    245    102   1116       C  
ATOM   3698  O   GLN L 308      20.087 -18.020 -13.956  1.00 52.77           O  
ANISOU 3698  O   GLN L 308     6543   7069   6436    -59    164   1022       O  
ATOM   3699  CB  GLN L 308      20.585 -20.953 -14.158  1.00 57.91           C  
ANISOU 3699  CB  GLN L 308     7137   7542   7322   1206   -326    727       C  
ATOM   3700  CG  GLN L 308      21.075 -21.335 -12.782  1.00 65.12           C  
ANISOU 3700  CG  GLN L 308     8438   8234   8071   1567   -867    752       C  
ATOM   3701  CD  GLN L 308      22.323 -22.206 -12.804  1.00 75.28           C  
ANISOU 3701  CD  GLN L 308     9474   9841   9285   2640  -1589    135       C  
ATOM   3702  OE1 GLN L 308      22.646 -22.850 -11.811  1.00 81.07           O  
ANISOU 3702  OE1 GLN L 308    10967  10067   9769   3259  -2363     96       O  
ATOM   3703  NE2 GLN L 308      23.021 -22.239 -13.941  1.00 80.22           N  
ANISOU 3703  NE2 GLN L 308     9106  11362  10011   2926  -1441   -497       N  
ATOM   3704  N   VAL L 309      18.566 -18.640 -12.461  1.00 49.64           N  
ANISOU 3704  N   VAL L 309     6636   6141   6081    107     85   1207       N  
ATOM   3705  CA  VAL L 309      18.561 -17.348 -11.788  1.00 49.39           C  
ANISOU 3705  CA  VAL L 309     6693   6165   5906    -94     30   1202       C  
ATOM   3706  C   VAL L 309      18.864 -17.527 -10.302  1.00 51.09           C  
ANISOU 3706  C   VAL L 309     7042   6383   5985   -194    -99   1319       C  
ATOM   3707  O   VAL L 309      18.244 -18.358  -9.656  1.00 52.16           O  
ANISOU 3707  O   VAL L 309     7477   6378   5963   -337    -55   1339       O  
ATOM   3708  CB  VAL L 309      17.181 -16.683 -11.916  1.00 50.03           C  
ANISOU 3708  CB  VAL L 309     6906   6195   5906     28     32    889       C  
ATOM   3709  CG1 VAL L 309      17.204 -15.279 -11.297  1.00 52.50           C  
ANISOU 3709  CG1 VAL L 309     7585   6384   5979     67   -251    773       C  
ATOM   3710  CG2 VAL L 309      16.737 -16.645 -13.371  1.00 49.23           C  
ANISOU 3710  CG2 VAL L 309     6871   5966   5869    252     -8    742       C  
ATOM   3711  N   ARG L 310      19.800 -16.736  -9.774  1.00 53.08           N  
ANISOU 3711  N   ARG L 310     7227   6797   6141   -324   -254   1370       N  
ATOM   3712  CA  ARG L 310      20.190 -16.759  -8.337  1.00 57.90           C  
ANISOU 3712  CA  ARG L 310     8019   7399   6579   -390   -468   1472       C  
ATOM   3713  C   ARG L 310      19.409 -15.719  -7.502  1.00 53.90           C  
ANISOU 3713  C   ARG L 310     7778   6827   5875   -645   -381   1406       C  
ATOM   3714  O   ARG L 310      19.444 -14.533  -7.783  1.00 51.95           O  
ANISOU 3714  O   ARG L 310     7669   6529   5539   -719   -448   1316       O  
ATOM   3715  CB  ARG L 310      21.706 -16.504  -8.221  1.00 64.80           C  
ANISOU 3715  CB  ARG L 310     8461   8750   7409   -369   -726   1351       C  
ATOM   3716  CG  ARG L 310      22.332 -16.654  -6.834  1.00 73.62           C  
ANISOU 3716  CG  ARG L 310     9731   9898   8341   -234  -1144   1373       C  
ATOM   3717  CD  ARG L 310      23.865 -16.531  -6.881  1.00 83.31           C  
ANISOU 3717  CD  ARG L 310    10146  12009   9499    -79  -1461    902       C  
ATOM   3718  NE  ARG L 310      24.334 -15.191  -7.283  1.00 88.24           N  
ANISOU 3718  NE  ARG L 310    10412  13213   9899  -1016  -1083    764       N  
ATOM   3719  CZ  ARG L 310      25.611 -14.842  -7.499  1.00 97.01           C  
ANISOU 3719  CZ  ARG L 310    10630  15500  10728  -1460  -1087    159       C  
ATOM   3720  NH1 ARG L 310      26.600 -15.726  -7.364  1.00105.63           N  
ANISOU 3720  NH1 ARG L 310    10750  17517  11865   -644  -1566   -568       N  
ATOM   3721  NH2 ARG L 310      25.908 -13.590  -7.850  1.00 97.87           N  
ANISOU 3721  NH2 ARG L 310    10908  15930  10346  -2769   -699    126       N  
ATOM   3722  N   GLY L 311      18.707 -16.171  -6.473  1.00 54.44           N  
ANISOU 3722  N   GLY L 311     8095   6881   5709   -849   -291   1358       N  
ATOM   3723  CA  GLY L 311      17.990 -15.270  -5.554  1.00 56.42           C  
ANISOU 3723  CA  GLY L 311     8402   7341   5693  -1020   -201   1046       C  
ATOM   3724  C   GLY L 311      16.540 -15.046  -5.949  1.00 58.53           C  
ANISOU 3724  C   GLY L 311     8310   8047   5881   -878     35    366       C  
ATOM   3725  O   GLY L 311      16.224 -14.961  -7.150  1.00 58.30           O  
ANISOU 3725  O   GLY L 311     8099   7961   6090   -466    -27    213       O  
ATOM   3726  N   ARG L 312      15.644 -14.960  -4.966  1.00 60.54           N  
ANISOU 3726  N   ARG L 312     9990   7710   5302   -249   -598   1713       N  
ATOM   3727  CA  ARG L 312      14.240 -14.771  -5.294  1.00 62.76           C  
ANISOU 3727  CA  ARG L 312    10121   8300   5425   -458   -337   1676       C  
ATOM   3728  C   ARG L 312      13.941 -13.411  -5.928  1.00 58.59           C  
ANISOU 3728  C   ARG L 312     9399   7840   5022   -104     -1   1042       C  
ATOM   3729  O   ARG L 312      13.019 -13.335  -6.715  1.00 55.88           O  
ANISOU 3729  O   ARG L 312     9000   7444   4785   -112    151    955       O  
ATOM   3730  CB  ARG L 312      13.277 -15.010  -4.122  1.00 71.21           C  
ANISOU 3730  CB  ARG L 312    10924  10335   5795   -984   -307   2044       C  
ATOM   3731  CG  ARG L 312      11.851 -15.261  -4.641  1.00 75.44           C  
ANISOU 3731  CG  ARG L 312    11286  11183   6195  -1300   -160   2201       C  
ATOM   3732  CD  ARG L 312      10.822 -15.684  -3.613  1.00 84.12           C  
ANISOU 3732  CD  ARG L 312    11961  13529   6469  -1994   -168   2748       C  
ATOM   3733  NE  ARG L 312      11.012 -17.046  -3.100  1.00 92.16           N  
ANISOU 3733  NE  ARG L 312    13253  14344   7419  -2759   -762   3778       N  
ATOM   3734  CZ  ARG L 312      10.537 -18.171  -3.640  1.00 93.76           C  
ANISOU 3734  CZ  ARG L 312    13777  13921   7926  -3325  -1260   4476       C  
ATOM   3735  NH1 ARG L 312       9.834 -18.162  -4.767  1.00 90.60           N  
ANISOU 3735  NH1 ARG L 312    13430  13108   7882  -3206  -1129   4240       N  
ATOM   3736  NH2 ARG L 312      10.791 -19.332  -3.040  1.00 99.67           N  
ANISOU 3736  NH2 ARG L 312    14847  14363   8660  -4042  -2031   5448       N  
ATOM   3737  N   GLU L 313      14.696 -12.355  -5.616  1.00 58.32           N  
ANISOU 3737  N   GLU L 313     9300   7838   5019    159    -15    650       N  
ATOM   3738  CA  GLU L 313      14.313 -11.012  -6.106  1.00 59.10           C  
ANISOU 3738  CA  GLU L 313     9302   7858   5293    423     33    112       C  
ATOM   3739  C   GLU L 313      14.541 -10.888  -7.620  1.00 53.18           C  
ANISOU 3739  C   GLU L 313     8647   6509   5049    473     37    181       C  
ATOM   3740  O   GLU L 313      13.699 -10.374  -8.349  1.00 52.91           O  
ANISOU 3740  O   GLU L 313     8568   6370   5165    544     97     -4       O  
ATOM   3741  CB  GLU L 313      15.011  -9.885  -5.332  1.00 63.68           C  
ANISOU 3741  CB  GLU L 313     9866   8501   5826    611   -219   -300       C  
ATOM   3742  CG  GLU L 313      14.800  -9.940  -3.806  1.00 72.32           C  
ANISOU 3742  CG  GLU L 313    10774  10420   6281    627   -224   -483       C  
ATOM   3743  CD  GLU L 313      13.409  -9.503  -3.321  1.00 79.90           C  
ANISOU 3743  CD  GLU L 313    11391  12220   6747    859   -105  -1007       C  
ATOM   3744  OE1 GLU L 313      12.403  -9.580  -4.080  1.00 79.32           O  
ANISOU 3744  OE1 GLU L 313    11218  12156   6762    887     69  -1031       O  
ATOM   3745  OE2 GLU L 313      13.325  -9.084  -2.137  1.00 89.42           O  
ANISOU 3745  OE2 GLU L 313    12344  14247   7384   1062   -201  -1461       O  
ATOM   3746  N   ARG L 314      15.668 -11.400  -8.082  1.00 49.94           N  
ANISOU 3746  N   ARG L 314     8289   5867   4816    467    -47    430       N  
ATOM   3747  CA  ARG L 314      15.963 -11.440  -9.494  1.00 49.98           C  
ANISOU 3747  CA  ARG L 314     8228   5667   5094    518    -23    496       C  
ATOM   3748  C   ARG L 314      14.979 -12.384 -10.204  1.00 46.53           C  
ANISOU 3748  C   ARG L 314     7874   5101   4704    534    112    561       C  
ATOM   3749  O   ARG L 314      14.429 -12.047 -11.237  1.00 44.09           O  
ANISOU 3749  O   ARG L 314     7496   4719   4534    536    209    492       O  
ATOM   3750  CB  ARG L 314      17.400 -11.891  -9.683  1.00 51.67           C  
ANISOU 3750  CB  ARG L 314     8317   6008   5307    632   -157    623       C  
ATOM   3751  CG  ARG L 314      18.133 -11.239 -10.819  1.00 53.39           C  
ANISOU 3751  CG  ARG L 314     8219   6476   5587    568   -194    686       C  
ATOM   3752  CD  ARG L 314      19.616 -11.542 -10.658  1.00 57.87           C  
ANISOU 3752  CD  ARG L 314     8504   7491   5993    689   -335    761       C  
ATOM   3753  NE  ARG L 314      20.166 -10.747  -9.579  1.00 58.02           N  
ANISOU 3753  NE  ARG L 314     8571   7493   5981    449   -523    846       N  
ATOM   3754  CZ  ARG L 314      21.006 -11.170  -8.637  1.00 59.06           C  
ANISOU 3754  CZ  ARG L 314     8690   7773   5976    571   -647    860       C  
ATOM   3755  NH1 ARG L 314      21.450 -12.416  -8.594  1.00 61.44           N  
ANISOU 3755  NH1 ARG L 314     8961   8175   6206    975   -688    804       N  
ATOM   3756  NH2 ARG L 314      21.398 -10.314  -7.718  1.00 57.55           N  
ANISOU 3756  NH2 ARG L 314     8553   7560   5754    319   -850    890       N  
ATOM   3757  N   TYR L 315      14.748 -13.556  -9.628  1.00 45.32           N  
ANISOU 3757  N   TYR L 315     7890   4884   4444    467     11    761       N  
ATOM   3758  CA  TYR L 315      13.785 -14.485 -10.168  1.00 46.93           C  
ANISOU 3758  CA  TYR L 315     8235   4877   4719    352    -35    899       C  
ATOM   3759  C   TYR L 315      12.433 -13.852 -10.443  1.00 47.06           C  
ANISOU 3759  C   TYR L 315     8109   5118   4654    188    233    808       C  
ATOM   3760  O   TYR L 315      11.885 -14.013 -11.530  1.00 45.92           O  
ANISOU 3760  O   TYR L 315     7969   4796   4682    220    282    752       O  
ATOM   3761  CB  TYR L 315      13.613 -15.676  -9.231  1.00 52.44           C  
ANISOU 3761  CB  TYR L 315     9169   5463   5293     62   -378   1322       C  
ATOM   3762  CG  TYR L 315      12.490 -16.592  -9.612  1.00 54.14           C  
ANISOU 3762  CG  TYR L 315     9552   5452   5565   -278   -580   1615       C  
ATOM   3763  CD1 TYR L 315      12.576 -17.407 -10.732  1.00 56.99           C  
ANISOU 3763  CD1 TYR L 315    10154   5195   6301    -36   -914   1480       C  
ATOM   3764  CD2 TYR L 315      11.337 -16.644  -8.853  1.00 60.45           C  
ANISOU 3764  CD2 TYR L 315    10198   6794   5973   -852   -495   2002       C  
ATOM   3765  CE1 TYR L 315      11.539 -18.270 -11.070  1.00 61.83           C  
ANISOU 3765  CE1 TYR L 315    10984   5490   7017   -423  -1244   1776       C  
ATOM   3766  CE2 TYR L 315      10.292 -17.500  -9.170  1.00 65.20           C  
ANISOU 3766  CE2 TYR L 315    10907   7277   6589  -1342   -759   2416       C  
ATOM   3767  CZ  TYR L 315      10.394 -18.312 -10.280  1.00 66.54           C  
ANISOU 3767  CZ  TYR L 315    11445   6583   7254  -1158  -1173   2326       C  
ATOM   3768  OH  TYR L 315       9.347 -19.157 -10.569  1.00 73.08           O  
ANISOU 3768  OH  TYR L 315    12428   7205   8134  -1723  -1563   2767       O  
ATOM   3769  N   GLU L 316      11.903 -13.110  -9.484  1.00 49.46           N  
ANISOU 3769  N   GLU L 316     8234   5899   4656    103    368    700       N  
ATOM   3770  CA  GLU L 316      10.587 -12.486  -9.658  1.00 50.19           C  
ANISOU 3770  CA  GLU L 316     8096   6361   4612    106    558    475       C  
ATOM   3771  C   GLU L 316      10.564 -11.420 -10.770  1.00 46.84           C  
ANISOU 3771  C   GLU L 316     7656   5584   4555    384    562    151       C  
ATOM   3772  O   GLU L 316       9.591 -11.318 -11.500  1.00 44.13           O  
ANISOU 3772  O   GLU L 316     7220   5268   4277    389    649     87       O  
ATOM   3773  CB  GLU L 316      10.082 -11.907  -8.336  1.00 57.02           C  
ANISOU 3773  CB  GLU L 316     8659   8042   4961    148    623    226       C  
ATOM   3774  CG  GLU L 316       9.508 -12.962  -7.379  1.00 63.69           C  
ANISOU 3774  CG  GLU L 316     9325   9634   5240   -361    642    726       C  
ATOM   3775  CD  GLU L 316       9.069 -12.386  -6.036  1.00 70.65           C  
ANISOU 3775  CD  GLU L 316     9727  11727   5390   -283    743    418       C  
ATOM   3776  OE1 GLU L 316       9.582 -11.323  -5.618  1.00 71.87           O  
ANISOU 3776  OE1 GLU L 316     9856  11885   5565    224    678   -211       O  
ATOM   3777  OE2 GLU L 316       8.194 -12.997  -5.382  1.00 80.47           O  
ANISOU 3777  OE2 GLU L 316    10568  14035   5971   -760    820    806       O  
ATOM   3778  N   ILE L 317      11.639 -10.652 -10.931  1.00 46.22           N  
ANISOU 3778  N   ILE L 317     7652   5204   4703    514    391     58       N  
ATOM   3779  CA  ILE L 317      11.684  -9.669 -12.011  1.00 45.28           C  
ANISOU 3779  CA  ILE L 317     7524   4763   4914    564    231    -11       C  
ATOM   3780  C   ILE L 317      11.714 -10.363 -13.373  1.00 41.56           C  
ANISOU 3780  C   ILE L 317     7025   4214   4551    459    363    241       C  
ATOM   3781  O   ILE L 317      10.919 -10.063 -14.231  1.00 40.15           O  
ANISOU 3781  O   ILE L 317     6793   3974   4488    448    378    217       O  
ATOM   3782  CB  ILE L 317      12.910  -8.753 -11.898  1.00 49.81           C  
ANISOU 3782  CB  ILE L 317     8144   5122   5658    498   -108     40       C  
ATOM   3783  CG1 ILE L 317      12.826  -7.925 -10.632  1.00 54.75           C  
ANISOU 3783  CG1 ILE L 317     8839   5742   6221    696   -382   -369       C  
ATOM   3784  CG2 ILE L 317      12.971  -7.796 -13.083  1.00 51.94           C  
ANISOU 3784  CG2 ILE L 317     8393   5100   6239    317   -422    223       C  
ATOM   3785  CD1 ILE L 317      14.179  -7.497 -10.109  1.00 58.67           C  
ANISOU 3785  CD1 ILE L 317     9406   6117   6769    551   -687   -254       C  
ATOM   3786  N   LEU L 318      12.629 -11.314 -13.550  1.00 40.84           N  
ANISOU 3786  N   LEU L 318     6944   4178   4394    469    398    394       N  
ATOM   3787  CA  LEU L 318      12.743 -12.035 -14.801  1.00 39.14           C  
ANISOU 3787  CA  LEU L 318     6649   4024   4196    542    440    427       C  
ATOM   3788  C   LEU L 318      11.474 -12.858 -15.122  1.00 39.27           C  
ANISOU 3788  C   LEU L 318     6798   3882   4239    511    512    391       C  
ATOM   3789  O   LEU L 318      11.069 -12.937 -16.266  1.00 39.50           O  
ANISOU 3789  O   LEU L 318     6743   3953   4310    534    547    345       O  
ATOM   3790  CB  LEU L 318      13.996 -12.914 -14.798  1.00 40.57           C  
ANISOU 3790  CB  LEU L 318     6778   4358   4278    778    325    384       C  
ATOM   3791  CG  LEU L 318      15.302 -12.127 -14.698  1.00 42.19           C  
ANISOU 3791  CG  LEU L 318     6706   4946   4375    724    256    492       C  
ATOM   3792  CD1 LEU L 318      16.474 -13.071 -14.535  1.00 45.65           C  
ANISOU 3792  CD1 LEU L 318     7023   5653   4666   1088    125    348       C  
ATOM   3793  CD2 LEU L 318      15.543 -11.229 -15.905  1.00 43.91           C  
ANISOU 3793  CD2 LEU L 318     6558   5615   4509    486    248    683       C  
ATOM   3794  N   LYS L 319      10.849 -13.430 -14.108  1.00 41.40           N  
ANISOU 3794  N   LYS L 319     7221   4088   4420    367    494    483       N  
ATOM   3795  CA  LYS L 319       9.571 -14.164 -14.246  1.00 44.35           C  
ANISOU 3795  CA  LYS L 319     7660   4433   4756    131    483    609       C  
ATOM   3796  C   LYS L 319       8.449 -13.266 -14.748  1.00 43.13           C  
ANISOU 3796  C   LYS L 319     7281   4516   4590    105    689    484       C  
ATOM   3797  O   LYS L 319       7.704 -13.611 -15.674  1.00 43.42           O  
ANISOU 3797  O   LYS L 319     7304   4495   4699     30    693    499       O  
ATOM   3798  CB  LYS L 319       9.156 -14.745 -12.902  1.00 46.11           C  
ANISOU 3798  CB  LYS L 319     7933   4860   4726   -211    391    910       C  
ATOM   3799  CG  LYS L 319       7.809 -15.443 -12.893  1.00 52.86           C  
ANISOU 3799  CG  LYS L 319     8741   5916   5428   -676    319   1223       C  
ATOM   3800  CD  LYS L 319       7.421 -15.844 -11.463  1.00 57.49           C  
ANISOU 3800  CD  LYS L 319     9192   7088   5563  -1179    235   1669       C  
ATOM   3801  CE  LYS L 319       6.562 -17.090 -11.436  1.00 63.47           C  
ANISOU 3801  CE  LYS L 319    10061   7817   6237  -1900   -170   2311       C  
ATOM   3802  NZ  LYS L 319       5.378 -16.950 -12.319  1.00 65.24           N  
ANISOU 3802  NZ  LYS L 319    10064   8267   6456  -2019    -11   2236       N  
ATOM   3803  N   LYS L 320       8.360 -12.100 -14.140  1.00 43.23           N  
ANISOU 3803  N   LYS L 320     7134   4752   4537    237    758    293       N  
ATOM   3804  CA  LYS L 320       7.355 -11.127 -14.507  1.00 45.13           C  
ANISOU 3804  CA  LYS L 320     7178   5147   4823    379    782     54       C  
ATOM   3805  C   LYS L 320       7.477 -10.743 -15.986  1.00 42.66           C  
ANISOU 3805  C   LYS L 320     6896   4512   4798    401    701    115       C  
ATOM   3806  O   LYS L 320       6.456 -10.549 -16.689  1.00 43.21           O  
ANISOU 3806  O   LYS L 320     6848   4651   4916    410    717     66       O  
ATOM   3807  CB  LYS L 320       7.499  -9.896 -13.583  1.00 47.46           C  
ANISOU 3807  CB  LYS L 320     7392   5549   5090    685    616   -321       C  
ATOM   3808  CG  LYS L 320       6.461  -8.809 -13.780  1.00 53.61           C  
ANISOU 3808  CG  LYS L 320     7988   6422   5959   1041    427   -753       C  
ATOM   3809  CD  LYS L 320       6.480  -7.809 -12.612  1.00 62.28           C  
ANISOU 3809  CD  LYS L 320     9000   7715   6949   1505    132  -1347       C  
ATOM   3810  CE  LYS L 320       5.108  -7.183 -12.378  1.00 71.08           C  
ANISOU 3810  CE  LYS L 320     9733   9401   7870   2040      7  -1991       C  
ATOM   3811  NZ  LYS L 320       4.512  -6.691 -13.657  1.00 73.36           N  
ANISOU 3811  NZ  LYS L 320    10093   9188   8590   2129   -233  -1954       N  
ATOM   3812  N   LEU L 321       8.722 -10.615 -16.453  1.00 39.43           N  
ANISOU 3812  N   LEU L 321     6559   3927   4494    375    600    255       N  
ATOM   3813  CA  LEU L 321       8.975 -10.191 -17.830  1.00 40.78           C  
ANISOU 3813  CA  LEU L 321     6624   4103   4767    282    501    422       C  
ATOM   3814  C   LEU L 321       8.655 -11.336 -18.754  1.00 40.93           C  
ANISOU 3814  C   LEU L 321     6609   4272   4669    285    657    408       C  
ATOM   3815  O   LEU L 321       8.012 -11.130 -19.790  1.00 39.64           O  
ANISOU 3815  O   LEU L 321     6335   4199   4525    219    648    454       O  
ATOM   3816  CB  LEU L 321      10.436  -9.808 -18.056  1.00 40.82           C  
ANISOU 3816  CB  LEU L 321     6527   4254   4726    159    353    644       C  
ATOM   3817  CG  LEU L 321      11.071  -8.700 -17.226  1.00 42.80           C  
ANISOU 3817  CG  LEU L 321     6858   4276   5128     61     31    721       C  
ATOM   3818  CD1 LEU L 321      12.536  -8.605 -17.590  1.00 45.41           C  
ANISOU 3818  CD1 LEU L 321     6962   4999   5291   -190    -73   1058       C  
ATOM   3819  CD2 LEU L 321      10.370  -7.362 -17.447  1.00 45.87           C  
ANISOU 3819  CD2 LEU L 321     7344   4243   5838     -8   -429    751       C  
ATOM   3820  N   ASN L 322       9.138 -12.529 -18.386  1.00 40.79           N  
ANISOU 3820  N   ASN L 322     6721   4217   4560    387    674    320       N  
ATOM   3821  CA  ASN L 322       8.884 -13.735 -19.162  1.00 42.11           C  
ANISOU 3821  CA  ASN L 322     6967   4338   4692    484    592    176       C  
ATOM   3822  C   ASN L 322       7.380 -13.983 -19.272  1.00 43.65           C  
ANISOU 3822  C   ASN L 322     7230   4405   4949    257    617    239       C  
ATOM   3823  O   ASN L 322       6.862 -14.130 -20.361  1.00 42.26           O  
ANISOU 3823  O   ASN L 322     6978   4312   4765    258    597    163       O  
ATOM   3824  CB  ASN L 322       9.555 -14.970 -18.537  1.00 43.93           C  
ANISOU 3824  CB  ASN L 322     7455   4287   4947    663    336     61       C  
ATOM   3825  CG  ASN L 322       9.592 -16.149 -19.492  1.00 47.06           C  
ANISOU 3825  CG  ASN L 322     7972   4535   5373    958      1   -278       C  
ATOM   3826  OD1 ASN L 322       9.875 -15.983 -20.682  1.00 45.13           O  
ANISOU 3826  OD1 ASN L 322     7440   4755   4952   1210     59   -546       O  
ATOM   3827  ND2 ASN L 322       9.334 -17.344 -18.982  1.00 48.84           N  
ANISOU 3827  ND2 ASN L 322     8611   4151   5792    916   -463   -268       N  
ATOM   3828  N   ASP L 323       6.669 -14.006 -18.147  1.00 45.87           N  
ANISOU 3828  N   ASP L 323     7558   4673   5195     38    661    388       N  
ATOM   3829  CA  ASP L 323       5.222 -14.253 -18.220  1.00 48.41           C  
ANISOU 3829  CA  ASP L 323     7785   5156   5451   -244    687    501       C  
ATOM   3830  C   ASP L 323       4.538 -13.188 -19.105  1.00 45.32           C  
ANISOU 3830  C   ASP L 323     7139   4970   5110   -116    825    375       C  
ATOM   3831  O   ASP L 323       3.609 -13.490 -19.859  1.00 41.25           O  
ANISOU 3831  O   ASP L 323     6546   4537   4590   -253    804    401       O  
ATOM   3832  CB  ASP L 323       4.595 -14.286 -16.834  1.00 52.12           C  
ANISOU 3832  CB  ASP L 323     8113   6022   5666   -514    753    691       C  
ATOM   3833  CG  ASP L 323       5.046 -15.493 -15.992  1.00 57.29           C  
ANISOU 3833  CG  ASP L 323     9046   6457   6262   -846    464   1029       C  
ATOM   3834  OD1 ASP L 323       5.189 -16.625 -16.508  1.00 62.86           O  
ANISOU 3834  OD1 ASP L 323    10093   6619   7171   -992     57   1152       O  
ATOM   3835  OD2 ASP L 323       5.219 -15.300 -14.773  1.00 63.84           O  
ANISOU 3835  OD2 ASP L 323     9761   7656   6839   -952    536   1157       O  
ATOM   3836  N   SER L 324       5.020 -11.950 -19.025  1.00 42.05           N  
ANISOU 3836  N   SER L 324     6633   4558   4783    107    837    279       N  
ATOM   3837  CA  SER L 324       4.423 -10.868 -19.807  1.00 42.91           C  
ANISOU 3837  CA  SER L 324     6582   4694   5028    210    744    235       C  
ATOM   3838  C   SER L 324       4.619 -11.066 -21.302  1.00 42.15           C  
ANISOU 3838  C   SER L 324     6460   4611   4944    104    700    377       C  
ATOM   3839  O   SER L 324       3.693 -10.845 -22.104  1.00 42.22           O  
ANISOU 3839  O   SER L 324     6340   4717   4981     63    657    401       O  
ATOM   3840  CB  SER L 324       5.041  -9.540 -19.421  1.00 45.84           C  
ANISOU 3840  CB  SER L 324     6984   4846   5586    385    490    184       C  
ATOM   3841  OG  SER L 324       4.267  -8.498 -19.924  1.00 52.07           O  
ANISOU 3841  OG  SER L 324     7688   5514   6583    528    190    114       O  
ATOM   3842  N   LEU L 325       5.824 -11.481 -21.682  1.00 39.19           N  
ANISOU 3842  N   LEU L 325     6123   4300   4467    102    699    425       N  
ATOM   3843  CA  LEU L 325       6.111 -11.767 -23.099  1.00 40.35           C  
ANISOU 3843  CA  LEU L 325     6099   4802   4427     75    672    451       C  
ATOM   3844  C   LEU L 325       5.286 -12.933 -23.623  1.00 39.67           C  
ANISOU 3844  C   LEU L 325     6097   4685   4288    112    675    220       C  
ATOM   3845  O   LEU L 325       4.772 -12.883 -24.729  1.00 42.10           O  
ANISOU 3845  O   LEU L 325     6250   5252   4492     56    644    221       O  
ATOM   3846  CB  LEU L 325       7.609 -11.975 -23.327  1.00 40.97           C  
ANISOU 3846  CB  LEU L 325     6026   5283   4259    178    661    428       C  
ATOM   3847  CG  LEU L 325       8.477 -10.734 -23.118  1.00 40.31           C  
ANISOU 3847  CG  LEU L 325     5785   5351   4179    -60    536    822       C  
ATOM   3848  CD1 LEU L 325       9.940 -11.128 -22.973  1.00 41.64           C  
ANISOU 3848  CD1 LEU L 325     5747   6018   4054     59    571    758       C  
ATOM   3849  CD2 LEU L 325       8.308  -9.775 -24.295  1.00 41.65           C  
ANISOU 3849  CD2 LEU L 325     5675   5908   4241   -433    332   1272       C  
ATOM   3850  N   GLU L 326       5.092 -13.948 -22.798  1.00 40.88           N  
ANISOU 3850  N   GLU L 326     6516   4489   4524    117    612     98       N  
ATOM   3851  CA  GLU L 326       4.278 -15.099 -23.179  1.00 44.65           C  
ANISOU 3851  CA  GLU L 326     7169   4761   5036     10    399    -22       C  
ATOM   3852  C   GLU L 326       2.824 -14.701 -23.380  1.00 44.42           C  
ANISOU 3852  C   GLU L 326     6976   4875   5025   -280    494    165       C  
ATOM   3853  O   GLU L 326       2.176 -15.168 -24.330  1.00 47.02           O  
ANISOU 3853  O   GLU L 326     7291   5249   5323   -361    355     77       O  
ATOM   3854  CB  GLU L 326       4.401 -16.214 -22.151  1.00 47.18           C  
ANISOU 3854  CB  GLU L 326     7847   4598   5479   -109    107     21       C  
ATOM   3855  CG  GLU L 326       5.813 -16.770 -22.056  1.00 50.90           C  
ANISOU 3855  CG  GLU L 326     8489   4886   5963    315   -119   -278       C  
ATOM   3856  CD  GLU L 326       5.884 -18.051 -21.227  1.00 56.46           C  
ANISOU 3856  CD  GLU L 326     9662   4907   6884    193   -679   -211       C  
ATOM   3857  OE1 GLU L 326       5.102 -18.177 -20.262  1.00 57.37           O  
ANISOU 3857  OE1 GLU L 326     9864   4905   7027   -370   -707    286       O  
ATOM   3858  OE2 GLU L 326       6.726 -18.918 -21.537  1.00 60.23           O  
ANISOU 3858  OE2 GLU L 326    10375   5048   7461    667  -1171   -650       O  
ATOM   3859  N   LEU L 327       2.325 -13.824 -22.518  1.00 41.38           N  
ANISOU 3859  N   LEU L 327     6421   4644   4655   -349    682    327       N  
ATOM   3860  CA  LEU L 327       0.983 -13.274 -22.693  1.00 44.00           C  
ANISOU 3860  CA  LEU L 327     6466   5291   4957   -448    748    385       C  
ATOM   3861  C   LEU L 327       0.838 -12.484 -24.014  1.00 44.44           C  
ANISOU 3861  C   LEU L 327     6379   5435   5071   -315    699    370       C  
ATOM   3862  O   LEU L 327      -0.116 -12.705 -24.762  1.00 47.62           O  
ANISOU 3862  O   LEU L 327     6651   6012   5430   -445    651    387       O  
ATOM   3863  CB  LEU L 327       0.545 -12.443 -21.465  1.00 43.33           C  
ANISOU 3863  CB  LEU L 327     6142   5514   4804   -319    867    335       C  
ATOM   3864  CG  LEU L 327      -0.896 -11.893 -21.453  1.00 45.01           C  
ANISOU 3864  CG  LEU L 327     5919   6284   4898   -244    891    233       C  
ATOM   3865  CD1 LEU L 327      -1.919 -13.013 -21.568  1.00 47.79           C  
ANISOU 3865  CD1 LEU L 327     6112   7025   5020   -761    900    477       C  
ATOM   3866  CD2 LEU L 327      -1.167 -11.058 -20.210  1.00 47.81           C  
ANISOU 3866  CD2 LEU L 327     5965   7106   5092    119    931    -65       C  
ATOM   3867  N   SER L 328       1.776 -11.595 -24.325  1.00 45.60           N  
ANISOU 3867  N   SER L 328     6526   5516   5280   -165    641    437       N  
ATOM   3868  CA  SER L 328       1.696 -10.841 -25.583  1.00 46.20           C  
ANISOU 3868  CA  SER L 328     6441   5762   5348   -217    480    625       C  
ATOM   3869  C   SER L 328       1.689 -11.771 -26.796  1.00 46.63           C  
ANISOU 3869  C   SER L 328     6433   6145   5138   -314    508    542       C  
ATOM   3870  O   SER L 328       1.165 -11.405 -27.822  1.00 47.90           O  
ANISOU 3870  O   SER L 328     6413   6569   5217   -417    404    683       O  
ATOM   3871  CB  SER L 328       2.880  -9.871 -25.763  1.00 47.03           C  
ANISOU 3871  CB  SER L 328     6527   5865   5476   -282    290    915       C  
ATOM   3872  OG  SER L 328       3.111  -9.087 -24.625  1.00 51.44           O  
ANISOU 3872  OG  SER L 328     7223   6024   6298   -148    146    892       O  
ATOM   3873  N   ASP L 329       2.328 -12.937 -26.699  1.00 48.77           N  
ANISOU 3873  N   ASP L 329     6860   6394   5276   -215    544    261       N  
ATOM   3874  CA  ASP L 329       2.316 -13.928 -27.790  1.00 52.44           C  
ANISOU 3874  CA  ASP L 329     7304   7120   5499   -128    415    -58       C  
ATOM   3875  C   ASP L 329       0.969 -14.582 -28.046  1.00 50.93           C  
ANISOU 3875  C   ASP L 329     7210   6729   5410   -320    278   -126       C  
ATOM   3876  O   ASP L 329       0.713 -14.967 -29.165  1.00 54.55           O  
ANISOU 3876  O   ASP L 329     7576   7479   5670   -284    135   -333       O  
ATOM   3877  CB  ASP L 329       3.287 -15.075 -27.507  1.00 55.67           C  
ANISOU 3877  CB  ASP L 329     7935   7366   5848    189    253   -502       C  
ATOM   3878  CG  ASP L 329       4.721 -14.709 -27.750  1.00 58.64           C  
ANISOU 3878  CG  ASP L 329     8035   8338   5907    453    346   -587       C  
ATOM   3879  OD1 ASP L 329       5.025 -14.031 -28.754  1.00 63.55           O  
ANISOU 3879  OD1 ASP L 329     8220   9784   6142    378    430   -426       O  
ATOM   3880  OD2 ASP L 329       5.557 -15.144 -26.941  1.00 63.91           O  
ANISOU 3880  OD2 ASP L 329     8870   8755   6654    682    291   -761       O  
ATOM   3881  N   VAL L 330       0.140 -14.758 -27.018  1.00 49.50           N  
ANISOU 3881  N   VAL L 330     7148   6210   5448   -559    290     48       N  
ATOM   3882  CA  VAL L 330      -1.103 -15.546 -27.145  1.00 51.33           C  
ANISOU 3882  CA  VAL L 330     7423   6359   5719   -907     83     93       C  
ATOM   3883  C   VAL L 330      -2.387 -14.716 -27.219  1.00 50.13           C  
ANISOU 3883  C   VAL L 330     6889   6612   5544  -1076    244    336       C  
ATOM   3884  O   VAL L 330      -3.416 -15.244 -27.600  1.00 53.58           O  
ANISOU 3884  O   VAL L 330     7243   7177   5938  -1386     83    400       O  
ATOM   3885  CB  VAL L 330      -1.257 -16.630 -26.035  1.00 53.20           C  
ANISOU 3885  CB  VAL L 330     7963   6166   6081  -1257   -181    236       C  
ATOM   3886  CG1 VAL L 330      -0.210 -17.717 -26.199  1.00 56.09           C  
ANISOU 3886  CG1 VAL L 330     8791   5961   6559  -1017   -627   -122       C  
ATOM   3887  CG2 VAL L 330      -1.169 -16.039 -24.639  1.00 51.64           C  
ANISOU 3887  CG2 VAL L 330     7627   6128   5863  -1321    109    501       C  
ATOM   3888  N   VAL L 331      -2.331 -13.433 -26.866  1.00 47.15           N  
ANISOU 3888  N   VAL L 331     6286   6409   5219   -834    443    426       N  
ATOM   3889  CA  VAL L 331      -3.493 -12.559 -26.972  1.00 47.05           C  
ANISOU 3889  CA  VAL L 331     5899   6753   5224   -769    449    496       C  
ATOM   3890  C   VAL L 331      -3.566 -11.998 -28.399  1.00 49.06           C  
ANISOU 3890  C   VAL L 331     6069   7096   5475   -706    296    571       C  
ATOM   3891  O   VAL L 331      -2.662 -11.272 -28.813  1.00 47.79           O  
ANISOU 3891  O   VAL L 331     5975   6830   5351   -584    218    692       O  
ATOM   3892  CB  VAL L 331      -3.382 -11.366 -26.016  1.00 45.97           C  
ANISOU 3892  CB  VAL L 331     5625   6622   5218   -387    477    417       C  
ATOM   3893  CG1 VAL L 331      -4.530 -10.388 -26.232  1.00 48.78           C  
ANISOU 3893  CG1 VAL L 331     5598   7293   5641    -90    299    316       C  
ATOM   3894  CG2 VAL L 331      -3.348 -11.838 -24.570  1.00 47.50           C  
ANISOU 3894  CG2 VAL L 331     5785   6987   5276   -455    653    352       C  
ATOM   3895  N   PRO L 332      -4.638 -12.312 -29.144  1.00 56.82           N  
ANISOU 3895  N   PRO L 332     9263   6574   5751   -313   -251    543       N  
ATOM   3896  CA  PRO L 332      -4.772 -11.739 -30.478  1.00 61.88           C  
ANISOU 3896  CA  PRO L 332    10013   7617   5880   -209   -672    413       C  
ATOM   3897  C   PRO L 332      -4.841 -10.212 -30.456  1.00 61.30           C  
ANISOU 3897  C   PRO L 332    10006   7674   5609     49   -993    878       C  
ATOM   3898  O   PRO L 332      -5.299  -9.625 -29.462  1.00 60.71           O  
ANISOU 3898  O   PRO L 332     9746   7445   5874     77  -1057    975       O  
ATOM   3899  CB  PRO L 332      -6.093 -12.326 -30.979  1.00 66.85           C  
ANISOU 3899  CB  PRO L 332    10308   8518   6572   -423   -927   -347       C  
ATOM   3900  CG  PRO L 332      -6.232 -13.608 -30.235  1.00 67.63           C  
ANISOU 3900  CG  PRO L 332    10364   8021   7311   -840   -347   -667       C  
ATOM   3901  CD  PRO L 332      -5.689 -13.306 -28.871  1.00 61.73           C  
ANISOU 3901  CD  PRO L 332     9683   6942   6829   -646    -45     42       C  
ATOM   3902  N   ALA L 333      -4.357  -9.590 -31.529  1.00 63.71           N  
ANISOU 3902  N   ALA L 333    10644   8186   5376    263  -1074   1182       N  
ATOM   3903  CA  ALA L 333      -4.356  -8.135 -31.679  1.00 66.02           C  
ANISOU 3903  CA  ALA L 333    11239   8323   5522    541  -1154   1742       C  
ATOM   3904  C   ALA L 333      -5.773  -7.555 -31.585  1.00 69.80           C  
ANISOU 3904  C   ALA L 333    11536   8969   6015    991  -1616   1651       C  
ATOM   3905  O   ALA L 333      -5.999  -6.508 -30.971  1.00 69.83           O  
ANISOU 3905  O   ALA L 333    11684   8544   6303   1192  -1590   1939       O  
ATOM   3906  CB  ALA L 333      -3.742  -7.774 -33.009  1.00 72.38           C  
ANISOU 3906  CB  ALA L 333    12487   9372   5639    765  -1035   2167       C  
ATOM   3907  N   SER L 334      -6.728  -8.253 -32.195  1.00 74.73           N  
ANISOU 3907  N   SER L 334    11769  10296   6327   1152  -2015   1118       N  
ATOM   3908  CA  SER L 334      -8.149  -7.895 -32.091  1.00 79.53           C  
ANISOU 3908  CA  SER L 334    11909  11427   6882   1603  -2501    841       C  
ATOM   3909  C   SER L 334      -8.705  -7.974 -30.667  1.00 75.26           C  
ANISOU 3909  C   SER L 334    10940  10561   7091   1304  -2403    575       C  
ATOM   3910  O   SER L 334      -9.805  -7.502 -30.400  1.00 79.66           O  
ANISOU 3910  O   SER L 334    11080  11521   7665   1726  -2725    406       O  
ATOM   3911  CB  SER L 334      -8.988  -8.798 -32.977  1.00 86.48           C  
ANISOU 3911  CB  SER L 334    12197  13370   7291   1592  -2914      8       C  
ATOM   3912  OG  SER L 334     -10.361  -8.519 -32.793  1.00 92.53           O  
ANISOU 3912  OG  SER L 334    12260  14894   8003   1977  -3383   -396       O  
ATOM   3913  N   ASP L 335      -7.968  -8.600 -29.760  1.00 68.07           N  
ANISOU 3913  N   ASP L 335    10080   9091   6690    704  -1945    552       N  
ATOM   3914  CA  ASP L 335      -8.372  -8.632 -28.375  1.00 64.12           C  
ANISOU 3914  CA  ASP L 335     9241   8389   6731    525  -1768    438       C  
ATOM   3915  C   ASP L 335      -7.548  -7.634 -27.558  1.00 59.52           C  
ANISOU 3915  C   ASP L 335     9008   7290   6315    622  -1554    872       C  
ATOM   3916  O   ASP L 335      -8.110  -6.896 -26.741  1.00 59.61           O  
ANISOU 3916  O   ASP L 335     8855   7249   6544    858  -1616    813       O  
ATOM   3917  CB  ASP L 335      -8.286 -10.059 -27.855  1.00 63.13           C  
ANISOU 3917  CB  ASP L 335     8895   8130   6958    -54  -1340    127       C  
ATOM   3918  CG  ASP L 335      -9.272 -10.980 -28.550  1.00 70.23           C  
ANISOU 3918  CG  ASP L 335     9350   9451   7880   -386  -1451   -599       C  
ATOM   3919  OD1 ASP L 335      -9.280 -11.024 -29.802  1.00 76.70           O  
ANISOU 3919  OD1 ASP L 335    10224  10690   8227   -268  -1780   -866       O  
ATOM   3920  OD2 ASP L 335     -10.054 -11.651 -27.854  1.00 72.75           O  
ANISOU 3920  OD2 ASP L 335     9213   9773   8656   -811  -1163   -974       O  
ATOM   3921  N   ALA L 336      -6.244  -7.581 -27.830  1.00 56.89           N  
ANISOU 3921  N   ALA L 336     9077   6676   5860    418  -1288   1169       N  
ATOM   3922  CA  ALA L 336      -5.309  -6.634 -27.199  1.00 56.19           C  
ANISOU 3922  CA  ALA L 336     9208   6216   5924    287  -1031   1354       C  
ATOM   3923  C   ALA L 336      -5.729  -5.162 -27.202  1.00 61.81           C  
ANISOU 3923  C   ALA L 336    10253   6451   6778    603  -1092   1481       C  
ATOM   3924  O   ALA L 336      -5.774  -4.547 -26.147  1.00 62.18           O  
ANISOU 3924  O   ALA L 336    10182   6294   7150    549   -985   1222       O  
ATOM   3925  CB  ALA L 336      -3.935  -6.765 -27.834  1.00 55.37           C  
ANISOU 3925  CB  ALA L 336     9369   6076   5590    -10   -734   1589       C  
ATOM   3926  N   GLU L 337      -6.000  -4.574 -28.370  1.00 71.23           N  
ANISOU 3926  N   GLU L 337    11923   7455   7685   1028  -1192   1890       N  
ATOM   3927  CA  GLU L 337      -6.338  -3.135 -28.423  1.00 78.32           C  
ANISOU 3927  CA  GLU L 337    13367   7636   8753   1508  -1063   2192       C  
ATOM   3928  C   GLU L 337      -7.714  -2.878 -27.835  1.00 79.40           C  
ANISOU 3928  C   GLU L 337    13150   7999   9018   2163  -1426   1911       C  
ATOM   3929  O   GLU L 337      -7.963  -1.800 -27.296  1.00 85.24           O  
ANISOU 3929  O   GLU L 337    14202   8073  10112   2489  -1239   1888       O  
ATOM   3930  CB  GLU L 337      -6.283  -2.557 -29.844  1.00 88.56           C  
ANISOU 3930  CB  GLU L 337    15375   8707   9565   2053   -964   2946       C  
ATOM   3931  CG  GLU L 337      -6.363  -1.017 -29.891  1.00 98.17           C  
ANISOU 3931  CG  GLU L 337    17452   8773  11075   2534   -509   3459       C  
ATOM   3932  CD  GLU L 337      -7.363  -0.479 -30.914  1.00109.90           C  
ANISOU 3932  CD  GLU L 337    19377  10432  11948   3897   -745   4179       C  
ATOM   3933  OE1 GLU L 337      -8.088  -1.297 -31.529  1.00111.33           O  
ANISOU 3933  OE1 GLU L 337    18978  11883  11437   4395  -1397   4060       O  
ATOM   3934  OE2 GLU L 337      -7.425   0.763 -31.108  1.00116.70           O  
ANISOU 3934  OE2 GLU L 337    21158  10190  12993   4518   -232   4829       O  
ATOM   3935  N   LYS L 338      -8.605  -3.856 -27.952  1.00 76.54           N  
ANISOU 3935  N   LYS L 338    12113   8562   8405   2314  -1869   1608       N  
ATOM   3936  CA  LYS L 338      -9.880  -3.802 -27.261  1.00 79.04           C  
ANISOU 3936  CA  LYS L 338    11824   9351   8857   2755  -2153   1204       C  
ATOM   3937  C   LYS L 338      -9.645  -3.715 -25.743  1.00 75.14           C  
ANISOU 3937  C   LYS L 338    11096   8590   8861   2323  -1858    818       C  
ATOM   3938  O   LYS L 338     -10.279  -2.893 -25.075  1.00 79.74           O  
ANISOU 3938  O   LYS L 338    11622   9022   9650   2816  -1858    622       O  
ATOM   3939  CB  LYS L 338     -10.744  -5.007 -27.649  1.00 80.26           C  
ANISOU 3939  CB  LYS L 338    11174  10575   8747   2632  -2522    775       C  
ATOM   3940  CG  LYS L 338     -12.168  -4.973 -27.109  1.00 85.53           C  
ANISOU 3940  CG  LYS L 338    11014  12001   9481   3054  -2798    301       C  
ATOM   3941  CD  LYS L 338     -13.206  -5.307 -28.181  1.00 93.81           C  
ANISOU 3941  CD  LYS L 338    11428  14244   9969   3527  -3342     -6       C  
ATOM   3942  CE  LYS L 338     -13.078  -6.730 -28.718  1.00 92.59           C  
ANISOU 3942  CE  LYS L 338    10865  14567   9748   2599  -3336   -530       C  
ATOM   3943  NZ  LYS L 338     -13.754  -6.886 -30.039  1.00101.09           N  
ANISOU 3943  NZ  LYS L 338    11473  16870  10065   3085  -3913   -887       N  
ATOM   3944  N   TYR L 339      -8.711  -4.518 -25.211  1.00 67.34           N  
ANISOU 3944  N   TYR L 339     9983   7637   7966   1562  -1594    711       N  
ATOM   3945  CA  TYR L 339      -8.344  -4.432 -23.782  1.00 64.01           C  
ANISOU 3945  CA  TYR L 339     9303   7243   7772   1280  -1331    372       C  
ATOM   3946  C   TYR L 339      -7.596  -3.131 -23.446  1.00 67.00           C  
ANISOU 3946  C   TYR L 339    10160   6910   8387   1204  -1084    221       C  
ATOM   3947  O   TYR L 339      -7.760  -2.603 -22.349  1.00 67.09           O  
ANISOU 3947  O   TYR L 339     9961   6960   8567   1263   -981   -269       O  
ATOM   3948  CB  TYR L 339      -7.449  -5.598 -23.317  1.00 57.87           C  
ANISOU 3948  CB  TYR L 339     8282   6834   6869    747  -1086    410       C  
ATOM   3949  CG  TYR L 339      -8.085  -6.952 -23.151  1.00 55.20           C  
ANISOU 3949  CG  TYR L 339     7520   6955   6499    646  -1013    440       C  
ATOM   3950  CD1 TYR L 339      -9.020  -7.195 -22.167  1.00 56.63           C  
ANISOU 3950  CD1 TYR L 339     7195   7550   6771    758   -904    244       C  
ATOM   3951  CD2 TYR L 339      -7.677  -8.018 -23.947  1.00 54.73           C  
ANISOU 3951  CD2 TYR L 339     7602   6836   6355    372   -908    630       C  
ATOM   3952  CE1 TYR L 339      -9.563  -8.452 -22.001  1.00 57.68           C  
ANISOU 3952  CE1 TYR L 339     7010   7911   6995    492   -607    297       C  
ATOM   3953  CE2 TYR L 339      -8.220  -9.275 -23.801  1.00 55.97           C  
ANISOU 3953  CE2 TYR L 339     7496   7124   6644    143   -645    578       C  
ATOM   3954  CZ  TYR L 339      -9.153  -9.488 -22.830  1.00 57.25           C  
ANISOU 3954  CZ  TYR L 339     7197   7576   6979    145   -448    445       C  
ATOM   3955  OH  TYR L 339      -9.667 -10.738 -22.726  1.00 59.96           O  
ANISOU 3955  OH  TYR L 339     7358   7856   7567   -241     10    412       O  
ATOM   3956  N   ARG L 340      -6.756  -2.634 -24.356  1.00 69.30           N  
ANISOU 3956  N   ARG L 340    11065   6564   8700    985   -895    551       N  
ATOM   3957  CA  ARG L 340      -6.029  -1.361 -24.114  1.00 77.29           C  
ANISOU 3957  CA  ARG L 340    12585   6678  10103    677   -461    318       C  
ATOM   3958  C   ARG L 340      -6.950  -0.122 -23.983  1.00 85.80           C  
ANISOU 3958  C   ARG L 340    14143   6920  11534   1375   -371    232       C  
ATOM   3959  O   ARG L 340      -6.467   1.014 -23.954  1.00 93.85           O  
ANISOU 3959  O   ARG L 340    15811   6832  13015   1149    142     73       O  
ATOM   3960  CB  ARG L 340      -4.937  -1.116 -25.179  1.00 79.58           C  
ANISOU 3960  CB  ARG L 340    13440   6421  10373    196    -91    778       C  
ATOM   3961  CG  ARG L 340      -3.718  -2.033 -25.048  1.00 75.27           C  
ANISOU 3961  CG  ARG L 340    12392   6627   9580   -530    -11    627       C  
ATOM   3962  CD  ARG L 340      -2.657  -1.747 -26.111  1.00 79.77           C  
ANISOU 3962  CD  ARG L 340    13419   6782  10105  -1022    428   1041       C  
ATOM   3963  NE  ARG L 340      -1.638  -2.809 -26.242  1.00 75.96           N  
ANISOU 3963  NE  ARG L 340    12413   7207   9238  -1412    427   1022       N  
ATOM   3964  CZ  ARG L 340      -0.527  -2.922 -25.496  1.00 76.55           C  
ANISOU 3964  CZ  ARG L 340    11871   7904   9307  -2025    631    457       C  
ATOM   3965  NH1 ARG L 340      -0.259  -2.044 -24.525  1.00 81.77           N  
ANISOU 3965  NH1 ARG L 340    12290   8441  10335  -2510    836   -312       N  
ATOM   3966  NH2 ARG L 340       0.331  -3.920 -25.720  1.00 70.78           N  
ANISOU 3966  NH2 ARG L 340    10699   8047   8147  -2089    632    561       N  
ATOM   3967  N   GLN L 341      -8.265  -0.347 -23.894  1.00 85.89           N  
ANISOU 3967  N   GLN L 341    13819   7443  11372   2209   -783    280       N  
ATOM   3968  CA  GLN L 341      -9.243   0.711 -23.700  1.00 95.04           C  
ANISOU 3968  CA  GLN L 341    15291   8048  12769   3138   -744    184       C  
ATOM   3969  C   GLN L 341     -10.290   0.287 -22.666  1.00 92.88           C  
ANISOU 3969  C   GLN L 341    14118   8777  12393   3509  -1062   -372       C  
ATOM   3970  O   GLN L 341      -9.960   0.028 -21.504  1.00 88.48           O  
ANISOU 3970  O   GLN L 341    13081   8642  11894   2978   -949   -998       O  
ATOM   3971  CB  GLN L 341      -9.900   1.040 -25.044  1.00101.42           C  
ANISOU 3971  CB  GLN L 341    16625   8639  13271   4152   -908   1037       C  
ATOM   3972  CG  GLN L 341      -8.919   1.586 -26.081  1.00106.04           C  
ANISOU 3972  CG  GLN L 341    18227   8164  13898   3906   -420   1751       C  
ATOM   3973  CD  GLN L 341      -9.425   1.494 -27.511  1.00110.78           C  
ANISOU 3973  CD  GLN L 341    19143   9128  13820   4877   -691   2692       C  
ATOM   3974  OE1 GLN L 341      -9.735   2.511 -28.148  1.00121.95           O  
ANISOU 3974  OE1 GLN L 341    21456   9698  15181   5910   -378   3413       O  
ATOM   3975  NE2 GLN L 341      -9.499   0.273 -28.030  1.00103.12           N  
ANISOU 3975  NE2 GLN L 341    17471   9429  12278   4621  -1216   2678       N  
TER    3976      GLN L 341                                                      
HETATM 3977 ZN    ZN B1343      17.973  48.685 -30.945  1.00 87.13          ZN  
HETATM 3978 ZN    ZN F1344       1.783  34.192  12.113  1.00 81.27          ZN  
HETATM 3979  O   HOH A2001      17.764  47.798  -2.250  1.00 60.56           O  
HETATM 3980  O   HOH A2002      26.673  42.003 -20.556  1.00 41.19           O  
HETATM 3981  O   HOH A2003      23.327  40.703 -26.653  1.00 51.49           O  
HETATM 3982  O   HOH A2004      25.748  41.656 -25.998  1.00 49.26           O  
HETATM 3983  O   HOH A2005      21.688  42.219 -28.951  1.00 45.81           O  
HETATM 3984  O   HOH A2006      24.699  36.796 -25.157  1.00 44.17           O  
HETATM 3985  O   HOH A2007      29.629  35.947 -25.221  1.00 48.88           O  
HETATM 3986  O   HOH A2008      26.983  36.503 -26.569  1.00 65.33           O  
HETATM 3987  O   HOH A2009      13.785  29.058 -22.996  1.00 49.30           O  
HETATM 3988  O   HOH A2010       9.153  25.841  -6.895  1.00 45.27           O  
HETATM 3989  O   HOH A2011       9.843  27.456  -3.866  1.00 39.47           O  
HETATM 3990  O   HOH A2012       8.800  24.796  -1.112  1.00 38.75           O  
HETATM 3991  O   HOH B2001      26.660  33.087  -1.748  1.00 67.89           O  
HETATM 3992  O   HOH B2002      32.554  30.708 -24.704  1.00 48.10           O  
HETATM 3993  O   HOH B2003      40.066  41.930 -26.446  1.00 57.98           O  
HETATM 3994  O   HOH C2001      14.196  22.238 -20.549  1.00 40.89           O  
HETATM 3995  O   HOH C2002      30.909  22.040 -18.892  1.00 48.00           O  
HETATM 3996  O   HOH C2003      32.154  20.998 -22.431  1.00 56.04           O  
HETATM 3997  O   HOH C2004      33.887  35.708 -15.665  1.00 51.24           O  
HETATM 3998  O   HOH C2005      37.155  27.484 -10.954  1.00 45.93           O  
HETATM 3999  O   HOH D2001       4.454  30.446 -16.263  1.00 48.76           O  
HETATM 4000  O   HOH D2002      -4.902  29.818 -17.195  1.00 60.48           O  
HETATM 4001  O   HOH E2001      21.368  22.724  11.827  1.00 47.28           O  
HETATM 4002  O   HOH E2002      20.082  19.547  18.468  1.00 55.27           O  
HETATM 4003  O   HOH E2003      16.827  18.144  15.296  1.00 38.75           O  
HETATM 4004  O   HOH E2004      13.502  21.185  13.830  1.00 42.41           O  
HETATM 4005  O   HOH E2005      23.032  12.147  22.447  1.00 46.63           O  
HETATM 4006  O   HOH E2006      18.694   4.815  14.584  1.00 39.88           O  
HETATM 4007  O   HOH E2007      30.149  11.288   3.705  1.00 48.81           O  
HETATM 4008  O   HOH E2008      24.709  -1.474   0.491  1.00 49.24           O  
HETATM 4009  O   HOH E2009      26.477  -0.569  -2.709  1.00 38.91           O  
HETATM 4010  O   HOH E2010      33.764  -1.715  -0.974  1.00 51.49           O  
HETATM 4011  O   HOH E2011      25.663  -3.308  -5.192  1.00 36.33           O  
HETATM 4012  O   HOH F2001      17.445  22.846   1.220  1.00 57.89           O  
HETATM 4013  O   HOH F2002      10.681  22.193   7.903  1.00 46.46           O  
HETATM 4014  O   HOH F2003       7.583  20.407  11.290  1.00 58.30           O  
HETATM 4015  O   HOH G2001       4.067   1.630   1.333  1.00 58.13           O  
HETATM 4016  O   HOH G2002      14.441   0.757  10.905  1.00 37.26           O  
HETATM 4017  O   HOH G2003       5.115  12.500   4.325  1.00 43.71           O  
HETATM 4018  O   HOH G2004       1.974  11.955   6.616  1.00 68.73           O  
HETATM 4019  O   HOH G2005      10.931  25.662   1.817  1.00 43.26           O  
HETATM 4020  O   HOH H2001      13.246   1.325   4.650  1.00 47.66           O  
HETATM 4021  O   HOH H2002      19.806   2.943   1.847  1.00 37.36           O  
HETATM 4022  O   HOH H2003      38.486  -3.909  10.086  1.00 44.87           O  
HETATM 4023  O   HOH H2004      42.331  -0.955   8.873  1.00 51.67           O  
HETATM 4024  O   HOH I2001      20.844   2.444 -22.181  1.00 47.12           O  
HETATM 4025  O   HOH I2002      21.031  -4.048 -24.646  1.00 51.34           O  
HETATM 4026  O   HOH I2003       3.972   1.990 -19.686  1.00 59.14           O  
HETATM 4027  O   HOH I2004       3.295   3.630 -23.099  1.00 61.94           O  
HETATM 4028  O   HOH I2005       1.894 -11.297 -17.113  1.00 40.29           O  
HETATM 4029  O   HOH I2006      -7.085 -17.503 -13.796  1.00 62.47           O  
HETATM 4030  O   HOH J2001      30.640  -5.820 -17.798  1.00 58.35           O  
HETATM 4031  O   HOH K2001       8.921 -17.522 -22.666  1.00 41.13           O  
HETATM 4032  O   HOH K2002      20.181 -14.816 -31.114  1.00 47.02           O  
HETATM 4033  O   HOH K2003      20.682 -14.604 -11.244  1.00 42.98           O  
HETATM 4034  O   HOH K2004      26.051  -1.318  -8.582  1.00 41.76           O  
HETATM 4035  O   HOH L2001      18.700 -12.317  -6.623  1.00 51.87           O  
HETATM 4036  O   HOH L2002       3.798 -10.464 -16.004  1.00 52.73           O  
HETATM 4037  O   HOH L2003      -0.655  -9.658 -27.892  1.00 50.14           O  
CONECT  325 3977                                                                
CONECT 1930 3978                                                                
CONECT 3977  325                                                                
CONECT 3978 1930                                                                
MASTER     1067    0    2   24   12    0    2    6 4025   12    4   48          
END                                                                             



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