CNRS Nantes University US2B US2B
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***  pnuc_transporter  ***

elNémo ID: 2309111737544005399

Job options:

ID        	=	 2309111737544005399
JOBID     	=	 pnuc_transporter
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER pnuc_transporter

HEADER    TRANSPORT PROTEIN                       08-JUL-14   4QTN              
TITLE     CRYSTAL STRUCTURE OF THE VITAMIN B3 TRANSPORTER PNUC                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NICOTINAMIDE RIBOSIDE TRANSPORTER PNUC;                    
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: UNP RESIDUES 28-263;                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: NEISSERIA MUCOSA ATCC 25996;                    
SOURCE   3 ORGANISM_TAXID: 546266;                                              
SOURCE   4 GENE: PNUC, NEIMUCOT_05996;                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    MEMBRANE TRANSPORT, VITAMIN TRANSPORT, NICOTINAMIDE RIBOSIDE UPTAKE,  
KEYWDS   2 TRANSPORT PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.GUSKOV,M.JAEHME,D.J.SLOTBOOM                                        
REVDAT   2   29-JUL-20 4QTN    1       COMPND REMARK SEQADV HETNAM              
REVDAT   2 2                   1       LINK   SITE                              
REVDAT   1   08-OCT-14 4QTN    0                                                
JRNL        AUTH   M.JAEHME,A.GUSKOV,D.J.SLOTBOOM                               
JRNL        TITL   CRYSTAL STRUCTURE OF THE VITAMIN B3 TRANSPORTER PNUC         
JRNL        REF    NAT.STRUCT.MOL.BIOL.                       2014              
JRNL        REFN                   ESSN 1545-9985                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 30336                          
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) : 0.246                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1597                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2211                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4600                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 116                          
REMARK   3   BIN FREE R VALUE                    : 0.4950                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5674                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 134                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 117.7                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.14000                                              
REMARK   3    B22 (A**2) : 4.37000                                              
REMARK   3    B33 (A**2) : -4.52000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.629         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.344         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.438         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 55.299        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.911                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5982 ; 0.012 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8169 ; 1.219 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   704 ; 7.044 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   214 ;39.608 ;22.570       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   869 ;22.426 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;20.626 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   960 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4281 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  2825 ; 3.983 ; 6.103       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3526 ; 6.378 ; 9.148       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3157 ; 4.769 ; 6.400       
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): 26163 ;11.534 ;59.022       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 3                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     2    236       B     2    236     310  0.15  0.05     
REMARK   3    2     A     2    235       C     2    235     309  0.12  0.05     
REMARK   3    3     B     2    235       C     2    235     309  0.16  0.05     
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     2        A    35                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.2929  81.7197  43.6112              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2256 T22:   0.5595                                     
REMARK   3      T33:   0.4934 T12:   0.1696                                     
REMARK   3      T13:   0.0866 T23:   0.1667                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8626 L22:   0.2002                                     
REMARK   3      L33:   7.9255 L12:   0.5439                                     
REMARK   3      L13:  -2.0607 L23:   0.6979                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4059 S12:   0.6215 S13:   0.3981                       
REMARK   3      S21:  -0.0021 S22:   0.0247 S23:  -0.0272                       
REMARK   3      S31:  -0.1098 S32:  -0.2587 S33:  -0.4306                       
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    36        A    42                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.7163  74.0632  23.9470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9379 T22:   1.0197                                     
REMARK   3      T33:   0.8741 T12:   0.0895                                     
REMARK   3      T13:   0.0036 T23:   0.0231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  21.3470 L22:  11.8508                                     
REMARK   3      L33:   6.4138 L12:  14.7886                                     
REMARK   3      L13: -10.3842 L23:  -5.7375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5316 S12:   0.7533 S13:  -1.2197                       
REMARK   3      S21:  -0.1174 S22:   0.1549 S23:  -0.8932                       
REMARK   3      S31:   0.4919 S32:  -0.6488 S33:   0.3767                       
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    43        A    68                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.3767  75.1536  41.4376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2189 T22:   0.9231                                     
REMARK   3      T33:   0.3720 T12:   0.2349                                     
REMARK   3      T13:  -0.0593 T23:   0.0392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0062 L22:   3.1771                                     
REMARK   3      L33:  10.7451 L12:   1.5759                                     
REMARK   3      L13:  -1.7058 L23:  -0.3969                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1574 S12:   0.3189 S13:   0.2013                       
REMARK   3      S21:  -0.5505 S22:   0.3830 S23:   0.4026                       
REMARK   3      S31:  -0.4938 S32:  -0.3174 S33:  -0.2256                       
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 :   A    69        A    80                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.7862  67.5040  29.4165              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7805 T22:   0.8303                                     
REMARK   3      T33:   0.4622 T12:  -0.1039                                     
REMARK   3      T13:   0.0171 T23:  -0.0708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.2403 L22:  13.7525                                     
REMARK   3      L33:   2.2436 L12: -11.6515                                     
REMARK   3      L13:   5.4467 L23:  -4.7364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0046 S12:   1.1528 S13:  -1.2432                       
REMARK   3      S21:  -0.2115 S22:   0.4953 S23:   1.2118                       
REMARK   3      S31:   0.0236 S32:   0.4971 S33:  -0.4908                       
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 :   A    81        A    87                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.5816  58.3424  26.9985              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1986 T22:   1.7217                                     
REMARK   3      T33:   0.9972 T12:  -0.0856                                     
REMARK   3      T13:   0.0291 T23:  -0.1061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.8460 L22:   8.8050                                     
REMARK   3      L33:  10.9447 L12:  11.8047                                     
REMARK   3      L13: -13.1566 L23:  -9.8130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7402 S12:  -0.7853 S13:  -1.7709                       
REMARK   3      S21:  -0.5378 S22:  -0.6260 S23:  -1.2281                       
REMARK   3      S31:   0.5686 S32:   0.5906 S33:   1.3662                       
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 :   A    88        A   112                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0644  69.5321  42.5881              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4286 T22:   1.1467                                     
REMARK   3      T33:   1.0428 T12:  -0.0143                                     
REMARK   3      T13:   0.1540 T23:  -0.0654                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5442 L22:   2.4349                                     
REMARK   3      L33:   3.0664 L12:   2.3184                                     
REMARK   3      L13:   1.3745 L23:  -1.6780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2884 S12:   0.5347 S13:   0.0457                       
REMARK   3      S21:  -0.4416 S22:   0.2793 S23:   0.8389                       
REMARK   3      S31:   0.9410 S32:  -0.0313 S33:  -0.5677                       
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 :   A   113        A   121                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.9411  82.5247  56.5346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6320 T22:   0.6790                                     
REMARK   3      T33:   0.5207 T12:   0.1606                                     
REMARK   3      T13:   0.1102 T23:  -0.0251                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  30.2845 L22:  48.0716                                     
REMARK   3      L33:   2.8957 L12:  34.0507                                     
REMARK   3      L13:   8.2211 L23:  11.7649                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2010 S12:   0.0809 S13:   0.3071                       
REMARK   3      S21:  -0.1053 S22:   0.3360 S23:  -0.2953                       
REMARK   3      S31:  -0.1057 S32:   0.0865 S33:  -0.1350                       
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 :   A   122        A   144                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8357  54.3969  54.2103              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1917 T22:   0.6570                                     
REMARK   3      T33:   0.5745 T12:  -0.0928                                     
REMARK   3      T13:  -0.0392 T23:   0.0426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4828 L22:  16.6853                                     
REMARK   3      L33:   7.5921 L12:  -0.3802                                     
REMARK   3      L13:   0.2885 L23:   4.0487                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2174 S12:   0.2737 S13:  -0.7667                       
REMARK   3      S21:   0.2607 S22:   0.4001 S23:   0.3995                       
REMARK   3      S31:   1.0783 S32:  -0.1215 S33:  -0.1827                       
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 :   A   145        A   156                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.2516  47.4268  31.6212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0401 T22:   1.3023                                     
REMARK   3      T33:   1.0775 T12:  -0.0532                                     
REMARK   3      T13:  -0.1869 T23:  -0.0985                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.2782 L22:   4.9929                                     
REMARK   3      L33:  15.1671 L12:  -1.5443                                     
REMARK   3      L13:   4.9378 L23:   7.1985                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8352 S12:   1.6271 S13:  -1.0017                       
REMARK   3      S21:  -0.1926 S22:  -0.1396 S23:  -0.1074                       
REMARK   3      S31:   0.2515 S32:   0.7327 S33:  -0.6956                       
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 :   A   157        A   195                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.7160  59.3407  45.1247              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2543 T22:   0.4870                                     
REMARK   3      T33:   0.4053 T12:  -0.0637                                     
REMARK   3      T13:  -0.1383 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.0941 L22:   5.7870                                     
REMARK   3      L33:   7.0015 L12:  -2.7873                                     
REMARK   3      L13:  -2.0054 L23:   2.3782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1257 S12:   0.9158 S13:  -0.5468                       
REMARK   3      S21:  -0.8308 S22:  -0.3794 S23:   0.4993                       
REMARK   3      S31:   0.4282 S32:  -0.2383 S33:   0.2537                       
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 :   A   196        A   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  62.4809  56.6362  27.0847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0345 T22:   0.9437                                     
REMARK   3      T33:   0.8503 T12:   0.1540                                     
REMARK   3      T13:   0.2076 T23:   0.1180                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.5577 L22:   1.6144                                     
REMARK   3      L33:  58.5789 L12:   0.4459                                     
REMARK   3      L13: -19.8293 L23:   7.3939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5084 S12:   1.0911 S13:  -0.9506                       
REMARK   3      S21:  -0.1840 S22:   0.3814 S23:  -0.4333                       
REMARK   3      S31:  -1.3814 S32:   0.9123 S33:  -0.8898                       
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 :   A   206        A   236                          
REMARK   3    ORIGIN FOR THE GROUP (A):  55.6950  68.6725  48.2978              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1567 T22:   0.3012                                     
REMARK   3      T33:   0.4112 T12:   0.0260                                     
REMARK   3      T13:  -0.0929 T23:   0.0478                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1734 L22:   3.8666                                     
REMARK   3      L33:  11.2731 L12:  -0.9919                                     
REMARK   3      L13:  -5.2846 L23:   1.7197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4397 S12:   0.4376 S13:   0.1776                       
REMARK   3      S21:  -0.3993 S22:  -0.1207 S23:   0.0371                       
REMARK   3      S31:  -1.0316 S32:  -0.2933 S33:  -0.3191                       
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 :   B     2        B    17                          
REMARK   3    ORIGIN FOR THE GROUP (A):  93.0581  70.1955  61.1070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3581 T22:   0.7337                                     
REMARK   3      T33:   0.5693 T12:  -0.0894                                     
REMARK   3      T13:  -0.0943 T23:  -0.0209                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  26.2087 L22:  10.2978                                     
REMARK   3      L33:   6.3032 L12:  13.1645                                     
REMARK   3      L13: -12.7727 L23:  -6.8725                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6184 S12:  -0.3584 S13:   1.2324                       
REMARK   3      S21:   0.1531 S22:  -0.1700 S23:  -0.4887                       
REMARK   3      S31:  -0.3466 S32:   0.2605 S33:  -0.4484                       
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 :   B    18        B    31                          
REMARK   3    ORIGIN FOR THE GROUP (A):  82.5110  58.7057  55.1272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3699 T22:   0.5761                                     
REMARK   3      T33:   0.4752 T12:   0.0944                                     
REMARK   3      T13:   0.0393 T23:  -0.0884                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.9416 L22:   3.2202                                     
REMARK   3      L33:   6.4662 L12:  -0.4771                                     
REMARK   3      L13:  -5.7094 L23:  -3.3357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.7734 S12:   0.7420 S13:  -1.3617                       
REMARK   3      S21:  -0.6897 S22:   0.3213 S23:   0.2445                       
REMARK   3      S31:   1.1855 S32:  -0.6512 S33:   0.4521                       
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 :   B    32        B    51                          
REMARK   3    ORIGIN FOR THE GROUP (A):  90.0599  54.7856  42.5351              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5590 T22:   0.8551                                     
REMARK   3      T33:   0.5763 T12:   0.2327                                     
REMARK   3      T13:   0.1162 T23:  -0.0720                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0417 L22:   7.4607                                     
REMARK   3      L33:   7.0460 L12:   4.1869                                     
REMARK   3      L13:  -0.7063 L23:  -6.5322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1811 S12:   1.2534 S13:  -1.0275                       
REMARK   3      S21:  -1.3744 S22:  -0.1010 S23:  -0.6327                       
REMARK   3      S31:   1.4495 S32:   0.7560 S33:   0.2821                       
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 :   B    52        B    66                          
REMARK   3    ORIGIN FOR THE GROUP (A):  87.1518  72.2456  52.1511              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0757 T22:   0.6475                                     
REMARK   3      T33:   0.5258 T12:   0.0149                                     
REMARK   3      T13:   0.0613 T23:   0.0914                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0330 L22:  17.5039                                     
REMARK   3      L33:   3.7569 L12:   9.3219                                     
REMARK   3      L13:  -1.0052 L23:  -1.7409                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3972 S12:   0.2095 S13:  -0.2358                       
REMARK   3      S21:  -0.8269 S22:   0.1642 S23:  -0.6060                       
REMARK   3      S31:  -0.1447 S32:   0.9841 S33:   0.2330                       
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 :   B    67        B    77                          
REMARK   3    ORIGIN FOR THE GROUP (A):  90.8027  67.2497  39.4751              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4313 T22:   1.0183                                     
REMARK   3      T33:   0.4296 T12:   0.1417                                     
REMARK   3      T13:   0.3268 T23:  -0.0656                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8770 L22:  10.3320                                     
REMARK   3      L33:   3.8598 L12:   3.3674                                     
REMARK   3      L13:   4.2450 L23:   2.4252                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1634 S12:   0.0110 S13:  -0.2988                       
REMARK   3      S21:   0.5104 S22:   0.0193 S23:   0.4133                       
REMARK   3      S31:   0.3587 S32:   0.2061 S33:  -0.1827                       
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 :   B    78        B    87                          
REMARK   3    ORIGIN FOR THE GROUP (A):  84.4744  63.2111  28.9141              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7687 T22:   1.0187                                     
REMARK   3      T33:   0.7151 T12:   0.2235                                     
REMARK   3      T13:   0.0646 T23:  -0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7670 L22:  37.5006                                     
REMARK   3      L33:   4.8972 L12:  -1.5033                                     
REMARK   3      L13:   1.3932 L23: -12.9104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1517 S12:   0.6588 S13:   0.8202                       
REMARK   3      S21:  -1.3243 S22:  -0.1440 S23:   0.4609                       
REMARK   3      S31:   0.3377 S32:   0.3353 S33:   0.2957                       
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 :   B    88        B   106                          
REMARK   3    ORIGIN FOR THE GROUP (A):  88.3174  77.4121  40.0154              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7388 T22:   0.7167                                     
REMARK   3      T33:   0.6578 T12:  -0.0036                                     
REMARK   3      T13:  -0.0618 T23:   0.1462                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.9557 L22:   3.0585                                     
REMARK   3      L33:   7.0130 L12:  -0.7559                                     
REMARK   3      L13:  -1.0444 L23:  -4.4304                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1192 S12:   0.7650 S13:   0.2128                       
REMARK   3      S21:  -0.1645 S22:  -0.0685 S23:   0.1269                       
REMARK   3      S31:  -0.0230 S32:   0.0048 S33:  -0.0506                       
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 :   B   107        B   139                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.9212  83.4537  52.5766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1870 T22:   0.4268                                     
REMARK   3      T33:   0.4776 T12:  -0.0686                                     
REMARK   3      T13:   0.1076 T23:   0.0220                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.0730 L22:   2.4402                                     
REMARK   3      L33:  13.1485 L12:  -2.3259                                     
REMARK   3      L13:  11.9140 L23:  -1.7573                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0194 S12:  -0.0012 S13:   0.2557                       
REMARK   3      S21:  -0.1039 S22:   0.1060 S23:  -0.1422                       
REMARK   3      S31:  -0.0493 S32:  -0.0116 S33:  -0.0866                       
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 :   B   140        B   154                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.1607  79.6777  23.3485              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4255 T22:   1.7666                                     
REMARK   3      T33:   0.7252 T12:   0.3775                                     
REMARK   3      T13:   0.0410 T23:   0.0465                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.2971 L22:   9.2315                                     
REMARK   3      L33:  15.7859 L12:  -1.0904                                     
REMARK   3      L13:  -3.5750 L23:  11.8429                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9014 S12:   1.7753 S13:  -1.1446                       
REMARK   3      S21:  -3.0157 S22:  -0.3697 S23:  -0.4807                       
REMARK   3      S31:  -3.7807 S32:  -0.5223 S33:  -0.5317                       
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 :   B   155        B   192                          
REMARK   3    ORIGIN FOR THE GROUP (A):  75.4817  75.0915  40.6209              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1019 T22:   0.7529                                     
REMARK   3      T33:   0.3484 T12:   0.0216                                     
REMARK   3      T13:   0.0457 T23:   0.1347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4941 L22:  11.5487                                     
REMARK   3      L33:   0.7356 L12:   2.3438                                     
REMARK   3      L13:   1.4586 L23:   2.5570                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1004 S12:   0.9381 S13:  -0.0156                       
REMARK   3      S21:  -0.8415 S22:   0.0953 S23:  -0.1453                       
REMARK   3      S31:  -0.1724 S32:   0.2816 S33:   0.0052                       
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 :   B   193        B   206                          
REMARK   3    ORIGIN FOR THE GROUP (A):  76.6764  56.5673  31.1018              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0044 T22:   0.8923                                     
REMARK   3      T33:   0.8145 T12:   0.1047                                     
REMARK   3      T13:   0.1648 T23:  -0.1522                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.3125 L22:  16.8704                                     
REMARK   3      L33:  12.7202 L12:   0.6851                                     
REMARK   3      L13:   1.0808 L23:  11.7490                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4472 S12:   0.8706 S13:  -2.6252                       
REMARK   3      S21:  -1.3011 S22:   0.3229 S23:  -0.1441                       
REMARK   3      S31:   1.0411 S32:   0.7165 S33:   0.1243                       
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 :   B   207        B   236                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.1870  69.8517  52.0142              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0484 T22:   0.4231                                     
REMARK   3      T33:   0.3214 T12:   0.0390                                     
REMARK   3      T13:  -0.0343 T23:   0.0433                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9410 L22:  14.1976                                     
REMARK   3      L33:   9.4316 L12:   0.4873                                     
REMARK   3      L13:  -1.0079 L23:   5.8996                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0066 S12:   0.1234 S13:   0.1681                       
REMARK   3      S21:   0.5633 S22:   0.1279 S23:  -0.0152                       
REMARK   3      S31:   0.6316 S32:   0.4558 S33:  -0.1213                       
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 :   C     2        C    41                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.0392  45.3189  57.3873              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3455 T22:   0.5280                                     
REMARK   3      T33:   0.6845 T12:  -0.0937                                     
REMARK   3      T13:  -0.0989 T23:  -0.0602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4393 L22:   6.4290                                     
REMARK   3      L33:   8.2610 L12:  -0.5502                                     
REMARK   3      L13:  -1.3322 L23:   2.1172                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1581 S12:   0.2929 S13:  -0.7499                       
REMARK   3      S21:  -0.3107 S22:  -0.1295 S23:   0.4945                       
REMARK   3      S31:   1.2884 S32:   0.1045 S33:  -0.0286                       
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 :   C    42        C    69                          
REMARK   3    ORIGIN FOR THE GROUP (A):  61.1806  41.5184  58.7049              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5181 T22:   0.3853                                     
REMARK   3      T33:   0.6828 T12:  -0.0523                                     
REMARK   3      T13:  -0.1928 T23:  -0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5196 L22:   1.2417                                     
REMARK   3      L33:   8.2596 L12:   0.0801                                     
REMARK   3      L13:  -2.1580 L23:  -1.8644                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1489 S12:  -0.1183 S13:  -1.3482                       
REMARK   3      S21:  -0.1273 S22:  -0.1748 S23:   0.3759                       
REMARK   3      S31:   1.2211 S32:  -0.5930 S33:   0.0260                       
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 :   C    70        C    78                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.8274  34.7946  48.9076              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8458 T22:   0.4704                                     
REMARK   3      T33:   0.7553 T12:   0.1435                                     
REMARK   3      T13:  -0.1202 T23:  -0.1613                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.0264 L22:   0.3706                                     
REMARK   3      L33:  30.6765 L12:  -2.1617                                     
REMARK   3      L13:  -8.8985 L23:   2.1636                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1262 S12:   1.1381 S13:  -1.4557                       
REMARK   3      S21:   0.0208 S22:  -0.1537 S23:   0.2062                       
REMARK   3      S31:   2.4945 S32:   0.8852 S33:   0.2798                       
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 :   C    79        C    87                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.6180  36.2029  40.2894              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0122 T22:   0.6981                                     
REMARK   3      T33:   0.7432 T12:   0.1001                                     
REMARK   3      T13:  -0.0603 T23:  -0.2567                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  43.3369 L22:  14.5421                                     
REMARK   3      L33:  21.7512 L12:  10.0970                                     
REMARK   3      L13:  16.1471 L23:  -1.9532                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2542 S12:   0.7263 S13:  -1.4416                       
REMARK   3      S21:   0.1200 S22:   0.2847 S23:  -1.7356                       
REMARK   3      S31:   0.3710 S32:   0.7955 S33:  -0.5389                       
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 :   C    88        C   104                          
REMARK   3    ORIGIN FOR THE GROUP (A):  72.2622  34.6603  57.2756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6233 T22:   0.5827                                     
REMARK   3      T33:   0.9753 T12:   0.0566                                     
REMARK   3      T13:  -0.1105 T23:  -0.0735                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0472 L22:   8.7540                                     
REMARK   3      L33:  12.9515 L12:  -1.8696                                     
REMARK   3      L13:   2.8125 L23:  -4.5860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3032 S12:   1.1144 S13:  -0.9557                       
REMARK   3      S21:  -1.1441 S22:  -0.2461 S23:  -0.3214                       
REMARK   3      S31:   0.8334 S32:   0.2029 S33:   0.5492                       
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 :   C   105        C   120                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.2098  45.0432  74.1942              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5630 T22:   0.4726                                     
REMARK   3      T33:   0.5010 T12:  -0.1405                                     
REMARK   3      T13:  -0.0747 T23:   0.0719                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  26.0927 L22:  12.9351                                     
REMARK   3      L33:  13.2882 L12:  -9.7220                                     
REMARK   3      L13:  -6.0855 L23:   2.5485                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3223 S12:   0.2018 S13:  -0.5112                       
REMARK   3      S21:   0.1494 S22:  -0.2551 S23:   0.2888                       
REMARK   3      S31:   0.0670 S32:  -0.0394 S33:  -0.0672                       
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 :   C   121        C   137                          
REMARK   3    ORIGIN FOR THE GROUP (A):  82.9011  52.0201  65.6670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3234 T22:   0.4138                                     
REMARK   3      T33:   0.3726 T12:   0.1168                                     
REMARK   3      T13:  -0.1656 T23:  -0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  24.0120 L22:   6.1653                                     
REMARK   3      L33:   7.7510 L12:   4.2288                                     
REMARK   3      L13: -12.4765 L23:  -3.6338                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4223 S12:  -0.8536 S13:   0.1006                       
REMARK   3      S21:   0.1792 S22:  -0.2011 S23:  -0.4296                       
REMARK   3      S31:   0.2764 S32:   0.6091 S33:  -0.2211                       
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 :   C   138        C   149                          
REMARK   3    ORIGIN FOR THE GROUP (A):  88.3115  39.4807  49.4583              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6930 T22:   1.0646                                     
REMARK   3      T33:   1.1562 T12:   0.1717                                     
REMARK   3      T13:   0.1700 T23:  -0.3610                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1316 L22:  34.2613                                     
REMARK   3      L33:  13.6115 L12:  12.9855                                     
REMARK   3      L13:  11.5269 L23:  12.0619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3069 S12:   0.6871 S13:  -0.8023                       
REMARK   3      S21:  -2.1039 S22:   0.1241 S23:  -2.4749                       
REMARK   3      S31:   0.7392 S32:   0.7074 S33:  -0.4310                       
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 :   C   150        C   156                          
REMARK   3    ORIGIN FOR THE GROUP (A):  86.1574  33.4726  40.8751              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3915 T22:   1.0832                                     
REMARK   3      T33:   1.3008 T12:   0.0798                                     
REMARK   3      T13:  -0.0690 T23:  -0.0859                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.1463 L22:  10.5368                                     
REMARK   3      L33:   9.9736 L12:  -3.3492                                     
REMARK   3      L13:  -9.9588 L23:   8.3570                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.2821 S12:  -0.5623 S13:   1.3993                       
REMARK   3      S21:  -1.1023 S22:  -0.3229 S23:  -0.6298                       
REMARK   3      S31:  -1.2026 S32:  -0.0709 S33:  -0.9593                       
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 :   C   157        C   195                          
REMARK   3    ORIGIN FOR THE GROUP (A):  75.6504  47.5662  54.4622              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2744 T22:   0.4003                                     
REMARK   3      T33:   0.4354 T12:   0.1718                                     
REMARK   3      T13:  -0.0603 T23:  -0.0810                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6922 L22:   3.8818                                     
REMARK   3      L33:   9.6044 L12:  -0.0406                                     
REMARK   3      L13:  -0.6168 L23:  -4.1298                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1391 S12:   0.2903 S13:  -0.5731                       
REMARK   3      S21:  -0.6158 S22:  -0.4010 S23:  -0.0789                       
REMARK   3      S31:   1.3162 S32:   0.3301 S33:   0.5402                       
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 :   C   196        C   205                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.7269  44.3751  33.9415              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.1745 T22:   1.5434                                     
REMARK   3      T33:   1.0173 T12:  -0.1399                                     
REMARK   3      T13:  -0.1330 T23:  -0.3447                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.8371 L22:   5.2029                                     
REMARK   3      L33:   2.0202 L12:  -7.7205                                     
REMARK   3      L13:   0.0177 L23:   0.2772                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7607 S12:   2.5190 S13:   0.5687                       
REMARK   3      S21:  -0.7023 S22:  -1.6583 S23:  -0.0069                       
REMARK   3      S31:   1.3327 S32:  -0.3554 S33:   0.8976                       
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 :   C   206        C   236                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.6986  51.9967  57.9421              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1390 T22:   0.3210                                     
REMARK   3      T33:   0.3999 T12:   0.0483                                     
REMARK   3      T13:  -0.0554 T23:   0.0394                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6274 L22:   5.6042                                     
REMARK   3      L33:  13.5739 L12:   0.9348                                     
REMARK   3      L13:   2.5812 L23:   4.0114                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1495 S12:   0.1741 S13:  -0.1510                       
REMARK   3      S21:   0.1215 S22:  -0.3723 S23:   0.5203                       
REMARK   3      S31:   1.0176 S32:  -0.5005 S33:   0.2228                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 4QTN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000086498.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794, 0.9800, 0.972              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31933                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG3350, 0.1 M SUCCINIC ACID, PH     
REMARK 280  7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       46.66000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.18500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.46500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.18500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       46.66000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.46500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 29750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     MSE A     1                                                      
REMARK 465     GLY A   237                                                      
REMARK 465     GLN A   238                                                      
REMARK 465     HIS A   239                                                      
REMARK 465     HIS A   240                                                      
REMARK 465     HIS A   241                                                      
REMARK 465     HIS A   242                                                      
REMARK 465     HIS A   243                                                      
REMARK 465     HIS A   244                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     GLY B   237                                                      
REMARK 465     GLN B   238                                                      
REMARK 465     HIS B   239                                                      
REMARK 465     HIS B   240                                                      
REMARK 465     HIS B   241                                                      
REMARK 465     HIS B   242                                                      
REMARK 465     HIS B   243                                                      
REMARK 465     HIS B   244                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     HIS C   239                                                      
REMARK 465     HIS C   240                                                      
REMARK 465     HIS C   241                                                      
REMARK 465     HIS C   242                                                      
REMARK 465     HIS C   243                                                      
REMARK 465     HIS C   244                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU C   149     OG   SER C   154              1.91            
REMARK 500   O    LEU B   149     OG   SER B   154              2.00            
REMARK 500   OE2  GLU B   120     NH1  ARG B   234              2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  73      -71.22    -70.16                                   
REMARK 500    ARG A 107      -35.84    -36.68                                   
REMARK 500    ARG A 177       33.56     78.40                                   
REMARK 500    HIS A 235       61.09   -117.12                                   
REMARK 500    TRP B   6      -71.36    -57.75                                   
REMARK 500    TRP B   7      -18.76    -41.16                                   
REMARK 500    VAL B  35        3.57    -67.85                                   
REMARK 500    SER B  40       75.35   -113.54                                   
REMARK 500    GLN B  99      -36.18    -38.96                                   
REMARK 500    LEU B 149      -11.99     76.32                                   
REMARK 500    SER B 154      109.38   -164.95                                   
REMARK 500    ALA B 199      -19.64    -45.91                                   
REMARK 500    HIS B 235       77.11   -116.09                                   
REMARK 500    VAL C  35       14.47    -67.60                                   
REMARK 500    THR C  81       -2.19    -59.66                                   
REMARK 500    ALA C 111      169.02    177.67                                   
REMARK 500    LEU C 149       -6.53     74.46                                   
REMARK 500    ARG C 177       30.40     71.56                                   
REMARK 500    SER C 236     -168.40   -170.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  113     GLU A  114                 -141.54                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4QTN A    3   238  UNP    D2ZZC1   D2ZZC1_NEIMU    28    263             
DBREF  4QTN B    3   238  UNP    D2ZZC1   D2ZZC1_NEIMU    28    263             
DBREF  4QTN C    3   238  UNP    D2ZZC1   D2ZZC1_NEIMU    28    263             
SEQADV 4QTN MSE A    1  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN GLY A    2  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS A  239  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS A  240  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS A  241  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS A  242  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS A  243  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS A  244  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN MSE B    1  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN GLY B    2  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS B  239  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS B  240  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS B  241  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS B  242  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS B  243  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS B  244  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN MSE C    1  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN GLY C    2  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS C  239  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS C  240  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS C  241  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS C  242  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS C  243  UNP  D2ZZC1              EXPRESSION TAG                 
SEQADV 4QTN HIS C  244  UNP  D2ZZC1              EXPRESSION TAG                 
SEQRES   1 A  244  MSE GLY SER LEU ALA TRP TRP LYS ARG GLU LEU PHE GLY          
SEQRES   2 A  244  GLY TRP THR HIS PHE GLU ALA VAL TRP LEU LEU MSE PHE          
SEQRES   3 A  244  LEU GLY ILE GLN ALA VAL VAL PHE VAL PHE ASN PRO ASP          
SEQRES   4 A  244  SER TRP LEU ALA SER VAL ALA ALA VAL THR GLY ILE LEU          
SEQRES   5 A  244  CYS VAL VAL PHE VAL GLY LYS GLY LYS ILE SER ASN TYR          
SEQRES   6 A  244  LEU PHE GLY LEU ILE SER VAL SER LEU TYR ALA TYR VAL          
SEQRES   7 A  244  SER TYR THR PHE LYS LEU TYR GLY GLU MSE MSE LEU ASN          
SEQRES   8 A  244  LEU LEU VAL TYR VAL PRO VAL GLN PHE VAL GLY PHE ALA          
SEQRES   9 A  244  MSE TRP ARG LYS HIS MSE ALA LEU GLY GLU THR ALA GLU          
SEQRES  10 A  244  THR GLU GLU VAL LYS ALA LYS ALA LEU THR VAL ARG GLN          
SEQRES  11 A  244  TRP LEU LEU VAL VAL ALA ALA SER VAL VAL GLY THR SER          
SEQRES  12 A  244  VAL TYR ILE GLU TRP LEU HIS HIS LEU GLY SER ALA LEU          
SEQRES  13 A  244  PRO THR LEU ASP GLY VAL THR VAL VAL VAL SER ILE VAL          
SEQRES  14 A  244  ALA GLN VAL LEU MSE ILE LEU ARG TYR ARG GLU GLN TRP          
SEQRES  15 A  244  ALA LEU TRP ILE VAL VAL ASN ILE LEU THR ILE SER LEU          
SEQRES  16 A  244  TRP ALA VAL ALA TRP PHE LYS ASN GLY GLU THR SER LEU          
SEQRES  17 A  244  PRO LEU LEU LEU MSE TYR VAL MSE TYR LEU CYS ASN SER          
SEQRES  18 A  244  VAL TYR GLY TYR ILE ASN TRP THR LYS LEU VAL LYS ARG          
SEQRES  19 A  244  HIS SER GLY GLN HIS HIS HIS HIS HIS HIS                      
SEQRES   1 B  244  MSE GLY SER LEU ALA TRP TRP LYS ARG GLU LEU PHE GLY          
SEQRES   2 B  244  GLY TRP THR HIS PHE GLU ALA VAL TRP LEU LEU MSE PHE          
SEQRES   3 B  244  LEU GLY ILE GLN ALA VAL VAL PHE VAL PHE ASN PRO ASP          
SEQRES   4 B  244  SER TRP LEU ALA SER VAL ALA ALA VAL THR GLY ILE LEU          
SEQRES   5 B  244  CYS VAL VAL PHE VAL GLY LYS GLY LYS ILE SER ASN TYR          
SEQRES   6 B  244  LEU PHE GLY LEU ILE SER VAL SER LEU TYR ALA TYR VAL          
SEQRES   7 B  244  SER TYR THR PHE LYS LEU TYR GLY GLU MSE MSE LEU ASN          
SEQRES   8 B  244  LEU LEU VAL TYR VAL PRO VAL GLN PHE VAL GLY PHE ALA          
SEQRES   9 B  244  MSE TRP ARG LYS HIS MSE ALA LEU GLY GLU THR ALA GLU          
SEQRES  10 B  244  THR GLU GLU VAL LYS ALA LYS ALA LEU THR VAL ARG GLN          
SEQRES  11 B  244  TRP LEU LEU VAL VAL ALA ALA SER VAL VAL GLY THR SER          
SEQRES  12 B  244  VAL TYR ILE GLU TRP LEU HIS HIS LEU GLY SER ALA LEU          
SEQRES  13 B  244  PRO THR LEU ASP GLY VAL THR VAL VAL VAL SER ILE VAL          
SEQRES  14 B  244  ALA GLN VAL LEU MSE ILE LEU ARG TYR ARG GLU GLN TRP          
SEQRES  15 B  244  ALA LEU TRP ILE VAL VAL ASN ILE LEU THR ILE SER LEU          
SEQRES  16 B  244  TRP ALA VAL ALA TRP PHE LYS ASN GLY GLU THR SER LEU          
SEQRES  17 B  244  PRO LEU LEU LEU MSE TYR VAL MSE TYR LEU CYS ASN SER          
SEQRES  18 B  244  VAL TYR GLY TYR ILE ASN TRP THR LYS LEU VAL LYS ARG          
SEQRES  19 B  244  HIS SER GLY GLN HIS HIS HIS HIS HIS HIS                      
SEQRES   1 C  244  MSE GLY SER LEU ALA TRP TRP LYS ARG GLU LEU PHE GLY          
SEQRES   2 C  244  GLY TRP THR HIS PHE GLU ALA VAL TRP LEU LEU MSE PHE          
SEQRES   3 C  244  LEU GLY ILE GLN ALA VAL VAL PHE VAL PHE ASN PRO ASP          
SEQRES   4 C  244  SER TRP LEU ALA SER VAL ALA ALA VAL THR GLY ILE LEU          
SEQRES   5 C  244  CYS VAL VAL PHE VAL GLY LYS GLY LYS ILE SER ASN TYR          
SEQRES   6 C  244  LEU PHE GLY LEU ILE SER VAL SER LEU TYR ALA TYR VAL          
SEQRES   7 C  244  SER TYR THR PHE LYS LEU TYR GLY GLU MSE MSE LEU ASN          
SEQRES   8 C  244  LEU LEU VAL TYR VAL PRO VAL GLN PHE VAL GLY PHE ALA          
SEQRES   9 C  244  MSE TRP ARG LYS HIS MSE ALA LEU GLY GLU THR ALA GLU          
SEQRES  10 C  244  THR GLU GLU VAL LYS ALA LYS ALA LEU THR VAL ARG GLN          
SEQRES  11 C  244  TRP LEU LEU VAL VAL ALA ALA SER VAL VAL GLY THR SER          
SEQRES  12 C  244  VAL TYR ILE GLU TRP LEU HIS HIS LEU GLY SER ALA LEU          
SEQRES  13 C  244  PRO THR LEU ASP GLY VAL THR VAL VAL VAL SER ILE VAL          
SEQRES  14 C  244  ALA GLN VAL LEU MSE ILE LEU ARG TYR ARG GLU GLN TRP          
SEQRES  15 C  244  ALA LEU TRP ILE VAL VAL ASN ILE LEU THR ILE SER LEU          
SEQRES  16 C  244  TRP ALA VAL ALA TRP PHE LYS ASN GLY GLU THR SER LEU          
SEQRES  17 C  244  PRO LEU LEU LEU MSE TYR VAL MSE TYR LEU CYS ASN SER          
SEQRES  18 C  244  VAL TYR GLY TYR ILE ASN TRP THR LYS LEU VAL LYS ARG          
SEQRES  19 C  244  HIS SER GLY GLN HIS HIS HIS HIS HIS HIS                      
MODRES 4QTN MSE A   25  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE A   88  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE A   89  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE A  105  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE A  110  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE A  174  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE A  213  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE A  216  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE B   25  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE B   88  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE B   89  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE B  105  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE B  110  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE B  174  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE B  213  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE B  216  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE C   25  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE C   88  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE C   89  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE C  105  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE C  110  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE C  174  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE C  213  MET  SELENOMETHIONINE                                   
MODRES 4QTN MSE C  216  MET  SELENOMETHIONINE                                   
HET    MSE  A  25       8                                                       
HET    MSE  A  88       8                                                       
HET    MSE  A  89       8                                                       
HET    MSE  A 105       8                                                       
HET    MSE  A 110       8                                                       
HET    MSE  A 174       8                                                       
HET    MSE  A 213       8                                                       
HET    MSE  A 216       8                                                       
HET    MSE  B  25       8                                                       
HET    MSE  B  88       8                                                       
HET    MSE  B  89       8                                                       
HET    MSE  B 105       8                                                       
HET    MSE  B 110       8                                                       
HET    MSE  B 174       8                                                       
HET    MSE  B 213       8                                                       
HET    MSE  B 216       8                                                       
HET    MSE  C  25       8                                                       
HET    MSE  C  88       8                                                       
HET    MSE  C  89       8                                                       
HET    MSE  C 105       8                                                       
HET    MSE  C 110       8                                                       
HET    MSE  C 174       8                                                       
HET    MSE  C 213       8                                                       
HET    MSE  C 216       8                                                       
HET    NNR  A 301      18                                                       
HET    BOG  A 302      20                                                       
HET    NNR  B 301      18                                                       
HET    BOG  B 302      20                                                       
HET    BOG  B 303      20                                                       
HET    NNR  C 301      18                                                       
HET    BOG  C 302      20                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     NNR NICOTINAMIDE RIBOSIDE                                            
HETNAM     BOG OCTYL BETA-D-GLUCOPYRANOSIDE                                     
HETSYN     NNR 3-(AMINOCARBONYL)-1-BETA-D-RIBOFURANOSYLPYRIDINIUM               
FORMUL   1  MSE    24(C5 H11 N O2 SE)                                           
FORMUL   4  NNR    3(C11 H15 N2 O5 1+)                                          
FORMUL   5  BOG    4(C14 H28 O6)                                                
HELIX    1   1 SER A    3  GLY A   13  1                                  11    
HELIX    2   2 THR A   16  ASN A   37  1                                  22    
HELIX    3   3 SER A   40  GLY A   60  1                                  21    
HELIX    4   4 SER A   63  PHE A   82  1                                  20    
HELIX    5   5 LEU A   84  VAL A   94  1                                  11    
HELIX    6   6 VAL A   94  ARG A  107  1                                  14    
HELIX    7   7 THR A  127  HIS A  151  1                                  25    
HELIX    8   8 PRO A  157  LEU A  176  1                                  20    
HELIX    9   9 GLU A  180  LYS A  202  1                                  23    
HELIX   10  10 SER A  207  HIS A  235  1                                  29    
HELIX   11  11 SER B    3  GLY B   13  1                                  11    
HELIX   12  12 THR B   16  VAL B   35  1                                  20    
HELIX   13  13 ASN B   37  ASP B   39  5                                   3    
HELIX   14  14 SER B   40  GLY B   60  1                                  21    
HELIX   15  15 SER B   63  THR B   81  1                                  19    
HELIX   16  16 LEU B   84  VAL B   94  1                                  11    
HELIX   17  17 VAL B   94  LYS B  108  1                                  15    
HELIX   18  18 THR B  127  TRP B  148  1                                  22    
HELIX   19  19 PRO B  157  LEU B  176  1                                  20    
HELIX   20  20 GLU B  180  ALA B  199  1                                  20    
HELIX   21  21 SER B  207  HIS B  235  1                                  29    
HELIX   22  22 SER C    3  GLY C   13  1                                  11    
HELIX   23  23 THR C   16  VAL C   35  1                                  20    
HELIX   24  24 SER C   40  GLY C   60  1                                  21    
HELIX   25  25 SER C   63  THR C   81  1                                  19    
HELIX   26  26 LEU C   84  VAL C   94  1                                  11    
HELIX   27  27 VAL C   94  LYS C  108  1                                  15    
HELIX   28  28 THR C  127  TRP C  148  1                                  22    
HELIX   29  29 PRO C  157  LEU C  176  1                                  20    
HELIX   30  30 GLU C  180  ALA C  199  1                                  20    
HELIX   31  31 SER C  207  HIS C  235  1                                  29    
SHEET    1   A 2 MSE A 110  ALA A 111  0                                        
SHEET    2   A 2 GLU A 120  VAL A 121 -1  O  GLU A 120   N  ALA A 111           
SHEET    1   B 2 MSE B 110  ALA B 111  0                                        
SHEET    2   B 2 GLU B 120  VAL B 121 -1  O  GLU B 120   N  ALA B 111           
LINK         C   LEU A  24                 N   MSE A  25     1555   1555  1.32  
LINK         C   MSE A  25                 N   PHE A  26     1555   1555  1.32  
LINK         C   GLU A  87                 N   MSE A  88     1555   1555  1.33  
LINK         C   MSE A  88                 N   MSE A  89     1555   1555  1.33  
LINK         C   MSE A  89                 N   LEU A  90     1555   1555  1.33  
LINK         C   ALA A 104                 N   MSE A 105     1555   1555  1.35  
LINK         C   MSE A 105                 N   TRP A 106     1555   1555  1.33  
LINK         C   HIS A 109                 N   MSE A 110     1555   1555  1.31  
LINK         C   MSE A 110                 N   ALA A 111     1555   1555  1.32  
LINK         C   LEU A 173                 N   MSE A 174     1555   1555  1.33  
LINK         C   MSE A 174                 N   ILE A 175     1555   1555  1.34  
LINK         C   LEU A 212                 N   MSE A 213     1555   1555  1.34  
LINK         C   MSE A 213                 N   TYR A 214     1555   1555  1.33  
LINK         C   VAL A 215                 N   MSE A 216     1555   1555  1.33  
LINK         C   MSE A 216                 N   TYR A 217     1555   1555  1.33  
LINK         C   LEU B  24                 N   MSE B  25     1555   1555  1.33  
LINK         C   MSE B  25                 N   PHE B  26     1555   1555  1.33  
LINK         C   GLU B  87                 N   MSE B  88     1555   1555  1.33  
LINK         C   MSE B  88                 N   MSE B  89     1555   1555  1.33  
LINK         C   MSE B  89                 N   LEU B  90     1555   1555  1.33  
LINK         C   ALA B 104                 N   MSE B 105     1555   1555  1.34  
LINK         C   MSE B 105                 N   TRP B 106     1555   1555  1.33  
LINK         C   HIS B 109                 N   MSE B 110     1555   1555  1.32  
LINK         C   MSE B 110                 N   ALA B 111     1555   1555  1.32  
LINK         C   LEU B 173                 N   MSE B 174     1555   1555  1.33  
LINK         C   MSE B 174                 N   ILE B 175     1555   1555  1.34  
LINK         C   LEU B 212                 N   MSE B 213     1555   1555  1.33  
LINK         C   MSE B 213                 N   TYR B 214     1555   1555  1.33  
LINK         C   VAL B 215                 N   MSE B 216     1555   1555  1.32  
LINK         C   MSE B 216                 N   TYR B 217     1555   1555  1.34  
LINK         C   LEU C  24                 N   MSE C  25     1555   1555  1.33  
LINK         C   MSE C  25                 N   PHE C  26     1555   1555  1.33  
LINK         C   GLU C  87                 N   MSE C  88     1555   1555  1.33  
LINK         C   MSE C  88                 N   MSE C  89     1555   1555  1.34  
LINK         C   MSE C  89                 N   LEU C  90     1555   1555  1.34  
LINK         C   ALA C 104                 N   MSE C 105     1555   1555  1.34  
LINK         C   MSE C 105                 N   TRP C 106     1555   1555  1.33  
LINK         C   HIS C 109                 N   MSE C 110     1555   1555  1.33  
LINK         C   MSE C 110                 N   ALA C 111     1555   1555  1.34  
LINK         C   LEU C 173                 N   MSE C 174     1555   1555  1.34  
LINK         C   MSE C 174                 N   ILE C 175     1555   1555  1.33  
LINK         C   LEU C 212                 N   MSE C 213     1555   1555  1.33  
LINK         C   MSE C 213                 N   TYR C 214     1555   1555  1.34  
LINK         C   VAL C 215                 N   MSE C 216     1555   1555  1.33  
LINK         C   MSE C 216                 N   TYR C 217     1555   1555  1.33  
CISPEP   1 LYS A  202    ASN A  203          0         3.26                     
CISPEP   2 LYS B  202    ASN B  203          0        -2.87                     
CISPEP   3 LYS C  202    ASN C  203          0         2.42                     
CRYST1   93.320  112.930  120.370  90.00  90.00  90.00 P 21 21 21   12          
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      0.010716  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008855  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008308        0.00000                         
ATOM      1  N   GLY A   2      38.645  87.161  42.135  1.00131.72           N  
ANISOU    1  N   GLY A   2    11541  23710  14794   4798   1613   3864       N  
ATOM      2  CA  GLY A   2      38.780  87.879  43.445  1.00126.94           C  
ANISOU    2  CA  GLY A   2    11225  22465  14542   4937   1764   3782       C  
ATOM      3  C   GLY A   2      39.518  89.183  43.257  1.00127.01           C  
ANISOU    3  C   GLY A   2    11591  21748  14916   5429   2026   4070       C  
ATOM      4  O   GLY A   2      40.052  89.441  42.174  1.00129.09           O  
ANISOU    4  O   GLY A   2    11918  21941  15189   5594   2068   4323       O  
ATOM      5  N   SER A   3      39.567  90.002  44.311  1.00123.01           N  
ANISOU    5  N   SER A   3    11336  20698  14703   5625   2218   4014       N  
ATOM      6  CA  SER A   3      40.200  91.340  44.238  1.00123.90           C  
ANISOU    6  CA  SER A   3    11847  20056  15174   6074   2529   4260       C  
ATOM      7  C   SER A   3      41.694  91.311  43.879  1.00124.43           C  
ANISOU    7  C   SER A   3    12303  19421  15554   5746   2545   4229       C  
ATOM      8  O   SER A   3      42.333  90.250  43.860  1.00122.77           O  
ANISOU    8  O   SER A   3    12088  19221  15336   5186   2314   3979       O  
ATOM      9  CB  SER A   3      39.980  92.131  45.533  1.00124.47           C  
ANISOU    9  CB  SER A   3    12125  19673  15494   6252   2742   4110       C  
ATOM     10  OG  SER A   3      39.809  91.273  46.652  1.00126.22           O  
ANISOU   10  OG  SER A   3    12244  20029  15683   5737   2556   3698       O  
ATOM     11  N   LEU A   4      42.245  92.475  43.573  1.00124.34           N  
ANISOU   11  N   LEU A   4    12631  18811  15798   6104   2834   4487       N  
ATOM     12  CA  LEU A   4      43.654  92.563  43.275  1.00118.60           C  
ANISOU   12  CA  LEU A   4    12259  17453  15347   5790   2883   4451       C  
ATOM     13  C   LEU A   4      44.406  92.577  44.574  1.00119.44           C  
ANISOU   13  C   LEU A   4    12665  16933  15782   5373   2931   4057       C  
ATOM     14  O   LEU A   4      45.560  92.162  44.637  1.00123.39           O  
ANISOU   14  O   LEU A   4    13343  17099  16440   4918   2852   3862       O  
ATOM     15  CB  LEU A   4      43.967  93.816  42.463  1.00122.70           C  
ANISOU   15  CB  LEU A   4    13057  17566  15997   6269   3202   4879       C  
ATOM     16  CG  LEU A   4      45.214  93.792  41.563  1.00125.54           C  
ANISOU   16  CG  LEU A   4    13620  17622  16456   6014   3209   4980       C  
ATOM     17  CD1 LEU A   4      46.430  94.396  42.264  1.00124.83           C  
ANISOU   17  CD1 LEU A   4    14014  16638  16774   5697   3425   4771       C  
ATOM     18  CD2 LEU A   4      45.523  92.391  41.012  1.00117.48           C  
ANISOU   18  CD2 LEU A   4    12292  17137  15207   5553   2839   4792       C  
ATOM     19  N   ALA A   5      43.741  93.040  45.628  1.00119.76           N  
ANISOU   19  N   ALA A   5    12728  16878  15894   5539   3059   3928       N  
ATOM     20  CA  ALA A   5      44.298  92.957  46.970  1.00113.37           C  
ANISOU   20  CA  ALA A   5    12121  15625  15328   5122   3079   3519       C  
ATOM     21  C   ALA A   5      44.381  91.509  47.429  1.00108.10           C  
ANISOU   21  C   ALA A   5    11223  15343  14505   4571   2715   3210       C  
ATOM     22  O   ALA A   5      45.354  91.106  48.070  1.00106.06           O  
ANISOU   22  O   ALA A   5    11135  14747  14414   4111   2644   2933       O  
ATOM     23  CB  ALA A   5      43.471  93.777  47.941  1.00113.01           C  
ANISOU   23  CB  ALA A   5    12116  15465  15356   5453   3305   3447       C  
ATOM     24  N   TRP A   6      43.359  90.726  47.095  1.00105.98           N  
ANISOU   24  N   TRP A   6    10573  15801  13894   4617   2500   3265       N  
ATOM     25  CA  TRP A   6      43.333  89.326  47.458  1.00100.23           C  
ANISOU   25  CA  TRP A   6     9668  15419  12995   4097   2185   2999       C  
ATOM     26  C   TRP A   6      44.364  88.476  46.673  1.00102.46           C  
ANISOU   26  C   TRP A   6    10028  15618  13285   3748   2004   2970       C  
ATOM     27  O   TRP A   6      44.905  87.491  47.191  1.00 98.83           O  
ANISOU   27  O   TRP A   6     9624  15080  12843   3285   1815   2711       O  
ATOM     28  CB  TRP A   6      41.951  88.754  47.278  1.00 93.71           C  
ANISOU   28  CB  TRP A   6     8424  15406  11776   4183   2041   3041       C  
ATOM     29  CG  TRP A   6      41.896  87.340  47.648  1.00 90.33           C  
ANISOU   29  CG  TRP A   6     7878  15268  11174   3617   1761   2774       C  
ATOM     30  CD1 TRP A   6      41.565  86.833  48.865  1.00 89.79           C  
ANISOU   30  CD1 TRP A   6     7783  15259  11074   3298   1677   2511       C  
ATOM     31  CD2 TRP A   6      42.248  86.213  46.823  1.00 89.88           C  
ANISOU   31  CD2 TRP A   6     7765  15422  10960   3273   1545   2735       C  
ATOM     32  NE1 TRP A   6      41.663  85.458  48.852  1.00 89.35           N  
ANISOU   32  NE1 TRP A   6     7686  15409  10853   2785   1432   2341       N  
ATOM     33  CE2 TRP A   6      42.081  85.054  47.609  1.00 89.35           C  
ANISOU   33  CE2 TRP A   6     7679  15486  10784   2765   1354   2456       C  
ATOM     34  CE3 TRP A   6      42.686  86.073  45.494  1.00 93.70           C  
ANISOU   34  CE3 TRP A   6     8225  15994  11379   3346   1509   2903       C  
ATOM     35  CZ2 TRP A   6      42.337  83.759  47.112  1.00 87.07           C  
ANISOU   35  CZ2 TRP A   6     7392  15348  10342   2340   1149   2331       C  
ATOM     36  CZ3 TRP A   6      42.929  84.785  44.997  1.00 92.29           C  
ANISOU   36  CZ3 TRP A   6     8002  16027  11036   2917   1292   2748       C  
ATOM     37  CH2 TRP A   6      42.751  83.648  45.810  1.00 88.03           C  
ANISOU   37  CH2 TRP A   6     7486  15548  10410   2428   1124   2461       C  
ATOM     38  N   TRP A   7      44.596  88.826  45.418  1.00107.66           N  
ANISOU   38  N   TRP A   7    10677  16328  13901   3996   2064   3246       N  
ATOM     39  CA  TRP A   7      45.538  88.070  44.616  1.00108.03           C  
ANISOU   39  CA  TRP A   7    10770  16343  13932   3705   1909   3210       C  
ATOM     40  C   TRP A   7      46.983  88.348  45.021  1.00109.44           C  
ANISOU   40  C   TRP A   7    11294  15849  14437   3479   1991   3070       C  
ATOM     41  O   TRP A   7      47.855  87.503  44.831  1.00107.51           O  
ANISOU   41  O   TRP A   7    11099  15547  14201   3146   1825   2913       O  
ATOM     42  CB  TRP A   7      45.311  88.306  43.120  1.00107.94           C  
ANISOU   42  CB  TRP A   7    10592  16697  13723   4013   1935   3542       C  
ATOM     43  CG  TRP A   7      44.284  87.380  42.544  1.00107.32           C  
ANISOU   43  CG  TRP A   7    10120  17416  13241   3956   1731   3539       C  
ATOM     44  CD1 TRP A   7      43.003  87.683  42.228  1.00109.74           C  
ANISOU   44  CD1 TRP A   7    10101  18338  13254   4312   1767   3740       C  
ATOM     45  CD2 TRP A   7      44.451  85.988  42.251  1.00105.42           C  
ANISOU   45  CD2 TRP A   7     9771  17458  12823   3493   1478   3296       C  
ATOM     46  NE1 TRP A   7      42.360  86.577  41.746  1.00109.69           N  
ANISOU   46  NE1 TRP A   7     9764  19032  12879   4046   1551   3619       N  
ATOM     47  CE2 TRP A   7      43.225  85.520  41.754  1.00104.66           C  
ANISOU   47  CE2 TRP A   7     9285  18156  12322   3530   1383   3339       C  
ATOM     48  CE3 TRP A   7      45.523  85.094  42.363  1.00106.26           C  
ANISOU   48  CE3 TRP A   7    10080  17230  13061   3067   1339   3041       C  
ATOM     49  CZ2 TRP A   7      43.028  84.196  41.369  1.00105.49           C  
ANISOU   49  CZ2 TRP A   7     9234  18681  12166   3093   1174   3108       C  
ATOM     50  CZ3 TRP A   7      45.328  83.776  41.978  1.00107.93           C  
ANISOU   50  CZ3 TRP A   7    10161  17813  13034   2706   1131   2839       C  
ATOM     51  CH2 TRP A   7      44.083  83.341  41.484  1.00108.53           C  
ANISOU   51  CH2 TRP A   7     9882  18632  12720   2692   1060   2862       C  
ATOM     52  N   LYS A   8      47.222  89.522  45.611  1.00110.40           N  
ANISOU   52  N   LYS A   8    11649  15487  14808   3654   2260   3102       N  
ATOM     53  CA  LYS A   8      48.537  89.858  46.163  1.00106.69           C  
ANISOU   53  CA  LYS A   8    11479  14440  14617   3382   2366   2916       C  
ATOM     54  C   LYS A   8      48.867  88.948  47.348  1.00104.72           C  
ANISOU   54  C   LYS A   8    11220  14178  14388   2959   2176   2554       C  
ATOM     55  O   LYS A   8      49.971  88.400  47.439  1.00108.65           O  
ANISOU   55  O   LYS A   8    11805  14531  14946   2647   2068   2388       O  
ATOM     56  CB  LYS A   8      48.592  91.327  46.587  1.00106.87           C  
ANISOU   56  CB  LYS A   8    11769  13955  14879   3622   2734   2990       C  
ATOM     57  CG  LYS A   8      49.996  91.886  46.673  1.00108.69           C  
ANISOU   57  CG  LYS A   8    12304  13646  15347   3365   2909   2881       C  
ATOM     58  CD  LYS A   8      50.010  93.406  46.614  1.00120.80           C  
ANISOU   58  CD  LYS A   8    14152  14658  17086   3641   3325   3050       C  
ATOM     59  CE  LYS A   8      51.424  93.916  46.361  1.00134.25           C  
ANISOU   59  CE  LYS A   8    16135  15915  18958   3338   3502   2988       C  
ATOM     60  NZ  LYS A   8      51.684  95.257  46.964  1.00149.78           N  
ANISOU   60  NZ  LYS A   8    18485  17244  21180   3341   3926   2916       N  
ATOM     61  N   ARG A   9      47.899  88.780  48.241  1.00 99.87           N  
ANISOU   61  N   ARG A   9    10484  13763  13697   2974   2136   2451       N  
ATOM     62  CA  ARG A   9      48.015  87.829  49.330  1.00 94.65           C  
ANISOU   62  CA  ARG A   9     9788  13176  12996   2596   1940   2165       C  
ATOM     63  C   ARG A   9      48.198  86.375  48.837  1.00 96.07           C  
ANISOU   63  C   ARG A   9     9865  13646  12988   2335   1639   2118       C  
ATOM     64  O   ARG A   9      49.067  85.665  49.312  1.00100.50           O  
ANISOU   64  O   ARG A   9    10529  14061  13596   2038   1511   1939       O  
ATOM     65  CB  ARG A   9      46.802  87.922  50.246  1.00 93.83           C  
ANISOU   65  CB  ARG A   9     9538  13317  12794   2672   1959   2096       C  
ATOM     66  CG  ARG A   9      46.634  89.256  50.937  1.00 93.75           C  
ANISOU   66  CG  ARG A   9     9657  12985  12977   2905   2264   2066       C  
ATOM     67  CD  ARG A   9      45.286  89.296  51.625  1.00 93.95           C  
ANISOU   67  CD  ARG A   9     9469  13380  12844   3053   2267   2026       C  
ATOM     68  NE  ARG A   9      45.189  90.338  52.632  1.00 95.46           N  
ANISOU   68  NE  ARG A   9     9789  13262  13216   3171   2529   1877       N  
ATOM     69  CZ  ARG A   9      45.610  90.206  53.887  1.00 96.83           C  
ANISOU   69  CZ  ARG A   9    10027  13292  13469   2832   2522   1574       C  
ATOM     70  NH1 ARG A   9      46.201  89.083  54.278  1.00 96.37           N  
ANISOU   70  NH1 ARG A   9     9936  13345  13334   2395   2264   1434       N  
ATOM     71  NH2 ARG A   9      45.459  91.206  54.754  1.00100.28           N  
ANISOU   71  NH2 ARG A   9    10571  13474  14055   2945   2788   1412       N  
ATOM     72  N   GLU A  10      47.387  85.946  47.884  1.00 99.83           N  
ANISOU   72  N   GLU A  10    10146  14544  13240   2457   1544   2272       N  
ATOM     73  CA  GLU A  10      47.452  84.566  47.422  1.00102.20           C  
ANISOU   73  CA  GLU A  10    10376  15100  13352   2184   1295   2188       C  
ATOM     74  C   GLU A  10      48.841  84.183  46.848  1.00103.08           C  
ANISOU   74  C   GLU A  10    10650  14941  13573   2059   1234   2140       C  
ATOM     75  O   GLU A  10      49.415  83.144  47.218  1.00 99.22           O  
ANISOU   75  O   GLU A  10    10256  14370  13071   1782   1069   1960       O  
ATOM     76  CB  GLU A  10      46.354  84.292  46.394  1.00106.51           C  
ANISOU   76  CB  GLU A  10    10654  16208  13607   2318   1240   2340       C  
ATOM     77  CG  GLU A  10      46.321  82.857  45.871  1.00104.22           C  
ANISOU   77  CG  GLU A  10    10309  16185  13102   1989   1019   2209       C  
ATOM     78  CD  GLU A  10      45.866  81.836  46.911  1.00110.24           C  
ANISOU   78  CD  GLU A  10    11106  17016  13764   1617    882   1992       C  
ATOM     79  OE1 GLU A  10      45.523  82.233  48.074  1.00121.14           O  
ANISOU   79  OE1 GLU A  10    12501  18310  15216   1612    938   1942       O  
ATOM     80  OE2 GLU A  10      45.848  80.630  46.569  1.00105.16           O  
ANISOU   80  OE2 GLU A  10    10492  16503  12961   1315    733   1866       O  
ATOM     81  N   LEU A  11      49.370  85.020  45.952  1.00 97.15           N  
ANISOU   81  N   LEU A  11     9933  14065  12912   2281   1376   2312       N  
ATOM     82  CA  LEU A  11      50.598  84.691  45.234  1.00 91.32           C  
ANISOU   82  CA  LEU A  11     9287  13186  12223   2185   1322   2279       C  
ATOM     83  C   LEU A  11      51.854  85.046  46.002  1.00 95.10           C  
ANISOU   83  C   LEU A  11     9961  13247  12922   2046   1396   2129       C  
ATOM     84  O   LEU A  11      52.872  84.365  45.876  1.00100.74           O  
ANISOU   84  O   LEU A  11    10733  13904  13640   1886   1279   1998       O  
ATOM     85  CB  LEU A  11      50.640  85.373  43.879  1.00 92.14           C  
ANISOU   85  CB  LEU A  11     9320  13407  12280   2440   1438   2538       C  
ATOM     86  CG  LEU A  11      49.433  85.188  42.968  1.00 92.52           C  
ANISOU   86  CG  LEU A  11     9115  13976  12062   2623   1391   2722       C  
ATOM     87  CD1 LEU A  11      49.411  86.319  41.937  1.00 91.40           C  
ANISOU   87  CD1 LEU A  11     8940  13871  11917   2979   1588   3059       C  
ATOM     88  CD2 LEU A  11      49.427  83.801  42.310  1.00 88.07           C  
ANISOU   88  CD2 LEU A  11     8432  13750  11277   2386   1160   2572       C  
ATOM     89  N   PHE A  12      51.812  86.113  46.783  1.00 93.82           N  
ANISOU   89  N   PHE A  12     9894  12826  12925   2110   1601   2129       N  
ATOM     90  CA  PHE A  12      53.020  86.537  47.453  1.00 94.56           C  
ANISOU   90  CA  PHE A  12    10144  12591  13190   1933   1700   1963       C  
ATOM     91  C   PHE A  12      52.945  86.471  48.965  1.00 97.52           C  
ANISOU   91  C   PHE A  12    10555  12872  13623   1757   1693   1745       C  
ATOM     92  O   PHE A  12      53.926  86.769  49.646  1.00110.15           O  
ANISOU   92  O   PHE A  12    12243  14285  15324   1574   1767   1571       O  
ATOM     93  CB  PHE A  12      53.445  87.906  46.962  1.00 95.20           C  
ANISOU   93  CB  PHE A  12    10357  12391  13421   2063   1994   2101       C  
ATOM     94  CG  PHE A  12      53.449  88.018  45.481  1.00 99.78           C  
ANISOU   94  CG  PHE A  12    10887  13108  13916   2251   2008   2357       C  
ATOM     95  CD1 PHE A  12      54.457  87.434  44.733  1.00101.14           C  
ANISOU   95  CD1 PHE A  12    11026  13382  14021   2121   1888   2314       C  
ATOM     96  CD2 PHE A  12      52.404  88.629  44.823  1.00105.42           C  
ANISOU   96  CD2 PHE A  12    11551  13924  14576   2585   2126   2645       C  
ATOM     97  CE1 PHE A  12      54.441  87.492  43.350  1.00103.80           C  
ANISOU   97  CE1 PHE A  12    11286  13906  14247   2277   1892   2540       C  
ATOM     98  CE2 PHE A  12      52.382  88.699  43.440  1.00108.43           C  
ANISOU   98  CE2 PHE A  12    11852  14511  14835   2765   2129   2903       C  
ATOM     99  CZ  PHE A  12      53.404  88.132  42.705  1.00107.25           C  
ANISOU   99  CZ  PHE A  12    11672  14450  14625   2589   2012   2843       C  
ATOM    100  N   GLY A  13      51.820  85.987  49.487  1.00 86.52           N  
ANISOU  100  N   GLY A  13     9064  11683  12124   1773   1590   1739       N  
ATOM    101  CA  GLY A  13      51.549  86.070  50.912  1.00 83.77           C  
ANISOU  101  CA  GLY A  13     8726  11292  11810   1634   1613   1562       C  
ATOM    102  C   GLY A  13      52.073  84.910  51.733  1.00 85.90           C  
ANISOU  102  C   GLY A  13     9000  11642  11995   1360   1390   1389       C  
ATOM    103  O   GLY A  13      51.817  83.732  51.413  1.00 86.84           O  
ANISOU  103  O   GLY A  13     9086  11944  11964   1297   1174   1422       O  
ATOM    104  N   GLY A  14      52.803  85.241  52.802  1.00 84.88           N  
ANISOU  104  N   GLY A  14     8922  11383  11946   1195   1459   1206       N  
ATOM    105  CA  GLY A  14      53.172  84.262  53.845  1.00 88.19           C  
ANISOU  105  CA  GLY A  14     9330  11917  12260    976   1273   1070       C  
ATOM    106  C   GLY A  14      54.094  83.106  53.434  1.00 91.92           C  
ANISOU  106  C   GLY A  14     9847  12435  12644    929   1061   1080       C  
ATOM    107  O   GLY A  14      53.894  81.960  53.869  1.00 86.35           O  
ANISOU  107  O   GLY A  14     9169  11831  11807    842    869   1084       O  
ATOM    108  N   TRP A  15      55.112  83.405  52.613  1.00 95.47           N  
ANISOU  108  N   TRP A  15    10318  12799  13156    991   1113   1085       N  
ATOM    109  CA  TRP A  15      56.144  82.418  52.242  1.00 91.41           C  
ANISOU  109  CA  TRP A  15     9829  12345  12558    994    940   1063       C  
ATOM    110  C   TRP A  15      57.337  82.552  53.185  1.00 89.23           C  
ANISOU  110  C   TRP A  15     9514  12127  12261    875    955    899       C  
ATOM    111  O   TRP A  15      57.844  83.661  53.387  1.00 95.99           O  
ANISOU  111  O   TRP A  15    10330  12937  13204    785   1155    794       O  
ATOM    112  CB  TRP A  15      56.663  82.688  50.831  1.00 96.81           C  
ANISOU  112  CB  TRP A  15    10506  12998  13278   1119    989   1139       C  
ATOM    113  CG  TRP A  15      55.692  82.516  49.688  1.00 94.45           C  
ANISOU  113  CG  TRP A  15    10198  12740  12949   1251    965   1303       C  
ATOM    114  CD1 TRP A  15      55.112  83.515  48.949  1.00 93.98           C  
ANISOU  114  CD1 TRP A  15    10103  12648  12956   1375   1137   1442       C  
ATOM    115  CD2 TRP A  15      55.324  81.291  49.059  1.00 89.49           C  
ANISOU  115  CD2 TRP A  15     9591  12219  12190   1277    778   1339       C  
ATOM    116  NE1 TRP A  15      54.373  82.980  47.931  1.00 91.97           N  
ANISOU  116  NE1 TRP A  15     9794  12559  12591   1477   1047   1568       N  
ATOM    117  CE2 TRP A  15      54.483  81.615  47.974  1.00 91.18           C  
ANISOU  117  CE2 TRP A  15     9730  12541  12371   1385    833   1481       C  
ATOM    118  CE3 TRP A  15      55.597  79.949  49.324  1.00 88.85           C  
ANISOU  118  CE3 TRP A  15     9606  12146  12007   1220    587   1267       C  
ATOM    119  CZ2 TRP A  15      53.900  80.647  47.170  1.00 92.87           C  
ANISOU  119  CZ2 TRP A  15     9927  12920  12437   1379    702   1507       C  
ATOM    120  CZ3 TRP A  15      55.035  78.985  48.510  1.00 91.88           C  
ANISOU  120  CZ3 TRP A  15    10035  12597  12277   1219    478   1293       C  
ATOM    121  CH2 TRP A  15      54.189  79.336  47.449  1.00 93.43           C  
ANISOU  121  CH2 TRP A  15    10122  12950  12428   1268    534   1390       C  
ATOM    122  N   THR A  16      57.815  81.435  53.728  1.00 80.29           N  
ANISOU  122  N   THR A  16     8397  11111  10996    872    761    878       N  
ATOM    123  CA  THR A  16      59.105  81.433  54.391  1.00 79.17           C  
ANISOU  123  CA  THR A  16     8166  11139  10773    822    748    747       C  
ATOM    124  C   THR A  16      60.208  81.690  53.344  1.00 85.67           C  
ANISOU  124  C   THR A  16     8935  12010  11605    900    792    711       C  
ATOM    125  O   THR A  16      60.034  81.369  52.137  1.00 80.00           O  
ANISOU  125  O   THR A  16     8276  11202  10915   1039    748    814       O  
ATOM    126  CB  THR A  16      59.370  80.118  55.190  1.00 79.37           C  
ANISOU  126  CB  THR A  16     8235  11294  10627    883    531    788       C  
ATOM    127  OG1 THR A  16      59.743  79.054  54.307  1.00 79.29           O  
ANISOU  127  OG1 THR A  16     8332  11232  10562   1088    382    876       O  
ATOM    128  CG2 THR A  16      58.154  79.706  55.948  1.00 84.58           C  
ANISOU  128  CG2 THR A  16     8981  11892  11261    791    475    865       C  
ATOM    129  N   HIS A  17      61.318  82.309  53.791  1.00 93.63           N  
ANISOU  129  N   HIS A  17     9804  13207  12561    777    892    547       N  
ATOM    130  CA  HIS A  17      62.483  82.603  52.901  1.00 89.59           C  
ANISOU  130  CA  HIS A  17     9199  12826  12012    795    947    483       C  
ATOM    131  C   HIS A  17      62.950  81.332  52.182  1.00 81.32           C  
ANISOU  131  C   HIS A  17     8167  11879  10850   1063    725    565       C  
ATOM    132  O   HIS A  17      63.178  81.344  50.973  1.00 76.04           O  
ANISOU  132  O   HIS A  17     7505  11180  10207   1155    738    607       O  
ATOM    133  CB  HIS A  17      63.641  83.252  53.697  1.00 98.09           C  
ANISOU  133  CB  HIS A  17    10085  14210  12972    573   1063    256       C  
ATOM    134  CG  HIS A  17      64.924  83.390  52.917  1.00106.05           C  
ANISOU  134  CG  HIS A  17    10951  15471  13870    568   1093    169       C  
ATOM    135  ND1 HIS A  17      65.909  82.417  52.917  1.00107.10           N  
ANISOU  135  ND1 HIS A  17    10935  15970  13786    768    900    145       N  
ATOM    136  CD2 HIS A  17      65.396  84.399  52.146  1.00106.52           C  
ANISOU  136  CD2 HIS A  17    10991  15495  13986    386   1306    101       C  
ATOM    137  CE1 HIS A  17      66.916  82.811  52.157  1.00105.29           C  
ANISOU  137  CE1 HIS A  17    10564  15968  13473    706    980     46       C  
ATOM    138  NE2 HIS A  17      66.632  84.011  51.682  1.00107.87           N  
ANISOU  138  NE2 HIS A  17    10972  16051  13961    446   1228     21       N  
ATOM    139  N   PHE A  18      63.045  80.236  52.936  1.00 74.51           N  
ANISOU  139  N   PHE A  18     7332  11117   9860   1197    538    596       N  
ATOM    140  CA  PHE A  18      63.312  78.929  52.378  1.00 73.17           C  
ANISOU  140  CA  PHE A  18     7260  10939   9602   1482    348    679       C  
ATOM    141  C   PHE A  18      62.379  78.543  51.234  1.00 75.72           C  
ANISOU  141  C   PHE A  18     7758  10977  10034   1550    321    787       C  
ATOM    142  O   PHE A  18      62.845  78.201  50.165  1.00 80.69           O  
ANISOU  142  O   PHE A  18     8383  11637  10636   1697    287    775       O  
ATOM    143  CB  PHE A  18      63.239  77.891  53.463  1.00 75.65           C  
ANISOU  143  CB  PHE A  18     7666  11283   9793   1598    193    751       C  
ATOM    144  CG  PHE A  18      63.664  76.538  53.030  1.00 77.10           C  
ANISOU  144  CG  PHE A  18     7997  11421   9877   1923     31    826       C  
ATOM    145  CD1 PHE A  18      65.010  76.165  53.078  1.00 81.13           C  
ANISOU  145  CD1 PHE A  18     8360  12253  10209   2174    -34    772       C  
ATOM    146  CD2 PHE A  18      62.743  75.626  52.612  1.00 76.11           C  
ANISOU  146  CD2 PHE A  18     8153  10952   9812   1981    -41    934       C  
ATOM    147  CE1 PHE A  18      65.413  74.897  52.698  1.00 82.31           C  
ANISOU  147  CE1 PHE A  18     8677  12324  10270   2539   -163    840       C  
ATOM    148  CE2 PHE A  18      63.142  74.356  52.226  1.00 81.98           C  
ANISOU  148  CE2 PHE A  18     9091  11581  10474   2278   -155    979       C  
ATOM    149  CZ  PHE A  18      64.481  73.992  52.266  1.00 80.33           C  
ANISOU  149  CZ  PHE A  18     8767  11639  10115   2588   -214    939       C  
ATOM    150  N   GLU A  19      61.056  78.575  51.459  1.00 78.18           N  
ANISOU  150  N   GLU A  19     8194  11075  10435   1434    337    875       N  
ATOM    151  CA  GLU A  19      60.091  78.166  50.391  1.00 76.05           C  
ANISOU  151  CA  GLU A  19     8048  10632  10214   1467    310    962       C  
ATOM    152  C   GLU A  19      60.279  79.048  49.197  1.00 73.01           C  
ANISOU  152  C   GLU A  19     7549  10293   9896   1474    434    963       C  
ATOM    153  O   GLU A  19      60.314  78.586  48.077  1.00 71.42           O  
ANISOU  153  O   GLU A  19     7370  10103   9663   1577    389    978       O  
ATOM    154  CB  GLU A  19      58.639  78.277  50.849  1.00 80.60           C  
ANISOU  154  CB  GLU A  19     8697  11089  10838   1315    334   1040       C  
ATOM    155  CG  GLU A  19      58.227  77.382  52.019  1.00 84.88           C  
ANISOU  155  CG  GLU A  19     9375  11577  11297   1252    223   1070       C  
ATOM    156  CD  GLU A  19      57.110  78.010  52.881  1.00 85.41           C  
ANISOU  156  CD  GLU A  19     9398  11654  11400   1059    298   1095       C  
ATOM    157  OE1 GLU A  19      56.697  77.377  53.860  1.00 87.56           O  
ANISOU  157  OE1 GLU A  19     9760  11917  11589    967    221   1128       O  
ATOM    158  OE2 GLU A  19      56.660  79.149  52.593  1.00 84.73           O  
ANISOU  158  OE2 GLU A  19     9192  11587  11415   1016    446   1087       O  
ATOM    159  N   ALA A  20      60.407  80.335  49.448  1.00 71.94           N  
ANISOU  159  N   ALA A  20     7308  10180   9846   1349    609    943       N  
ATOM    160  CA  ALA A  20      60.628  81.281  48.388  1.00 74.22           C  
ANISOU  160  CA  ALA A  20     7523  10479  10195   1340    761    980       C  
ATOM    161  C   ALA A  20      61.865  80.915  47.547  1.00 77.74           C  
ANISOU  161  C   ALA A  20     7882  11114  10539   1440    707    908       C  
ATOM    162  O   ALA A  20      61.808  80.920  46.325  1.00 79.38           O  
ANISOU  162  O   ALA A  20     8069  11356  10734   1513    719    973       O  
ATOM    163  CB  ALA A  20      60.747  82.687  48.959  1.00 73.63           C  
ANISOU  163  CB  ALA A  20     7410  10338  10225   1165    992    939       C  
ATOM    164  N   VAL A  21      62.973  80.579  48.213  1.00 82.30           N  
ANISOU  164  N   VAL A  21     8380  11875  11015   1457    644    774       N  
ATOM    165  CA  VAL A  21      64.245  80.300  47.518  1.00 83.31           C  
ANISOU  165  CA  VAL A  21     8374  12266  11012   1568    603    679       C  
ATOM    166  C   VAL A  21      64.135  79.045  46.680  1.00 83.90           C  
ANISOU  166  C   VAL A  21     8536  12319  11021   1814    435    702       C  
ATOM    167  O   VAL A  21      64.511  79.035  45.526  1.00 88.83           O  
ANISOU  167  O   VAL A  21     9090  13060  11600   1882    447    686       O  
ATOM    168  CB  VAL A  21      65.431  80.196  48.510  1.00 83.98           C  
ANISOU  168  CB  VAL A  21     8306  12650  10950   1564    568    529       C  
ATOM    169  CG1 VAL A  21      66.513  79.268  47.990  1.00 84.26           C  
ANISOU  169  CG1 VAL A  21     8240  12969  10805   1834    429    452       C  
ATOM    170  CG2 VAL A  21      65.993  81.576  48.799  1.00 86.06           C  
ANISOU  170  CG2 VAL A  21     8422  13052  11224   1259    788    423       C  
ATOM    171  N   TRP A  22      63.561  78.001  47.239  1.00 82.99           N  
ANISOU  171  N   TRP A  22     8595  12038  10897   1919    298    734       N  
ATOM    172  CA  TRP A  22      63.369  76.800  46.469  1.00 84.63           C  
ANISOU  172  CA  TRP A  22     8947  12153  11055   2106    178    726       C  
ATOM    173  C   TRP A  22      62.290  76.915  45.395  1.00 88.57           C  
ANISOU  173  C   TRP A  22     9495  12545  11612   2012    220    794       C  
ATOM    174  O   TRP A  22      62.310  76.182  44.422  1.00 92.62           O  
ANISOU  174  O   TRP A  22    10056  13074  12061   2119    166    738       O  
ATOM    175  CB  TRP A  22      63.088  75.658  47.365  1.00 81.46           C  
ANISOU  175  CB  TRP A  22     8767  11564  10618   2210     55    748       C  
ATOM    176  CG  TRP A  22      64.279  75.101  47.910  1.00 82.57           C  
ANISOU  176  CG  TRP A  22     8870  11867  10633   2455    -23    690       C  
ATOM    177  CD1 TRP A  22      64.797  75.328  49.143  1.00 80.98           C  
ANISOU  177  CD1 TRP A  22     8573  11828  10366   2460    -37    702       C  
ATOM    178  CD2 TRP A  22      65.142  74.182  47.268  1.00 82.35           C  
ANISOU  178  CD2 TRP A  22     8877  11913  10497   2773    -99    606       C  
ATOM    179  NE1 TRP A  22      65.922  74.591  49.311  1.00 86.89           N  
ANISOU  179  NE1 TRP A  22     9280  12780  10953   2786   -126    659       N  
ATOM    180  CE2 TRP A  22      66.158  73.876  48.166  1.00 85.82           C  
ANISOU  180  CE2 TRP A  22     9236  12571  10798   3003   -162    598       C  
ATOM    181  CE3 TRP A  22      65.140  73.573  46.017  1.00 85.52           C  
ANISOU  181  CE3 TRP A  22     9361  12247  10885   2898   -114    524       C  
ATOM    182  CZ2 TRP A  22      67.180  72.993  47.860  1.00 96.10           C  
ANISOU  182  CZ2 TRP A  22    10541  14015  11955   3406   -238    530       C  
ATOM    183  CZ3 TRP A  22      66.156  72.711  45.702  1.00 91.90           C  
ANISOU  183  CZ3 TRP A  22    10188  13160  11568   3261   -179    424       C  
ATOM    184  CH2 TRP A  22      67.162  72.419  46.619  1.00 99.29           C  
ANISOU  184  CH2 TRP A  22    11051  14299  12374   3538   -240    437       C  
ATOM    185  N   LEU A  23      61.360  77.844  45.556  1.00 88.19           N  
ANISOU  185  N   LEU A  23     9417  12429  11661   1830    326    905       N  
ATOM    186  CA  LEU A  23      60.372  78.051  44.517  1.00 89.04           C  
ANISOU  186  CA  LEU A  23     9509  12545  11776   1780    372    995       C  
ATOM    187  C   LEU A  23      60.980  78.761  43.327  1.00 89.75           C  
ANISOU  187  C   LEU A  23     9432  12830  11838   1818    464   1018       C  
ATOM    188  O   LEU A  23      60.904  78.259  42.214  1.00 97.77           O  
ANISOU  188  O   LEU A  23    10417  13966  12763   1882    421    994       O  
ATOM    189  CB  LEU A  23      59.165  78.825  45.031  1.00 91.41           C  
ANISOU  189  CB  LEU A  23     9813  12755  12163   1647    462   1128       C  
ATOM    190  CG  LEU A  23      58.074  78.986  43.978  1.00 93.21           C  
ANISOU  190  CG  LEU A  23     9981  13087  12345   1639    499   1243       C  
ATOM    191  CD1 LEU A  23      57.495  77.637  43.606  1.00 94.86           C  
ANISOU  191  CD1 LEU A  23    10293  13313  12433   1607    364   1156       C  
ATOM    192  CD2 LEU A  23      56.984  79.899  44.480  1.00103.13           C  
ANISOU  192  CD2 LEU A  23    11204  14305  13672   1583    611   1385       C  
ATOM    193  N   LEU A  24      61.582  79.937  43.563  1.00 85.68           N  
ANISOU  193  N   LEU A  24     8817  12353  11385   1744    607   1054       N  
ATOM    194  CA  LEU A  24      62.146  80.730  42.480  1.00 83.41           C  
ANISOU  194  CA  LEU A  24     8395  12232  11063   1731    728   1108       C  
ATOM    195  C   LEU A  24      63.160  79.932  41.723  1.00 86.17           C  
ANISOU  195  C   LEU A  24     8655  12815  11269   1851    623    963       C  
ATOM    196  O   LEU A  24      63.262  80.053  40.530  1.00 92.70           O  
ANISOU  196  O   LEU A  24     9385  13817  12017   1879    653   1004       O  
ATOM    197  CB  LEU A  24      62.750  82.041  42.979  1.00 82.83           C  
ANISOU  197  CB  LEU A  24     8281  12119  11068   1570    925   1126       C  
ATOM    198  CG  LEU A  24      61.757  83.122  43.471  1.00 90.46           C  
ANISOU  198  CG  LEU A  24     9346  12832  12191   1478   1101   1284       C  
ATOM    199  CD1 LEU A  24      62.438  84.459  43.669  1.00 89.21           C  
ANISOU  199  CD1 LEU A  24     9194  12597  12104   1291   1350   1283       C  
ATOM    200  CD2 LEU A  24      60.541  83.285  42.564  1.00 89.10           C  
ANISOU  200  CD2 LEU A  24     9190  12641  12023   1593   1130   1508       C  
HETATM  201  N   MSE A  25      63.866  79.052  42.413  1.00 90.20           N  
ANISOU  201  N   MSE A  25     9197  13346  11726   1956    497    801       N  
HETATM  202  CA  MSE A  25      64.890  78.254  41.777  1.00 92.37           C  
ANISOU  202  CA  MSE A  25     9389  13852  11855   2137    403    644       C  
HETATM  203  C   MSE A  25      64.293  77.134  40.986  1.00 90.14           C  
ANISOU  203  C   MSE A  25     9221  13504  11523   2264    298    597       C  
HETATM  204  O   MSE A  25      64.743  76.851  39.901  1.00 93.25           O  
ANISOU  204  O   MSE A  25     9514  14109  11806   2352    285    511       O  
HETATM  205  CB  MSE A  25      65.874  77.720  42.785  1.00 98.42           C  
ANISOU  205  CB  MSE A  25    10140  14701  12553   2273    318    512       C  
HETATM  206  CG  MSE A  25      67.025  77.096  42.021  1.00117.17           C  
ANISOU  206  CG  MSE A  25    12377  17386  14755   2499    253    352       C  
HETATM  207 SE   MSE A  25      67.475  75.397  42.875  1.00144.43          SE  
ANISOU  207 SE   MSE A  25    16021  20730  18125   2905     63    239      SE  
HETATM  208  CE  MSE A  25      68.138  76.216  44.527  1.00142.18           C  
ANISOU  208  CE  MSE A  25    15573  20639  17807   2787     98    268       C  
ATOM    209  N   PHE A  26      63.273  76.487  41.524  1.00 91.39           N  
ANISOU  209  N   PHE A  26     9589  13390  11744   2240    235    629       N  
ATOM    210  CA  PHE A  26      62.526  75.477  40.765  1.00 97.54           C  
ANISOU  210  CA  PHE A  26    10499  14095  12466   2261    172    561       C  
ATOM    211  C   PHE A  26      62.053  76.030  39.403  1.00 97.73           C  
ANISOU  211  C   PHE A  26    10347  14362  12422   2169    245    624       C  
ATOM    212  O   PHE A  26      62.041  75.309  38.391  1.00 94.57           O  
ANISOU  212  O   PHE A  26     9937  14090  11905   2214    209    493       O  
ATOM    213  CB  PHE A  26      61.314  74.994  41.567  1.00102.20           C  
ANISOU  213  CB  PHE A  26    11310  14401  13118   2132    136    618       C  
ATOM    214  CG  PHE A  26      61.591  73.814  42.456  1.00105.78           C  
ANISOU  214  CG  PHE A  26    12029  14592  13571   2253     40    526       C  
ATOM    215  CD1 PHE A  26      62.712  73.009  42.254  1.00106.13           C  
ANISOU  215  CD1 PHE A  26    12131  14647  13544   2524    -15    380       C  
ATOM    216  CD2 PHE A  26      60.695  73.476  43.478  1.00107.13           C  
ANISOU  216  CD2 PHE A  26    12400  14511  13793   2116     15    601       C  
ATOM    217  CE1 PHE A  26      62.955  71.915  43.073  1.00110.17           C  
ANISOU  217  CE1 PHE A  26    12925  14886  14047   2697    -85    343       C  
ATOM    218  CE2 PHE A  26      60.927  72.374  44.288  1.00107.99           C  
ANISOU  218  CE2 PHE A  26    12791  14352  13888   2232    -56    563       C  
ATOM    219  CZ  PHE A  26      62.059  71.595  44.088  1.00110.29           C  
ANISOU  219  CZ  PHE A  26    13168  14616  14119   2542   -103    449       C  
ATOM    220  N   LEU A  27      61.646  77.304  39.392  1.00 94.43           N  
ANISOU  220  N   LEU A  27     9803  14009  12066   2051    359    829       N  
ATOM    221  CA  LEU A  27      61.184  77.950  38.171  1.00 96.27           C  
ANISOU  221  CA  LEU A  27     9866  14492  12219   2005    443    964       C  
ATOM    222  C   LEU A  27      62.370  78.331  37.252  1.00102.02           C  
ANISOU  222  C   LEU A  27    10410  15500  12850   2062    490    925       C  
ATOM    223  O   LEU A  27      62.332  78.100  36.030  1.00103.74           O  
ANISOU  223  O   LEU A  27    10501  15995  12921   2084    484    898       O  
ATOM    224  CB  LEU A  27      60.310  79.168  38.495  1.00 92.34           C  
ANISOU  224  CB  LEU A  27     9341  13923  11819   1923    572   1228       C  
ATOM    225  CG  LEU A  27      58.999  78.943  39.293  1.00 96.37           C  
ANISOU  225  CG  LEU A  27     9967  14261  12385   1856    541   1285       C  
ATOM    226  CD1 LEU A  27      58.266  80.257  39.468  1.00 98.08           C  
ANISOU  226  CD1 LEU A  27    10130  14452  12684   1853    694   1545       C  
ATOM    227  CD2 LEU A  27      58.054  77.924  38.666  1.00 95.92           C  
ANISOU  227  CD2 LEU A  27     9914  14353  12178   1804    448   1201       C  
ATOM    228  N   GLY A  28      63.432  78.862  37.857  1.00103.13           N  
ANISOU  228  N   GLY A  28    10517  15622  13043   2060    538    897       N  
ATOM    229  CA  GLY A  28      64.689  79.138  37.158  1.00 98.01           C  
ANISOU  229  CA  GLY A  28     9683  15281  12274   2082    578    817       C  
ATOM    230  C   GLY A  28      65.213  77.961  36.362  1.00100.00           C  
ANISOU  230  C   GLY A  28     9876  15751  12367   2252    456    584       C  
ATOM    231  O   GLY A  28      65.556  78.109  35.193  1.00109.49           O  
ANISOU  231  O   GLY A  28    10900  17275  13425   2249    490    571       O  
ATOM    232  N   ILE A  29      65.265  76.787  36.984  1.00 95.48           N  
ANISOU  232  N   ILE A  29     9471  14994  11814   2407    329    403       N  
ATOM    233  CA  ILE A  29      65.861  75.601  36.341  1.00 97.25           C  
ANISOU  233  CA  ILE A  29     9697  15351  11902   2619    236    146       C  
ATOM    234  C   ILE A  29      64.969  75.105  35.209  1.00101.79           C  
ANISOU  234  C   ILE A  29    10285  15995  12395   2555    232     99       C  
ATOM    235  O   ILE A  29      65.449  74.648  34.173  1.00103.97           O  
ANISOU  235  O   ILE A  29    10441  16545  12516   2642    220    -75       O  
ATOM    236  CB  ILE A  29      66.135  74.469  37.365  1.00 98.53           C  
ANISOU  236  CB  ILE A  29    10101  15224  12112   2839    131      1       C  
ATOM    237  CG1 ILE A  29      67.101  74.952  38.482  1.00106.75           C  
ANISOU  237  CG1 ILE A  29    11058  16329  13172   2911    129     35       C  
ATOM    238  CG2 ILE A  29      66.644  73.199  36.678  1.00 96.01           C  
ANISOU  238  CG2 ILE A  29     9855  14952  11671   3101     68   -266       C  
ATOM    239  CD1 ILE A  29      68.066  76.078  38.083  1.00105.90           C  
ANISOU  239  CD1 ILE A  29    10627  16642  12967   2802    222     55       C  
ATOM    240  N   GLN A  30      63.667  75.249  35.398  1.00102.30           N  
ANISOU  240  N   GLN A  30    10457  15879  12533   2387    248    246       N  
ATOM    241  CA  GLN A  30      62.708  74.989  34.353  1.00101.21           C  
ANISOU  241  CA  GLN A  30    10261  15917  12274   2268    261    232       C  
ATOM    242  C   GLN A  30      62.845  75.999  33.168  1.00104.21           C  
ANISOU  242  C   GLN A  30    10330  16745  12520   2211    348    396       C  
ATOM    243  O   GLN A  30      62.816  75.596  31.974  1.00108.50           O  
ANISOU  243  O   GLN A  30    10727  17623  12871   2200    344    271       O  
ATOM    244  CB  GLN A  30      61.296  75.013  34.946  1.00 97.88           C  
ANISOU  244  CB  GLN A  30     9977  15282  11929   2103    263    368       C  
ATOM    245  CG  GLN A  30      60.332  73.995  34.349  1.00100.67           C  
ANISOU  245  CG  GLN A  30    10410  15689  12151   1969    232    190       C  
ATOM    246  CD  GLN A  30      60.919  72.585  34.215  1.00 97.89           C  
ANISOU  246  CD  GLN A  30    10277  15155  11759   2063    180   -162       C  
ATOM    247  OE1 GLN A  30      61.333  72.181  33.129  1.00101.05           O  
ANISOU  247  OE1 GLN A  30    10566  15820  12008   2105    191   -360       O  
ATOM    248  NE2 GLN A  30      60.900  71.821  35.304  1.00 93.08           N  
ANISOU  248  NE2 GLN A  30     9998  14092  11275   2103    139   -236       N  
ATOM    249  N   ALA A  31      63.009  77.291  33.493  1.00 95.05           N  
ANISOU  249  N   ALA A  31     9085  15582  11445   2163    445    670       N  
ATOM    250  CA  ALA A  31      63.167  78.331  32.464  1.00 93.61           C  
ANISOU  250  CA  ALA A  31     8668  15753  11146   2109    558    886       C  
ATOM    251  C   ALA A  31      64.370  78.050  31.586  1.00103.02           C  
ANISOU  251  C   ALA A  31     9677  17299  12165   2168    543    695       C  
ATOM    252  O   ALA A  31      64.316  78.228  30.372  1.00115.90           O  
ANISOU  252  O   ALA A  31    11104  19327  13605   2135    579    748       O  
ATOM    253  CB  ALA A  31      63.302  79.685  33.100  1.00 86.80           C  
ANISOU  253  CB  ALA A  31     7835  14713  10430   2039    697   1165       C  
ATOM    254  N   VAL A  32      65.458  77.601  32.223  1.00108.85           N  
ANISOU  254  N   VAL A  32    10465  17946  12946   2272    489    473       N  
ATOM    255  CA  VAL A  32      66.749  77.321  31.554  1.00102.71           C  
ANISOU  255  CA  VAL A  32     9491  17541  11992   2368    472    258       C  
ATOM    256  C   VAL A  32      66.645  76.133  30.613  1.00100.52           C  
ANISOU  256  C   VAL A  32     9178  17460  11554   2485    390    -22       C  
ATOM    257  O   VAL A  32      67.080  76.215  29.500  1.00103.33           O  
ANISOU  257  O   VAL A  32     9298  18251  11709   2472    418    -84       O  
ATOM    258  CB  VAL A  32      67.899  77.091  32.594  1.00102.16           C  
ANISOU  258  CB  VAL A  32     9458  17379  11976   2502    429     91       C  
ATOM    259  CG1 VAL A  32      69.029  76.243  32.003  1.00101.15           C  
ANISOU  259  CG1 VAL A  32     9175  17604  11653   2725    361   -226       C  
ATOM    260  CG2 VAL A  32      68.424  78.423  33.131  1.00 98.17           C  
ANISOU  260  CG2 VAL A  32     8868  16906  11523   2308    556    289       C  
ATOM    261  N   VAL A  33      66.055  75.030  31.069  1.00104.28           N  
ANISOU  261  N   VAL A  33     9904  17604  12111   2571    307   -201       N  
ATOM    262  CA  VAL A  33      65.801  73.893  30.178  1.00112.03           C  
ANISOU  262  CA  VAL A  33    10911  18705  12949   2620    268   -498       C  
ATOM    263  C   VAL A  33      64.963  74.356  28.981  1.00117.02           C  
ANISOU  263  C   VAL A  33    11321  19733  13408   2412    323   -369       C  
ATOM    264  O   VAL A  33      64.951  73.706  27.923  1.00117.54           O  
ANISOU  264  O   VAL A  33    11271  20111  13275   2402    320   -611       O  
ATOM    265  CB  VAL A  33      65.080  72.726  30.897  1.00114.89           C  
ANISOU  265  CB  VAL A  33    11644  18574  13433   2652    213   -670       C  
ATOM    266  CG1 VAL A  33      64.754  71.606  29.911  1.00120.52           C  
ANISOU  266  CG1 VAL A  33    12410  19393  13988   2628    217  -1010       C  
ATOM    267  CG2 VAL A  33      65.924  72.193  32.041  1.00111.54           C  
ANISOU  267  CG2 VAL A  33    11440  17795  13143   2916    158   -766       C  
ATOM    268  N   PHE A  34      64.289  75.497  29.144  1.00118.48           N  
ANISOU  268  N   PHE A  34    11435  19930  13650   2268    385     12       N  
ATOM    269  CA  PHE A  34      63.503  76.084  28.059  1.00118.62           C  
ANISOU  269  CA  PHE A  34    11217  20372  13480   2130    445    223       C  
ATOM    270  C   PHE A  34      64.286  76.997  27.112  1.00117.03           C  
ANISOU  270  C   PHE A  34    10721  20633  13109   2118    526    394       C  
ATOM    271  O   PHE A  34      64.008  77.001  25.923  1.00120.71           O  
ANISOU  271  O   PHE A  34    10952  21583  13329   2059    547    410       O  
ATOM    272  CB  PHE A  34      62.289  76.821  28.583  1.00121.93           C  
ANISOU  272  CB  PHE A  34    11704  20616  14005   2041    489    571       C  
ATOM    273  CG  PHE A  34      61.636  77.694  27.556  1.00126.62           C  
ANISOU  273  CG  PHE A  34    12034  21673  14401   1984    571    895       C  
ATOM    274  CD1 PHE A  34      60.798  77.142  26.589  1.00129.46           C  
ANISOU  274  CD1 PHE A  34    12214  22470  14502   1901    543    800       C  
ATOM    275  CD2 PHE A  34      61.889  79.073  27.523  1.00128.95           C  
ANISOU  275  CD2 PHE A  34    12263  21989  14742   2010    695   1299       C  
ATOM    276  CE1 PHE A  34      60.201  77.947  25.630  1.00133.47           C  
ANISOU  276  CE1 PHE A  34    12444  23485  14783   1892    614   1135       C  
ATOM    277  CE2 PHE A  34      61.298  79.879  26.562  1.00131.77           C  
ANISOU  277  CE2 PHE A  34    12403  22761  14902   2014    785   1652       C  
ATOM    278  CZ  PHE A  34      60.453  79.317  25.615  1.00134.42           C  
ANISOU  278  CZ  PHE A  34    12522  23590  14960   1979    734   1587       C  
ATOM    279  N   VAL A  35      65.216  77.806  27.647  1.00111.94           N  
ANISOU  279  N   VAL A  35    10086  19870  12575   2136    585    530       N  
ATOM    280  CA  VAL A  35      66.137  78.635  26.801  1.00114.03           C  
ANISOU  280  CA  VAL A  35    10096  20565  12664   2074    680    660       C  
ATOM    281  C   VAL A  35      67.099  77.762  25.960  1.00111.40           C  
ANISOU  281  C   VAL A  35     9560  20660  12104   2157    615    274       C  
ATOM    282  O   VAL A  35      67.784  78.258  25.080  1.00111.26           O  
ANISOU  282  O   VAL A  35     9289  21105  11878   2089    679    331       O  
ATOM    283  CB  VAL A  35      66.955  79.665  27.653  1.00112.54           C  
ANISOU  283  CB  VAL A  35     9981  20150  12629   2000    783    833       C  
ATOM    284  CG1 VAL A  35      67.904  80.477  26.789  1.00109.10           C  
ANISOU  284  CG1 VAL A  35     9307  20156  11990   1870    901    948       C  
ATOM    285  CG2 VAL A  35      66.025  80.591  28.402  1.00116.07           C  
ANISOU  285  CG2 VAL A  35    10630  20179  13291   1930    879   1195       C  
ATOM    286  N   PHE A  36      67.122  76.465  26.246  1.00134.28           N  
ANISOU  286  N   PHE A  36    16450  17300  17268   1020   -941   1819       N  
ATOM    287  CA  PHE A  36      67.924  75.528  25.495  1.00137.27           C  
ANISOU  287  CA  PHE A  36    16411  17173  18569   1283   -707   1961       C  
ATOM    288  C   PHE A  36      67.093  74.871  24.418  1.00138.12           C  
ANISOU  288  C   PHE A  36    16642  17015  18819   1414   -195   1342       C  
ATOM    289  O   PHE A  36      67.586  74.615  23.334  1.00143.39           O  
ANISOU  289  O   PHE A  36    17200  17365  19914   1466    265    976       O  
ATOM    290  CB  PHE A  36      68.511  74.464  26.419  1.00145.43           C  
ANISOU  290  CB  PHE A  36    16893  18011  20350   1200   -953   2879       C  
ATOM    291  CG  PHE A  36      69.908  74.778  26.912  1.00155.38           C  
ANISOU  291  CG  PHE A  36    17677  19423  21936   1051  -1338   3671       C  
ATOM    292  CD1 PHE A  36      70.166  75.934  27.657  1.00156.46           C  
ANISOU  292  CD1 PHE A  36    18061  20286  21098    564  -1796   3763       C  
ATOM    293  CD2 PHE A  36      70.963  73.900  26.662  1.00161.48           C  
ANISOU  293  CD2 PHE A  36    17681  19587  24084   1309  -1145   4355       C  
ATOM    294  CE1 PHE A  36      71.451  76.211  28.118  1.00155.85           C  
ANISOU  294  CE1 PHE A  36    17505  20519  21192    258  -2204   4537       C  
ATOM    295  CE2 PHE A  36      72.245  74.180  27.121  1.00163.83           C  
ANISOU  295  CE2 PHE A  36    17392  20104  24751   1146  -1568   5274       C  
ATOM    296  CZ  PHE A  36      72.486  75.336  27.848  1.00160.69           C  
ANISOU  296  CZ  PHE A  36    17277  20629  23148    578  -2177   5378       C  
ATOM    297  N   ASN A  37      65.829  74.583  24.724  1.00140.29           N  
ANISOU  297  N   ASN A  37    17143  17480  18680   1324   -225   1188       N  
ATOM    298  CA  ASN A  37      64.922  73.962  23.752  1.00145.67           C  
ANISOU  298  CA  ASN A  37    17932  18116  19299   1241    207    623       C  
ATOM    299  C   ASN A  37      63.611  74.711  23.591  1.00147.89           C  
ANISOU  299  C   ASN A  37    18498  18952  18740   1156     55    408       C  
ATOM    300  O   ASN A  37      62.555  74.196  24.009  1.00154.74           O  
ANISOU  300  O   ASN A  37    19436  19918  19441   1067     35    389       O  
ATOM    301  CB  ASN A  37      64.585  72.521  24.161  1.00148.29           C  
ANISOU  301  CB  ASN A  37    18079  18019  20245   1188    461    733       C  
ATOM    302  CG  ASN A  37      65.806  71.659  24.343  1.00155.12           C  
ANISOU  302  CG  ASN A  37    18436  18158  22342   1333    741   1189       C  
ATOM    303  OD1 ASN A  37      65.694  70.479  24.673  1.00157.89           O  
ANISOU  303  OD1 ASN A  37    18498  17979  23512   1347   1063   1437       O  
ATOM    304  ND2 ASN A  37      66.980  72.231  24.126  1.00158.35           N  
ANISOU  304  ND2 ASN A  37    18644  18473  23046   1459    678   1391       N  
ATOM    305  N   PRO A  38      63.638  75.916  22.956  1.00145.35           N  
ANISOU  305  N   PRO A  38    18252  18954  18019   1195     -7    343       N  
ATOM    306  CA  PRO A  38      62.327  76.480  22.592  1.00147.13           C  
ANISOU  306  CA  PRO A  38    18505  19639  17757   1127    -54    359       C  
ATOM    307  C   PRO A  38      61.473  75.450  21.806  1.00152.05           C  
ANISOU  307  C   PRO A  38    19064  20530  18174    755    133     83       C  
ATOM    308  O   PRO A  38      60.256  75.616  21.672  1.00147.88           O  
ANISOU  308  O   PRO A  38    18449  20438  17298    632     27    236       O  
ATOM    309  CB  PRO A  38      62.701  77.689  21.731  1.00140.01           C  
ANISOU  309  CB  PRO A  38    17529  18975  16693   1179    -65    478       C  
ATOM    310  CG  PRO A  38      64.015  78.137  22.300  1.00135.06           C  
ANISOU  310  CG  PRO A  38    16987  17979  16348   1364   -101    500       C  
ATOM    311  CD  PRO A  38      64.739  76.876  22.707  1.00136.99           C  
ANISOU  311  CD  PRO A  38    17177  17853  17019   1317    -58    419       C  
ATOM    312  N   ASP A  39      62.128  74.355  21.397  1.00159.76           N  
ANISOU  312  N   ASP A  39    20036  21173  19490    529    508   -310       N  
ATOM    313  CA  ASP A  39      61.534  73.272  20.599  1.00170.19           C  
ANISOU  313  CA  ASP A  39    21357  22655  20652    -53    949   -817       C  
ATOM    314  C   ASP A  39      60.122  72.835  21.038  1.00173.60           C  
ANISOU  314  C   ASP A  39    21803  23395  20759   -182    806   -744       C  
ATOM    315  O   ASP A  39      59.217  72.729  20.205  1.00181.93           O  
ANISOU  315  O   ASP A  39    22796  25148  21179   -758    844   -895       O  
ATOM    316  CB  ASP A  39      62.490  72.062  20.559  1.00169.26           C  
ANISOU  316  CB  ASP A  39    21179  21700  21429   -142   1629  -1229       C  
ATOM    317  CG  ASP A  39      62.487  71.352  19.207  1.00170.56           C  
ANISOU  317  CG  ASP A  39    21395  21984  21424  -1005   2439  -2072       C  
ATOM    318  OD1 ASP A  39      61.395  71.158  18.637  1.00168.96           O  
ANISOU  318  OD1 ASP A  39    21282  22517  20398  -1668   2465  -2350       O  
ATOM    319  OD2 ASP A  39      63.578  70.990  18.720  1.00171.33           O  
ANISOU  319  OD2 ASP A  39    21415  21474  22207  -1139   3113  -2472       O  
ATOM    320  N   SER A  40      59.946  72.547  22.327  1.00168.66           N  
ANISOU  320  N   SER A  40    21224  22350  20506    222    631   -473       N  
ATOM    321  CA  SER A  40      58.612  72.239  22.848  1.00166.57           C  
ANISOU  321  CA  SER A  40    20985  22342  19962    142    498   -394       C  
ATOM    322  C   SER A  40      58.334  72.961  24.158  1.00164.36           C  
ANISOU  322  C   SER A  40    20775  21960  19714    553    129     47       C  
ATOM    323  O   SER A  40      58.442  72.383  25.245  1.00165.70           O  
ANISOU  323  O   SER A  40    21032  21772  20152    634     84    176       O  
ATOM    324  CB  SER A  40      58.393  70.723  22.982  1.00164.93           C  
ANISOU  324  CB  SER A  40    20811  21738  20115   -133    950   -763       C  
ATOM    325  OG  SER A  40      58.888  70.234  24.209  1.00163.76           O  
ANISOU  325  OG  SER A  40    20651  20952  20617    235    878   -406       O  
ATOM    326  N   TRP A  41      57.988  74.238  24.040  1.00158.69           N  
ANISOU  326  N   TRP A  41    19979  21552  18762    704    -42    300       N  
ATOM    327  CA  TRP A  41      57.503  75.041  25.169  1.00153.47           C  
ANISOU  327  CA  TRP A  41    19389  20766  18155    900    -94    520       C  
ATOM    328  C   TRP A  41      56.282  74.400  25.877  1.00150.51           C  
ANISOU  328  C   TRP A  41    19049  20425  17714    773    -40    477       C  
ATOM    329  O   TRP A  41      55.968  74.729  27.032  1.00148.38           O  
ANISOU  329  O   TRP A  41    18935  19966  17477    756     43    491       O  
ATOM    330  CB  TRP A  41      57.132  76.443  24.676  1.00155.07           C  
ANISOU  330  CB  TRP A  41    19345  21149  18424   1077    -27    823       C  
ATOM    331  CG  TRP A  41      56.103  76.430  23.581  1.00156.27           C  
ANISOU  331  CG  TRP A  41    19080  21875  18419    927   -108   1134       C  
ATOM    332  CD1 TRP A  41      56.323  76.613  22.247  1.00154.38           C  
ANISOU  332  CD1 TRP A  41    18582  22167  17906    697   -256   1343       C  
ATOM    333  CD2 TRP A  41      54.694  76.195  23.730  1.00160.11           C  
ANISOU  333  CD2 TRP A  41    19299  22614  18920    833    -90   1360       C  
ATOM    334  NE1 TRP A  41      55.139  76.514  21.555  1.00161.25           N  
ANISOU  334  NE1 TRP A  41    19000  23736  18528    368   -410   1785       N  
ATOM    335  CE2 TRP A  41      54.124  76.259  22.442  1.00163.30           C  
ANISOU  335  CE2 TRP A  41    19215  23800  19028    508   -313   1822       C  
ATOM    336  CE3 TRP A  41      53.856  75.944  24.834  1.00155.08           C  
ANISOU  336  CE3 TRP A  41    18760  21685  18476    895     91   1249       C  
ATOM    337  CZ2 TRP A  41      52.755  76.083  22.221  1.00165.68           C  
ANISOU  337  CZ2 TRP A  41    19044  24629  19277    283   -420   2282       C  
ATOM    338  CZ3 TRP A  41      52.505  75.753  24.614  1.00154.61           C  
ANISOU  338  CZ3 TRP A  41    18293  22000  18451    772     77   1574       C  
ATOM    339  CH2 TRP A  41      51.963  75.831  23.318  1.00162.70           C  
ANISOU  339  CH2 TRP A  41    18753  23828  19237    491   -204   2138       C  
ATOM    340  N   LEU A  42      55.583  73.521  25.162  1.00147.55           N  
ANISOU  340  N   LEU A  42    18544  20340  17176    547    -16    353       N  
ATOM    341  CA  LEU A  42      54.370  72.897  25.675  1.00142.76           C  
ANISOU  341  CA  LEU A  42    17929  19822  16491    401     40    306       C  
ATOM    342  C   LEU A  42      54.644  72.191  26.984  1.00144.26           C  
ANISOU  342  C   LEU A  42    18421  19568  16822    389     57    220       C  
ATOM    343  O   LEU A  42      53.975  72.446  27.985  1.00148.48           O  
ANISOU  343  O   LEU A  42    19059  20043  17312    351    105    264       O  
ATOM    344  CB  LEU A  42      53.823  71.900  24.665  1.00140.88           C  
ANISOU  344  CB  LEU A  42    17558  19998  15971    -34    122     69       C  
ATOM    345  CG  LEU A  42      52.328  71.932  24.346  1.00138.90           C  
ANISOU  345  CG  LEU A  42    16980  20350  15444   -289     53    279       C  
ATOM    346  CD1 LEU A  42      51.935  70.633  23.665  1.00139.71           C  
ANISOU  346  CD1 LEU A  42    17116  20796  15168   -947    244   -176       C  
ATOM    347  CD2 LEU A  42      51.486  72.158  25.585  1.00136.13           C  
ANISOU  347  CD2 LEU A  42    16659  19699  15362    -18    106    426       C  
ATOM    348  N   ALA A  43      55.638  71.303  26.975  1.00126.79           N  
ANISOU  348  N   ALA A  43    15947  20012  12216   -220    -43   -270       N  
ATOM    349  CA  ALA A  43      56.055  70.591  28.190  1.00117.53           C  
ANISOU  349  CA  ALA A  43    14497  18910  11248    139    125   -372       C  
ATOM    350  C   ALA A  43      56.576  71.552  29.232  1.00109.31           C  
ANISOU  350  C   ALA A  43    13084  18029  10419    342    140   -373       C  
ATOM    351  O   ALA A  43      56.429  71.303  30.422  1.00104.80           O  
ANISOU  351  O   ALA A  43    12247  17507  10065    615    123   -362       O  
ATOM    352  CB  ALA A  43      57.101  69.541  27.866  1.00122.08           C  
ANISOU  352  CB  ALA A  43    15223  19488  11672    244    491   -578       C  
ATOM    353  N   SER A  44      57.155  72.669  28.770  1.00107.31           N  
ANISOU  353  N   SER A  44    12871  17838  10062    153    173   -386       N  
ATOM    354  CA  SER A  44      57.720  73.688  29.652  1.00109.05           C  
ANISOU  354  CA  SER A  44    12837  18200  10396    223    212   -402       C  
ATOM    355  C   SER A  44      56.672  74.468  30.421  1.00109.49           C  
ANISOU  355  C   SER A  44    12824  18136  10641    332    -54   -213       C  
ATOM    356  O   SER A  44      56.800  74.652  31.638  1.00115.19           O  
ANISOU  356  O   SER A  44    13274  18940  11552    538    -31   -224       O  
ATOM    357  CB  SER A  44      58.632  74.640  28.886  1.00111.05           C  
ANISOU  357  CB  SER A  44    13247  18536  10410   -100    352   -484       C  
ATOM    358  OG  SER A  44      59.990  74.363  29.178  1.00123.09           O  
ANISOU  358  OG  SER A  44    14502  20387  11878    -60    659   -686       O  
ATOM    359  N   VAL A  45      55.638  74.935  29.730  1.00109.67           N  
ANISOU  359  N   VAL A  45    13087  17988  10595    220   -302    -31       N  
ATOM    360  CA  VAL A  45      54.482  75.532  30.424  1.00108.88           C  
ANISOU  360  CA  VAL A  45    12891  17807  10669    420   -550    172       C  
ATOM    361  C   VAL A  45      53.804  74.488  31.361  1.00103.81           C  
ANISOU  361  C   VAL A  45    11950  17236  10254    660   -607    184       C  
ATOM    362  O   VAL A  45      53.439  74.809  32.510  1.00 99.81           O  
ANISOU  362  O   VAL A  45    11219  16744   9958    892   -648    237       O  
ATOM    363  CB  VAL A  45      53.474  76.197  29.429  1.00110.87           C  
ANISOU  363  CB  VAL A  45    13421  17938  10767    319   -824    397       C  
ATOM    364  CG1 VAL A  45      52.093  76.364  30.061  1.00107.12           C  
ANISOU  364  CG1 VAL A  45    12743  17489  10469    600  -1084    618       C  
ATOM    365  CG2 VAL A  45      54.009  77.547  28.957  1.00110.12           C  
ANISOU  365  CG2 VAL A  45    13663  17696  10480    169   -777    422       C  
ATOM    366  N   ALA A  46      53.717  73.238  30.887  1.00100.45           N  
ANISOU  366  N   ALA A  46    11587  16829   9750    572   -570    117       N  
ATOM    367  CA  ALA A  46      53.205  72.124  31.694  1.00 99.81           C  
ANISOU  367  CA  ALA A  46    11339  16778   9806    723   -574     96       C  
ATOM    368  C   ALA A  46      54.015  71.927  32.947  1.00101.53           C  
ANISOU  368  C   ALA A  46    11318  17054  10203    989   -379    -30       C  
ATOM    369  O   ALA A  46      53.470  71.558  33.983  1.00106.74           O  
ANISOU  369  O   ALA A  46    11792  17726  11036   1166   -429      1       O  
ATOM    370  CB  ALA A  46      53.176  70.834  30.886  1.00 98.56           C  
ANISOU  370  CB  ALA A  46    11444  16559   9445    533   -500     16       C  
ATOM    371  N   ALA A  47      55.331  72.128  32.841  1.00102.67           N  
ANISOU  371  N   ALA A  47    11452  17281  10276    996   -153   -177       N  
ATOM    372  CA  ALA A  47      56.230  71.988  33.986  1.00 95.61           C  
ANISOU  372  CA  ALA A  47    10286  16538   9503   1236     18   -287       C  
ATOM    373  C   ALA A  47      56.076  73.160  34.935  1.00 95.48           C  
ANISOU  373  C   ALA A  47    10087  16553   9636   1280    -70   -215       C  
ATOM    374  O   ALA A  47      55.820  72.963  36.102  1.00 93.17           O  
ANISOU  374  O   ALA A  47     9600  16279   9519   1483    -94   -197       O  
ATOM    375  CB  ALA A  47      57.656  71.860  33.526  1.00 92.44           C  
ANISOU  375  CB  ALA A  47     9860  16327   8936   1211    279   -453       C  
ATOM    376  N   VAL A  48      56.156  74.385  34.403  1.00 99.70           N  
ANISOU  376  N   VAL A  48    10767  17044  10069   1073   -112   -165       N  
ATOM    377  CA  VAL A  48      56.102  75.609  35.230  1.00100.68           C  
ANISOU  377  CA  VAL A  48    10856  17132  10263   1082   -144   -108       C  
ATOM    378  C   VAL A  48      54.829  75.723  36.089  1.00107.37           C  
ANISOU  378  C   VAL A  48    11619  17847  11327   1316   -319     44       C  
ATOM    379  O   VAL A  48      54.918  75.791  37.326  1.00110.02           O  
ANISOU  379  O   VAL A  48    11767  18226  11807   1465   -270     18       O  
ATOM    380  CB  VAL A  48      56.319  76.888  34.393  1.00 98.73           C  
ANISOU  380  CB  VAL A  48    10935  16774   9802    807   -146    -69       C  
ATOM    381  CG1 VAL A  48      55.997  78.134  35.212  1.00 94.63           C  
ANISOU  381  CG1 VAL A  48    10531  16102   9323    846   -179     19       C  
ATOM    382  CG2 VAL A  48      57.756  76.946  33.908  1.00101.07           C  
ANISOU  382  CG2 VAL A  48    11228  17292   9881    534     82   -255       C  
ATOM    383  N   THR A  49      53.656  75.760  35.441  1.00108.15           N  
ANISOU  383  N   THR A  49    11834  17830  11425   1339   -519    207       N  
ATOM    384  CA  THR A  49      52.378  75.522  36.144  1.00103.00           C  
ANISOU  384  CA  THR A  49    11004  17169  10960   1561   -674    342       C  
ATOM    385  C   THR A  49      52.346  74.049  36.455  1.00104.79           C  
ANISOU  385  C   THR A  49    11073  17491  11251   1583   -636    248       C  
ATOM    386  O   THR A  49      52.434  73.225  35.550  1.00114.25           O  
ANISOU  386  O   THR A  49    12396  18701  12309   1428   -635    206       O  
ATOM    387  CB  THR A  49      51.154  75.838  35.248  1.00101.25           C  
ANISOU  387  CB  THR A  49    10877  16926  10666   1562   -916    552       C  
ATOM    388  OG1 THR A  49      51.023  74.830  34.232  1.00 94.03           O  
ANISOU  388  OG1 THR A  49    10029  16085   9612   1346   -983    530       O  
ATOM    389  CG2 THR A  49      51.296  77.198  34.588  1.00103.27           C  
ANISOU  389  CG2 THR A  49    11443  17026  10766   1530   -948    652       C  
ATOM    390  N   GLY A  50      52.264  73.694  37.719  1.00 99.67           N  
ANISOU  390  N   GLY A  50    10222  16874  10772   1758   -581    209       N  
ATOM    391  CA  GLY A  50      52.455  72.289  38.080  1.00104.00           C  
ANISOU  391  CA  GLY A  50    10723  17459  11332   1793   -499    103       C  
ATOM    392  C   GLY A  50      53.506  72.142  39.144  1.00112.83           C  
ANISOU  392  C   GLY A  50    11712  18639  12518   1952   -327    -22       C  
ATOM    393  O   GLY A  50      53.280  71.485  40.160  1.00125.05           O  
ANISOU  393  O   GLY A  50    13160  20183  14169   2096   -305    -42       O  
ATOM    394  N   ILE A  51      54.658  72.772  38.930  1.00107.00           N  
ANISOU  394  N   ILE A  51    10970  17991  11691   1897   -211   -101       N  
ATOM    395  CA  ILE A  51      55.520  73.118  40.031  1.00105.87           C  
ANISOU  395  CA  ILE A  51    10642  17987  11595   1987   -103   -175       C  
ATOM    396  C   ILE A  51      54.773  74.100  40.931  1.00106.90           C  
ANISOU  396  C   ILE A  51    10745  18010  11862   2014   -182    -80       C  
ATOM    397  O   ILE A  51      54.656  73.881  42.143  1.00118.87           O  
ANISOU  397  O   ILE A  51    12123  19544  13497   2153   -165    -90       O  
ATOM    398  CB  ILE A  51      56.855  73.704  39.551  1.00106.23           C  
ANISOU  398  CB  ILE A  51    10664  18234  11463   1823     33   -277       C  
ATOM    399  CG1 ILE A  51      57.823  72.575  39.248  1.00111.94           C  
ANISOU  399  CG1 ILE A  51    11291  19158  12082   1953    180   -394       C  
ATOM    400  CG2 ILE A  51      57.464  74.607  40.609  1.00102.38           C  
ANISOU  400  CG2 ILE A  51    10037  17888  10975   1758     88   -310       C  
ATOM    401  CD1 ILE A  51      58.825  72.913  38.167  1.00122.59           C  
ANISOU  401  CD1 ILE A  51    12669  20693  13215   1752    314   -485       C  
ATOM    402  N   LEU A  52      54.216  75.145  40.328  1.00 98.23           N  
ANISOU  402  N   LEU A  52     9817  16775  10727   1913   -260     20       N  
ATOM    403  CA  LEU A  52      53.384  76.085  41.062  1.00 94.68           C  
ANISOU  403  CA  LEU A  52     9408  16182  10383   2016   -308    129       C  
ATOM    404  C   LEU A  52      52.177  75.412  41.683  1.00 97.49           C  
ANISOU  404  C   LEU A  52     9597  16523  10919   2214   -403    210       C  
ATOM    405  O   LEU A  52      51.828  75.697  42.824  1.00101.19           O  
ANISOU  405  O   LEU A  52     9986  16951  11507   2343   -364    225       O  
ATOM    406  CB  LEU A  52      52.926  77.208  40.162  1.00 92.92           C  
ANISOU  406  CB  LEU A  52     9457  15795  10052   1960   -378    253       C  
ATOM    407  CG  LEU A  52      53.950  78.295  39.930  1.00 92.72           C  
ANISOU  407  CG  LEU A  52     9692  15710   9823   1725   -250    186       C  
ATOM    408  CD1 LEU A  52      53.692  78.927  38.588  1.00 94.66           C  
ANISOU  408  CD1 LEU A  52    10253  15815   9897   1622   -330    286       C  
ATOM    409  CD2 LEU A  52      53.901  79.331  41.043  1.00 93.58           C  
ANISOU  409  CD2 LEU A  52     9945  15668   9941   1766   -153    201       C  
ATOM    410  N   CYS A  53      51.517  74.539  40.923  1.00 99.30           N  
ANISOU  410  N   CYS A  53     9796  16797  11135   2188   -516    256       N  
ATOM    411  CA  CYS A  53      50.454  73.735  41.492  1.00 95.60           C  
ANISOU  411  CA  CYS A  53     9163  16379  10779   2272   -588    303       C  
ATOM    412  C   CYS A  53      50.923  73.100  42.800  1.00 93.82           C  
ANISOU  412  C   CYS A  53     8841  16160  10644   2358   -466    190       C  
ATOM    413  O   CYS A  53      50.360  73.391  43.859  1.00 92.15           O  
ANISOU  413  O   CYS A  53     8519  15932  10559   2474   -449    223       O  
ATOM    414  CB  CYS A  53      49.965  72.665  40.522  1.00 97.32           C  
ANISOU  414  CB  CYS A  53     9426  16664  10887   2110   -687    319       C  
ATOM    415  SG  CYS A  53      48.680  71.600  41.224  1.00108.10           S  
ANISOU  415  SG  CYS A  53    10627  18134  12311   2076   -754    353       S  
ATOM    416  N   VAL A  54      51.967  72.261  42.749  1.00 86.34           N  
ANISOU  416  N   VAL A  54     7947  15245   9614   2334   -371     64       N  
ATOM    417  CA  VAL A  54      52.256  71.410  43.919  1.00 89.46           C  
ANISOU  417  CA  VAL A  54     8283  15649  10057   2457   -290    -11       C  
ATOM    418  C   VAL A  54      52.922  72.100  45.088  1.00 88.79           C  
ANISOU  418  C   VAL A  54     8089  15613  10034   2541   -213    -49       C  
ATOM    419  O   VAL A  54      52.659  71.754  46.235  1.00 92.32           O  
ANISOU  419  O   VAL A  54     8481  16037  10559   2631   -191    -58       O  
ATOM    420  CB  VAL A  54      52.948  70.058  43.597  1.00 91.55           C  
ANISOU  420  CB  VAL A  54     8683  15912  10188   2505   -210   -103       C  
ATOM    421  CG1 VAL A  54      52.138  69.270  42.591  1.00 96.26           C  
ANISOU  421  CG1 VAL A  54     9470  16421  10682   2345   -272    -74       C  
ATOM    422  CG2 VAL A  54      54.379  70.254  43.134  1.00 96.78           C  
ANISOU  422  CG2 VAL A  54     9321  16711  10738   2555   -104   -185       C  
ATOM    423  N   VAL A  55      53.743  73.104  44.816  1.00 86.43           N  
ANISOU  423  N   VAL A  55     7793  15381   9666   2457   -169    -72       N  
ATOM    424  CA  VAL A  55      54.201  73.967  45.883  1.00 84.84           C  
ANISOU  424  CA  VAL A  55     7543  15216   9476   2433   -104    -97       C  
ATOM    425  C   VAL A  55      53.001  74.645  46.527  1.00 86.85           C  
ANISOU  425  C   VAL A  55     7846  15286   9865   2491   -127     -6       C  
ATOM    426  O   VAL A  55      52.909  74.720  47.749  1.00 88.23           O  
ANISOU  426  O   VAL A  55     7981  15440  10101   2541    -76    -24       O  
ATOM    427  CB  VAL A  55      55.215  74.996  45.393  1.00 82.96           C  
ANISOU  427  CB  VAL A  55     7365  15080   9075   2226    -38   -143       C  
ATOM    428  CG1 VAL A  55      55.654  75.908  46.544  1.00 75.57           C  
ANISOU  428  CG1 VAL A  55     6444  14176   8090   2109     37   -175       C  
ATOM    429  CG2 VAL A  55      56.394  74.270  44.794  1.00 82.50           C  
ANISOU  429  CG2 VAL A  55     7183  15284   8879   2208     11   -236       C  
ATOM    430  N   PHE A  56      52.038  75.061  45.711  1.00 90.03           N  
ANISOU  430  N   PHE A  56     8321  15584  10301   2514   -204     99       N  
ATOM    431  CA  PHE A  56      50.817  75.669  46.254  1.00 90.92           C  
ANISOU  431  CA  PHE A  56     8429  15583  10532   2659   -213    206       C  
ATOM    432  C   PHE A  56      49.987  74.709  47.109  1.00 87.10           C  
ANISOU  432  C   PHE A  56     7764  15153  10174   2748   -226    205       C  
ATOM    433  O   PHE A  56      49.604  75.064  48.216  1.00 87.63           O  
ANISOU  433  O   PHE A  56     7809  15162  10321   2836   -143    208       O  
ATOM    434  CB  PHE A  56      49.987  76.349  45.171  1.00 92.88           C  
ANISOU  434  CB  PHE A  56     8757  15777  10755   2727   -310    350       C  
ATOM    435  CG  PHE A  56      50.382  77.784  44.913  1.00 98.17           C  
ANISOU  435  CG  PHE A  56     9725  16266  11310   2715   -236    387       C  
ATOM    436  CD1 PHE A  56      51.708  78.151  44.858  1.00101.08           C  
ANISOU  436  CD1 PHE A  56    10257  16621  11526   2477   -141    269       C  
ATOM    437  CD2 PHE A  56      49.424  78.755  44.709  1.00106.14           C  
ANISOU  437  CD2 PHE A  56    10871  17136  12321   2942   -253    546       C  
ATOM    438  CE1 PHE A  56      52.071  79.462  44.611  1.00105.46           C  
ANISOU  438  CE1 PHE A  56    11173  16984  11912   2375    -54    289       C  
ATOM    439  CE2 PHE A  56      49.781  80.070  44.472  1.00107.50           C  
ANISOU  439  CE2 PHE A  56    11449  17060  12334   2934   -159    583       C  
ATOM    440  CZ  PHE A  56      51.104  80.420  44.418  1.00107.80           C  
ANISOU  440  CZ  PHE A  56    11714  17044  12199   2606    -56    446       C  
ATOM    441  N   VAL A  57      49.786  73.475  46.642  1.00 82.39           N  
ANISOU  441  N   VAL A  57     7101  14647   9555   2684   -302    185       N  
ATOM    442  CA  VAL A  57      49.182  72.444  47.502  1.00 81.23           C  
ANISOU  442  CA  VAL A  57     6871  14530   9460   2685   -288    155       C  
ATOM    443  C   VAL A  57      49.945  72.309  48.813  1.00 80.09           C  
ANISOU  443  C   VAL A  57     6760  14335   9333   2735   -179     63       C  
ATOM    444  O   VAL A  57      49.341  72.197  49.896  1.00 81.71           O  
ANISOU  444  O   VAL A  57     6919  14514   9612   2769   -126     60       O  
ATOM    445  CB  VAL A  57      49.135  71.061  46.838  1.00 81.47           C  
ANISOU  445  CB  VAL A  57     6980  14594   9381   2555   -341    117       C  
ATOM    446  CG1 VAL A  57      48.515  70.058  47.793  1.00 83.46           C  
ANISOU  446  CG1 VAL A  57     7241  14833   9634   2504   -303     80       C  
ATOM    447  CG2 VAL A  57      48.332  71.105  45.562  1.00 82.77           C  
ANISOU  447  CG2 VAL A  57     7111  14851   9486   2434   -470    211       C  
ATOM    448  N   GLY A  58      51.271  72.271  48.710  1.00 78.86           N  
ANISOU  448  N   GLY A  58     6664  14214   9085   2729   -147     -8       N  
ATOM    449  CA  GLY A  58      52.146  72.238  49.880  1.00 75.30           C  
ANISOU  449  CA  GLY A  58     6204  13803   8603   2767    -76    -76       C  
ATOM    450  C   GLY A  58      51.802  73.325  50.869  1.00 75.23           C  
ANISOU  450  C   GLY A  58     6206  13717   8661   2745     -7    -58       C  
ATOM    451  O   GLY A  58      51.515  73.039  52.004  1.00 76.20           O  
ANISOU  451  O   GLY A  58     6329  13800   8822   2774     36    -77       O  
ATOM    452  N   LYS A  59      51.792  74.580  50.418  1.00 78.53           N  
ANISOU  452  N   LYS A  59     6698  14074   9064   2692     22    -22       N  
ATOM    453  CA  LYS A  59      51.537  75.732  51.322  1.00 83.32           C  
ANISOU  453  CA  LYS A  59     7436  14541   9681   2678    137    -10       C  
ATOM    454  C   LYS A  59      50.141  75.752  51.862  1.00 90.29           C  
ANISOU  454  C   LYS A  59     8279  15317  10709   2838    180     54       C  
ATOM    455  O   LYS A  59      49.830  76.551  52.754  1.00 97.39           O  
ANISOU  455  O   LYS A  59     9306  16078  11619   2876    313     56       O  
ATOM    456  CB  LYS A  59      51.784  77.059  50.607  1.00 84.96           C  
ANISOU  456  CB  LYS A  59     7856  14637   9787   2600    184     23       C  
ATOM    457  CG  LYS A  59      53.229  77.539  50.640  1.00 85.35           C  
ANISOU  457  CG  LYS A  59     8001  14799   9627   2328    229    -68       C  
ATOM    458  CD  LYS A  59      53.736  77.665  52.046  1.00 83.16           C  
ANISOU  458  CD  LYS A  59     7749  14569   9278   2201    310   -138       C  
ATOM    459  CE  LYS A  59      53.528  79.050  52.582  1.00 82.05           C  
ANISOU  459  CE  LYS A  59     7978  14167   9030   2077    472   -133       C  
ATOM    460  NZ  LYS A  59      53.722  79.009  54.046  1.00 85.90           N  
ANISOU  460  NZ  LYS A  59     8495  14671   9472   1974    547   -191       N  
ATOM    461  N   GLY A  60      49.277  74.916  51.285  1.00 91.32           N  
ANISOU  461  N   GLY A  60     8243  15533  10919   2910     84    105       N  
ATOM    462  CA  GLY A  60      47.871  74.887  51.655  1.00 90.33           C  
ANISOU  462  CA  GLY A  60     7984  15428  10906   3035    115    174       C  
ATOM    463  C   GLY A  60      47.085  76.036  51.040  1.00 95.18           C  
ANISOU  463  C   GLY A  60     8606  16007  11551   3233    130    304       C  
ATOM    464  O   GLY A  60      46.004  76.404  51.543  1.00 96.24           O  
ANISOU  464  O   GLY A  60     8632  16169  11763   3424    215    371       O  
ATOM    465  N   LYS A  61      47.630  76.603  49.951  1.00 94.34           N  
ANISOU  465  N   LYS A  61     8637  15847  11359   3215     60    345       N  
ATOM    466  CA  LYS A  61      46.999  77.729  49.217  1.00 97.48           C  
ANISOU  466  CA  LYS A  61     9134  16169  11734   3438     55    492       C  
ATOM    467  C   LYS A  61      45.968  77.225  48.209  1.00101.68           C  
ANISOU  467  C   LYS A  61     9385  16954  12295   3524   -126    622       C  
ATOM    468  O   LYS A  61      46.167  76.156  47.593  1.00 97.01           O  
ANISOU  468  O   LYS A  61     8670  16515  11673   3303   -261    578       O  
ATOM    469  CB  LYS A  61      48.064  78.560  48.481  1.00 92.48           C  
ANISOU  469  CB  LYS A  61     8837  15357  10944   3315     63    475       C  
ATOM    470  CG  LYS A  61      48.863  79.483  49.373  1.00 90.29           C  
ANISOU  470  CG  LYS A  61     8899  14841  10562   3215    257    388       C  
ATOM    471  CD  LYS A  61      49.925  80.236  48.597  1.00 88.13           C  
ANISOU  471  CD  LYS A  61     8955  14450  10080   2988    270    356       C  
ATOM    472  CE  LYS A  61      50.723  81.126  49.537  1.00 87.50           C  
ANISOU  472  CE  LYS A  61     9233  14177   9833   2776    468    257       C  
ATOM    473  NZ  LYS A  61      50.187  82.514  49.567  1.00 87.82           N  
ANISOU  473  NZ  LYS A  61     9765  13847   9755   2958    633    352       N  
ATOM    474  N   ILE A  62      44.886  78.004  48.010  1.00102.06           N  
ANISOU  474  N   ILE A  62     9353  17058  12365   3850   -124    790       N  
ATOM    475  CA  ILE A  62      43.742  77.537  47.189  1.00102.65           C  
ANISOU  475  CA  ILE A  62     9061  17498  12442   3928   -313    937       C  
ATOM    476  C   ILE A  62      43.916  77.652  45.649  1.00102.11           C  
ANISOU  476  C   ILE A  62     9075  17478  12244   3862   -521   1040       C  
ATOM    477  O   ILE A  62      43.433  76.789  44.890  1.00 97.03           O  
ANISOU  477  O   ILE A  62     8180  17137  11550   3677   -711   1084       O  
ATOM    478  CB  ILE A  62      42.391  78.146  47.644  1.00106.39           C  
ANISOU  478  CB  ILE A  62     9276  18168  12979   4348   -243   1095       C  
ATOM    479  CG1 ILE A  62      41.281  77.729  46.699  1.00110.50           C  
ANISOU  479  CG1 ILE A  62     9364  19172  13449   4392   -475   1267       C  
ATOM    480  CG2 ILE A  62      42.452  79.662  47.716  1.00109.47           C  
ANISOU  480  CG2 ILE A  62    10037  18230  13325   4766    -93   1200       C  
ATOM    481  CD1 ILE A  62      40.308  76.731  47.295  1.00121.73           C  
ANISOU  481  CD1 ILE A  62    10301  21034  14916   4234   -482   1237       C  
ATOM    482  N   SER A  63      44.607  78.700  45.199  1.00103.36           N  
ANISOU  482  N   SER A  63     9630  17330  12309   3955   -476   1071       N  
ATOM    483  CA  SER A  63      44.767  78.936  43.772  1.00101.25           C  
ANISOU  483  CA  SER A  63     9503  17071  11894   3900   -653   1174       C  
ATOM    484  C   SER A  63      45.740  77.944  43.169  1.00 96.07           C  
ANISOU  484  C   SER A  63     8888  16436  11178   3459   -726   1018       C  
ATOM    485  O   SER A  63      46.129  78.069  42.015  1.00100.05           O  
ANISOU  485  O   SER A  63     9567  16904  11542   3328   -834   1054       O  
ATOM    486  CB  SER A  63      45.178  80.387  43.484  1.00104.48           C  
ANISOU  486  CB  SER A  63    10409  17114  12173   4107   -556   1253       C  
ATOM    487  OG  SER A  63      46.568  80.569  43.619  1.00111.84           O  
ANISOU  487  OG  SER A  63    11697  17772  13023   3783   -426   1070       O  
ATOM    488  N   ASN A  64      46.089  76.924  43.944  1.00 89.29           N  
ANISOU  488  N   ASN A  64     7885  15634  10406   3260   -656    854       N  
ATOM    489  CA  ASN A  64      46.749  75.778  43.392  1.00 91.50           C  
ANISOU  489  CA  ASN A  64     8169  15978  10618   2938   -717    733       C  
ATOM    490  C   ASN A  64      45.913  75.187  42.286  1.00 98.50           C  
ANISOU  490  C   ASN A  64     8904  17111  11409   2821   -924    844       C  
ATOM    491  O   ASN A  64      46.438  74.616  41.329  1.00109.46           O  
ANISOU  491  O   ASN A  64    10428  18492  12667   2578   -990    794       O  
ATOM    492  CB  ASN A  64      47.057  74.731  44.476  1.00 92.08           C  
ANISOU  492  CB  ASN A  64     8146  16066  10772   2826   -612    575       C  
ATOM    493  CG  ASN A  64      45.861  73.848  44.821  1.00 92.24           C  
ANISOU  493  CG  ASN A  64     7893  16321  10831   2778   -675    614       C  
ATOM    494  OD1 ASN A  64      45.436  72.992  44.027  1.00 89.38           O  
ANISOU  494  OD1 ASN A  64     7473  16126  10360   2561   -802    635       O  
ATOM    495  ND2 ASN A  64      45.386  73.977  46.046  1.00 93.16           N  
ANISOU  495  ND2 ASN A  64     7878  16451  11067   2910   -565    600       N  
ATOM    496  N   TYR A  65      44.612  75.407  42.368  1.00102.48           N  
ANISOU  496  N   TYR A  65     9127  17863  11946   2996  -1022   1007       N  
ATOM    497  CA  TYR A  65      43.672  74.696  41.522  1.00102.68           C  
ANISOU  497  CA  TYR A  65     8916  18245  11851   2809  -1233   1111       C  
ATOM    498  C   TYR A  65      43.630  75.129  40.056  1.00104.92           C  
ANISOU  498  C   TYR A  65     9324  18580  11961   2772  -1428   1254       C  
ATOM    499  O   TYR A  65      43.524  74.277  39.162  1.00107.29           O  
ANISOU  499  O   TYR A  65     9632  19035  12097   2425  -1565   1245       O  
ATOM    500  CB  TYR A  65      42.286  74.681  42.148  1.00 99.16           C  
ANISOU  500  CB  TYR A  65     8029  18179  11468   2968  -1275   1233       C  
ATOM    501  CG  TYR A  65      42.132  73.613  43.211  1.00 94.90           C  
ANISOU  501  CG  TYR A  65     7362  17706  10990   2742  -1153   1074       C  
ATOM    502  CD1 TYR A  65      42.141  72.258  42.866  1.00 94.19           C  
ANISOU  502  CD1 TYR A  65     7324  17711  10750   2278  -1209    969       C  
ATOM    503  CD2 TYR A  65      41.994  73.950  44.562  1.00 92.79           C  
ANISOU  503  CD2 TYR A  65     7004  17359  10891   2973   -962   1024       C  
ATOM    504  CE1 TYR A  65      41.996  71.270  43.826  1.00 94.30           C  
ANISOU  504  CE1 TYR A  65     7321  17735  10771   2060  -1088    830       C  
ATOM    505  CE2 TYR A  65      41.828  72.969  45.531  1.00 93.20           C  
ANISOU  505  CE2 TYR A  65     6982  17461  10969   2747   -854    885       C  
ATOM    506  CZ  TYR A  65      41.835  71.624  45.154  1.00 95.32           C  
ANISOU  506  CZ  TYR A  65     7327  17813  11077   2293   -921    791       C  
ATOM    507  OH  TYR A  65      41.700  70.622  46.103  1.00 97.99           O  
ANISOU  507  OH  TYR A  65     7700  18139  11391   2052   -802    654       O  
ATOM    508  N   LEU A  66      43.723  76.429  39.791  1.00106.08           N  
ANISOU  508  N   LEU A  66     9640  18562  12100   3100  -1429   1384       N  
ATOM    509  CA  LEU A  66      43.736  76.864  38.398  1.00113.86           C  
ANISOU  509  CA  LEU A  66    10813  19558  12890   3059  -1615   1524       C  
ATOM    510  C   LEU A  66      45.034  76.419  37.748  1.00114.02           C  
ANISOU  510  C   LEU A  66    11193  19318  12810   2687  -1546   1338       C  
ATOM    511  O   LEU A  66      45.025  75.865  36.642  1.00117.21           O  
ANISOU  511  O   LEU A  66    11664  19832  13037   2398  -1692   1356       O  
ATOM    512  CB  LEU A  66      43.513  78.377  38.248  1.00115.48           C  
ANISOU  512  CB  LEU A  66    11221  19596  13060   3520  -1618   1721       C  
ATOM    513  CG  LEU A  66      44.722  79.281  38.371  1.00116.01           C  
ANISOU  513  CG  LEU A  66    11816  19162  13098   3539  -1414   1612       C  
ATOM    514  CD1 LEU A  66      44.388  80.693  37.896  1.00113.73           C  
ANISOU  514  CD1 LEU A  66    11862  18680  12670   3939  -1450   1838       C  
ATOM    515  CD2 LEU A  66      45.219  79.256  39.818  1.00113.46           C  
ANISOU  515  CD2 LEU A  66    11483  18663  12961   3572  -1152   1427       C  
ATOM    516  N   PHE A  67      46.141  76.601  38.474  1.00109.04           N  
ANISOU  516  N   PHE A  67    10767  18391  12272   2680  -1314   1153       N  
ATOM    517  CA  PHE A  67      47.452  76.150  38.027  1.00 98.06           C  
ANISOU  517  CA  PHE A  67     9631  16832  10793   2379  -1205    961       C  
ATOM    518  C   PHE A  67      47.424  74.674  37.701  1.00 97.50           C  
ANISOU  518  C   PHE A  67     9466  16911  10667   2088  -1243    861       C  
ATOM    519  O   PHE A  67      47.905  74.257  36.653  1.00100.62           O  
ANISOU  519  O   PHE A  67    10060  17277  10892   1841  -1269    812       O  
ATOM    520  CB  PHE A  67      48.484  76.401  39.097  1.00 92.08           C  
ANISOU  520  CB  PHE A  67     8957  15887  10142   2421   -969    791       C  
ATOM    521  CG  PHE A  67      48.822  77.842  39.288  1.00 93.45           C  
ANISOU  521  CG  PHE A  67     9396  15834  10276   2569   -878    840       C  
ATOM    522  CD1 PHE A  67      49.225  78.629  38.211  1.00 94.78           C  
ANISOU  522  CD1 PHE A  67     9907  15861  10244   2471   -910    895       C  
ATOM    523  CD2 PHE A  67      48.802  78.408  40.563  1.00 95.03           C  
ANISOU  523  CD2 PHE A  67     9586  15921  10596   2759   -732    816       C  
ATOM    524  CE1 PHE A  67      49.569  79.962  38.399  1.00 97.83           C  
ANISOU  524  CE1 PHE A  67    10658  15979  10531   2553   -795    929       C  
ATOM    525  CE2 PHE A  67      49.134  79.741  40.755  1.00 97.87           C  
ANISOU  525  CE2 PHE A  67    10307  16015  10861   2845   -612    848       C  
ATOM    526  CZ  PHE A  67      49.514  80.521  39.669  1.00 99.95           C  
ANISOU  526  CZ  PHE A  67    10951  16120  10905   2737   -640    905       C  
ATOM    527  N   GLY A  68      46.850  73.882  38.603  1.00 97.67           N  
ANISOU  527  N   GLY A  68     9245  17063  10799   2098  -1222    824       N  
ATOM    528  CA  GLY A  68      46.708  72.437  38.376  1.00105.44           C  
ANISOU  528  CA  GLY A  68    10239  18141  11679   1797  -1234    731       C  
ATOM    529  C   GLY A  68      45.970  72.133  37.076  1.00110.56           C  
ANISOU  529  C   GLY A  68    10912  18989  12106   1531  -1449    851       C  
ATOM    530  O   GLY A  68      46.398  71.280  36.274  1.00110.00           O  
ANISOU  530  O   GLY A  68    11099  18847  11846   1229  -1427    757       O  
ATOM    531  N   LEU A  69      44.870  72.856  36.880  1.00119.24           N  
ANISOU  531  N   LEU A  69    18295  15344  11667   2337   1692   1961       N  
ATOM    532  CA  LEU A  69      44.039  72.771  35.700  1.00115.08           C  
ANISOU  532  CA  LEU A  69    17200  14790  11735   1584   1747   2166       C  
ATOM    533  C   LEU A  69      44.863  72.895  34.402  1.00111.62           C  
ANISOU  533  C   LEU A  69    16532  14497  11381    667   1226   1614       C  
ATOM    534  O   LEU A  69      44.854  71.971  33.558  1.00113.29           O  
ANISOU  534  O   LEU A  69    16301  14742  12002    190   1229   1529       O  
ATOM    535  CB  LEU A  69      42.949  73.862  35.783  1.00115.57           C  
ANISOU  535  CB  LEU A  69    17392  14796  11721   1841   1826   2519       C  
ATOM    536  CG  LEU A  69      41.694  73.873  34.902  1.00113.10           C  
ANISOU  536  CG  LEU A  69    16551  14370  12050   1376   1978   2932       C  
ATOM    537  CD1 LEU A  69      41.923  74.755  33.665  1.00108.71           C  
ANISOU  537  CD1 LEU A  69    15939  13923  11442    587   1405   2500       C  
ATOM    538  CD2 LEU A  69      41.205  72.459  34.546  1.00109.68           C  
ANISOU  538  CD2 LEU A  69    15458  13737  12479   1121   2258   3268       C  
ATOM    539  N   ILE A  70      45.582  74.020  34.245  1.00105.29           N  
ANISOU  539  N   ILE A  70    16002  13759  10241    520    755   1284       N  
ATOM    540  CA  ILE A  70      46.490  74.199  33.093  1.00 98.59           C  
ANISOU  540  CA  ILE A  70    14890  13115   9453   -192    390    959       C  
ATOM    541  C   ILE A  70      47.512  73.075  33.027  1.00102.25           C  
ANISOU  541  C   ILE A  70    15212  13699   9939   -300    426    673       C  
ATOM    542  O   ILE A  70      47.739  72.495  31.971  1.00100.47           O  
ANISOU  542  O   ILE A  70    14638  13704   9830   -735    417    540       O  
ATOM    543  CB  ILE A  70      47.268  75.512  33.169  1.00 94.05           C  
ANISOU  543  CB  ILE A  70    14512  12457   8763   -248   -128    800       C  
ATOM    544  CG1 ILE A  70      46.418  76.606  33.764  1.00 93.97           C  
ANISOU  544  CG1 ILE A  70    14838  12214   8649    164   -261    966       C  
ATOM    545  CG2 ILE A  70      47.792  75.900  31.797  1.00 91.32           C  
ANISOU  545  CG2 ILE A  70    13744  12375   8579   -939   -309    822       C  
ATOM    546  CD1 ILE A  70      47.177  77.886  33.968  1.00 97.86           C  
ANISOU  546  CD1 ILE A  70    15510  12446   9225    190   -962    759       C  
ATOM    547  N   SER A  71      48.130  72.782  34.172  1.00108.91           N  
ANISOU  547  N   SER A  71    16376  14397  10607    203    428    545       N  
ATOM    548  CA  SER A  71      49.200  71.806  34.252  1.00111.74           C  
ANISOU  548  CA  SER A  71    16642  14830  10983    145    419    257       C  
ATOM    549  C   SER A  71      48.763  70.437  33.798  1.00110.14           C  
ANISOU  549  C   SER A  71    16072  14694  11081    -14    752    320       C  
ATOM    550  O   SER A  71      49.403  69.842  32.943  1.00105.55           O  
ANISOU  550  O   SER A  71    15212  14313  10575   -394    642     41       O  
ATOM    551  CB  SER A  71      49.732  71.712  35.665  1.00119.58           C  
ANISOU  551  CB  SER A  71    18106  15618  11710    855    352    140       C  
ATOM    552  OG  SER A  71      50.716  70.701  35.747  1.00133.86           O  
ANISOU  552  OG  SER A  71    19799  17482  13579    784    363   -117       O  
ATOM    553  N   VAL A  72      47.682  69.926  34.388  1.00113.98           N  
ANISOU  553  N   VAL A  72    16518  14975  11812    354   1131    730       N  
ATOM    554  CA  VAL A  72      47.238  68.563  34.084  1.00117.58           C  
ANISOU  554  CA  VAL A  72    16522  15298  12853    241   1323    848       C  
ATOM    555  C   VAL A  72      46.769  68.372  32.630  1.00121.85           C  
ANISOU  555  C   VAL A  72    16653  15893  13749   -323   1035    658       C  
ATOM    556  O   VAL A  72      46.843  67.270  32.106  1.00131.59           O  
ANISOU  556  O   VAL A  72    17558  17038  15402   -473    882    436       O  
ATOM    557  CB  VAL A  72      46.178  68.020  35.081  1.00117.86           C  
ANISOU  557  CB  VAL A  72    16435  15024  13323    809   1846   1556       C  
ATOM    558  CG1 VAL A  72      46.816  67.708  36.415  1.00116.16           C  
ANISOU  558  CG1 VAL A  72    16596  14820  12717   1510   2127   1671       C  
ATOM    559  CG2 VAL A  72      45.022  68.992  35.239  1.00118.68           C  
ANISOU  559  CG2 VAL A  72    16612  15062  13416   1026   2044   2042       C  
ATOM    560  N   SER A  73      46.320  69.448  31.979  1.00117.91           N  
ANISOU  560  N   SER A  73    16214  15529  13057   -554    881    695       N  
ATOM    561  CA  SER A  73      45.918  69.379  30.563  1.00114.66           C  
ANISOU  561  CA  SER A  73    15523  15239  12803   -946    547    471       C  
ATOM    562  C   SER A  73      47.115  69.183  29.658  1.00113.12           C  
ANISOU  562  C   SER A  73    15338  15479  12161  -1134    301    -38       C  
ATOM    563  O   SER A  73      47.317  68.106  29.072  1.00111.13           O  
ANISOU  563  O   SER A  73    14890  15246  12085  -1122     96   -400       O  
ATOM    564  CB  SER A  73      45.214  70.663  30.152  1.00113.23           C  
ANISOU  564  CB  SER A  73    15435  15135  12450  -1090    487    698       C  
ATOM    565  OG  SER A  73      44.308  71.071  31.145  1.00120.13           O  
ANISOU  565  OG  SER A  73    16396  15703  13545   -786    798   1205       O  
ATOM    566  N   LEU A  74      47.911  70.236  29.541  1.00112.08           N  
ANISOU  566  N   LEU A  74    15391  15667  11526  -1244    300    -19       N  
ATOM    567  CA  LEU A  74      49.094  70.213  28.714  1.00112.32           C  
ANISOU  567  CA  LEU A  74    15344  16161  11169  -1350    206   -268       C  
ATOM    568  C   LEU A  74      49.863  68.915  28.929  1.00117.78           C  
ANISOU  568  C   LEU A  74    15968  16856  11926  -1205    218   -626       C  
ATOM    569  O   LEU A  74      50.108  68.175  27.976  1.00119.61           O  
ANISOU  569  O   LEU A  74    16061  17365  12019  -1138     66   -966       O  
ATOM    570  CB  LEU A  74      49.955  71.430  29.004  1.00106.49           C  
ANISOU  570  CB  LEU A  74    14689  15524  10248  -1455    215    -30       C  
ATOM    571  CG  LEU A  74      49.132  72.721  29.089  1.00107.37           C  
ANISOU  571  CG  LEU A  74    14901  15477  10416  -1553    145    315       C  
ATOM    572  CD1 LEU A  74      49.996  73.913  29.455  1.00108.01           C  
ANISOU  572  CD1 LEU A  74    15003  15472  10563  -1635    -36    519       C  
ATOM    573  CD2 LEU A  74      48.372  72.979  27.787  1.00109.10           C  
ANISOU  573  CD2 LEU A  74    14960  15994  10497  -1705     99    411       C  
ATOM    574  N   TYR A  75      50.158  68.599  30.196  1.00118.77           N  
ANISOU  574  N   TYR A  75    16230  16663  12234  -1050    362   -574       N  
ATOM    575  CA  TYR A  75      50.801  67.322  30.555  1.00119.22           C  
ANISOU  575  CA  TYR A  75    16215  16643  12438   -903    386   -864       C  
ATOM    576  C   TYR A  75      50.081  66.081  30.008  1.00118.39           C  
ANISOU  576  C   TYR A  75    15845  16358  12780   -858    214  -1088       C  
ATOM    577  O   TYR A  75      50.714  65.220  29.398  1.00117.98           O  
ANISOU  577  O   TYR A  75    15675  16485  12664   -802     21  -1523       O  
ATOM    578  CB  TYR A  75      50.991  67.196  32.073  1.00119.15           C  
ANISOU  578  CB  TYR A  75    16439  16295  12537   -614    579   -689       C  
ATOM    579  CG  TYR A  75      51.537  65.841  32.515  1.00120.30           C  
ANISOU  579  CG  TYR A  75    16486  16313  12907   -449    632   -904       C  
ATOM    580  CD1 TYR A  75      52.916  65.573  32.495  1.00119.56           C  
ANISOU  580  CD1 TYR A  75    16415  16428  12582   -476    542  -1236       C  
ATOM    581  CD2 TYR A  75      50.679  64.832  32.946  1.00118.52           C  
ANISOU  581  CD2 TYR A  75    16062  15713  13256   -267    770   -694       C  
ATOM    582  CE1 TYR A  75      53.416  64.334  32.891  1.00120.80           C  
ANISOU  582  CE1 TYR A  75    16484  16461  12953   -327    569  -1449       C  
ATOM    583  CE2 TYR A  75      51.169  63.593  33.345  1.00123.46           C  
ANISOU  583  CE2 TYR A  75    16542  16173  14191   -125    791   -837       C  
ATOM    584  CZ  TYR A  75      52.533  63.345  33.317  1.00122.24           C  
ANISOU  584  CZ  TYR A  75    16498  16267  13680   -155    682  -1263       C  
ATOM    585  OH  TYR A  75      53.007  62.116  33.727  1.00119.44           O  
ANISOU  585  OH  TYR A  75    16003  15733  13642    -10    689  -1412       O  
ATOM    586  N   ALA A  76      48.770  65.985  30.239  1.00118.58           N  
ANISOU  586  N   ALA A  76    15734  15967  13352   -831    222   -780       N  
ATOM    587  CA  ALA A  76      47.991  64.821  29.772  1.00123.41           C  
ANISOU  587  CA  ALA A  76    15971  16184  14733   -800   -115   -940       C  
ATOM    588  C   ALA A  76      48.176  64.606  28.279  1.00124.66           C  
ANISOU  588  C   ALA A  76    16099  16666  14597   -810   -648  -1555       C  
ATOM    589  O   ALA A  76      48.369  63.472  27.823  1.00126.33           O  
ANISOU  589  O   ALA A  76    16144  16738  15115   -654  -1073  -2045       O  
ATOM    590  CB  ALA A  76      46.522  64.985  30.103  1.00127.37           C  
ANISOU  590  CB  ALA A  76    16228  16179  15987   -798    -41   -382       C  
ATOM    591  N   TYR A  77      48.136  65.703  27.524  1.00121.31           N  
ANISOU  591  N   TYR A  77    15861  16689  13541   -892   -648  -1524       N  
ATOM    592  CA  TYR A  77      48.483  65.679  26.108  1.00125.91           C  
ANISOU  592  CA  TYR A  77    16523  17794  13523   -700  -1013  -2009       C  
ATOM    593  C   TYR A  77      49.906  65.179  25.906  1.00126.96           C  
ANISOU  593  C   TYR A  77    16731  18405  13102   -491   -904  -2344       C  
ATOM    594  O   TYR A  77      50.122  64.177  25.228  1.00124.93           O  
ANISOU  594  O   TYR A  77    16448  18220  12800   -145  -1327  -2927       O  
ATOM    595  CB  TYR A  77      48.308  67.074  25.487  1.00126.73           C  
ANISOU  595  CB  TYR A  77    16779  18347  13026   -798   -858  -1692       C  
ATOM    596  CG  TYR A  77      48.814  67.204  24.060  1.00131.14           C  
ANISOU  596  CG  TYR A  77    17454  19628  12745   -432  -1038  -1994       C  
ATOM    597  CD1 TYR A  77      48.673  66.152  23.135  1.00135.21           C  
ANISOU  597  CD1 TYR A  77    18011  20200  13163     59  -1639  -2687       C  
ATOM    598  CD2 TYR A  77      49.399  68.390  23.624  1.00131.39           C  
ANISOU  598  CD2 TYR A  77    17540  20265  12116   -465   -646  -1544       C  
ATOM    599  CE1 TYR A  77      49.136  66.279  21.836  1.00139.60           C  
ANISOU  599  CE1 TYR A  77    18766  21526  12747    641  -1760  -2945       C  
ATOM    600  CE2 TYR A  77      49.857  68.530  22.326  1.00136.13           C  
ANISOU  600  CE2 TYR A  77    18215  21621  11884     23   -658  -1626       C  
ATOM    601  CZ  TYR A  77      49.727  67.478  21.438  1.00141.04           C  
ANISOU  601  CZ  TYR A  77    18984  22417  12187    642  -1176  -2335       C  
ATOM    602  OH  TYR A  77      50.189  67.627  20.157  1.00146.97           O  
ANISOU  602  OH  TYR A  77    19896  24024  11920   1358  -1142  -2395       O  
ATOM    603  N   VAL A  78      50.864  65.870  26.538  1.00127.80           N  
ANISOU  603  N   VAL A  78    16913  18765  12880   -658   -411  -1990       N  
ATOM    604  CA  VAL A  78      52.308  65.593  26.380  1.00121.89           C  
ANISOU  604  CA  VAL A  78    16153  18477  11680   -499   -224  -2144       C  
ATOM    605  C   VAL A  78      52.695  64.154  26.774  1.00116.56           C  
ANISOU  605  C   VAL A  78    15410  17531  11343   -329   -406  -2615       C  
ATOM    606  O   VAL A  78      53.494  63.512  26.086  1.00113.26           O  
ANISOU  606  O   VAL A  78    14979  17517  10538      4   -506  -3015       O  
ATOM    607  CB  VAL A  78      53.173  66.633  27.155  1.00117.53           C  
ANISOU  607  CB  VAL A  78    15605  17991  11060   -759    169  -1641       C  
ATOM    608  CG1 VAL A  78      54.661  66.360  26.972  1.00117.75           C  
ANISOU  608  CG1 VAL A  78    15498  18423  10818   -617    351  -1696       C  
ATOM    609  CG2 VAL A  78      52.838  68.046  26.697  1.00117.03           C  
ANISOU  609  CG2 VAL A  78    15534  18140  10791   -924    268  -1162       C  
ATOM    610  N   SER A  79      52.107  63.647  27.858  1.00112.26           N  
ANISOU  610  N   SER A  79    14805  16328  11520   -478   -421  -2505       N  
ATOM    611  CA  SER A  79      52.316  62.251  28.239  1.00119.64           C  
ANISOU  611  CA  SER A  79    15594  16902  12961   -332   -628  -2857       C  
ATOM    612  C   SER A  79      51.710  61.278  27.199  1.00129.91           C  
ANISOU  612  C   SER A  79    16748  18034  14575    -58  -1316  -3450       C  
ATOM    613  O   SER A  79      52.030  60.077  27.186  1.00131.63           O  
ANISOU  613  O   SER A  79    16833  18015  15166    144  -1663  -3903       O  
ATOM    614  CB  SER A  79      51.807  61.959  29.678  1.00118.94           C  
ANISOU  614  CB  SER A  79    15417  16176  13599   -441   -382  -2402       C  
ATOM    615  OG  SER A  79      50.455  62.346  29.867  1.00121.86           O  
ANISOU  615  OG  SER A  79    15676  16153  14472   -528   -375  -1970       O  
ATOM    616  N   TYR A  80      50.870  61.812  26.308  1.00133.32           N  
ANISOU  616  N   TYR A  80    17228  18560  14867      3  -1615  -3503       N  
ATOM    617  CA  TYR A  80      50.387  61.043  25.157  1.00138.13           C  
ANISOU  617  CA  TYR A  80    17810  19069  15603    426  -2453  -4210       C  
ATOM    618  C   TYR A  80      51.441  60.993  24.052  1.00136.84           C  
ANISOU  618  C   TYR A  80    17933  19779  14278    993  -2514  -4727       C  
ATOM    619  O   TYR A  80      51.778  59.913  23.561  1.00143.58           O  
ANISOU  619  O   TYR A  80    18811  20603  15136   1483  -3072  -5438       O  
ATOM    620  CB  TYR A  80      49.060  61.608  24.621  1.00143.98           C  
ANISOU  620  CB  TYR A  80    18515  19543  16646    370  -2835  -4101       C  
ATOM    621  CG  TYR A  80      48.624  61.018  23.291  1.00152.50           C  
ANISOU  621  CG  TYR A  80    19691  20595  17653    957  -3845  -4933       C  
ATOM    622  CD1 TYR A  80      48.429  59.637  23.146  1.00159.38           C  
ANISOU  622  CD1 TYR A  80    20348  20798  19409   1257  -4747  -5610       C  
ATOM    623  CD2 TYR A  80      48.404  61.840  22.177  1.00154.68           C  
ANISOU  623  CD2 TYR A  80    20289  21478  17000   1305  -3989  -5066       C  
ATOM    624  CE1 TYR A  80      48.042  59.089  21.929  1.00172.51           C  
ANISOU  624  CE1 TYR A  80    22173  22363  21007   1946  -5888  -6524       C  
ATOM    625  CE2 TYR A  80      48.008  61.303  20.957  1.00166.29           C  
ANISOU  625  CE2 TYR A  80    21962  22952  18268   2040  -5017  -5917       C  
ATOM    626  CZ  TYR A  80      47.828  59.924  20.836  1.00174.53           C  
ANISOU  626  CZ  TYR A  80    22847  23285  20180   2389  -6032  -6710       C  
ATOM    627  OH  TYR A  80      47.433  59.375  19.633  1.00183.04           O  
ANISOU  627  OH  TYR A  80    24188  24276  21082   3257  -7270  -7701       O  
ATOM    628  N   THR A  81      51.986  62.157  23.694  1.00145.51           N  
ANISOU  628  N   THR A  81    17972  22983  14332  -1245   -314  -2031       N  
ATOM    629  CA  THR A  81      52.992  62.237  22.635  1.00140.30           C  
ANISOU  629  CA  THR A  81    17375  22229  13704  -1307   -170  -2103       C  
ATOM    630  C   THR A  81      54.286  61.474  22.975  1.00141.62           C  
ANISOU  630  C   THR A  81    17445  22111  14251  -1140    125  -1906       C  
ATOM    631  O   THR A  81      55.146  61.280  22.108  1.00144.66           O  
ANISOU  631  O   THR A  81    17888  22270  14803  -1162    439  -1946       O  
ATOM    632  CB  THR A  81      53.329  63.695  22.259  1.00136.27           C  
ANISOU  632  CB  THR A  81    16833  21869  13072  -1246   -379  -2046       C  
ATOM    633  OG1 THR A  81      54.278  64.223  23.185  1.00134.11           O  
ANISOU  633  OG1 THR A  81    16511  21575  12866  -1133   -440  -1919       O  
ATOM    634  CG2 THR A  81      52.089  64.547  22.267  1.00136.28           C  
ANISOU  634  CG2 THR A  81    16740  22062  12978  -1235   -506  -1914       C  
ATOM    635  N   PHE A  82      54.429  61.054  24.229  1.00139.22           N  
ANISOU  635  N   PHE A  82    16917  21860  14121   -996     72  -1566       N  
ATOM    636  CA  PHE A  82      55.546  60.191  24.598  1.00141.75           C  
ANISOU  636  CA  PHE A  82    16909  22007  14942   -799    408  -1023       C  
ATOM    637  C   PHE A  82      55.075  58.811  24.961  1.00145.35           C  
ANISOU  637  C   PHE A  82    17294  22130  15801   -695    865   -885       C  
ATOM    638  O   PHE A  82      55.823  58.036  25.550  1.00152.71           O  
ANISOU  638  O   PHE A  82    17787  22946  17290   -451   1192   -175       O  
ATOM    639  CB  PHE A  82      56.381  60.790  25.735  1.00139.80           C  
ANISOU  639  CB  PHE A  82    16261  22294  14561   -856     -2   -430       C  
ATOM    640  CG  PHE A  82      57.286  61.896  25.296  1.00137.00           C  
ANISOU  640  CG  PHE A  82    15926  22145  13981   -969   -206   -442       C  
ATOM    641  CD1 PHE A  82      56.807  63.196  25.180  1.00134.64           C  
ANISOU  641  CD1 PHE A  82    15974  21993  13187  -1192   -487   -956       C  
ATOM    642  CD2 PHE A  82      58.603  61.650  24.991  1.00139.28           C  
ANISOU  642  CD2 PHE A  82    15855  22416  14649   -821     -1    131       C  
ATOM    643  CE1 PHE A  82      57.634  64.231  24.770  1.00133.72           C  
ANISOU  643  CE1 PHE A  82    15911  22008  12887  -1314   -592  -1000       C  
ATOM    644  CE2 PHE A  82      59.433  62.683  24.579  1.00139.88           C  
ANISOU  644  CE2 PHE A  82    15959  22709  14478   -957   -210    101       C  
ATOM    645  CZ  PHE A  82      58.947  63.975  24.474  1.00135.85           C  
ANISOU  645  CZ  PHE A  82    15863  22351  13401  -1230   -522   -516       C  
ATOM    646  N   LYS A  83      53.824  58.508  24.612  1.00143.36           N  
ANISOU  646  N   LYS A  83    17398  21774  15297   -904    918  -1438       N  
ATOM    647  CA  LYS A  83      53.321  57.129  24.603  1.00146.37           C  
ANISOU  647  CA  LYS A  83    17888  21700  16024   -945   1557  -1528       C  
ATOM    648  C   LYS A  83      53.187  56.525  26.026  1.00146.99           C  
ANISOU  648  C   LYS A  83    17566  21882  16399   -678   1468   -952       C  
ATOM    649  O   LYS A  83      53.246  55.302  26.207  1.00149.75           O  
ANISOU  649  O   LYS A  83    17810  21743  17342   -528   2171   -697       O  
ATOM    650  CB  LYS A  83      54.199  56.244  23.687  1.00152.88           C  
ANISOU  650  CB  LYS A  83    18842  21792  17451   -944   2594  -1547       C  
ATOM    651  CG  LYS A  83      54.596  56.917  22.357  1.00152.16           C  
ANISOU  651  CG  LYS A  83    19086  21690  17035  -1266   2654  -2018       C  
ATOM    652  CD  LYS A  83      55.861  56.310  21.749  1.00156.04           C  
ANISOU  652  CD  LYS A  83    19567  21440  18278  -1107   3680  -1809       C  
ATOM    653  CE  LYS A  83      55.533  55.181  20.784  1.00162.46           C  
ANISOU  653  CE  LYS A  83    20996  21479  19252  -1677   4939  -2495       C  
ATOM    654  NZ  LYS A  83      56.747  54.438  20.330  1.00169.96           N  
ANISOU  654  NZ  LYS A  83    21943  21418  21215  -1442   6325  -2223       N  
ATOM    655  N   LEU A  84      52.991  57.400  27.017  1.00145.38           N  
ANISOU  655  N   LEU A  84    17172  22287  15779   -704    717   -761       N  
ATOM    656  CA  LEU A  84      52.736  56.983  28.409  1.00150.40           C  
ANISOU  656  CA  LEU A  84    17464  23223  16456   -666    507   -274       C  
ATOM    657  C   LEU A  84      51.234  57.037  28.726  1.00149.29           C  
ANISOU  657  C   LEU A  84    17643  23152  15926   -827    270   -807       C  
ATOM    658  O   LEU A  84      50.703  58.091  29.127  1.00146.47           O  
ANISOU  658  O   LEU A  84    17430  23131  15088  -1012   -173  -1052       O  
ATOM    659  CB  LEU A  84      53.503  57.880  29.397  1.00151.07           C  
ANISOU  659  CB  LEU A  84    17193  24019  16187   -883    -45    240       C  
ATOM    660  CG  LEU A  84      55.002  57.664  29.614  1.00154.81           C  
ANISOU  660  CG  LEU A  84    17023  24768  17027   -803     40   1237       C  
ATOM    661  CD1 LEU A  84      55.664  58.976  30.019  1.00153.71           C  
ANISOU  661  CD1 LEU A  84    16838  25357  16208  -1303   -523   1306       C  
ATOM    662  CD2 LEU A  84      55.244  56.588  30.663  1.00160.11           C  
ANISOU  662  CD2 LEU A  84    16990  25704  18138   -699    169   2299       C  
ATOM    663  N   TYR A  85      50.562  55.899  28.578  1.00151.18           N  
ANISOU  663  N   TYR A  85    17988  23013  16438   -777    699   -943       N  
ATOM    664  CA  TYR A  85      49.107  55.888  28.488  1.00150.11           C  
ANISOU  664  CA  TYR A  85    18166  22935  15932   -981    541  -1462       C  
ATOM    665  C   TYR A  85      48.393  55.847  29.832  1.00148.55           C  
ANISOU  665  C   TYR A  85    17816  23018  15605   -957    208  -1279       C  
ATOM    666  O   TYR A  85      47.318  56.410  29.974  1.00145.90           O  
ANISOU  666  O   TYR A  85    17649  22864  14922  -1079    -72  -1571       O  
ATOM    667  CB  TYR A  85      48.619  54.777  27.541  1.00154.20           C  
ANISOU  667  CB  TYR A  85    18998  23004  16586  -1210   1188  -1862       C  
ATOM    668  CG  TYR A  85      49.097  54.972  26.116  1.00155.66           C  
ANISOU  668  CG  TYR A  85    19468  23015  16661  -1502   1520  -2223       C  
ATOM    669  CD1 TYR A  85      48.868  56.178  25.445  1.00152.86           C  
ANISOU  669  CD1 TYR A  85    19179  23114  15785  -1694    984  -2400       C  
ATOM    670  CD2 TYR A  85      49.806  53.970  25.452  1.00161.23           C  
ANISOU  670  CD2 TYR A  85    20360  23047  17851  -1601   2500  -2332       C  
ATOM    671  CE1 TYR A  85      49.325  56.378  24.155  1.00155.87           C  
ANISOU  671  CE1 TYR A  85    19783  23446  15994  -2038   1232  -2678       C  
ATOM    672  CE2 TYR A  85      50.270  54.161  24.157  1.00164.35           C  
ANISOU  672  CE2 TYR A  85    21082  23279  18081  -1995   2882  -2734       C  
ATOM    673  CZ  TYR A  85      50.028  55.368  23.514  1.00161.73           C  
ANISOU  673  CZ  TYR A  85    20789  23569  17090  -2243   2153  -2907       C  
ATOM    674  OH  TYR A  85      50.486  55.568  22.232  1.00165.62           O  
ANISOU  674  OH  TYR A  85    21574  24008  17346  -2712   2477  -3263       O  
ATOM    675  N   GLY A  86      49.002  55.199  30.817  1.00152.79           N  
ANISOU  675  N   GLY A  86    17964  23629  16460   -821    286   -674       N  
ATOM    676  CA  GLY A  86      48.511  55.270  32.188  1.00155.04           C  
ANISOU  676  CA  GLY A  86    18077  24332  16498   -955    -76   -446       C  
ATOM    677  C   GLY A  86      48.448  56.709  32.675  1.00156.26           C  
ANISOU  677  C   GLY A  86    18393  24915  16060  -1296   -512   -675       C  
ATOM    678  O   GLY A  86      47.471  57.115  33.312  1.00153.15           O  
ANISOU  678  O   GLY A  86    18209  24611  15369  -1479   -631   -975       O  
ATOM    679  N   GLU A  87      49.483  57.487  32.341  1.00159.53           N  
ANISOU  679  N   GLU A  87    18755  25499  16359  -1406   -601   -563       N  
ATOM    680  CA  GLU A  87      49.597  58.879  32.782  1.00160.30           C  
ANISOU  680  CA  GLU A  87    19078  25908  15920  -1850   -792   -824       C  
ATOM    681  C   GLU A  87      48.630  59.809  32.066  1.00155.85           C  
ANISOU  681  C   GLU A  87    18952  24950  15313  -1728   -642  -1449       C  
ATOM    682  O   GLU A  87      48.131  60.769  32.658  1.00154.20           O  
ANISOU  682  O   GLU A  87    19010  24730  14847  -2025   -504  -1735       O  
ATOM    683  CB  GLU A  87      51.030  59.384  32.610  1.00166.09           C  
ANISOU  683  CB  GLU A  87    19594  26976  16533  -2058   -905   -467       C  
ATOM    684  CG  GLU A  87      52.020  58.745  33.567  1.00178.40           C  
ANISOU  684  CG  GLU A  87    20518  29225  18038  -2363  -1111    477       C  
ATOM    685  CD  GLU A  87      51.764  59.118  35.026  1.00188.92           C  
ANISOU  685  CD  GLU A  87    21861  31272  18649  -3207  -1349    539       C  
ATOM    686  OE1 GLU A  87      51.964  60.298  35.387  1.00197.44           O  
ANISOU  686  OE1 GLU A  87    23297  32664  19058  -3945  -1366    131       O  
ATOM    687  OE2 GLU A  87      51.385  58.226  35.818  1.00191.22           O  
ANISOU  687  OE2 GLU A  87    21836  31803  19017  -3233  -1427    973       O  
HETATM  688  N   MSE A  88      48.361  59.526  30.794  1.00167.19           N  
ANISOU  688  N   MSE A  88    19530  25202  18789   1971    521  -6118       N  
HETATM  689  CA  MSE A  88      47.516  60.409  29.990  1.00165.14           C  
ANISOU  689  CA  MSE A  88    19126  25461  18158   1526    413  -5811       C  
HETATM  690  C   MSE A  88      46.060  60.266  30.350  1.00161.30           C  
ANISOU  690  C   MSE A  88    18744  24534  18006   1121     94  -5480       C  
HETATM  691  O   MSE A  88      45.327  61.244  30.346  1.00155.15           O  
ANISOU  691  O   MSE A  88    17742  23993  17212    798     44  -4935       O  
HETATM  692  CB  MSE A  88      47.789  60.237  28.497  1.00173.77           C  
ANISOU  692  CB  MSE A  88    20259  27173  18589   1470    420  -6325       C  
HETATM  693  CG  MSE A  88      47.118  59.007  27.893  1.00183.96           C  
ANISOU  693  CG  MSE A  88    21921  28123  19853   1327    135  -6904       C  
HETATM  694 SE   MSE A  88      46.355  59.465  26.133  1.00192.98          SE  
ANISOU  694 SE   MSE A  88    23002  30152  20167    763    -52  -6992      SE  
HETATM  695  CE  MSE A  88      45.476  61.161  26.676  1.00179.71           C  
ANISOU  695  CE  MSE A  88    20893  28701  18688    358   -106  -5817       C  
HETATM  696  N   MSE A  89      45.646  59.050  30.708  1.00164.51           N  
ANISOU  696  N   MSE A  89    19465  24272  18768   1145   -125  -5778       N  
HETATM  697  CA  MSE A  89      44.251  58.783  31.076  1.00166.17           C  
ANISOU  697  CA  MSE A  89    19779  24044  19312    753   -451  -5467       C  
HETATM  698  C   MSE A  89      43.979  59.245  32.470  1.00157.37           C  
ANISOU  698  C   MSE A  89    18498  22602  18694    751   -385  -4873       C  
HETATM  699  O   MSE A  89      42.894  59.751  32.764  1.00155.32           O  
ANISOU  699  O   MSE A  89    18112  22303  18600    405   -516  -4386       O  
HETATM  700  CB  MSE A  89      43.868  57.306  30.862  1.00179.86           C  
ANISOU  700  CB  MSE A  89    21906  25198  21234    725   -755  -5994       C  
HETATM  701  CG  MSE A  89      44.335  56.323  31.943  1.00187.35           C  
ANISOU  701  CG  MSE A  89    23020  25408  22755   1051   -775  -6128       C  
HETATM  702 SE   MSE A  89      43.653  54.494  31.547  1.00213.33          SE  
ANISOU  702 SE   MSE A  89    26800  27901  26351    922  -1251  -6755      SE  
HETATM  703  CE  MSE A  89      44.261  54.243  29.679  1.00209.91           C  
ANISOU  703  CE  MSE A  89    26527  28070  25157   1009  -1166  -7694       C  
ATOM    704  N   LEU A  90      44.971  59.092  33.340  1.00154.18           N  
ANISOU  704  N   LEU A  90    18066  21995  18518   1131   -172  -4910       N  
ATOM    705  CA  LEU A  90      44.892  59.599  34.709  1.00147.31           C  
ANISOU  705  CA  LEU A  90    17013  20915  18041   1139    -59  -4380       C  
ATOM    706  C   LEU A  90      44.653  61.115  34.721  1.00143.14           C  
ANISOU  706  C   LEU A  90    16140  20885  17359    962    119  -3885       C  
ATOM    707  O   LEU A  90      43.749  61.599  35.406  1.00141.45           O  
ANISOU  707  O   LEU A  90    15788  20537  17419    712     71  -3430       O  
ATOM    708  CB  LEU A  90      46.176  59.261  35.484  1.00144.56           C  
ANISOU  708  CB  LEU A  90    16661  20400  17864   1573    152  -4514       C  
ATOM    709  CG  LEU A  90      46.178  59.064  37.014  1.00139.62           C  
ANISOU  709  CG  LEU A  90    15986  19341  17722   1609    163  -4148       C  
ATOM    710  CD1 LEU A  90      47.519  59.504  37.559  1.00137.14           C  
ANISOU  710  CD1 LEU A  90    15499  19240  17366   1957    474  -4104       C  
ATOM    711  CD2 LEU A  90      45.052  59.795  37.742  1.00134.32           C  
ANISOU  711  CD2 LEU A  90    15142  18660  17231   1239    123  -3592       C  
ATOM    712  N   ASN A  91      45.457  61.861  33.963  1.00141.73           N  
ANISOU  712  N   ASN A  91    15803  21278  16769   1090    323  -3971       N  
ATOM    713  CA  ASN A  91      45.351  63.317  33.982  1.00136.84           C  
ANISOU  713  CA  ASN A  91    14837  21086  16066    945    479  -3491       C  
ATOM    714  C   ASN A  91      44.055  63.850  33.417  1.00135.98           C  
ANISOU  714  C   ASN A  91    14614  21113  15939    519    275  -3170       C  
ATOM    715  O   ASN A  91      43.446  64.747  34.010  1.00131.74           O  
ANISOU  715  O   ASN A  91    13834  20546  15676    351    321  -2689       O  
ATOM    716  CB  ASN A  91      46.541  63.971  33.312  1.00138.63           C  
ANISOU  716  CB  ASN A  91    14897  21900  15874   1157    714  -3602       C  
ATOM    717  CG  ASN A  91      47.741  64.022  34.215  1.00141.02           C  
ANISOU  717  CG  ASN A  91    15144  22128  16307   1522    973  -3626       C  
ATOM    718  OD1 ASN A  91      48.023  65.048  34.844  1.00138.55           O  
ANISOU  718  OD1 ASN A  91    14583  21954  16105   1522   1149  -3246       O  
ATOM    719  ND2 ASN A  91      48.428  62.895  34.336  1.00145.12           N  
ANISOU  719  ND2 ASN A  91    15889  22386  16863   1827    982  -4064       N  
ATOM    720  N   LEU A  92      43.604  63.262  32.299  1.00138.29           N  
ANISOU  720  N   LEU A  92    15075  21535  15933    336     43  -3448       N  
ATOM    721  CA  LEU A  92      42.442  63.788  31.560  1.00135.04           C  
ANISOU  721  CA  LEU A  92    14523  21359  15426    -98   -176  -3122       C  
ATOM    722  C   LEU A  92      41.126  63.416  32.212  1.00132.47           C  
ANISOU  722  C   LEU A  92    14255  20532  15543   -363   -405  -2856       C  
ATOM    723  O   LEU A  92      40.373  64.296  32.607  1.00128.95           O  
ANISOU  723  O   LEU A  92    13530  20098  15364   -558   -394  -2337       O  
ATOM    724  CB  LEU A  92      42.467  63.348  30.096  1.00138.27           C  
ANISOU  724  CB  LEU A  92    15069  22185  15280   -248   -344  -3506       C  
ATOM    725  CG  LEU A  92      42.166  64.411  29.026  1.00137.59           C  
ANISOU  725  CG  LEU A  92    14678  22782  14818   -565   -402  -3154       C  
ATOM    726  CD1 LEU A  92      42.751  65.780  29.375  1.00132.24           C  
ANISOU  726  CD1 LEU A  92    13613  22406  14226   -450   -142  -2691       C  
ATOM    727  CD2 LEU A  92      42.685  63.934  27.676  1.00143.03           C  
ANISOU  727  CD2 LEU A  92    15502  24006  14833   -603   -455  -3665       C  
ATOM    728  N   LEU A  93      40.874  62.112  32.357  1.00134.64           N  
ANISOU  728  N   LEU A  93    14871  20352  15932   -356   -606  -3209       N  
ATOM    729  CA  LEU A  93      39.620  61.612  32.956  1.00136.08           C  
ANISOU  729  CA  LEU A  93    15121  20062  16520   -634   -861  -2957       C  
ATOM    730  C   LEU A  93      39.505  61.875  34.471  1.00134.72           C  
ANISOU  730  C   LEU A  93    14802  19545  16838   -532   -698  -2597       C  
ATOM    731  O   LEU A  93      38.412  62.171  34.981  1.00136.11           O  
ANISOU  731  O   LEU A  93    14813  19583  17317   -794   -788  -2169       O  
ATOM    732  CB  LEU A  93      39.446  60.118  32.684  1.00138.31           C  
ANISOU  732  CB  LEU A  93    15811  19926  16814   -667  -1152  -3435       C  
ATOM    733  CG  LEU A  93      39.966  59.592  31.352  1.00143.54           C  
ANISOU  733  CG  LEU A  93    16698  20871  16970   -634  -1236  -4031       C  
ATOM    734  CD1 LEU A  93      39.804  58.084  31.288  1.00148.00           C  
ANISOU  734  CD1 LEU A  93    17671  20878  17681   -632  -1517  -4532       C  
ATOM    735  CD2 LEU A  93      39.265  60.264  30.180  1.00145.44           C  
ANISOU  735  CD2 LEU A  93    16781  21671  16807  -1030  -1382  -3840       C  
ATOM    736  N   VAL A  94      40.615  61.742  35.195  1.00133.40           N  
ANISOU  736  N   VAL A  94    14680  19268  16735   -167   -459  -2771       N  
ATOM    737  CA  VAL A  94      40.562  61.843  36.656  1.00127.41           C  
ANISOU  737  CA  VAL A  94    13814  18213  16383   -100   -323  -2481       C  
ATOM    738  C   VAL A  94      40.964  63.220  37.206  1.00123.10           C  
ANISOU  738  C   VAL A  94    12926  17978  15868     -5     16  -2167       C  
ATOM    739  O   VAL A  94      40.242  63.784  38.018  1.00119.26           O  
ANISOU  739  O   VAL A  94    12224  17418  15672   -161     83  -1793       O  
ATOM    740  CB  VAL A  94      41.329  60.699  37.358  1.00127.55           C  
ANISOU  740  CB  VAL A  94    14083  17814  16566    163   -342  -2770       C  
ATOM    741  CG1 VAL A  94      40.873  60.570  38.799  1.00125.58           C  
ANISOU  741  CG1 VAL A  94    13740  17249  16724     70   -328  -2408       C  
ATOM    742  CG2 VAL A  94      41.111  59.383  36.627  1.00131.53           C  
ANISOU  742  CG2 VAL A  94    14936  18000  17039    116   -672  -3181       C  
ATOM    743  N   TYR A  95      42.076  63.789  36.732  1.00123.23           N  
ANISOU  743  N   TYR A  95    12874  18355  15591    232    224  -2324       N  
ATOM    744  CA  TYR A  95      42.557  65.058  37.323  1.00123.85           C  
ANISOU  744  CA  TYR A  95    12647  18673  15737    324    529  -2047       C  
ATOM    745  C   TYR A  95      41.750  66.313  36.935  1.00123.06           C  
ANISOU  745  C   TYR A  95    12220  18830  15705     75    544  -1652       C  
ATOM    746  O   TYR A  95      41.459  67.153  37.810  1.00122.09           O  
ANISOU  746  O   TYR A  95    11852  18652  15883     32    715  -1356       O  
ATOM    747  CB  TYR A  95      44.086  65.281  37.132  1.00124.93           C  
ANISOU  747  CB  TYR A  95    12782  19092  15591    661    753  -2278       C  
ATOM    748  CG  TYR A  95      44.991  64.328  37.950  1.00125.84           C  
ANISOU  748  CG  TYR A  95    13097  18919  15795    950    820  -2530       C  
ATOM    749  CD1 TYR A  95      44.497  63.622  39.050  1.00124.53           C  
ANISOU  749  CD1 TYR A  95    13030  18305  15979    882    731  -2433       C  
ATOM    750  CD2 TYR A  95      46.332  64.148  37.615  1.00126.52           C  
ANISOU  750  CD2 TYR A  95    13235  19209  15628   1276    961  -2819       C  
ATOM    751  CE1 TYR A  95      45.304  62.757  39.769  1.00122.38           C  
ANISOU  751  CE1 TYR A  95    12903  17773  15820   1115    752  -2589       C  
ATOM    752  CE2 TYR A  95      47.138  63.280  38.331  1.00124.58           C  
ANISOU  752  CE2 TYR A  95    13132  18685  15516   1541   1001  -3002       C  
ATOM    753  CZ  TYR A  95      46.616  62.597  39.406  1.00123.96           C  
ANISOU  753  CZ  TYR A  95    13148  18141  15808   1451    883  -2869       C  
ATOM    754  OH  TYR A  95      47.409  61.753  40.123  1.00126.87           O  
ANISOU  754  OH  TYR A  95    13621  18236  16345   1688    890  -2977       O  
ATOM    755  N   VAL A  96      41.389  66.459  35.644  1.00122.34           N  
ANISOU  755  N   VAL A  96    12105  19025  15354    -97    366  -1644       N  
ATOM    756  CA  VAL A  96      40.713  67.714  35.199  1.00116.81           C  
ANISOU  756  CA  VAL A  96    11042  18585  14752   -328    358  -1205       C  
ATOM    757  C   VAL A  96      39.330  67.897  35.832  1.00116.78           C  
ANISOU  757  C   VAL A  96    10879  18287  15204   -574    273   -855       C  
ATOM    758  O   VAL A  96      38.961  69.017  36.186  1.00118.16           O  
ANISOU  758  O   VAL A  96    10714  18500  15682   -633    407   -505       O  
ATOM    759  CB  VAL A  96      40.635  67.916  33.660  1.00115.82           C  
ANISOU  759  CB  VAL A  96    10867  18915  14221   -511    168  -1187       C  
ATOM    760  CG1 VAL A  96      40.456  69.393  33.358  1.00112.45           C  
ANISOU  760  CG1 VAL A  96    10012  18787  13926   -641    233   -706       C  
ATOM    761  CG2 VAL A  96      41.882  67.408  32.962  1.00116.90           C  
ANISOU  761  CG2 VAL A  96    11211  19355  13850   -283    228  -1637       C  
ATOM    762  N   PRO A  97      38.566  66.795  35.983  1.00116.62           N  
ANISOU  762  N   PRO A  97    11087  17962  15260   -714     50   -952       N  
ATOM    763  CA  PRO A  97      37.351  66.842  36.797  1.00116.23           C  
ANISOU  763  CA  PRO A  97    10885  17632  15645   -914      6   -636       C  
ATOM    764  C   PRO A  97      37.651  67.318  38.216  1.00116.55           C  
ANISOU  764  C   PRO A  97    10779  17520  15985   -742    325   -564       C  
ATOM    765  O   PRO A  97      36.992  68.244  38.716  1.00115.79           O  
ANISOU  765  O   PRO A  97    10348  17421  16224   -831    463   -254       O  
ATOM    766  CB  PRO A  97      36.903  65.382  36.831  1.00117.36           C  
ANISOU  766  CB  PRO A  97    11371  17463  15756  -1025   -272   -842       C  
ATOM    767  CG  PRO A  97      37.432  64.794  35.573  1.00119.21           C  
ANISOU  767  CG  PRO A  97    11869  17877  15546  -1009   -458  -1196       C  
ATOM    768  CD  PRO A  97      38.649  65.562  35.174  1.00118.32           C  
ANISOU  768  CD  PRO A  97    11665  18137  15154   -756   -212  -1324       C  
ATOM    769  N   VAL A  98      38.676  66.701  38.832  1.00119.60           N  
ANISOU  769  N   VAL A  98    11398  17797  16248   -499    442   -864       N  
ATOM    770  CA  VAL A  98      39.018  66.873  40.266  1.00116.81           C  
ANISOU  770  CA  VAL A  98    10968  17307  16105   -376    703   -836       C  
ATOM    771  C   VAL A  98      39.439  68.317  40.608  1.00112.83           C  
ANISOU  771  C   VAL A  98    10146  17015  15706   -280   1017   -700       C  
ATOM    772  O   VAL A  98      39.048  68.844  41.652  1.00108.31           O  
ANISOU  772  O   VAL A  98     9367  16368  15417   -327   1213   -560       O  
ATOM    773  CB  VAL A  98      40.137  65.873  40.707  1.00118.87           C  
ANISOU  773  CB  VAL A  98    11535  17435  16195   -141    718  -1151       C  
ATOM    774  CG1 VAL A  98      40.520  66.086  42.159  1.00119.01           C  
ANISOU  774  CG1 VAL A  98    11451  17390  16376    -65    967  -1080       C  
ATOM    775  CG2 VAL A  98      39.694  64.440  40.499  1.00121.50           C  
ANISOU  775  CG2 VAL A  98    12170  17462  16532   -236    395  -1288       C  
ATOM    776  N   GLN A  99      40.220  68.957  39.727  1.00111.31           N  
ANISOU  776  N   GLN A  99     9903  17098  15289   -163   1061   -749       N  
ATOM    777  CA  GLN A  99      40.565  70.365  39.922  1.00112.19           C  
ANISOU  777  CA  GLN A  99     9701  17378  15548   -108   1301   -584       C  
ATOM    778  C   GLN A  99      39.322  71.172  40.272  1.00114.33           C  
ANISOU  778  C   GLN A  99     9641  17533  16266   -303   1343   -275       C  
ATOM    779  O   GLN A  99      39.382  72.115  41.055  1.00115.82           O  
ANISOU  779  O   GLN A  99     9590  17687  16728   -260   1594   -206       O  
ATOM    780  CB  GLN A  99      41.234  70.953  38.686  1.00117.19           C  
ANISOU  780  CB  GLN A  99    10264  18352  15910    -59   1248   -554       C  
ATOM    781  CG  GLN A  99      42.615  70.394  38.377  1.00125.11           C  
ANISOU  781  CG  GLN A  99    11510  19539  16486    181   1288   -867       C  
ATOM    782  CD  GLN A  99      43.519  70.342  39.593  1.00130.12           C  
ANISOU  782  CD  GLN A  99    12204  20067  17167    386   1531  -1009       C  
ATOM    783  OE1 GLN A  99      43.941  71.382  40.128  1.00131.90           O  
ANISOU  783  OE1 GLN A  99    12212  20368  17536    427   1742   -890       O  
ATOM    784  NE2 GLN A  99      43.830  69.127  40.038  1.00134.42           N  
ANISOU  784  NE2 GLN A  99    13035  20426  17612    498   1481  -1253       N  
ATOM    785  N   PHE A 100      38.182  70.773  39.713  1.00117.37           N  
ANISOU  785  N   PHE A 100    10007  17848  16740   -519   1099   -108       N  
ATOM    786  CA  PHE A 100      36.923  71.459  39.981  1.00112.85           C  
ANISOU  786  CA  PHE A 100     9087  17166  16621   -698   1123    209       C  
ATOM    787  C   PHE A 100      36.317  71.023  41.292  1.00110.19           C  
ANISOU  787  C   PHE A 100     8741  16610  16515   -740   1253    176       C  
ATOM    788  O   PHE A 100      36.130  71.839  42.194  1.00108.07           O  
ANISOU  788  O   PHE A 100     8207  16295  16559   -704   1529    218       O  
ATOM    789  CB  PHE A 100      35.955  71.305  38.803  1.00113.10           C  
ANISOU  789  CB  PHE A 100     9048  17268  16654   -942    795    468       C  
ATOM    790  CG  PHE A 100      36.297  72.189  37.649  1.00113.97           C  
ANISOU  790  CG  PHE A 100     8976  17656  16671   -968    714    653       C  
ATOM    791  CD1 PHE A 100      35.898  73.527  37.642  1.00113.56           C  
ANISOU  791  CD1 PHE A 100     8483  17605  17060  -1002    817    992       C  
ATOM    792  CD2 PHE A 100      37.115  71.731  36.619  1.00115.83           C  
ANISOU  792  CD2 PHE A 100     9456  18162  16391   -941    556    477       C  
ATOM    793  CE1 PHE A 100      36.260  74.379  36.601  1.00114.73           C  
ANISOU  793  CE1 PHE A 100     8427  18016  17149  -1050    716   1232       C  
ATOM    794  CE2 PHE A 100      37.486  72.581  35.576  1.00117.60           C  
ANISOU  794  CE2 PHE A 100     9476  18722  16484   -994    486    687       C  
ATOM    795  CZ  PHE A 100      37.054  73.908  35.567  1.00116.32           C  
ANISOU  795  CZ  PHE A 100     8864  18553  16776  -1063    547   1101       C  
ATOM    796  N   VAL A 101      36.074  69.724  41.415  1.00111.97           N  
ANISOU  796  N   VAL A 101     9255  16714  16573   -823   1056     79       N  
ATOM    797  CA  VAL A 101      35.605  69.123  42.666  1.00115.36           C  
ANISOU  797  CA  VAL A 101     9701  16982  17145   -893   1138     73       C  
ATOM    798  C   VAL A 101      36.422  69.652  43.843  1.00115.71           C  
ANISOU  798  C   VAL A 101     9674  17079  17209   -725   1497    -84       C  
ATOM    799  O   VAL A 101      35.864  70.093  44.865  1.00113.85           O  
ANISOU  799  O   VAL A 101     9192  16838  17225   -794   1723    -15       O  
ATOM    800  CB  VAL A 101      35.724  67.584  42.607  1.00116.98           C  
ANISOU  800  CB  VAL A 101    10300  17029  17117   -945    858    -62       C  
ATOM    801  CG1 VAL A 101      35.551  66.973  43.984  1.00116.34           C  
ANISOU  801  CG1 VAL A 101    10237  16831  17134  -1005    948    -46       C  
ATOM    802  CG2 VAL A 101      34.705  67.008  41.635  1.00120.29           C  
ANISOU  802  CG2 VAL A 101    10778  17375  17551  -1184    493     94       C  
ATOM    803  N   GLY A 102      37.750  69.623  43.672  1.00115.27           N  
ANISOU  803  N   GLY A 102     9819  17108  16870   -517   1554   -305       N  
ATOM    804  CA  GLY A 102      38.698  70.111  44.664  1.00110.78           C  
ANISOU  804  CA  GLY A 102     9210  16622  16257   -371   1857   -456       C  
ATOM    805  C   GLY A 102      38.491  71.553  45.075  1.00107.99           C  
ANISOU  805  C   GLY A 102     8494  16337  16197   -367   2148   -396       C  
ATOM    806  O   GLY A 102      38.381  71.851  46.268  1.00107.80           O  
ANISOU  806  O   GLY A 102     8333  16327  16296   -404   2399   -459       O  
ATOM    807  N   PHE A 103      38.426  72.458  44.105  1.00106.02           N  
ANISOU  807  N   PHE A 103     8069  16136  16075   -338   2111   -276       N  
ATOM    808  CA  PHE A 103      38.225  73.845  44.455  1.00106.36           C  
ANISOU  808  CA  PHE A 103     7752  16168  16489   -323   2360   -219       C  
ATOM    809  C   PHE A 103      36.928  74.021  45.218  1.00111.82           C  
ANISOU  809  C   PHE A 103     8178  16742  17564   -463   2486   -131       C  
ATOM    810  O   PHE A 103      36.813  74.894  46.078  1.00115.11           O  
ANISOU  810  O   PHE A 103     8344  17132  18258   -440   2786   -230       O  
ATOM    811  CB  PHE A 103      38.203  74.755  43.245  1.00105.00           C  
ANISOU  811  CB  PHE A 103     7385  16040  16469   -313   2241     -7       C  
ATOM    812  CG  PHE A 103      37.932  76.186  43.600  1.00105.38           C  
ANISOU  812  CG  PHE A 103     7037  15988  17013   -294   2468     67       C  
ATOM    813  CD1 PHE A 103      38.956  76.992  44.070  1.00102.96           C  
ANISOU  813  CD1 PHE A 103     6693  15715  16713   -170   2685   -100       C  
ATOM    814  CD2 PHE A 103      36.616  76.704  43.574  1.00107.20           C  
ANISOU  814  CD2 PHE A 103     6917  16062  17751   -400   2476    287       C  
ATOM    815  CE1 PHE A 103      38.709  78.300  44.443  1.00105.31           C  
ANISOU  815  CE1 PHE A 103     6635  15858  17518   -153   2889    -82       C  
ATOM    816  CE2 PHE A 103      36.359  78.007  43.960  1.00106.98           C  
ANISOU  816  CE2 PHE A 103     6509  15880  18258   -352   2701    308       C  
ATOM    817  CZ  PHE A 103      37.401  78.806  44.401  1.00108.52           C  
ANISOU  817  CZ  PHE A 103     6693  16073  18467   -230   2906    102       C  
ATOM    818  N   ALA A 104      35.933  73.219  44.869  1.00115.37           N  
ANISOU  818  N   ALA A 104     8662  17132  18038   -616   2256     46       N  
ATOM    819  CA  ALA A 104      34.644  73.332  45.490  1.00119.97           C  
ANISOU  819  CA  ALA A 104     8961  17645  18977   -757   2354    177       C  
ATOM    820  C   ALA A 104      34.812  73.135  46.971  1.00123.09           C  
ANISOU  820  C   ALA A 104     9360  18106  19301   -768   2639    -40       C  
ATOM    821  O   ALA A 104      34.357  73.977  47.774  1.00125.20           O  
ANISOU  821  O   ALA A 104     9301  18387  19879   -769   2952   -115       O  
ATOM    822  CB  ALA A 104      33.691  72.301  44.920  1.00121.79           C  
ANISOU  822  CB  ALA A 104     9289  17824  19159   -949   2017    408       C  
HETATM  823  N   MSE A 105      35.563  72.074  47.323  1.00124.36           N  
ANISOU  823  N   MSE A 105     9877  18321  19053   -768   2540   -160       N  
HETATM  824  CA  MSE A 105      35.540  71.471  48.672  1.00126.22           C  
ANISOU  824  CA  MSE A 105    10147  18659  19151   -874   2688   -250       C  
HETATM  825  C   MSE A 105      36.436  72.153  49.636  1.00121.41           C  
ANISOU  825  C   MSE A 105     9485  18195  18447   -790   3023   -507       C  
HETATM  826  O   MSE A 105      36.069  72.359  50.799  1.00123.23           O  
ANISOU  826  O   MSE A 105     9524  18572  18725   -902   3287   -596       O  
HETATM  827  CB  MSE A 105      36.035  70.059  48.587  1.00127.99           C  
ANISOU  827  CB  MSE A 105    10754  18837  19038   -909   2397   -226       C  
HETATM  828  CG  MSE A 105      34.996  69.132  49.169  1.00137.86           C  
ANISOU  828  CG  MSE A 105    11965  20075  20338  -1153   2270    -29       C  
HETATM  829 SE   MSE A 105      35.138  67.424  48.210  1.00154.19          SE  
ANISOU  829 SE   MSE A 105    14496  21886  22202  -1201   1718     76      SE  
HETATM  830  CE  MSE A 105      36.613  67.898  46.984  1.00148.75           C  
ANISOU  830  CE  MSE A 105    14049  21176  21292   -867   1695   -188       C  
ATOM    831  N   TRP A 106      37.642  72.464  49.183  1.00112.69           N  
ANISOU  831  N   TRP A 106     8551  17096  17170   -613   3012   -632       N  
ATOM    832  CA  TRP A 106      38.583  73.208  49.977  1.00107.78           C  
ANISOU  832  CA  TRP A 106     7884  16607  16459   -543   3301   -864       C  
ATOM    833  C   TRP A 106      38.013  74.582  50.334  1.00111.65           C  
ANISOU  833  C   TRP A 106     7995  17074  17352   -547   3610   -974       C  
ATOM    834  O   TRP A 106      38.049  74.997  51.487  1.00113.44           O  
ANISOU  834  O   TRP A 106     8084  17438  17578   -619   3911  -1186       O  
ATOM    835  CB  TRP A 106      39.864  73.383  49.205  1.00103.48           C  
ANISOU  835  CB  TRP A 106     7538  16066  15714   -354   3200   -915       C  
ATOM    836  CG  TRP A 106      40.902  72.278  49.374  1.00102.39           C  
ANISOU  836  CG  TRP A 106     7734  16002  15166   -299   3054   -950       C  
ATOM    837  CD1 TRP A 106      40.685  70.913  49.422  1.00103.52           C  
ANISOU  837  CD1 TRP A 106     8094  16080  15157   -364   2817   -852       C  
ATOM    838  CD2 TRP A 106      42.311  72.454  49.421  1.00 97.76           C  
ANISOU  838  CD2 TRP A 106     7277  15533  14332   -155   3107  -1065       C  
ATOM    839  NE1 TRP A 106      41.884  70.249  49.524  1.00 98.95           N  
ANISOU  839  NE1 TRP A 106     7759  15549  14289   -247   2735   -914       N  
ATOM    840  CE2 TRP A 106      42.896  71.171  49.518  1.00 96.69           C  
ANISOU  840  CE2 TRP A 106     7418  15398  13922   -115   2917  -1036       C  
ATOM    841  CE3 TRP A 106      43.140  73.571  49.400  1.00 95.64           C  
ANISOU  841  CE3 TRP A 106     6903  15358  14078    -62   3284  -1170       C  
ATOM    842  CZ2 TRP A 106      44.254  70.988  49.595  1.00 97.04           C  
ANISOU  842  CZ2 TRP A 106     7608  15552  13709     30   2920  -1105       C  
ATOM    843  CZ3 TRP A 106      44.488  73.386  49.476  1.00 95.92           C  
ANISOU  843  CZ3 TRP A 106     7098  15529  13818     54   3277  -1226       C  
ATOM    844  CH2 TRP A 106      45.040  72.102  49.570  1.00 96.54           C  
ANISOU  844  CH2 TRP A 106     7428  15627  13623    110   3105  -1192       C  
ATOM    845  N   ARG A 107      37.475  75.273  49.329  1.00117.53           N  
ANISOU  845  N   ARG A 107     8558  17647  18451   -478   3525   -830       N  
ATOM    846  CA  ARG A 107      36.893  76.638  49.483  1.00122.79           C  
ANISOU  846  CA  ARG A 107     8824  18195  19633   -444   3778   -900       C  
ATOM    847  C   ARG A 107      36.144  76.868  50.824  1.00120.69           C  
ANISOU  847  C   ARG A 107     8307  18022  19526   -552   4127  -1114       C  
ATOM    848  O   ARG A 107      36.202  77.965  51.394  1.00114.06           O  
ANISOU  848  O   ARG A 107     7226  17141  18968   -504   4437  -1373       O  
ATOM    849  CB  ARG A 107      35.959  76.937  48.301  1.00130.03           C  
ANISOU  849  CB  ARG A 107     9536  18926  20940   -435   3564   -580       C  
ATOM    850  CG  ARG A 107      35.632  78.411  48.082  1.00138.75           C  
ANISOU  850  CG  ARG A 107    10242  19832  22641   -348   3725   -571       C  
ATOM    851  CD  ARG A 107      34.544  78.583  47.012  1.00138.57           C  
ANISOU  851  CD  ARG A 107     9968  19658  23021   -386   3490   -175       C  
ATOM    852  NE  ARG A 107      33.620  77.452  47.008  1.00137.06           N  
ANISOU  852  NE  ARG A 107     9853  19549  22673   -534   3330     -4       N  
ATOM    853  CZ  ARG A 107      32.428  77.453  47.598  1.00139.72           C  
ANISOU  853  CZ  ARG A 107     9896  19864  23326   -612   3478     36       C  
ATOM    854  NH1 ARG A 107      31.666  76.354  47.567  1.00135.99           N  
ANISOU  854  NH1 ARG A 107     9516  19481  22671   -777   3289    228       N  
ATOM    855  NH2 ARG A 107      31.993  78.552  48.219  1.00139.44           N  
ANISOU  855  NH2 ARG A 107     9460  19713  23808   -527   3817   -124       N  
ATOM    856  N   LYS A 108      35.466  75.817  51.305  1.00120.52           N  
ANISOU  856  N   LYS A 108     8337  18137  19315   -710   4067  -1012       N  
ATOM    857  CA  LYS A 108      34.731  75.829  52.585  1.00126.34           C  
ANISOU  857  CA  LYS A 108     8836  19073  20091   -856   4379  -1176       C  
ATOM    858  C   LYS A 108      35.608  75.963  53.849  1.00128.08           C  
ANISOU  858  C   LYS A 108     9133  19563  19966   -926   4663  -1522       C  
ATOM    859  O   LYS A 108      35.123  76.427  54.898  1.00136.01           O  
ANISOU  859  O   LYS A 108     9870  20755  21050  -1022   5017  -1776       O  
ATOM    860  CB  LYS A 108      33.921  74.548  52.723  1.00130.43           C  
ANISOU  860  CB  LYS A 108     9421  19706  20429  -1047   4173   -903       C  
ATOM    861  CG  LYS A 108      32.770  74.391  51.748  1.00137.03           C  
ANISOU  861  CG  LYS A 108    10105  20351  21608  -1063   3937   -566       C  
ATOM    862  CD  LYS A 108      31.753  73.372  52.273  1.00142.52           C  
ANISOU  862  CD  LYS A 108    10729  21210  22209  -1300   3852   -348       C  
ATOM    863  CE  LYS A 108      31.052  73.882  53.536  1.00147.79           C  
ANISOU  863  CE  LYS A 108    11002  22142  23007  -1393   4287   -543       C  
ATOM    864  NZ  LYS A 108      30.512  72.785  54.389  1.00149.51           N  
ANISOU  864  NZ  LYS A 108    11216  22660  22930  -1669   4239   -374       N  
ATOM    865  N   HIS A 109      36.857  75.482  53.776  1.00120.82           N  
ANISOU  865  N   HIS A 109     8563  18704  18638   -899   4505  -1524       N  
ATOM    866  CA  HIS A 109      37.682  75.252  54.982  1.00117.08           C  
ANISOU  866  CA  HIS A 109     8200  18545  17737  -1033   4677  -1732       C  
ATOM    867  C   HIS A 109      38.997  76.005  54.970  1.00114.86           C  
ANISOU  867  C   HIS A 109     8037  18251  17351   -918   4761  -1949       C  
ATOM    868  O   HIS A 109      40.048  75.427  55.216  1.00113.56           O  
ANISOU  868  O   HIS A 109     8128  18234  16783   -946   4650  -1914       O  
ATOM    869  CB  HIS A 109      38.000  73.774  55.132  1.00115.91           C  
ANISOU  869  CB  HIS A 109     8342  18525  17172  -1153   4388  -1473       C  
ATOM    870  CG  HIS A 109      36.803  72.912  55.286  1.00117.15           C  
ANISOU  870  CG  HIS A 109     8403  18728  17377  -1325   4271  -1228       C  
ATOM    871  ND1 HIS A 109      36.263  72.199  54.238  1.00116.27           N  
ANISOU  871  ND1 HIS A 109     8410  18365  17403  -1279   3921   -931       N  
ATOM    872  CD2 HIS A 109      36.046  72.625  56.369  1.00120.18           C  
ANISOU  872  CD2 HIS A 109     8578  19416  17667  -1572   4445  -1221       C  
ATOM    873  CE1 HIS A 109      35.224  71.510  54.667  1.00118.68           C  
ANISOU  873  CE1 HIS A 109     8587  18777  17725  -1489   3865   -732       C  
ATOM    874  NE2 HIS A 109      35.063  71.759  55.955  1.00122.96           N  
ANISOU  874  NE2 HIS A 109     8916  19673  18131  -1665   4186   -888       N  
HETATM  875  N   MSE A 110      38.955  77.285  54.687  1.00115.68           N  
ANISOU  875  N   MSE A 110     7938  18168  17846   -794   4938  -2143       N  
HETATM  876  CA  MSE A 110      40.174  78.064  54.679  1.00111.30           C  
ANISOU  876  CA  MSE A 110     7471  17591  17224   -714   5002  -2328       C  
HETATM  877  C   MSE A 110      40.309  78.708  56.031  1.00112.90           C  
ANISOU  877  C   MSE A 110     7528  18022  17346   -872   5380  -2743       C  
HETATM  878  O   MSE A 110      39.353  78.748  56.811  1.00113.67           O  
ANISOU  878  O   MSE A 110     7399  18258  17530   -999   5623  -2911       O  
HETATM  879  CB  MSE A 110      40.159  79.050  53.510  1.00113.81           C  
ANISOU  879  CB  MSE A 110     7666  17557  18018   -514   4911  -2244       C  
HETATM  880  CG  MSE A 110      39.879  78.305  52.199  1.00117.11           C  
ANISOU  880  CG  MSE A 110     8215  17839  18440   -416   4538  -1841       C  
HETATM  881 SE   MSE A 110      41.449  77.207  51.823  1.00130.72          SE  
ANISOU  881 SE   MSE A 110    10401  19752  19515   -359   4250  -1700      SE  
HETATM  882  CE  MSE A 110      40.821  75.817  50.613  1.00126.04           C  
ANISOU  882  CE  MSE A 110    10012  19061  18816   -316   3833  -1336       C  
ATOM    883  N   ALA A 111      41.522  79.123  56.356  1.00113.33           N  
ANISOU  883  N   ALA A 111     7714  18175  17171   -892   5428  -2908       N  
ATOM    884  CA  ALA A 111      41.805  79.789  57.617  1.00116.84           C  
ANISOU  884  CA  ALA A 111     8049  18859  17484  -1075   5769  -3341       C  
ATOM    885  C   ALA A 111      43.022  80.679  57.408  1.00115.41           C  
ANISOU  885  C   ALA A 111     7953  18566  17329  -1012   5756  -3473       C  
ATOM    886  O   ALA A 111      43.661  80.620  56.364  1.00107.91           O  
ANISOU  886  O   ALA A 111     7147  17433  16419   -840   5483  -3188       O  
ATOM    887  CB  ALA A 111      42.066  78.762  58.712  1.00121.46           C  
ANISOU  887  CB  ALA A 111     8761  19925  17463  -1340   5794  -3311       C  
ATOM    888  N   LEU A 112      43.338  81.525  58.371  1.00116.44           N  
ANISOU  888  N   LEU A 112     7984  18822  17435  -1163   6045  -3910       N  
ATOM    889  CA  LEU A 112      44.351  82.496  58.113  1.00117.83           C  
ANISOU  889  CA  LEU A 112     8200  18827  17743  -1112   6020  -4030       C  
ATOM    890  C   LEU A 112      45.818  81.995  58.237  1.00123.99           C  
ANISOU  890  C   LEU A 112     9260  19886  17962  -1198   5829  -3843       C  
ATOM    891  O   LEU A 112      46.521  81.896  57.241  1.00128.22           O  
ANISOU  891  O   LEU A 112     9923  20278  18513  -1026   5560  -3519       O  
ATOM    892  CB  LEU A 112      44.096  83.772  58.869  1.00117.31           C  
ANISOU  892  CB  LEU A 112     7902  18652  18017  -1202   6370  -4592       C  
ATOM    893  CG  LEU A 112      44.589  84.997  58.099  1.00115.38           C  
ANISOU  893  CG  LEU A 112     7581  17951  18304  -1048   6285  -4623       C  
ATOM    894  CD1 LEU A 112      44.096  84.987  56.662  1.00109.95           C  
ANISOU  894  CD1 LEU A 112     6818  16880  18077   -779   6017  -4174       C  
ATOM    895  CD2 LEU A 112      44.181  86.279  58.805  1.00122.28           C  
ANISOU  895  CD2 LEU A 112     8199  18606  19653  -1107   6630  -5224       C  
ATOM    896  N   GLY A 113      46.282  81.687  59.435  1.00112.03           N  
ANISOU  896  N   GLY A 113    14977  15082  12507    802   1416   -620       N  
ATOM    897  CA  GLY A 113      47.682  81.245  59.590  1.00120.53           C  
ANISOU  897  CA  GLY A 113    16236  16011  13547    818    634   -126       C  
ATOM    898  C   GLY A 113      48.615  82.388  59.932  1.00117.97           C  
ANISOU  898  C   GLY A 113    15877  15632  13312    787    552   -228       C  
ATOM    899  O   GLY A 113      48.370  83.526  59.544  1.00113.84           O  
ANISOU  899  O   GLY A 113    15035  15160  13057   1042   1056   -572       O  
ATOM    900  N   GLU A 114      49.724  82.063  60.595  1.00119.03           N  
ANISOU  900  N   GLU A 114    16241  15452  13533    469   -359    168       N  
ATOM    901  CA  GLU A 114      50.261  82.915  61.655  1.00125.06           C  
ANISOU  901  CA  GLU A 114    17506  16248  13763   -215   -628    167       C  
ATOM    902  C   GLU A 114      50.587  84.367  61.291  1.00119.60           C  
ANISOU  902  C   GLU A 114    16347  15672  13421    254     38   -328       C  
ATOM    903  O   GLU A 114      50.399  85.252  62.107  1.00130.60           O  
ANISOU  903  O   GLU A 114    18077  17276  14268   -368    452   -742       O  
ATOM    904  CB  GLU A 114      51.437  82.240  62.367  1.00135.99           C  
ANISOU  904  CB  GLU A 114    19189  16947  15531   -739  -2328    951       C  
ATOM    905  CG  GLU A 114      51.577  82.638  63.833  1.00148.82           C  
ANISOU  905  CG  GLU A 114    22100  18697  15746  -2337  -2996   1274       C  
ATOM    906  CD  GLU A 114      51.531  81.444  64.784  1.00166.59           C  
ANISOU  906  CD  GLU A 114    25550  20530  17216  -3859  -4677   2333       C  
ATOM    907  OE1 GLU A 114      51.669  80.287  64.323  1.00168.61           O  
ANISOU  907  OE1 GLU A 114    25265  20082  18714  -3315  -5693   2908       O  
ATOM    908  OE2 GLU A 114      51.355  81.664  66.002  1.00180.16           O  
ANISOU  908  OE2 GLU A 114    28847  22567  17038  -5876  -5018   2563       O  
ATOM    909  N   THR A 115      51.054  84.619  60.079  1.00110.49           N  
ANISOU  909  N   THR A 115    14503  14365  13113   1069    229   -391       N  
ATOM    910  CA  THR A 115      51.458  85.983  59.716  1.00109.37           C  
ANISOU  910  CA  THR A 115    14064  14223  13266   1306    601   -654       C  
ATOM    911  C   THR A 115      50.298  86.888  59.347  1.00110.71           C  
ANISOU  911  C   THR A 115    14043  14447  13572   1393   1143   -919       C  
ATOM    912  O   THR A 115      50.465  88.100  59.261  1.00113.58           O  
ANISOU  912  O   THR A 115    14139  14628  14386   1462   1238  -1090       O  
ATOM    913  CB  THR A 115      52.447  85.992  58.571  1.00110.66           C  
ANISOU  913  CB  THR A 115    13782  14173  14087   1599    686   -717       C  
ATOM    914  OG1 THR A 115      52.202  84.859  57.718  1.00111.75           O  
ANISOU  914  OG1 THR A 115    13792  14297  14370   1620    859   -764       O  
ATOM    915  CG2 THR A 115      53.857  85.941  59.112  1.00118.62           C  
ANISOU  915  CG2 THR A 115    14471  14729  15868   1586    149   -805       C  
ATOM    916  N   ALA A 116      49.120  86.286  59.146  1.00111.81           N  
ANISOU  916  N   ALA A 116    14162  14619  13699   1381   1318   -960       N  
ATOM    917  CA  ALA A 116      47.933  86.972  58.604  1.00109.94           C  
ANISOU  917  CA  ALA A 116    13409  13987  14374   1518   1405  -1150       C  
ATOM    918  C   ALA A 116      48.197  87.562  57.219  1.00110.37           C  
ANISOU  918  C   ALA A 116    13439  13728  14769   1622    756   -507       C  
ATOM    919  O   ALA A 116      47.923  88.741  56.959  1.00117.08           O  
ANISOU  919  O   ALA A 116    13884  13968  16631   1601    312   -432       O  
ATOM    920  CB  ALA A 116      47.417  88.036  59.569  1.00116.31           C  
ANISOU  920  CB  ALA A 116    13682  14473  16035   1248   1976  -2082       C  
ATOM    921  N   GLU A 117      48.735  86.738  56.332  1.00105.12           N  
ANISOU  921  N   GLU A 117    13246  13378  13317   1448    689   -122       N  
ATOM    922  CA  GLU A 117      48.941  87.153  54.970  1.00109.11           C  
ANISOU  922  CA  GLU A 117    14179  13743  13534    840    256    401       C  
ATOM    923  C   GLU A 117      48.049  86.350  54.046  1.00109.78           C  
ANISOU  923  C   GLU A 117    14635  13814  13260    420   -110    787       C  
ATOM    924  O   GLU A 117      47.200  86.902  53.376  1.00115.31           O  
ANISOU  924  O   GLU A 117    15486  13934  14390     -9  -1170   1457       O  
ATOM    925  CB  GLU A 117      50.435  87.045  54.578  1.00116.03           C  
ANISOU  925  CB  GLU A 117    15323  14964  13797    417    886     81       C  
ATOM    926  CG  GLU A 117      51.372  87.855  55.503  1.00119.45           C  
ANISOU  926  CG  GLU A 117    15369  15317  14698    830   1049   -226       C  
ATOM    927  CD  GLU A 117      52.752  88.142  54.908  1.00124.58           C  
ANISOU  927  CD  GLU A 117    16108  16023  15202    259   1586   -601       C  
ATOM    928  OE1 GLU A 117      53.297  87.287  54.168  1.00130.09           O  
ANISOU  928  OE1 GLU A 117    16850  16863  15713   -327   2300  -1161       O  
ATOM    929  OE2 GLU A 117      53.301  89.225  55.207  1.00123.19           O  
ANISOU  929  OE2 GLU A 117    15827  15682  15298    305   1474   -574       O  
ATOM    930  N   THR A 118      48.199  85.037  54.069  1.00107.35           N  
ANISOU  930  N   THR A 118    14382  13952  12451    519    521    414       N  
ATOM    931  CA  THR A 118      47.514  84.177  53.113  1.00113.30           C  
ANISOU  931  CA  THR A 118    15565  14799  12682    -27    358    639       C  
ATOM    932  C   THR A 118      46.532  83.263  53.802  1.00108.88           C  
ANISOU  932  C   THR A 118    14570  14219  12578    688    385    509       C  
ATOM    933  O   THR A 118      46.526  83.181  54.999  1.00114.27           O  
ANISOU  933  O   THR A 118    14828  14925  13664   1295    681    179       O  
ATOM    934  CB  THR A 118      48.509  83.318  52.334  1.00121.84           C  
ANISOU  934  CB  THR A 118    16972  16317  13005   -810   1324     -1       C  
ATOM    935  OG1 THR A 118      47.823  82.656  51.267  1.00138.39           O  
ANISOU  935  OG1 THR A 118    19720  18554  14307  -1758   1206    170       O  
ATOM    936  CG2 THR A 118      49.189  82.265  53.260  1.00118.44           C  
ANISOU  936  CG2 THR A 118    15714  15902  13386     47   1969   -747       C  
ATOM    937  N   GLU A 119      45.720  82.549  53.037  1.00110.11           N  
ANISOU  937  N   GLU A 119    15002  14361  12471    328     93    754       N  
ATOM    938  CA  GLU A 119      44.760  81.623  53.628  1.00106.05           C  
ANISOU  938  CA  GLU A 119    14088  13821  12383    902    204    579       C  
ATOM    939  C   GLU A 119      45.231  80.196  53.460  1.00101.54           C  
ANISOU  939  C   GLU A 119    13617  13666  11297    846    850    202       C  
ATOM    940  O   GLU A 119      45.360  79.720  52.335  1.00111.73           O  
ANISOU  940  O   GLU A 119    15330  15127  11994     94   1001    126       O  
ATOM    941  CB  GLU A 119      43.382  81.788  52.973  1.00119.47           C  
ANISOU  941  CB  GLU A 119    15745  14942  14703    671   -787   1085       C  
ATOM    942  CG  GLU A 119      42.920  83.234  52.776  1.00128.40           C  
ANISOU  942  CG  GLU A 119    16571  15149  17066    513  -1983   1583       C  
ATOM    943  CD  GLU A 119      41.559  83.329  52.091  1.00140.99           C  
ANISOU  943  CD  GLU A 119    17898  15717  19956    220  -3516   2205       C  
ATOM    944  OE1 GLU A 119      41.207  82.411  51.303  1.00141.43           O  
ANISOU  944  OE1 GLU A 119    18600  16023  19112   -324  -3819   2574       O  
ATOM    945  OE2 GLU A 119      40.841  84.319  52.344  1.00150.65           O  
ANISOU  945  OE2 GLU A 119    18112  15703  23424    487  -4504   2235       O  
ATOM    946  N   GLU A 120      45.499  79.511  54.570  1.00 97.20           N  
ANISOU  946  N   GLU A 120    12724  13164  11040   1368   1141    -65       N  
ATOM    947  CA  GLU A 120      45.857  78.061  54.523  1.00 99.77           C  
ANISOU  947  CA  GLU A 120    12856  13488  11562   1397   1370   -350       C  
ATOM    948  C   GLU A 120      44.600  77.227  54.656  1.00 94.36           C  
ANISOU  948  C   GLU A 120    12214  12821  10816   1524   1242   -173       C  
ATOM    949  O   GLU A 120      43.701  77.561  55.454  1.00 92.68           O  
ANISOU  949  O   GLU A 120    12023  12572  10620   1650   1159    -51       O  
ATOM    950  CB  GLU A 120      46.823  77.644  55.672  1.00105.88           C  
ANISOU  950  CB  GLU A 120    13325  13948  12954   1634   1075   -377       C  
ATOM    951  CG  GLU A 120      47.948  78.612  56.034  1.00114.32           C  
ANISOU  951  CG  GLU A 120    14284  14886  14266   1641    991   -460       C  
ATOM    952  CD  GLU A 120      48.319  78.524  57.515  1.00128.03           C  
ANISOU  952  CD  GLU A 120    16189  16335  16118   1580    187    -32       C  
ATOM    953  OE1 GLU A 120      47.456  78.091  58.326  1.00135.41           O  
ANISOU  953  OE1 GLU A 120    17635  17398  16414   1267    -60    319       O  
ATOM    954  OE2 GLU A 120      49.460  78.893  57.876  1.00136.03           O  
ANISOU  954  OE2 GLU A 120    16953  16969  17762   1571   -230    -57       O  
ATOM    955  N   VAL A 121      44.544  76.122  53.928  1.00 88.05           N  
ANISOU  955  N   VAL A 121    11318  12025  10110   1360   1434   -411       N  
ATOM    956  CA  VAL A 121      43.515  75.142  54.169  1.00 86.64           C  
ANISOU  956  CA  VAL A 121    11105  11811  10001   1522   1311   -272       C  
ATOM    957  C   VAL A 121      43.653  74.576  55.590  1.00 89.53           C  
ANISOU  957  C   VAL A 121    11448  11966  10601   1656    987    -37       C  
ATOM    958  O   VAL A 121      44.709  74.683  56.207  1.00 91.87           O  
ANISOU  958  O   VAL A 121    11670  12003  11231   1620    628     55       O  
ATOM    959  CB  VAL A 121      43.511  74.036  53.075  1.00 90.77           C  
ANISOU  959  CB  VAL A 121    11498  12345  10644   1204   1641   -701       C  
ATOM    960  CG1 VAL A 121      44.760  73.184  53.133  1.00 95.66           C  
ANISOU  960  CG1 VAL A 121    11423  12541  12383   1209   1916  -1365       C  
ATOM    961  CG2 VAL A 121      42.276  73.173  53.179  1.00 91.98           C  
ANISOU  961  CG2 VAL A 121    11668  12483  10798   1369   1458   -483       C  
ATOM    962  N   LYS A 122      42.564  74.052  56.136  1.00 86.13           N  
ANISOU  962  N   LYS A 122     9146  12703  10876   -200   -786   1244       N  
ATOM    963  CA  LYS A 122      42.615  73.402  57.443  1.00 87.73           C  
ANISOU  963  CA  LYS A 122     9095  13053  11183    -64   -675   1133       C  
ATOM    964  C   LYS A 122      42.940  71.937  57.259  1.00 92.82           C  
ANISOU  964  C   LYS A 122     9436  13949  11881   -188   -616   1095       C  
ATOM    965  O   LYS A 122      42.142  71.173  56.702  1.00 98.29           O  
ANISOU  965  O   LYS A 122     9938  14757  12651   -142   -639   1174       O  
ATOM    966  CB  LYS A 122      41.303  73.593  58.212  1.00 89.19           C  
ANISOU  966  CB  LYS A 122     9204  13195  11489    312   -623   1172       C  
ATOM    967  CG  LYS A 122      41.082  75.033  58.673  1.00 94.81           C  
ANISOU  967  CG  LYS A 122    10246  13616  12159    504   -655   1149       C  
ATOM    968  CD  LYS A 122      40.150  75.150  59.874  1.00 97.16           C  
ANISOU  968  CD  LYS A 122    10497  13861  12557    858   -429   1081       C  
ATOM    969  CE  LYS A 122      38.763  75.622  59.450  1.00108.32           C  
ANISOU  969  CE  LYS A 122    11698  15178  14278   1185   -475   1119       C  
ATOM    970  NZ  LYS A 122      38.345  76.847  60.203  1.00114.37           N  
ANISOU  970  NZ  LYS A 122    12740  15647  15066   1507   -379   1024       N  
ATOM    971  N   ALA A 123      44.145  71.563  57.677  1.00 94.09           N  
ANISOU  971  N   ALA A 123     9544  14158  12049   -341   -595    939       N  
ATOM    972  CA  ALA A 123      44.673  70.215  57.482  1.00 93.92           C  
ANISOU  972  CA  ALA A 123     9267  14313  12102   -434   -570    860       C  
ATOM    973  C   ALA A 123      44.165  69.257  58.563  1.00 91.96           C  
ANISOU  973  C   ALA A 123     8978  14114  11845   -200   -558    886       C  
ATOM    974  O   ALA A 123      44.096  69.624  59.741  1.00104.89           O  
ANISOU  974  O   ALA A 123    10831  15639  13381    -20   -575    861       O  
ATOM    975  CB  ALA A 123      46.191  70.260  57.502  1.00 95.19           C  
ANISOU  975  CB  ALA A 123     9319  14460  12388   -641   -598    624       C  
ATOM    976  N   LYS A 124      43.832  68.030  58.177  1.00 84.70           N  
ANISOU  976  N   LYS A 124     7886  13307  10986   -223   -502    928       N  
ATOM    977  CA  LYS A 124      43.404  67.024  59.161  1.00 86.39           C  
ANISOU  977  CA  LYS A 124     8163  13492  11168    -67   -416    970       C  
ATOM    978  C   LYS A 124      44.299  65.847  59.035  1.00 84.34           C  
ANISOU  978  C   LYS A 124     7832  13264  10948   -114   -523    864       C  
ATOM    979  O   LYS A 124      45.058  65.753  58.076  1.00 88.52           O  
ANISOU  979  O   LYS A 124     8167  13878  11587   -274   -582    745       O  
ATOM    980  CB  LYS A 124      41.938  66.584  58.916  1.00 92.41           C  
ANISOU  980  CB  LYS A 124     8766  14282  12062    -54   -214   1106       C  
ATOM    981  CG  LYS A 124      40.905  67.720  58.906  1.00 93.08           C  
ANISOU  981  CG  LYS A 124     8796  14323  12245     60   -142   1165       C  
ATOM    982  CD  LYS A 124      39.476  67.187  58.886  1.00103.28           C  
ANISOU  982  CD  LYS A 124     9784  15622  13836     92     65   1211       C  
ATOM    983  CE  LYS A 124      39.342  65.907  58.058  1.00 99.91           C  
ANISOU  983  CE  LYS A 124     9127  15281  13552   -106    -14   1206       C  
ATOM    984  NZ  LYS A 124      38.055  65.833  57.299  1.00 95.65           N  
ANISOU  984  NZ  LYS A 124     8166  14767  13407   -128   -107   1184       N  
ATOM    985  N   ALA A 125      44.201  64.914  59.974  1.00 85.19           N  
ANISOU  985  N   ALA A 125     8151  13259  10957     29   -506    898       N  
ATOM    986  CA  ALA A 125      44.941  63.656  59.849  1.00 88.45           C  
ANISOU  986  CA  ALA A 125     8535  13639  11432     50   -649    803       C  
ATOM    987  C   ALA A 125      44.103  62.404  60.112  1.00 94.35           C  
ANISOU  987  C   ALA A 125     9449  14267  12131     55   -452    948       C  
ATOM    988  O   ALA A 125      43.262  62.380  61.009  1.00112.29           O  
ANISOU  988  O   ALA A 125    12020  16396  14246    112   -210   1095       O  
ATOM    989  CB  ALA A 125      46.158  63.674  60.737  1.00 85.68           C  
ANISOU  989  CB  ALA A 125     8366  13159  11028    254  -1012    628       C  
ATOM    990  N   LEU A 126      44.339  61.366  59.318  1.00 94.51           N  
ANISOU  990  N   LEU A 126     9303  14307  12298    -32   -491    884       N  
ATOM    991  CA  LEU A 126      43.777  60.046  59.584  1.00 96.78           C  
ANISOU  991  CA  LEU A 126     9804  14401  12564    -52   -349    985       C  
ATOM    992  C   LEU A 126      44.355  59.464  60.861  1.00101.02           C  
ANISOU  992  C   LEU A 126    10892  14641  12850    209   -508   1013       C  
ATOM    993  O   LEU A 126      45.448  59.843  61.277  1.00107.02           O  
ANISOU  993  O   LEU A 126    11725  15378  13557    431   -884    865       O  
ATOM    994  CB  LEU A 126      44.077  59.100  58.422  1.00 96.68           C  
ANISOU  994  CB  LEU A 126     9557  14432  12742   -173   -419    858       C  
ATOM    995  CG  LEU A 126      43.499  59.490  57.070  1.00 91.50           C  
ANISOU  995  CG  LEU A 126     8547  13992  12225   -419   -348    825       C  
ATOM    996  CD1 LEU A 126      43.959  58.520  56.007  1.00 88.98           C  
ANISOU  996  CD1 LEU A 126     8154  13662  11991   -507   -411    657       C  
ATOM    997  CD2 LEU A 126      41.994  59.497  57.169  1.00 95.56           C  
ANISOU  997  CD2 LEU A 126     8984  14480  12843   -567   -145    982       C  
ATOM    998  N   THR A 127      43.609  58.552  61.491  1.00105.66           N  
ANISOU  998  N   THR A 127    11906  14950  13288    173   -241   1188       N  
ATOM    999  CA  THR A 127      44.165  57.665  62.529  1.00106.47           C  
ANISOU  999  CA  THR A 127    12719  14655  13079    428   -442   1241       C  
ATOM   1000  C   THR A 127      44.653  56.376  61.889  1.00103.55           C  
ANISOU 1000  C   THR A 127    12298  14150  12893    454   -637   1148       C  
ATOM   1001  O   THR A 127      44.425  56.140  60.702  1.00 92.97           O  
ANISOU 1001  O   THR A 127    10434  13018  11872    229   -528   1056       O  
ATOM   1002  CB  THR A 127      43.141  57.328  63.633  1.00109.96           C  
ANISOU 1002  CB  THR A 127    13858  14750  13170    349     58   1499       C  
ATOM   1003  OG1 THR A 127      42.172  56.398  63.130  1.00112.50           O  
ANISOU 1003  OG1 THR A 127    14039  14976  13729     16    508   1594       O  
ATOM   1004  CG2 THR A 127      42.446  58.597  64.136  1.00110.24           C  
ANISOU 1004  CG2 THR A 127    13861  14926  13099    298    404   1554       C  
ATOM   1005  N   VAL A 128      45.350  55.557  62.668  1.00110.43           N  
ANISOU 1005  N   VAL A 128    13787  14634  13537    767   -981   1153       N  
ATOM   1006  CA  VAL A 128      45.982  54.367  62.129  1.00113.18           C  
ANISOU 1006  CA  VAL A 128    14114  14801  14088    898  -1250   1016       C  
ATOM   1007  C   VAL A 128      44.907  53.388  61.689  1.00118.10           C  
ANISOU 1007  C   VAL A 128    14850  15252  14769    544   -764   1175       C  
ATOM   1008  O   VAL A 128      45.014  52.777  60.623  1.00121.43           O  
ANISOU 1008  O   VAL A 128    14884  15752  15501    431   -778   1018       O  
ATOM   1009  CB  VAL A 128      46.940  53.716  63.148  1.00116.40           C  
ANISOU 1009  CB  VAL A 128    15239  14745  14240   1397  -1844    984       C  
ATOM   1010  CG1 VAL A 128      47.602  52.480  62.553  1.00115.04           C  
ANISOU 1010  CG1 VAL A 128    15004  14352  14353   1596  -2134    802       C  
ATOM   1011  CG2 VAL A 128      47.992  54.721  63.594  1.00118.38           C  
ANISOU 1011  CG2 VAL A 128    15290  15155  14532   1723  -2417    758       C  
ATOM   1012  N   ARG A 129      43.845  53.291  62.489  1.00121.30           N  
ANISOU 1012  N   ARG A 129    15768  15414  14904    331   -283   1452       N  
ATOM   1013  CA  ARG A 129      42.649  52.531  62.117  1.00128.95           C  
ANISOU 1013  CA  ARG A 129    16706  16234  16054   -117    272   1572       C  
ATOM   1014  C   ARG A 129      42.139  52.907  60.692  1.00122.98           C  
ANISOU 1014  C   ARG A 129    14992  15944  15790   -431    352   1396       C  
ATOM   1015  O   ARG A 129      42.139  52.067  59.774  1.00121.36           O  
ANISOU 1015  O   ARG A 129    14594  15689  15826   -569    268   1268       O  
ATOM   1016  CB  ARG A 129      41.543  52.747  63.168  1.00142.17           C  
ANISOU 1016  CB  ARG A 129    18858  17677  17483   -353    931   1829       C  
ATOM   1017  CG  ARG A 129      41.692  51.913  64.454  1.00159.00           C  
ANISOU 1017  CG  ARG A 129    22227  19141  19044   -202   1043   2065       C  
ATOM   1018  CD  ARG A 129      42.634  52.560  65.487  1.00161.58           C  
ANISOU 1018  CD  ARG A 129    23205  19370  18818    302    555   2090       C  
ATOM   1019  NE  ARG A 129      42.328  52.155  66.871  1.00169.49           N  
ANISOU 1019  NE  ARG A 129    25524  19744  19129    348    896   2372       N  
ATOM   1020  CZ  ARG A 129      42.947  51.176  67.542  1.00175.77           C  
ANISOU 1020  CZ  ARG A 129    27422  19918  19444    656    512   2499       C  
ATOM   1021  NH1 ARG A 129      42.592  50.904  68.793  1.00181.78           N  
ANISOU 1021  NH1 ARG A 129    29529  20071  19468    661    896   2780       N  
ATOM   1022  NH2 ARG A 129      43.915  50.467  66.971  1.00178.17           N  
ANISOU 1022  NH2 ARG A 129    27555  20159  19983    979   -235   2334       N  
ATOM   1023  N   GLN A 130      41.740  54.174  60.525  1.00111.82           N  
ANISOU 1023  N   GLN A 130    13089  14926  14469   -504    455   1380       N  
ATOM   1024  CA  GLN A 130      41.330  54.722  59.226  1.00102.99           C  
ANISOU 1024  CA  GLN A 130    11215  14209  13705   -715    400   1229       C  
ATOM   1025  C   GLN A 130      42.336  54.467  58.114  1.00106.96           C  
ANISOU 1025  C   GLN A 130    11490  14865  14284   -605      0    999       C  
ATOM   1026  O   GLN A 130      41.961  54.060  57.010  1.00109.82           O  
ANISOU 1026  O   GLN A 130    11577  15298  14851   -826    -25    877       O  
ATOM   1027  CB  GLN A 130      41.098  56.210  59.341  1.00 94.19           C  
ANISOU 1027  CB  GLN A 130     9787  13418  12583   -662    434   1248       C  
ATOM   1028  CG  GLN A 130      40.161  56.578  60.453  1.00101.61           C  
ANISOU 1028  CG  GLN A 130    10939  14214  13453   -726    908   1419       C  
ATOM   1029  CD  GLN A 130      40.127  58.059  60.702  1.00106.64           C  
ANISOU 1029  CD  GLN A 130    11387  15104  14026   -578    893   1414       C  
ATOM   1030  OE1 GLN A 130      41.025  58.793  60.284  1.00110.96           O  
ANISOU 1030  OE1 GLN A 130    11796  15870  14491   -406    500   1315       O  
ATOM   1031  NE2 GLN A 130      39.097  58.516  61.404  1.00114.08           N  
ANISOU 1031  NE2 GLN A 130    12331  15978  15035   -658   1382   1497       N  
ATOM   1032  N   TRP A 131      43.611  54.741  58.392  1.00110.57           N  
ANISOU 1032  N   TRP A 131    12051  15357  14603   -268   -301    897       N  
ATOM   1033  CA  TRP A 131      44.671  54.512  57.409  1.00106.22           C  
ANISOU 1033  CA  TRP A 131    11239  14925  14192   -155   -549    621       C  
ATOM   1034  C   TRP A 131      44.670  53.075  56.925  1.00104.76           C  
ANISOU 1034  C   TRP A 131    11241  14456  14103   -195   -558    528       C  
ATOM   1035  O   TRP A 131      44.817  52.835  55.737  1.00109.03           O  
ANISOU 1035  O   TRP A 131    11542  15115  14769   -314   -557    325       O  
ATOM   1036  CB  TRP A 131      46.052  54.896  57.960  1.00108.51           C  
ANISOU 1036  CB  TRP A 131    11527  15224  14477    221   -876    464       C  
ATOM   1037  CG  TRP A 131      47.160  54.765  56.937  1.00106.81           C  
ANISOU 1037  CG  TRP A 131    10911  15144  14527    305   -982    115       C  
ATOM   1038  CD1 TRP A 131      48.181  53.867  56.949  1.00110.90           C  
ANISOU 1038  CD1 TRP A 131    11442  15449  15243    615  -1219   -132       C  
ATOM   1039  CD2 TRP A 131      47.327  55.541  55.746  1.00103.53           C  
ANISOU 1039  CD2 TRP A 131    10075  15054  14205     77   -787    -41       C  
ATOM   1040  NE1 TRP A 131      48.982  54.040  55.846  1.00108.88           N  
ANISOU 1040  NE1 TRP A 131    10713  15397  15259    574  -1093   -470       N  
ATOM   1041  CE2 TRP A 131      48.477  55.060  55.092  1.00103.49           C  
ANISOU 1041  CE2 TRP A 131     9830  15029  14459    219   -799   -398       C  
ATOM   1042  CE3 TRP A 131      46.617  56.594  55.171  1.00 98.66           C  
ANISOU 1042  CE3 TRP A 131     9324  14693  13468   -210   -599     79       C  
ATOM   1043  CZ2 TRP A 131      48.931  55.596  53.905  1.00102.19           C  
ANISOU 1043  CZ2 TRP A 131     9365  15085  14376     19   -514   -622       C  
ATOM   1044  CZ3 TRP A 131      47.079  57.132  53.991  1.00 96.31           C  
ANISOU 1044  CZ3 TRP A 131     8811  14583  13197   -375   -432   -108       C  
ATOM   1045  CH2 TRP A 131      48.223  56.633  53.371  1.00 98.16           C  
ANISOU 1045  CH2 TRP A 131     8876  14788  13632   -292   -333   -449       C  
ATOM   1046  N   LEU A 132      44.455  52.125  57.840  1.00104.42           N  
ANISOU 1046  N   LEU A 132    11738  13987  13949   -114   -538    684       N  
ATOM   1047  CA  LEU A 132      44.359  50.700  57.467  1.00105.15           C  
ANISOU 1047  CA  LEU A 132    12114  13708  14128   -175   -531    619       C  
ATOM   1048  C   LEU A 132      43.275  50.406  56.419  1.00105.51           C  
ANISOU 1048  C   LEU A 132    11892  13832  14364   -641   -308    575       C  
ATOM   1049  O   LEU A 132      43.539  49.719  55.429  1.00105.99           O  
ANISOU 1049  O   LEU A 132    11898  13836  14535   -679   -407    345       O  
ATOM   1050  CB  LEU A 132      44.172  49.809  58.691  1.00103.98           C  
ANISOU 1050  CB  LEU A 132    12742  13004  13761    -69   -487    854       C  
ATOM   1051  CG  LEU A 132      44.601  48.353  58.480  1.00103.33           C  
ANISOU 1051  CG  LEU A 132    13087  12437  13736     74   -655    746       C  
ATOM   1052  CD1 LEU A 132      45.714  48.246  57.453  1.00 99.88           C  
ANISOU 1052  CD1 LEU A 132    12203  12199  13545    351   -962    357       C  
ATOM   1053  CD2 LEU A 132      45.033  47.719  59.794  1.00109.68           C  
ANISOU 1053  CD2 LEU A 132    14782  12672  14218    440   -863    940       C  
ATOM   1054  N   LEU A 133      42.068  50.927  56.642  1.00104.53           N  
ANISOU 1054  N   LEU A 133    11595  13813  14307   -969    -39    751       N  
ATOM   1055  CA  LEU A 133      40.988  50.868  55.637  1.00106.53           C  
ANISOU 1055  CA  LEU A 133    11457  14183  14834  -1382     22    657       C  
ATOM   1056  C   LEU A 133      41.420  51.457  54.282  1.00106.53           C  
ANISOU 1056  C   LEU A 133    11115  14549  14812  -1346   -255    421       C  
ATOM   1057  O   LEU A 133      41.404  50.774  53.248  1.00106.80           O  
ANISOU 1057  O   LEU A 133    11182  14502  14894  -1476   -393    211       O  
ATOM   1058  CB  LEU A 133      39.740  51.595  56.157  1.00105.79           C  
ANISOU 1058  CB  LEU A 133    11068  14198  14927  -1635    314    822       C  
ATOM   1059  CG  LEU A 133      38.812  50.849  57.145  1.00113.74           C  
ANISOU 1059  CG  LEU A 133    12345  14785  16084  -1919    794    996       C  
ATOM   1060  CD1 LEU A 133      39.557  49.898  58.094  1.00114.30           C  
ANISOU 1060  CD1 LEU A 133    13239  14377  15810  -1718    887   1145       C  
ATOM   1061  CD2 LEU A 133      37.949  51.835  57.925  1.00114.60           C  
ANISOU 1061  CD2 LEU A 133    12194  15039  16310  -2007   1187   1137       C  
ATOM   1062  N   VAL A 134      41.829  52.718  54.300  1.00106.71           N  
ANISOU 1062  N   VAL A 134    10916  14917  14709  -1183   -306    451       N  
ATOM   1063  CA  VAL A 134      42.227  53.416  53.080  1.00 99.25           C  
ANISOU 1063  CA  VAL A 134     9783  14265  13663  -1187   -466    273       C  
ATOM   1064  C   VAL A 134      43.276  52.646  52.255  1.00 99.67           C  
ANISOU 1064  C   VAL A 134    10016  14223  13631  -1078   -510     -1       C  
ATOM   1065  O   VAL A 134      43.199  52.623  51.042  1.00 97.42           O  
ANISOU 1065  O   VAL A 134     9773  14002  13241  -1221   -577   -179       O  
ATOM   1066  CB  VAL A 134      42.679  54.856  53.386  1.00 93.04           C  
ANISOU 1066  CB  VAL A 134     8825  13770  12754  -1033   -452    357       C  
ATOM   1067  CG1 VAL A 134      43.264  55.535  52.141  1.00 90.02           C  
ANISOU 1067  CG1 VAL A 134     8402  13597  12202  -1065   -510    184       C  
ATOM   1068  CG2 VAL A 134      41.503  55.641  53.943  1.00 85.14           C  
ANISOU 1068  CG2 VAL A 134     7633  12854  11862  -1138   -397    565       C  
ATOM   1069  N   VAL A 135      44.218  51.979  52.911  1.00103.50           N  
ANISOU 1069  N   VAL A 135    10658  14507  14157   -799   -489    -61       N  
ATOM   1070  CA  VAL A 135      45.192  51.180  52.164  1.00108.68           C  
ANISOU 1070  CA  VAL A 135    11418  15034  14839   -646   -487   -380       C  
ATOM   1071  C   VAL A 135      44.535  49.915  51.623  1.00114.25           C  
ANISOU 1071  C   VAL A 135    12415  15418  15577   -842   -524   -466       C  
ATOM   1072  O   VAL A 135      44.665  49.602  50.428  1.00110.93           O  
ANISOU 1072  O   VAL A 135    12088  14994  15066   -943   -507   -727       O  
ATOM   1073  CB  VAL A 135      46.452  50.829  52.987  1.00109.08           C  
ANISOU 1073  CB  VAL A 135    11480  14929  15035   -205   -571   -489       C  
ATOM   1074  CG1 VAL A 135      47.359  49.903  52.189  1.00113.42           C  
ANISOU 1074  CG1 VAL A 135    12071  15301  15721    -19   -526   -874       C  
ATOM   1075  CG2 VAL A 135      47.208  52.098  53.379  1.00107.64           C  
ANISOU 1075  CG2 VAL A 135    10951  15054  14890    -53   -581   -499       C  
ATOM   1076  N   ALA A 136      43.792  49.211  52.491  1.00115.48           N  
ANISOU 1076  N   ALA A 136    12779  15263  15834   -937   -535   -256       N  
ATOM   1077  CA  ALA A 136      43.078  47.979  52.083  1.00119.21           C  
ANISOU 1077  CA  ALA A 136    13528  15356  16408  -1200   -557   -335       C  
ATOM   1078  C   ALA A 136      42.066  48.263  50.958  1.00118.00           C  
ANISOU 1078  C   ALA A 136    13185  15374  16274  -1601   -671   -440       C  
ATOM   1079  O   ALA A 136      41.999  47.528  49.970  1.00111.71           O  
ANISOU 1079  O   ALA A 136    12596  14404  15442  -1730   -792   -700       O  
ATOM   1080  CB  ALA A 136      42.401  47.321  53.276  1.00119.62           C  
ANISOU 1080  CB  ALA A 136    13861  15017  16573  -1319   -428    -62       C  
ATOM   1081  N   ALA A 137      41.326  49.365  51.095  1.00116.78           N  
ANISOU 1081  N   ALA A 137    12676  15535  16161  -1747   -695   -270       N  
ATOM   1082  CA  ALA A 137      40.541  49.902  49.991  1.00114.97           C  
ANISOU 1082  CA  ALA A 137    12267  15502  15912  -1991   -958   -387       C  
ATOM   1083  C   ALA A 137      41.357  49.978  48.687  1.00115.28           C  
ANISOU 1083  C   ALA A 137    12589  15632  15579  -1888  -1062   -662       C  
ATOM   1084  O   ALA A 137      40.909  49.508  47.654  1.00124.95           O  
ANISOU 1084  O   ALA A 137    14034  16725  16714  -2085  -1315   -880       O  
ATOM   1085  CB  ALA A 137      39.964  51.261  50.351  1.00108.63           C  
ANISOU 1085  CB  ALA A 137    11073  15031  15170  -1994   -986   -182       C  
ATOM   1086  N   SER A 138      42.565  50.531  48.755  1.00111.90           N  
ANISOU 1086  N   SER A 138    12181  15385  14950  -1601   -836   -685       N  
ATOM   1087  CA  SER A 138      43.419  50.643  47.572  1.00115.68           C  
ANISOU 1087  CA  SER A 138    12937  15922  15091  -1537   -730   -966       C  
ATOM   1088  C   SER A 138      43.702  49.303  46.917  1.00123.17           C  
ANISOU 1088  C   SER A 138    14266  16531  15999  -1540   -708  -1280       C  
ATOM   1089  O   SER A 138      43.976  49.241  45.710  1.00131.96           O  
ANISOU 1089  O   SER A 138    15756  17614  16767  -1600   -659  -1548       O  
ATOM   1090  CB  SER A 138      44.733  51.317  47.919  1.00110.54           C  
ANISOU 1090  CB  SER A 138    12107  15466  14426  -1263   -394   -996       C  
ATOM   1091  OG  SER A 138      44.507  52.641  48.305  1.00109.33           O  
ANISOU 1091  OG  SER A 138    11710  15597  14232  -1291   -418   -753       O  
ATOM   1092  N   VAL A 139      43.672  48.236  47.714  1.00120.41           N  
ANISOU 1092  N   VAL A 139    13926  15874  15950  -1465   -712  -1253       N  
ATOM   1093  CA  VAL A 139      44.015  46.908  47.223  1.00120.59           C  
ANISOU 1093  CA  VAL A 139    14337  15502  15980  -1412   -687  -1556       C  
ATOM   1094  C   VAL A 139      42.811  46.298  46.523  1.00126.04           C  
ANISOU 1094  C   VAL A 139    15281  15963  16643  -1811  -1014  -1646       C  
ATOM   1095  O   VAL A 139      42.936  45.745  45.427  1.00133.30           O  
ANISOU 1095  O   VAL A 139    16628  16701  17316  -1873  -1076  -1978       O  
ATOM   1096  CB  VAL A 139      44.529  45.983  48.360  1.00117.15           C  
ANISOU 1096  CB  VAL A 139    13936  14727  15847  -1127   -617  -1489       C  
ATOM   1097  CG1 VAL A 139      45.040  44.668  47.797  1.00120.97           C  
ANISOU 1097  CG1 VAL A 139    14843  14770  16350   -986   -582  -1844       C  
ATOM   1098  CG2 VAL A 139      45.639  46.671  49.132  1.00115.25           C  
ANISOU 1098  CG2 VAL A 139    13380  14710  15698   -721   -468  -1422       C  
ATOM   1099  N   VAL A 140      41.639  46.431  47.146  1.00126.35           N  
ANISOU 1099  N   VAL A 140    15042  15998  16966  -2092  -1214  -1393       N  
ATOM   1100  CA  VAL A 140      40.382  45.964  46.549  1.00126.09           C  
ANISOU 1100  CA  VAL A 140    15058  15765  17083  -2516  -1600  -1515       C  
ATOM   1101  C   VAL A 140      40.125  46.717  45.247  1.00127.10           C  
ANISOU 1101  C   VAL A 140    15341  16121  16827  -2595  -1956  -1694       C  
ATOM   1102  O   VAL A 140      39.992  46.102  44.186  1.00131.97           O  
ANISOU 1102  O   VAL A 140    16426  16504  17210  -2724  -2225  -2015       O  
ATOM   1103  CB  VAL A 140      39.181  46.150  47.512  1.00122.09           C  
ANISOU 1103  CB  VAL A 140    14051  15256  17081  -2807  -1638  -1244       C  
ATOM   1104  CG1 VAL A 140      37.883  45.745  46.834  1.00128.32           C  
ANISOU 1104  CG1 VAL A 140    14716  15857  18183  -3260  -2096  -1453       C  
ATOM   1105  CG2 VAL A 140      39.389  45.345  48.781  1.00121.22           C  
ANISOU 1105  CG2 VAL A 140    14031  14810  17215  -2767  -1254  -1043       C  
ATOM   1106  N   GLY A 141      40.118  48.052  45.335  1.00121.24           N  
ANISOU 1106  N   GLY A 141    14329  15784  15951  -2491  -1962  -1488       N  
ATOM   1107  CA  GLY A 141      39.888  48.926  44.187  1.00126.92           C  
ANISOU 1107  CA  GLY A 141    15319  16678  16227  -2523  -2315  -1585       C  
ATOM   1108  C   GLY A 141      40.859  48.738  43.026  1.00139.29           C  
ANISOU 1108  C   GLY A 141    17617  18153  17152  -2411  -2134  -1874       C  
ATOM   1109  O   GLY A 141      40.668  49.305  41.953  1.00145.14           O  
ANISOU 1109  O   GLY A 141    18844  18919  17380  -2463  -2426  -1977       O  
ATOM   1110  N   THR A 142      41.899  47.938  43.239  1.00145.10           N  
ANISOU 1110  N   THR A 142    18485  18738  17907  -2235  -1641  -2023       N  
ATOM   1111  CA  THR A 142      42.871  47.640  42.186  1.00145.94           C  
ANISOU 1111  CA  THR A 142    19231  18718  17498  -2121  -1306  -2370       C  
ATOM   1112  C   THR A 142      42.360  46.533  41.253  1.00156.43           C  
ANISOU 1112  C   THR A 142    21177  19634  18623  -2307  -1665  -2722       C  
ATOM   1113  O   THR A 142      42.400  46.683  40.030  1.00167.66           O  
ANISOU 1113  O   THR A 142    23323  20965  19415  -2374  -1765  -2962       O  
ATOM   1114  CB  THR A 142      44.239  47.257  42.782  1.00140.92           C  
ANISOU 1114  CB  THR A 142    18380  18073  17090  -1790   -657  -2466       C  
ATOM   1115  OG1 THR A 142      44.734  48.345  43.567  1.00137.25           O  
ANISOU 1115  OG1 THR A 142    17386  17972  16790  -1641   -405  -2194       O  
ATOM   1116  CG2 THR A 142      45.223  46.955  41.704  1.00142.55           C  
ANISOU 1116  CG2 THR A 142    19147  18140  16873  -1678   -185  -2883       C  
ATOM   1117  N   SER A 143      41.867  45.432  41.834  1.00155.91           N  
ANISOU 1117  N   SER A 143    20920  19269  19050  -2412  -1857  -2753       N  
ATOM   1118  CA  SER A 143      41.267  44.337  41.043  1.00158.12           C  
ANISOU 1118  CA  SER A 143    21737  19102  19239  -2648  -2275  -3102       C  
ATOM   1119  C   SER A 143      39.972  44.801  40.399  1.00159.15           C  
ANISOU 1119  C   SER A 143    21933  19261  19276  -2969  -3071  -3117       C  
ATOM   1120  O   SER A 143      39.572  44.290  39.357  1.00166.57           O  
ANISOU 1120  O   SER A 143    23511  19899  19877  -3135  -3538  -3462       O  
ATOM   1121  CB  SER A 143      40.992  43.117  41.916  1.00157.86           C  
ANISOU 1121  CB  SER A 143    21472  18690  19817  -2743  -2264  -3090       C  
ATOM   1122  OG  SER A 143      41.634  43.237  43.169  1.00157.19           O  
ANISOU 1122  OG  SER A 143    20906  18735  20081  -2477  -1800  -2790       O  
ATOM   1123  N   VAL A 144      39.320  45.769  41.045  1.00151.10           N  
ANISOU 1123  N   VAL A 144    20249  18574  18587  -3021  -3272  -2774       N  
ATOM   1124  CA  VAL A 144      38.114  46.406  40.522  1.00150.30           C  
ANISOU 1124  CA  VAL A 144    20053  18541  18513  -3223  -4085  -2783       C  
ATOM   1125  C   VAL A 144      38.421  47.403  39.393  1.00150.74           C  
ANISOU 1125  C   VAL A 144    20829  18733  17709  -3066  -4288  -2829       C  
ATOM   1126  O   VAL A 144      37.595  47.636  38.539  1.00158.26           O  
ANISOU 1126  O   VAL A 144    22138  19564  18427  -3175  -5105  -2986       O  
ATOM   1127  CB  VAL A 144      37.289  47.075  41.665  1.00146.86           C  
ANISOU 1127  CB  VAL A 144    18612  18371  18813  -3297  -4158  -2436       C  
ATOM   1128  CG1 VAL A 144      36.704  48.426  41.236  1.00143.77           C  
ANISOU 1128  CG1 VAL A 144    18124  18257  18244  -3209  -4693  -2316       C  
ATOM   1129  CG2 VAL A 144      36.204  46.124  42.175  1.00148.65           C  
ANISOU 1129  CG2 VAL A 144    18313  18304  19862  -3677  -4434  -2547       C  
ATOM   1130  N   TYR A 145      39.617  47.972  39.392  1.00147.54           N  
ANISOU 1130  N   TYR A 145    18625  18819  18613  -1885  -1774    529       N  
ATOM   1131  CA  TYR A 145      40.060  48.789  38.266  1.00146.56           C  
ANISOU 1131  CA  TYR A 145    18328  18898  18457  -1644  -1655    350       C  
ATOM   1132  C   TYR A 145      40.733  47.908  37.198  1.00150.68           C  
ANISOU 1132  C   TYR A 145    18821  19362  19068  -1430  -1839     88       C  
ATOM   1133  O   TYR A 145      41.014  48.359  36.083  1.00152.61           O  
ANISOU 1133  O   TYR A 145    18909  19876  19198  -1277  -1732    -59       O  
ATOM   1134  CB  TYR A 145      40.983  49.915  38.756  1.00145.41           C  
ANISOU 1134  CB  TYR A 145    18134  18861  18252  -1580  -1509    382       C  
ATOM   1135  CG  TYR A 145      41.932  50.480  37.718  1.00146.62           C  
ANISOU 1135  CG  TYR A 145    18175  19180  18352  -1480  -1389    244       C  
ATOM   1136  CD1 TYR A 145      43.178  49.884  37.484  1.00148.86           C  
ANISOU 1136  CD1 TYR A 145    18329  19566  18664  -1352  -1484     -7       C  
ATOM   1137  CD2 TYR A 145      41.615  51.634  37.011  1.00145.91           C  
ANISOU 1137  CD2 TYR A 145    18121  19187  18129  -1521  -1202    348       C  
ATOM   1138  CE1 TYR A 145      44.056  50.400  36.548  1.00147.51           C  
ANISOU 1138  CE1 TYR A 145    17956  19736  18355  -1375  -1301   -166       C  
ATOM   1139  CE2 TYR A 145      42.494  52.158  36.078  1.00148.46           C  
ANISOU 1139  CE2 TYR A 145    18396  19695  18314  -1580  -1037    321       C  
ATOM   1140  CZ  TYR A 145      43.713  51.535  35.856  1.00148.09           C  
ANISOU 1140  CZ  TYR A 145    18109  19894  18262  -1562  -1040     55       C  
ATOM   1141  OH  TYR A 145      44.588  52.050  34.939  1.00151.86           O  
ANISOU 1141  OH  TYR A 145    18441  20738  18519  -1728   -807     -7       O  
ATOM   1142  N   ILE A 146      40.954  46.643  37.530  1.00155.09           N  
ANISOU 1142  N   ILE A 146    19563  19575  19790  -1405  -2154     23       N  
ATOM   1143  CA  ILE A 146      41.416  45.680  36.538  1.00162.89           C  
ANISOU 1143  CA  ILE A 146    20511  20482  20896  -1122  -2446   -350       C  
ATOM   1144  C   ILE A 146      40.219  45.097  35.743  1.00173.23           C  
ANISOU 1144  C   ILE A 146    21793  21713  22310  -1249  -2522   -462       C  
ATOM   1145  O   ILE A 146      40.344  44.787  34.550  1.00174.55           O  
ANISOU 1145  O   ILE A 146    21766  22078  22477   -977  -2635   -838       O  
ATOM   1146  CB  ILE A 146      42.337  44.591  37.168  1.00162.33           C  
ANISOU 1146  CB  ILE A 146    20712  19986  20978   -883  -2899   -485       C  
ATOM   1147  CG1 ILE A 146      43.732  45.174  37.449  1.00155.77           C  
ANISOU 1147  CG1 ILE A 146    19673  19503  20010   -589  -2853   -682       C  
ATOM   1148  CG2 ILE A 146      42.453  43.363  36.269  1.00167.88           C  
ANISOU 1148  CG2 ILE A 146    21467  20433  21886   -585  -3352   -925       C  
ATOM   1149  CD1 ILE A 146      44.310  46.001  36.308  1.00153.18           C  
ANISOU 1149  CD1 ILE A 146    18869  19835  19496   -494  -2547   -975       C  
ATOM   1150  N   GLU A 147      39.052  45.023  36.397  1.00178.73           N  
ANISOU 1150  N   GLU A 147    22600  22262  23046  -1674  -2431   -201       N  
ATOM   1151  CA  GLU A 147      37.769  44.775  35.705  1.00177.94           C  
ANISOU 1151  CA  GLU A 147    22325  22286  22997  -1863  -2406   -373       C  
ATOM   1152  C   GLU A 147      37.502  45.842  34.654  1.00172.69           C  
ANISOU 1152  C   GLU A 147    21342  22188  22084  -1563  -2186   -540       C  
ATOM   1153  O   GLU A 147      37.425  45.544  33.469  1.00178.84           O  
ANISOU 1153  O   GLU A 147    21956  23147  22848  -1298  -2306   -884       O  
ATOM   1154  CB  GLU A 147      36.594  44.733  36.707  1.00176.89           C  
ANISOU 1154  CB  GLU A 147    22225  22146  22839  -2441  -2249   -113       C  
ATOM   1155  CG  GLU A 147      36.544  43.484  37.558  1.00179.36           C  
ANISOU 1155  CG  GLU A 147    22954  21847  23347  -2901  -2483    119       C  
ATOM   1156  CD  GLU A 147      37.175  42.301  36.863  1.00187.34           C  
ANISOU 1156  CD  GLU A 147    24224  22273  24682  -2656  -2959   -154       C  
ATOM   1157  OE1 GLU A 147      38.246  41.854  37.316  1.00195.62           O  
ANISOU 1157  OE1 GLU A 147    25646  22885  25792  -2394  -3255    -55       O  
ATOM   1158  OE2 GLU A 147      36.627  41.847  35.836  1.00190.17           O  
ANISOU 1158  OE2 GLU A 147    24377  22660  25219  -2628  -3089   -564       O  
ATOM   1159  N   TRP A 148      37.381  47.088  35.112  1.00163.49           N  
ANISOU 1159  N   TRP A 148    20145  21274  20699  -1570  -1916   -299       N  
ATOM   1160  CA  TRP A 148      37.085  48.243  34.264  1.00158.28           C  
ANISOU 1160  CA  TRP A 148    19370  21005  19764  -1288  -1767   -340       C  
ATOM   1161  C   TRP A 148      37.987  48.340  33.039  1.00159.40           C  
ANISOU 1161  C   TRP A 148    19486  21331  19744   -968  -1774   -461       C  
ATOM   1162  O   TRP A 148      37.513  48.620  31.942  1.00165.10           O  
ANISOU 1162  O   TRP A 148    20124  22369  20236   -717  -1784   -608       O  
ATOM   1163  CB  TRP A 148      37.196  49.530  35.085  1.00153.41           C  
ANISOU 1163  CB  TRP A 148    18856  20418  19015  -1316  -1582    -61       C  
ATOM   1164  CG  TRP A 148      36.986  50.774  34.297  1.00152.21           C  
ANISOU 1164  CG  TRP A 148    18780  20461  18591  -1025  -1517    -20       C  
ATOM   1165  CD1 TRP A 148      35.868  51.543  34.282  1.00154.67           C  
ANISOU 1165  CD1 TRP A 148    19070  20947  18748   -840  -1574   -105       C  
ATOM   1166  CD2 TRP A 148      37.931  51.416  33.411  1.00152.09           C  
ANISOU 1166  CD2 TRP A 148    18929  20484  18374   -888  -1421    124       C  
ATOM   1167  NE1 TRP A 148      36.044  52.622  33.441  1.00159.50           N  
ANISOU 1167  NE1 TRP A 148    19951  21555  19095   -535  -1589     32       N  
ATOM   1168  CE2 TRP A 148      37.301  52.566  32.895  1.00154.91           C  
ANISOU 1168  CE2 TRP A 148    19500  20896  18462   -646  -1448    231       C  
ATOM   1169  CE3 TRP A 148      39.244  51.131  33.014  1.00150.93           C  
ANISOU 1169  CE3 TRP A 148    18754  20390  18202   -962  -1323    141       C  
ATOM   1170  CZ2 TRP A 148      37.939  53.437  31.988  1.00153.39           C  
ANISOU 1170  CZ2 TRP A 148    19613  20705  17960   -582  -1352    497       C  
ATOM   1171  CZ3 TRP A 148      39.875  51.990  32.110  1.00150.75           C  
ANISOU 1171  CZ3 TRP A 148    18875  20549  17853   -949  -1156    320       C  
ATOM   1172  CH2 TRP A 148      39.220  53.131  31.613  1.00151.86           C  
ANISOU 1172  CH2 TRP A 148    19345  20638  17716   -814  -1156    567       C  
ATOM   1173  N   LEU A 149      39.290  48.147  33.238  1.00156.95           N  
ANISOU 1173  N   LEU A 149    19213  20937  19484   -960  -1768   -437       N  
ATOM   1174  CA  LEU A 149      40.257  48.341  32.164  1.00158.46           C  
ANISOU 1174  CA  LEU A 149    19277  21504  19424   -746  -1694   -583       C  
ATOM   1175  C   LEU A 149      40.241  47.208  31.145  1.00159.69           C  
ANISOU 1175  C   LEU A 149    19224  21846  19604   -465  -1955  -1056       C  
ATOM   1176  O   LEU A 149      40.489  47.431  29.960  1.00161.33           O  
ANISOU 1176  O   LEU A 149    19265  22566  19464   -243  -1881  -1218       O  
ATOM   1177  CB  LEU A 149      41.662  48.551  32.723  1.00160.17           C  
ANISOU 1177  CB  LEU A 149    19457  21744  19654   -832  -1596   -554       C  
ATOM   1178  CG  LEU A 149      42.783  48.779  31.703  1.00164.50           C  
ANISOU 1178  CG  LEU A 149    19754  22871  19876   -743  -1442   -760       C  
ATOM   1179  CD1 LEU A 149      42.419  49.788  30.616  1.00161.76           C  
ANISOU 1179  CD1 LEU A 149    19493  22880  19086   -796  -1174   -504       C  
ATOM   1180  CD2 LEU A 149      44.057  49.183  32.409  1.00168.00           C  
ANISOU 1180  CD2 LEU A 149    20084  23411  20337   -923  -1298   -777       C  
ATOM   1181  N   HIS A 150      39.909  46.003  31.606  1.00159.48           N  
ANISOU 1181  N   HIS A 150    19241  21393  19959   -494  -2282  -1273       N  
ATOM   1182  CA  HIS A 150      39.804  44.822  30.726  1.00164.05           C  
ANISOU 1182  CA  HIS A 150    19659  21993  20678   -217  -2646  -1816       C  
ATOM   1183  C   HIS A 150      38.974  45.052  29.422  1.00166.29           C  
ANISOU 1183  C   HIS A 150    19706  22788  20687      6  -2605  -2058       C  
ATOM   1184  O   HIS A 150      39.271  44.455  28.381  1.00168.20           O  
ANISOU 1184  O   HIS A 150    19697  23377  20831    374  -2815  -2561       O  
ATOM   1185  CB  HIS A 150      39.253  43.623  31.507  1.00161.74           C  
ANISOU 1185  CB  HIS A 150    19608  20970  20875   -454  -3006  -1880       C  
ATOM   1186  CG  HIS A 150      39.693  42.296  30.970  1.00162.25           C  
ANISOU 1186  CG  HIS A 150    19658  20776  21213   -128  -3531  -2456       C  
ATOM   1187  ND1 HIS A 150      39.464  41.906  29.667  1.00163.30           N  
ANISOU 1187  ND1 HIS A 150    19463  21302  21280    228  -3713  -3029       N  
ATOM   1188  CD2 HIS A 150      40.336  41.262  31.564  1.00163.58           C  
ANISOU 1188  CD2 HIS A 150    20133  20304  21714    -29  -3995  -2602       C  
ATOM   1189  CE1 HIS A 150      39.951  40.693  29.481  1.00166.65           C  
ANISOU 1189  CE1 HIS A 150    19950  21339  22028    530  -4271  -3558       C  
ATOM   1190  NE2 HIS A 150      40.483  40.279  30.617  1.00166.69           N  
ANISOU 1190  NE2 HIS A 150    20384  20662  22288    394  -4479  -3296       N  
ATOM   1191  N   HIS A 151      37.964  45.926  29.490  1.00165.38           N  
ANISOU 1191  N   HIS A 151    19650  22779  20406   -127  -2387  -1770       N  
ATOM   1192  CA  HIS A 151      37.095  46.211  28.339  1.00168.03           C  
ANISOU 1192  CA  HIS A 151    19808  23605  20429    174  -2409  -2004       C  
ATOM   1193  C   HIS A 151      37.718  47.181  27.331  1.00166.18           C  
ANISOU 1193  C   HIS A 151    19599  23960  19580    468  -2189  -1829       C  
ATOM   1194  O   HIS A 151      38.061  48.314  27.668  1.00158.81           O  
ANISOU 1194  O   HIS A 151    18931  22995  18415    314  -1913  -1319       O  
ATOM   1195  CB  HIS A 151      35.720  46.709  28.801  1.00175.22           C  
ANISOU 1195  CB  HIS A 151    20742  24460  21372     22  -2360  -1898       C  
ATOM   1196  CG  HIS A 151      35.096  45.857  29.867  1.00185.09           C  
ANISOU 1196  CG  HIS A 151    21965  25244  23113   -457  -2464  -1970       C  
ATOM   1197  ND1 HIS A 151      35.285  44.491  29.937  1.00190.86           N  
ANISOU 1197  ND1 HIS A 151    22679  25576  24263   -633  -2743  -2268       N  
ATOM   1198  CD2 HIS A 151      34.282  46.176  30.901  1.00187.69           C  
ANISOU 1198  CD2 HIS A 151    22309  25470  23535   -833  -2336  -1777       C  
ATOM   1199  CE1 HIS A 151      34.621  44.008  30.973  1.00192.15           C  
ANISOU 1199  CE1 HIS A 151    22925  25343  24737  -1193  -2747  -2144       C  
ATOM   1200  NE2 HIS A 151      34.005  45.010  31.575  1.00191.30           N  
ANISOU 1200  NE2 HIS A 151    22774  25504  24405  -1334  -2466  -1869       N  
ATOM   1201  N   LEU A 152      37.770  46.732  26.074  1.00176.18           N  
ANISOU 1201  N   LEU A 152    20607  25770  20563    861  -2333  -2266       N  
ATOM   1202  CA  LEU A 152      38.652  47.287  25.013  1.00182.43           C  
ANISOU 1202  CA  LEU A 152    21345  27270  20697   1074  -2127  -2182       C  
ATOM   1203  C   LEU A 152      40.179  47.184  25.303  1.00183.30           C  
ANISOU 1203  C   LEU A 152    21341  27509  20793    873  -1956  -2160       C  
ATOM   1204  O   LEU A 152      40.971  48.036  24.869  1.00187.19           O  
ANISOU 1204  O   LEU A 152    21881  28488  20754    727  -1607  -1837       O  
ATOM   1205  CB  LEU A 152      38.208  48.701  24.542  1.00179.99           C  
ANISOU 1205  CB  LEU A 152    21414  27183  19792   1126  -1892  -1618       C  
ATOM   1206  CG  LEU A 152      37.060  48.756  23.488  1.00178.14           C  
ANISOU 1206  CG  LEU A 152    21138  27374  19174   1650  -2118  -1880       C  
ATOM   1207  CD1 LEU A 152      36.759  50.185  23.042  1.00174.56           C  
ANISOU 1207  CD1 LEU A 152    21223  27027  18073   1784  -1982  -1262       C  
ATOM   1208  CD2 LEU A 152      37.333  47.856  22.279  1.00178.60           C  
ANISOU 1208  CD2 LEU A 152    20743  28173  18942   2060  -2287  -2512       C  
ATOM   1209  N   GLY A 153      40.571  46.110  26.001  1.00179.56           N  
ANISOU 1209  N   GLY A 153    20722  26624  20876    864  -2237  -2544       N  
ATOM   1210  CA  GLY A 153      41.987  45.755  26.180  1.00179.31           C  
ANISOU 1210  CA  GLY A 153    20457  26828  20844    884  -2239  -2806       C  
ATOM   1211  C   GLY A 153      42.761  46.747  27.028  1.00179.39           C  
ANISOU 1211  C   GLY A 153    20647  26729  20783    443  -1852  -2267       C  
ATOM   1212  O   GLY A 153      42.205  47.747  27.488  1.00177.72           O  
ANISOU 1212  O   GLY A 153    20796  26185  20542    131  -1602  -1660       O  
ATOM   1213  N   SER A 154      44.048  46.466  27.244  1.00183.86           N  
ANISOU 1213  N   SER A 154    20920  27603  21333    466  -1855  -2593       N  
ATOM   1214  CA  SER A 154      44.927  47.369  28.011  1.00183.22           C  
ANISOU 1214  CA  SER A 154    20890  27536  21189     33  -1497  -2233       C  
ATOM   1215  C   SER A 154      46.395  47.145  27.686  1.00189.55           C  
ANISOU 1215  C   SER A 154    21129  29185  21706    111  -1427  -2797       C  
ATOM   1216  O   SER A 154      46.939  46.081  27.981  1.00193.42           O  
ANISOU 1216  O   SER A 154    21366  29650  22474    544  -1872  -3451       O  
ATOM   1217  CB  SER A 154      44.738  47.169  29.513  1.00178.06           C  
ANISOU 1217  CB  SER A 154    20551  25987  21114    -78  -1692  -2029       C  
ATOM   1218  OG  SER A 154      43.440  46.724  29.831  1.00179.81           O  
ANISOU 1218  OG  SER A 154    21096  25545  21675    -22  -1937  -1862       O  
ATOM   1219  N   ALA A 155      47.038  48.160  27.099  1.00192.24           N  
ANISOU 1219  N   ALA A 155    21291  30278  21473   -326   -894  -2562       N  
ATOM   1220  CA  ALA A 155      48.509  48.228  27.035  1.00195.33           C  
ANISOU 1220  CA  ALA A 155    21076  31567  21572   -490   -683  -3048       C  
ATOM   1221  C   ALA A 155      49.081  48.897  28.313  1.00196.95           C  
ANISOU 1221  C   ALA A 155    21405  31324  22102   -935   -514  -2788       C  
ATOM   1222  O   ALA A 155      49.826  49.886  28.234  1.00201.36           O  
ANISOU 1222  O   ALA A 155    21801  32374  22331  -1576     -7  -2583       O  
ATOM   1223  CB  ALA A 155      48.957  48.972  25.782  1.00195.03           C  
ANISOU 1223  CB  ALA A 155    20755  32652  20694   -910   -135  -2916       C  
ATOM   1224  N   LEU A 156      48.716  48.334  29.480  1.00192.03           N  
ANISOU 1224  N   LEU A 156    21079  29782  22098   -627   -946  -2804       N  
ATOM   1225  CA  LEU A 156      49.049  48.891  30.812  1.00178.90           C  
ANISOU 1225  CA  LEU A 156    19595  27606  20769   -919   -880  -2558       C  
ATOM   1226  C   LEU A 156      50.202  48.113  31.445  1.00177.23           C  
ANISOU 1226  C   LEU A 156    18924  27706  20707   -516  -1229  -3342       C  
ATOM   1227  O   LEU A 156      49.989  47.046  32.025  1.00174.37           O  
ANISOU 1227  O   LEU A 156    18757  26789  20705     60  -1812  -3606       O  
ATOM   1228  CB  LEU A 156      47.821  48.797  31.746  1.00171.11           C  
ANISOU 1228  CB  LEU A 156    19255  25506  20251   -835  -1128  -2032       C  
ATOM   1229  CG  LEU A 156      47.426  47.358  32.181  1.00170.06           C  
ANISOU 1229  CG  LEU A 156    19269  24845  20500   -251  -1752  -2363       C  
ATOM   1230  CD1 LEU A 156      46.903  47.281  33.617  1.00164.41           C  
ANISOU 1230  CD1 LEU A 156    19017  23271  20180   -305  -1943  -1982       C  
ATOM   1231  CD2 LEU A 156      46.467  46.692  31.194  1.00168.51           C  
ANISOU 1231  CD2 LEU A 156    19163  24584  20279     -2  -1941  -2428       C  
ATOM   1232  N   PRO A 157      51.424  48.639  31.353  1.00161.64           N  
ANISOU 1232  N   PRO A 157    20088  23614  17711   1188  -2365  -7446       N  
ATOM   1233  CA  PRO A 157      52.488  47.939  32.068  1.00161.88           C  
ANISOU 1233  CA  PRO A 157    20261  22901  18345   1196  -1924  -7267       C  
ATOM   1234  C   PRO A 157      52.194  47.949  33.578  1.00156.78           C  
ANISOU 1234  C   PRO A 157    19576  21411  18580    815  -1799  -6643       C  
ATOM   1235  O   PRO A 157      51.531  48.874  34.064  1.00156.04           O  
ANISOU 1235  O   PRO A 157    19388  21470  18429    629  -1947  -6097       O  
ATOM   1236  CB  PRO A 157      53.739  48.775  31.746  1.00159.54           C  
ANISOU 1236  CB  PRO A 157    20115  23172  17330   1576  -1606  -6618       C  
ATOM   1237  CG  PRO A 157      53.355  49.618  30.560  1.00161.17           C  
ANISOU 1237  CG  PRO A 157    20318  24420  16496   1820  -1854  -6676       C  
ATOM   1238  CD  PRO A 157      51.898  49.881  30.729  1.00159.01           C  
ANISOU 1238  CD  PRO A 157    19870  24160  16386   1541  -2314  -6807       C  
ATOM   1239  N   THR A 158      52.642  46.911  34.297  1.00153.95           N  
ANISOU 1239  N   THR A 158    19295  20187  19013    738  -1528  -6735       N  
ATOM   1240  CA  THR A 158      52.369  46.776  35.748  1.00143.97           C  
ANISOU 1240  CA  THR A 158    18019  18132  18551    422  -1373  -6147       C  
ATOM   1241  C   THR A 158      52.712  48.062  36.467  1.00133.72           C  
ANISOU 1241  C   THR A 158    16720  17156  16928    453  -1290  -5155       C  
ATOM   1242  O   THR A 158      51.937  48.559  37.294  1.00128.88           O  
ANISOU 1242  O   THR A 158    16002  16392  16572    160  -1375  -4739       O  
ATOM   1243  CB  THR A 158      53.197  45.642  36.382  1.00144.75           C  
ANISOU 1243  CB  THR A 158    18276  17379  19343    537  -1013  -6144       C  
ATOM   1244  OG1 THR A 158      53.631  44.734  35.365  1.00154.61           O  
ANISOU 1244  OG1 THR A 158    19591  18613  20539    788   -987  -7008       O  
ATOM   1245  CG2 THR A 158      52.380  44.890  37.425  1.00142.22           C  
ANISOU 1245  CG2 THR A 158    17930  16121  19983    135   -931  -6071       C  
ATOM   1246  N   LEU A 159      53.871  48.609  36.131  1.00131.54           N  
ANISOU 1246  N   LEU A 159    16532  17337  16110    797  -1104  -4830       N  
ATOM   1247  CA  LEU A 159      54.343  49.828  36.744  1.00128.50           C  
ANISOU 1247  CA  LEU A 159    16123  17235  15466    818   -989  -3979       C  
ATOM   1248  C   LEU A 159      53.344  50.970  36.576  1.00130.73           C  
ANISOU 1248  C   LEU A 159    16311  17964  15395    645  -1267  -3737       C  
ATOM   1249  O   LEU A 159      52.887  51.544  37.567  1.00127.02           O  
ANISOU 1249  O   LEU A 159    15761  17285  15212    420  -1292  -3246       O  
ATOM   1250  CB  LEU A 159      55.697  50.223  36.178  1.00127.96           C  
ANISOU 1250  CB  LEU A 159    16104  17648  14867   1175   -728  -3798       C  
ATOM   1251  CG  LEU A 159      56.317  51.451  36.834  1.00122.71           C  
ANISOU 1251  CG  LEU A 159    15369  17205  14048   1157   -559  -2986       C  
ATOM   1252  CD1 LEU A 159      57.273  51.056  37.952  1.00116.87           C  
ANISOU 1252  CD1 LEU A 159    14579  16036  13789   1231   -310  -2672       C  
ATOM   1253  CD2 LEU A 159      57.023  52.279  35.783  1.00125.79           C  
ANISOU 1253  CD2 LEU A 159    15773  18322  13698   1382   -405  -2853       C  
ATOM   1254  N   ASP A 160      53.004  51.283  35.317  1.00140.01           N  
ANISOU 1254  N   ASP A 160    17492  19784  15919    803  -1478  -4093       N  
ATOM   1255  CA  ASP A 160      51.994  52.319  34.981  1.00139.83           C  
ANISOU 1255  CA  ASP A 160    17384  20244  15500    747  -1791  -3909       C  
ATOM   1256  C   ASP A 160      50.726  52.118  35.783  1.00132.68           C  
ANISOU 1256  C   ASP A 160    16293  18915  15202    377  -2029  -4017       C  
ATOM   1257  O   ASP A 160      50.083  53.086  36.215  1.00125.49           O  
ANISOU 1257  O   ASP A 160    15284  18129  14265    274  -2159  -3571       O  
ATOM   1258  CB  ASP A 160      51.644  52.273  33.481  1.00156.27           C  
ANISOU 1258  CB  ASP A 160    19482  23061  16832   1015  -2056  -4481       C  
ATOM   1259  CG  ASP A 160      52.696  52.963  32.594  1.00167.20           C  
ANISOU 1259  CG  ASP A 160    21039  25098  17391   1404  -1809  -4137       C  
ATOM   1260  OD1 ASP A 160      53.897  52.632  32.703  1.00173.49           O  
ANISOU 1260  OD1 ASP A 160    21918  25742  18256   1513  -1429  -4046       O  
ATOM   1261  OD2 ASP A 160      52.305  53.805  31.755  1.00173.32           O  
ANISOU 1261  OD2 ASP A 160    21852  26561  17441   1625  -1983  -3962       O  
ATOM   1262  N   GLY A 161      50.371  50.847  35.970  1.00135.15           N  
ANISOU 1262  N   GLY A 161    16548  18700  16102    177  -2049  -4624       N  
ATOM   1263  CA  GLY A 161      49.113  50.461  36.596  1.00139.37           C  
ANISOU 1263  CA  GLY A 161    16861  18825  17266   -222  -2228  -4857       C  
ATOM   1264  C   GLY A 161      49.044  50.795  38.067  1.00134.70           C  
ANISOU 1264  C   GLY A 161    16243  17746  17190   -454  -2012  -4150       C  
ATOM   1265  O   GLY A 161      48.032  51.320  38.542  1.00132.01           O  
ANISOU 1265  O   GLY A 161    15699  17451  17008   -678  -2174  -3997       O  
ATOM   1266  N   VAL A 162      50.123  50.479  38.794  1.00135.45           N  
ANISOU 1266  N   VAL A 162    16517  17431  17515   -361  -1654  -3748       N  
ATOM   1267  CA  VAL A 162      50.243  50.831  40.221  1.00129.31           C  
ANISOU 1267  CA  VAL A 162    15730  16310  17092   -493  -1442  -3052       C  
ATOM   1268  C   VAL A 162      50.197  52.347  40.397  1.00126.01           C  
ANISOU 1268  C   VAL A 162    15245  16400  16232   -432  -1534  -2514       C  
ATOM   1269  O   VAL A 162      49.398  52.866  41.189  1.00124.69           O  
ANISOU 1269  O   VAL A 162    14927  16172  16275   -642  -1594  -2250       O  
ATOM   1270  CB  VAL A 162      51.538  50.243  40.869  1.00124.30           C  
ANISOU 1270  CB  VAL A 162    15279  15285  16665   -289  -1092  -2744       C  
ATOM   1271  CG1 VAL A 162      51.795  50.851  42.236  1.00113.50           C  
ANISOU 1271  CG1 VAL A 162    13879  13821  15424   -326   -933  -2023       C  
ATOM   1272  CG2 VAL A 162      51.427  48.737  40.994  1.00134.36           C  
ANISOU 1272  CG2 VAL A 162    16636  15846  18569   -373   -949  -3149       C  
ATOM   1273  N   THR A 163      51.016  53.060  39.626  1.00124.38           N  
ANISOU 1273  N   THR A 163    15139  16679  15439   -148  -1518  -2373       N  
ATOM   1274  CA  THR A 163      51.109  54.507  39.779  1.00121.61           C  
ANISOU 1274  CA  THR A 163    14756  16691  14756    -88  -1532  -1831       C  
ATOM   1275  C   THR A 163      49.780  55.249  39.509  1.00119.56           C  
ANISOU 1275  C   THR A 163    14349  16706  14370   -177  -1859  -1874       C  
ATOM   1276  O   THR A 163      49.591  56.358  39.991  1.00111.47           O  
ANISOU 1276  O   THR A 163    13267  15777  13309   -191  -1866  -1425       O  
ATOM   1277  CB  THR A 163      52.326  55.132  39.012  1.00125.05           C  
ANISOU 1277  CB  THR A 163    15325  17536  14651    200  -1351  -1603       C  
ATOM   1278  OG1 THR A 163      52.025  56.478  38.620  1.00130.92           O  
ANISOU 1278  OG1 THR A 163    16061  18670  15010    267  -1442  -1243       O  
ATOM   1279  CG2 THR A 163      52.683  54.330  37.791  1.00132.13           C  
ANISOU 1279  CG2 THR A 163    16331  18667  15205    414  -1362  -2122       C  
ATOM   1280  N   VAL A 164      48.852  54.609  38.787  1.00124.33           N  
ANISOU 1280  N   VAL A 164    14854  17423  14961   -229  -2139  -2466       N  
ATOM   1281  CA  VAL A 164      47.503  55.181  38.605  1.00124.63           C  
ANISOU 1281  CA  VAL A 164    14666  17740  14946   -297  -2490  -2582       C  
ATOM   1282  C   VAL A 164      46.614  54.923  39.822  1.00120.07           C  
ANISOU 1282  C   VAL A 164    13857  16722  15042   -663  -2466  -2559       C  
ATOM   1283  O   VAL A 164      45.938  55.834  40.300  1.00116.44           O  
ANISOU 1283  O   VAL A 164    13239  16384  14618   -696  -2566  -2269       O  
ATOM   1284  CB  VAL A 164      46.814  54.702  37.294  1.00132.26           C  
ANISOU 1284  CB  VAL A 164    15534  19157  15562   -180  -2862  -3292       C  
ATOM   1285  CG1 VAL A 164      45.295  54.856  37.382  1.00128.12           C  
ANISOU 1285  CG1 VAL A 164    14649  18781  15249   -349  -3229  -3590       C  
ATOM   1286  CG2 VAL A 164      47.348  55.484  36.102  1.00134.39           C  
ANISOU 1286  CG2 VAL A 164    15995  20093  14971    258  -2941  -3112       C  
ATOM   1287  N   VAL A 165      46.634  53.688  40.326  1.00120.71           N  
ANISOU 1287  N   VAL A 165    13926  16273  15665   -914  -2290  -2839       N  
ATOM   1288  CA  VAL A 165      45.938  53.350  41.579  1.00122.10           C  
ANISOU 1288  CA  VAL A 165    13923  15987  16481  -1265  -2139  -2706       C  
ATOM   1289  C   VAL A 165      46.358  54.323  42.690  1.00118.83           C  
ANISOU 1289  C   VAL A 165    13558  15563  16027  -1206  -1941  -1992       C  
ATOM   1290  O   VAL A 165      45.514  55.019  43.285  1.00118.19           O  
ANISOU 1290  O   VAL A 165    13261  15588  16056  -1320  -2014  -1823       O  
ATOM   1291  CB  VAL A 165      46.219  51.877  42.024  1.00122.00           C  
ANISOU 1291  CB  VAL A 165    14005  15295  17054  -1473  -1851  -2917       C  
ATOM   1292  CG1 VAL A 165      45.507  51.551  43.340  1.00116.28           C  
ANISOU 1292  CG1 VAL A 165    13122  14115  16941  -1821  -1616  -2662       C  
ATOM   1293  CG2 VAL A 165      45.808  50.897  40.930  1.00126.14           C  
ANISOU 1293  CG2 VAL A 165    14454  15771  17700  -1562  -2041  -3749       C  
ATOM   1294  N   VAL A 166      47.666  54.392  42.935  1.00114.31           N  
ANISOU 1294  N   VAL A 166    13230  14908  15291  -1012  -1708  -1642       N  
ATOM   1295  CA  VAL A 166      48.200  55.164  44.036  1.00108.79           C  
ANISOU 1295  CA  VAL A 166    12549  14192  14592   -969  -1519  -1081       C  
ATOM   1296  C   VAL A 166      47.885  56.651  43.868  1.00111.39           C  
ANISOU 1296  C   VAL A 166    12786  14920  14616   -871  -1687   -860       C  
ATOM   1297  O   VAL A 166      47.348  57.282  44.784  1.00110.24           O  
ANISOU 1297  O   VAL A 166    12485  14762  14637   -971  -1668   -643       O  
ATOM   1298  CB  VAL A 166      49.705  54.933  44.190  1.00110.75           C  
ANISOU 1298  CB  VAL A 166    13004  14360  14715   -757  -1283   -854       C  
ATOM   1299  CG1 VAL A 166      50.283  55.850  45.254  1.00112.91           C  
ANISOU 1299  CG1 VAL A 166    13231  14727  14942   -706  -1148   -378       C  
ATOM   1300  CG2 VAL A 166      49.971  53.479  44.547  1.00115.42           C  
ANISOU 1300  CG2 VAL A 166    13699  14466  15687   -798  -1092   -987       C  
ATOM   1301  N   SER A 167      48.142  57.181  42.671  1.00115.14           N  
ANISOU 1301  N   SER A 167    13357  15739  14649   -654  -1836   -923       N  
ATOM   1302  CA  SER A 167      47.854  58.596  42.352  1.00115.49           C  
ANISOU 1302  CA  SER A 167    13367  16099  14414   -502  -1972   -656       C  
ATOM   1303  C   SER A 167      46.391  59.050  42.611  1.00121.72           C  
ANISOU 1303  C   SER A 167    13893  16977  15378   -587  -2223   -755       C  
ATOM   1304  O   SER A 167      46.152  60.217  42.981  1.00118.29           O  
ANISOU 1304  O   SER A 167    13395  16607  14940   -506  -2242   -452       O  
ATOM   1305  CB  SER A 167      48.237  58.900  40.910  1.00119.30           C  
ANISOU 1305  CB  SER A 167    14018  16960  14349   -224  -2074   -691       C  
ATOM   1306  OG  SER A 167      49.392  59.716  40.842  1.00129.37           O  
ANISOU 1306  OG  SER A 167    15454  18280  15418    -90  -1822   -262       O  
ATOM   1307  N   ILE A 168      45.420  58.151  42.381  1.00117.33           N  
ANISOU 1307  N   ILE A 168    13153  16417  15010   -745  -2408  -1222       N  
ATOM   1308  CA  ILE A 168      44.018  58.462  42.690  1.00108.23           C  
ANISOU 1308  CA  ILE A 168    11659  15373  14087   -854  -2623  -1378       C  
ATOM   1309  C   ILE A 168      43.825  58.538  44.189  1.00106.15           C  
ANISOU 1309  C   ILE A 168    11265  14808  14259  -1086  -2365  -1140       C  
ATOM   1310  O   ILE A 168      43.369  59.557  44.711  1.00107.10           O  
ANISOU 1310  O   ILE A 168    11243  15034  14414  -1016  -2399   -928       O  
ATOM   1311  CB  ILE A 168      43.032  57.440  42.097  1.00110.26           C  
ANISOU 1311  CB  ILE A 168    11668  15711  14514  -1031  -2864  -2018       C  
ATOM   1312  CG1 ILE A 168      43.082  57.463  40.569  1.00109.35           C  
ANISOU 1312  CG1 ILE A 168    11637  16062  13849   -732  -3193  -2328       C  
ATOM   1313  CG2 ILE A 168      41.612  57.748  42.557  1.00112.68           C  
ANISOU 1313  CG2 ILE A 168    11537  16142  15132  -1176  -3038  -2184       C  
ATOM   1314  CD1 ILE A 168      42.657  56.155  39.932  1.00110.02           C  
ANISOU 1314  CD1 ILE A 168    11574  16135  14091   -926  -3349  -3073       C  
ATOM   1315  N   VAL A 169      44.209  57.473  44.886  1.00102.42           N  
ANISOU 1315  N   VAL A 169    10857  13965  14093  -1317  -2091  -1158       N  
ATOM   1316  CA  VAL A 169      44.131  57.442  46.350  1.00102.65           C  
ANISOU 1316  CA  VAL A 169    10800  13767  14433  -1490  -1804   -877       C  
ATOM   1317  C   VAL A 169      44.778  58.663  47.014  1.00100.08           C  
ANISOU 1317  C   VAL A 169    10551  13566  13909  -1302  -1716   -468       C  
ATOM   1318  O   VAL A 169      44.245  59.201  47.978  1.00104.09           O  
ANISOU 1318  O   VAL A 169    10870  14119  14558  -1361  -1640   -349       O  
ATOM   1319  CB  VAL A 169      44.760  56.169  46.920  1.00100.07           C  
ANISOU 1319  CB  VAL A 169    10642  13024  14354  -1635  -1493   -809       C  
ATOM   1320  CG1 VAL A 169      44.431  56.034  48.401  1.00 99.49           C  
ANISOU 1320  CG1 VAL A 169    10453  12796  14550  -1799  -1199   -515       C  
ATOM   1321  CG2 VAL A 169      44.266  54.961  46.147  1.00106.14           C  
ANISOU 1321  CG2 VAL A 169    11368  13571  15390  -1830  -1559  -1286       C  
ATOM   1322  N   ALA A 170      45.928  59.086  46.507  1.00 98.27           N  
ANISOU 1322  N   ALA A 170    10564  13393  13377  -1093  -1703   -300       N  
ATOM   1323  CA  ALA A 170      46.546  60.320  46.982  1.00 95.98           C  
ANISOU 1323  CA  ALA A 170    10306  13192  12969   -955  -1630     -1       C  
ATOM   1324  C   ALA A 170      45.625  61.502  46.723  1.00 94.57           C  
ANISOU 1324  C   ALA A 170     9971  13182  12776   -852  -1834     -2       C  
ATOM   1325  O   ALA A 170      45.335  62.282  47.631  1.00 91.19           O  
ANISOU 1325  O   ALA A 170     9397  12752  12499   -860  -1774     88       O  
ATOM   1326  CB  ALA A 170      47.912  60.542  46.324  1.00101.29           C  
ANISOU 1326  CB  ALA A 170    11217  13894  13374   -794  -1547    146       C  
ATOM   1327  N   GLN A 171      45.113  61.603  45.498  1.00 97.51           N  
ANISOU 1327  N   GLN A 171    10359  13732  12957   -714  -2089   -135       N  
ATOM   1328  CA  GLN A 171      44.243  62.729  45.149  1.00100.51           C  
ANISOU 1328  CA  GLN A 171    10606  14287  13294   -513  -2312    -86       C  
ATOM   1329  C   GLN A 171      42.901  62.770  45.930  1.00100.92           C  
ANISOU 1329  C   GLN A 171    10284  14390  13671   -628  -2401   -288       C  
ATOM   1330  O   GLN A 171      42.398  63.849  46.218  1.00103.97           O  
ANISOU 1330  O   GLN A 171    10541  14819  14144   -467  -2464   -188       O  
ATOM   1331  CB  GLN A 171      44.007  62.816  43.646  1.00 97.58           C  
ANISOU 1331  CB  GLN A 171    10334  14200  12542   -255  -2592   -149       C  
ATOM   1332  CG  GLN A 171      43.460  64.169  43.219  1.00100.15           C  
ANISOU 1332  CG  GLN A 171    10633  14667  12752     81  -2772     89       C  
ATOM   1333  CD  GLN A 171      44.537  65.116  42.746  1.00100.64           C  
ANISOU 1333  CD  GLN A 171    11026  14620  12592    284  -2583    551       C  
ATOM   1334  OE1 GLN A 171      45.240  64.838  41.781  1.00106.83           O  
ANISOU 1334  OE1 GLN A 171    12049  15549  12991    391  -2547    643       O  
ATOM   1335  NE2 GLN A 171      44.669  66.244  43.419  1.00100.71           N  
ANISOU 1335  NE2 GLN A 171    11028  14366  12868    324  -2430    815       N  
ATOM   1336  N   VAL A 172      42.354  61.600  46.286  1.00 95.20           N  
ANISOU 1336  N   VAL A 172     9380  13625  13167   -908  -2360   -568       N  
ATOM   1337  CA  VAL A 172      41.179  61.526  47.182  1.00 94.49           C  
ANISOU 1337  CA  VAL A 172     8902  13576  13424  -1086  -2324   -734       C  
ATOM   1338  C   VAL A 172      41.515  62.084  48.567  1.00 90.78           C  
ANISOU 1338  C   VAL A 172     8422  12997  13072  -1121  -2032   -488       C  
ATOM   1339  O   VAL A 172      40.698  62.749  49.207  1.00 88.14           O  
ANISOU 1339  O   VAL A 172     7808  12782  12898  -1084  -2031   -541       O  
ATOM   1340  CB  VAL A 172      40.677  60.073  47.368  1.00 97.99           C  
ANISOU 1340  CB  VAL A 172     9182  13892  14157  -1453  -2215  -1022       C  
ATOM   1341  CG1 VAL A 172      39.394  60.056  48.183  1.00 98.33           C  
ANISOU 1341  CG1 VAL A 172     8769  14029  14562  -1654  -2141  -1187       C  
ATOM   1342  CG2 VAL A 172      40.470  59.383  46.028  1.00 99.57           C  
ANISOU 1342  CG2 VAL A 172     9384  14194  14252  -1452  -2501  -1396       C  
ATOM   1343  N   LEU A 173      42.716  61.784  49.035  1.00 91.62           N  
ANISOU 1343  N   LEU A 173     8801  12928  13080  -1166  -1797   -270       N  
ATOM   1344  CA  LEU A 173      43.156  62.252  50.331  1.00 88.99           C  
ANISOU 1344  CA  LEU A 173     8452  12583  12776  -1168  -1558   -100       C  
ATOM   1345  C   LEU A 173      43.399  63.745  50.332  1.00 88.19           C  
ANISOU 1345  C   LEU A 173     8359  12521  12625   -940  -1641    -32       C  
ATOM   1346  O   LEU A 173      43.039  64.431  51.286  1.00 86.87           O  
ANISOU 1346  O   LEU A 173     8004  12429  12571   -910  -1556    -82       O  
ATOM   1347  CB  LEU A 173      44.382  61.481  50.797  1.00 86.88           C  
ANISOU 1347  CB  LEU A 173     8427  12185  12397  -1223  -1334     84       C  
ATOM   1348  CG  LEU A 173      43.953  60.130  51.363  1.00 95.06           C  
ANISOU 1348  CG  LEU A 173     9409  13105  13602  -1448  -1129     90       C  
ATOM   1349  CD1 LEU A 173      45.064  59.113  51.316  1.00 96.64           C  
ANISOU 1349  CD1 LEU A 173     9894  13098  13724  -1437   -985    249       C  
ATOM   1350  CD2 LEU A 173      43.419  60.283  52.777  1.00100.09           C  
ANISOU 1350  CD2 LEU A 173     9834  13888  14304  -1512   -899    179       C  
HETATM 1351  N   MSE A 174      43.935  64.257  49.228  1.00 87.29           N  
ANISOU 1351  N   MSE A 174     8454  12347  12362   -772  -1784     69       N  
HETATM 1352  CA  MSE A 174      44.150  65.685  49.083  1.00 90.28           C  
ANISOU 1352  CA  MSE A 174     8876  12648  12778   -565  -1821    186       C  
HETATM 1353  C   MSE A 174      42.851  66.422  49.169  1.00 97.54           C  
ANISOU 1353  C   MSE A 174     9534  13646  13877   -413  -1983     62       C  
HETATM 1354  O   MSE A 174      42.733  67.384  49.939  1.00102.28           O  
ANISOU 1354  O   MSE A 174    10017  14170  14673   -334  -1903     19       O  
HETATM 1355  CB  MSE A 174      44.800  66.009  47.753  1.00 90.30           C  
ANISOU 1355  CB  MSE A 174     9156  12586  12565   -402  -1902    395       C  
HETATM 1356  CG  MSE A 174      45.293  67.445  47.787  1.00 97.83           C  
ANISOU 1356  CG  MSE A 174    10194  13321  13655   -258  -1807    588       C  
HETATM 1357 SE   MSE A 174      44.917  68.259  46.053  1.00124.88          SE  
ANISOU 1357 SE   MSE A 174    13839  16745  16862    130  -2012    915      SE  
HETATM 1358  CE  MSE A 174      44.985  70.179  46.483  1.00127.83           C  
ANISOU 1358  CE  MSE A 174    14228  16665  17677    312  -1858   1126       C  
ATOM   1359  N   ILE A 175      41.867  66.007  48.357  1.00101.47           N  
ANISOU 1359  N   ILE A 175     9905  14322  14324   -342  -2231    -53       N  
ATOM   1360  CA  ILE A 175      40.579  66.741  48.273  1.00102.66           C  
ANISOU 1360  CA  ILE A 175     9756  14615  14635   -114  -2444   -181       C  
ATOM   1361  C   ILE A 175      39.884  66.742  49.633  1.00 99.40           C  
ANISOU 1361  C   ILE A 175     8995  14276  14496   -262  -2275   -400       C  
ATOM   1362  O   ILE A 175      39.367  67.783  50.087  1.00 99.65           O  
ANISOU 1362  O   ILE A 175     8848  14293  14718    -53  -2287   -463       O  
ATOM   1363  CB  ILE A 175      39.630  66.216  47.136  1.00103.92           C  
ANISOU 1363  CB  ILE A 175     9757  15070  14658     -1  -2796   -352       C  
ATOM   1364  CG1 ILE A 175      39.378  64.706  47.266  1.00112.80           C  
ANISOU 1364  CG1 ILE A 175    10733  16294  15831   -384  -2748   -636       C  
ATOM   1365  CG2 ILE A 175      40.193  66.555  45.761  1.00101.37           C  
ANISOU 1365  CG2 ILE A 175     9772  14773  13968    291  -2981    -99       C  
ATOM   1366  CD1 ILE A 175      38.295  64.154  46.342  1.00116.98           C  
ANISOU 1366  CD1 ILE A 175    10963  17150  16331   -349  -3101   -985       C  
ATOM   1367  N   LEU A 176      39.961  65.600  50.319  1.00 93.53           N  
ANISOU 1367  N   LEU A 176     8184  13586  13766   -598  -2070   -486       N  
ATOM   1368  CA  LEU A 176      39.390  65.463  51.656  1.00 91.28           C  
ANISOU 1368  CA  LEU A 176     7600  13428  13652   -753  -1827   -624       C  
ATOM   1369  C   LEU A 176      40.229  66.196  52.726  1.00 92.80           C  
ANISOU 1369  C   LEU A 176     7909  13550  13798   -694  -1604   -550       C  
ATOM   1370  O   LEU A 176      39.806  66.310  53.876  1.00 97.20           O  
ANISOU 1370  O   LEU A 176     8231  14286  14415   -737  -1405   -680       O  
ATOM   1371  CB  LEU A 176      39.202  63.977  52.017  1.00 84.30           C  
ANISOU 1371  CB  LEU A 176     6643  12578  12806  -1115  -1625   -650       C  
ATOM   1372  CG  LEU A 176      38.197  63.186  51.148  1.00 85.34           C  
ANISOU 1372  CG  LEU A 176     6528  12798  13100  -1261  -1817   -887       C  
ATOM   1373  CD1 LEU A 176      38.209  61.686  51.454  1.00 82.29           C  
ANISOU 1373  CD1 LEU A 176     6143  12270  12851  -1660  -1556   -890       C  
ATOM   1374  CD2 LEU A 176      36.797  63.760  51.264  1.00 82.50           C  
ANISOU 1374  CD2 LEU A 176     5661  12718  12965  -1163  -1946  -1159       C  
ATOM   1375  N   ARG A 177      41.411  66.690  52.323  1.00 89.01           N  
ANISOU 1375  N   ARG A 177     7759  12855  13206   -601  -1631   -383       N  
ATOM   1376  CA  ARG A 177      42.271  67.527  53.175  1.00 87.63           C  
ANISOU 1376  CA  ARG A 177     7648  12603  13042   -549  -1478   -413       C  
ATOM   1377  C   ARG A 177      43.095  66.757  54.231  1.00 88.21           C  
ANISOU 1377  C   ARG A 177     7771  12832  12910   -724  -1245   -385       C  
ATOM   1378  O   ARG A 177      43.373  67.286  55.328  1.00 87.88           O  
ANISOU 1378  O   ARG A 177     7615  12934  12841   -686  -1117   -551       O  
ATOM   1379  CB  ARG A 177      41.461  68.644  53.834  1.00 87.72           C  
ANISOU 1379  CB  ARG A 177     7384  12659  13286   -369  -1476   -666       C  
ATOM   1380  CG  ARG A 177      41.041  69.731  52.884  1.00 94.30           C  
ANISOU 1380  CG  ARG A 177     8248  13242  14340    -84  -1687   -625       C  
ATOM   1381  CD  ARG A 177      39.768  70.436  53.350  1.00103.34           C  
ANISOU 1381  CD  ARG A 177     9029  14500  15734    133  -1736   -893       C  
ATOM   1382  NE  ARG A 177      39.613  70.443  54.800  1.00105.22           N  
ANISOU 1382  NE  ARG A 177     9020  14983  15974     38  -1501  -1193       N  
ATOM   1383  CZ  ARG A 177      38.673  69.762  55.452  1.00111.52           C  
ANISOU 1383  CZ  ARG A 177     9490  16163  16717    -63  -1390  -1338       C  
ATOM   1384  NH1 ARG A 177      37.789  69.018  54.772  1.00115.79           N  
ANISOU 1384  NH1 ARG A 177     9871  16839  17284   -129  -1515  -1274       N  
ATOM   1385  NH2 ARG A 177      38.612  69.819  56.786  1.00111.25           N  
ANISOU 1385  NH2 ARG A 177     9263  16409  16596   -108  -1137  -1572       N  
ATOM   1386  N   TYR A 178      43.517  65.540  53.900  1.00 82.37           N  
ANISOU 1386  N   TYR A 178     7201  12079  12015   -869  -1202   -197       N  
ATOM   1387  CA  TYR A 178      44.322  64.759  54.841  1.00 89.73           C  
ANISOU 1387  CA  TYR A 178     8208  13149  12733   -948   -994    -89       C  
ATOM   1388  C   TYR A 178      45.846  64.908  54.659  1.00 90.70           C  
ANISOU 1388  C   TYR A 178     8548  13193  12718   -895  -1004     -5       C  
ATOM   1389  O   TYR A 178      46.352  64.782  53.545  1.00 91.91           O  
ANISOU 1389  O   TYR A 178     8897  13142  12882   -897  -1099    103       O  
ATOM   1390  CB  TYR A 178      43.903  63.294  54.814  1.00 90.01           C  
ANISOU 1390  CB  TYR A 178     8281  13167  12750  -1116   -873     73       C  
ATOM   1391  CG  TYR A 178      42.595  63.083  55.488  1.00 94.71           C  
ANISOU 1391  CG  TYR A 178     8582  13933  13468  -1218   -731     -8       C  
ATOM   1392  CD1 TYR A 178      42.512  63.013  56.871  1.00100.16           C  
ANISOU 1392  CD1 TYR A 178     9146  14914  13992  -1199   -469     38       C  
ATOM   1393  CD2 TYR A 178      41.424  63.043  54.758  1.00 98.37           C  
ANISOU 1393  CD2 TYR A 178     8845  14345  14183  -1306   -861   -162       C  
ATOM   1394  CE1 TYR A 178      41.296  62.868  57.500  1.00105.76           C  
ANISOU 1394  CE1 TYR A 178     9553  15823  14806  -1298   -276    -28       C  
ATOM   1395  CE2 TYR A 178      40.205  62.890  55.370  1.00102.26           C  
ANISOU 1395  CE2 TYR A 178     8989  15028  14836  -1420   -706   -276       C  
ATOM   1396  CZ  TYR A 178      40.139  62.806  56.734  1.00107.78           C  
ANISOU 1396  CZ  TYR A 178     9579  15980  15391  -1431   -385   -193       C  
ATOM   1397  OH  TYR A 178      38.905  62.674  57.331  1.00122.63           O  
ANISOU 1397  OH  TYR A 178    11081  18085  17426  -1553   -173   -298       O  
ATOM   1398  N   ARG A 179      46.569  65.164  55.761  1.00 89.77           N  
ANISOU 1398  N   ARG A 179     8355  13305  12447   -837   -903    -91       N  
ATOM   1399  CA  ARG A 179      48.058  65.219  55.719  1.00 93.97           C  
ANISOU 1399  CA  ARG A 179     8995  13849  12860   -797   -910    -68       C  
ATOM   1400  C   ARG A 179      48.693  63.975  55.053  1.00 95.28           C  
ANISOU 1400  C   ARG A 179     9393  13904  12903   -812   -884    207       C  
ATOM   1401  O   ARG A 179      49.708  64.090  54.348  1.00 92.45           O  
ANISOU 1401  O   ARG A 179     9143  13435  12548   -798   -919    238       O  
ATOM   1402  CB  ARG A 179      48.659  65.431  57.112  1.00 95.79           C  
ANISOU 1402  CB  ARG A 179     9049  14479  12865   -700   -844   -248       C  
ATOM   1403  CG  ARG A 179      50.066  64.846  57.259  1.00 98.78           C  
ANISOU 1403  CG  ARG A 179     9496  15014  13021   -620   -840   -150       C  
ATOM   1404  CD  ARG A 179      50.731  65.177  58.596  1.00106.13           C  
ANISOU 1404  CD  ARG A 179    10197  16449  13678   -472   -849   -406       C  
ATOM   1405  NE  ARG A 179      50.021  64.634  59.763  1.00110.19           N  
ANISOU 1405  NE  ARG A 179    10652  17357  13858   -340   -735   -310       N  
ATOM   1406  CZ  ARG A 179      49.866  63.333  60.025  1.00115.13           C  
ANISOU 1406  CZ  ARG A 179    11446  18055  14243   -248   -594    123       C  
ATOM   1407  NH1 ARG A 179      50.354  62.408  59.189  1.00120.37           N  
ANISOU 1407  NH1 ARG A 179    12343  18400  14989   -262   -586    433       N  
ATOM   1408  NH2 ARG A 179      49.209  62.951  61.122  1.00109.52           N  
ANISOU 1408  NH2 ARG A 179    10675  17713  13224   -134   -424    253       N  
ATOM   1409  N   GLU A 180      48.064  62.806  55.249  1.00 88.30           N  
ANISOU 1409  N   GLU A 180     8570  13015  11962   -852   -788    388       N  
ATOM   1410  CA  GLU A 180      48.611  61.523  54.783  1.00 85.80           C  
ANISOU 1410  CA  GLU A 180     8473  12539  11587   -843   -729    612       C  
ATOM   1411  C   GLU A 180      48.726  61.396  53.277  1.00 87.80           C  
ANISOU 1411  C   GLU A 180     8889  12513  11957   -897   -850    584       C  
ATOM   1412  O   GLU A 180      49.329  60.449  52.784  1.00 90.84           O  
ANISOU 1412  O   GLU A 180     9450  12760  12302   -861   -811    684       O  
ATOM   1413  CB  GLU A 180      47.794  60.379  55.322  1.00 87.46           C  
ANISOU 1413  CB  GLU A 180     8705  12696  11829   -917   -548    800       C  
ATOM   1414  CG  GLU A 180      48.065  60.075  56.784  1.00109.30           C  
ANISOU 1414  CG  GLU A 180    11418  15780  14328   -769   -361    989       C  
ATOM   1415  CD  GLU A 180      47.593  61.176  57.742  1.00119.10           C  
ANISOU 1415  CD  GLU A 180    12398  17409  15446   -732   -364    778       C  
ATOM   1416  OE1 GLU A 180      46.858  62.103  57.304  1.00116.96           O  
ANISOU 1416  OE1 GLU A 180    11982  17070  15385   -839   -480    515       O  
ATOM   1417  OE2 GLU A 180      47.958  61.105  58.944  1.00126.31           O  
ANISOU 1417  OE2 GLU A 180    13248  18719  16025   -550   -255    865       O  
ATOM   1418  N   GLN A 181      48.139  62.341  52.542  1.00 87.24           N  
ANISOU 1418  N   GLN A 181     8763  12380  12003   -937   -994    451       N  
ATOM   1419  CA  GLN A 181      48.299  62.387  51.093  1.00 81.94           C  
ANISOU 1419  CA  GLN A 181     8251  11556  11326   -920  -1116    448       C  
ATOM   1420  C   GLN A 181      49.768  62.386  50.710  1.00 83.98           C  
ANISOU 1420  C   GLN A 181     8643  11812  11453   -839  -1048    526       C  
ATOM   1421  O   GLN A 181      50.175  61.659  49.809  1.00 97.55           O  
ANISOU 1421  O   GLN A 181    10529  13453  13081   -806  -1049    554       O  
ATOM   1422  CB  GLN A 181      47.610  63.606  50.501  1.00 72.38           C  
ANISOU 1422  CB  GLN A 181     6972  10320  10207   -876  -1264    385       C  
ATOM   1423  CG  GLN A 181      48.020  64.886  51.154  1.00 75.66           C  
ANISOU 1423  CG  GLN A 181     7277  10748  10720   -834  -1211    347       C  
ATOM   1424  CD  GLN A 181      47.725  66.090  50.306  1.00 80.59           C  
ANISOU 1424  CD  GLN A 181     7940  11216  11464   -736  -1304    391       C  
ATOM   1425  OE1 GLN A 181      48.015  66.107  49.111  1.00 83.12           O  
ANISOU 1425  OE1 GLN A 181     8450  11462  11670   -668  -1346    548       O  
ATOM   1426  NE2 GLN A 181      47.169  67.128  50.925  1.00 80.08           N  
ANISOU 1426  NE2 GLN A 181     7708  11102  11617   -689  -1317    269       N  
ATOM   1427  N   TRP A 182      50.573  63.176  51.405  1.00 77.36           N  
ANISOU 1427  N   TRP A 182     7688  11085  10617   -810   -982    501       N  
ATOM   1428  CA  TRP A 182      51.971  63.324  51.016  1.00 77.12           C  
ANISOU 1428  CA  TRP A 182     7692  11086  10522   -766   -903    530       C  
ATOM   1429  C   TRP A 182      52.825  62.048  51.099  1.00 75.37           C  
ANISOU 1429  C   TRP A 182     7551  10935  10150   -659   -831    600       C  
ATOM   1430  O   TRP A 182      53.808  61.928  50.395  1.00 83.93           O  
ANISOU 1430  O   TRP A 182     8687  12028  11171   -605   -766    618       O  
ATOM   1431  CB  TRP A 182      52.631  64.441  51.775  1.00 76.36           C  
ANISOU 1431  CB  TRP A 182     7378  11098  10537   -802   -857    388       C  
ATOM   1432  CG  TRP A 182      51.968  65.712  51.593  1.00 76.90           C  
ANISOU 1432  CG  TRP A 182     7398  10993  10827   -871   -889    323       C  
ATOM   1433  CD1 TRP A 182      51.115  66.323  52.469  1.00 81.31           C  
ANISOU 1433  CD1 TRP A 182     7802  11582  11510   -879   -944    156       C  
ATOM   1434  CD2 TRP A 182      52.074  66.566  50.473  1.00 75.18           C  
ANISOU 1434  CD2 TRP A 182     7295  10529  10740   -897   -844    447       C  
ATOM   1435  NE1 TRP A 182      50.710  67.527  51.972  1.00 79.03           N  
ANISOU 1435  NE1 TRP A 182     7519  11029  11479   -895   -952    142       N  
ATOM   1436  CE2 TRP A 182      51.284  67.708  50.743  1.00 79.27           C  
ANISOU 1436  CE2 TRP A 182     7731  10871  11515   -902   -884    364       C  
ATOM   1437  CE3 TRP A 182      52.782  66.503  49.273  1.00 76.23           C  
ANISOU 1437  CE3 TRP A 182     7594  10585  10783   -887   -740    644       C  
ATOM   1438  CZ2 TRP A 182      51.168  68.773  49.844  1.00 80.92           C  
ANISOU 1438  CZ2 TRP A 182     8055  10768  11922   -878   -827    536       C  
ATOM   1439  CZ3 TRP A 182      52.665  67.552  48.380  1.00 81.76           C  
ANISOU 1439  CZ3 TRP A 182     8407  11043  11614   -882   -664    832       C  
ATOM   1440  CH2 TRP A 182      51.850  68.677  48.669  1.00 80.84           C  
ANISOU 1440  CH2 TRP A 182     8239  10693  11783   -867   -710    808       C  
ATOM   1441  N   ALA A 183      52.463  61.101  51.945  1.00 71.54           N  
ANISOU 1441  N   ALA A 183     7076  10486   9620   -605   -807    666       N  
ATOM   1442  CA  ALA A 183      53.157  59.830  51.909  1.00 72.78           C  
ANISOU 1442  CA  ALA A 183     7360  10598   9694   -454   -729    779       C  
ATOM   1443  C   ALA A 183      52.925  59.164  50.568  1.00 79.90           C  
ANISOU 1443  C   ALA A 183     8472  11242  10645   -488   -743    738       C  
ATOM   1444  O   ALA A 183      53.886  58.771  49.901  1.00 87.21           O  
ANISOU 1444  O   ALA A 183     9475  12165  11496   -365   -692    716       O  
ATOM   1445  CB  ALA A 183      52.718  58.941  53.033  1.00 77.37           C  
ANISOU 1445  CB  ALA A 183     7960  11187  10249   -378   -649    949       C  
ATOM   1446  N   LEU A 184      51.649  59.095  50.140  1.00 82.00           N  
ANISOU 1446  N   LEU A 184     8784  11350  11019   -643   -823    668       N  
ATOM   1447  CA  LEU A 184      51.295  58.590  48.791  1.00 82.37           C  
ANISOU 1447  CA  LEU A 184     8982  11246  11066   -675   -901    517       C  
ATOM   1448  C   LEU A 184      52.012  59.355  47.651  1.00 86.37           C  
ANISOU 1448  C   LEU A 184     9547  11898  11371   -592   -932    488       C  
ATOM   1449  O   LEU A 184      52.639  58.733  46.780  1.00 86.34           O  
ANISOU 1449  O   LEU A 184     9676  11883  11245   -487   -888    405       O  
ATOM   1450  CB  LEU A 184      49.773  58.582  48.561  1.00 80.45           C  
ANISOU 1450  CB  LEU A 184     8675  10925  10964   -849  -1036    379       C  
ATOM   1451  CG  LEU A 184      48.838  57.418  49.049  1.00 87.90           C  
ANISOU 1451  CG  LEU A 184     9592  11623  12180  -1013   -965    318       C  
ATOM   1452  CD1 LEU A 184      49.498  56.042  49.200  1.00 84.06           C  
ANISOU 1452  CD1 LEU A 184     9282  10845  11810   -948   -784    374       C  
ATOM   1453  CD2 LEU A 184      48.132  57.786  50.333  1.00 85.60           C  
ANISOU 1453  CD2 LEU A 184     9115  11409  11997  -1112   -877    464       C  
ATOM   1454  N   TRP A 185      51.956  60.691  47.679  1.00 81.24           N  
ANISOU 1454  N   TRP A 185     8800  11361  10703   -627   -962    566       N  
ATOM   1455  CA  TRP A 185      52.608  61.487  46.650  1.00 83.20           C  
ANISOU 1455  CA  TRP A 185     9118  11699  10795   -567   -911    641       C  
ATOM   1456  C   TRP A 185      54.092  61.154  46.539  1.00 90.53           C  
ANISOU 1456  C   TRP A 185    10040  12716  11639   -482   -719    661       C  
ATOM   1457  O   TRP A 185      54.646  61.118  45.429  1.00 93.45           O  
ANISOU 1457  O   TRP A 185    10521  13174  11810   -400   -629    677       O  
ATOM   1458  CB  TRP A 185      52.449  62.975  46.917  1.00 87.82           C  
ANISOU 1458  CB  TRP A 185     9595  12269  11501   -629   -900    757       C  
ATOM   1459  CG  TRP A 185      51.053  63.474  46.878  1.00 97.60           C  
ANISOU 1459  CG  TRP A 185    10813  13452  12817   -639  -1087    743       C  
ATOM   1460  CD1 TRP A 185      50.410  64.171  47.857  1.00100.99           C  
ANISOU 1460  CD1 TRP A 185    11071  13829  13469   -700  -1130    702       C  
ATOM   1461  CD2 TRP A 185      50.123  63.350  45.798  1.00101.36           C  
ANISOU 1461  CD2 TRP A 185    11399  13982  13130   -545  -1272    724       C  
ATOM   1462  NE1 TRP A 185      49.141  64.488  47.456  1.00 98.45           N  
ANISOU 1462  NE1 TRP A 185    10735  13498  13173   -645  -1315    682       N  
ATOM   1463  CE2 TRP A 185      48.938  63.993  46.195  1.00100.38           C  
ANISOU 1463  CE2 TRP A 185    11139  13826  13174   -546  -1427    695       C  
ATOM   1464  CE3 TRP A 185      50.173  62.751  44.540  1.00106.48           C  
ANISOU 1464  CE3 TRP A 185    12217  14763  13477   -430  -1339    678       C  
ATOM   1465  CZ2 TRP A 185      47.812  64.048  45.383  1.00105.25           C  
ANISOU 1465  CZ2 TRP A 185    11754  14553  13681   -426  -1672    637       C  
ATOM   1466  CZ3 TRP A 185      49.060  62.819  43.733  1.00113.23           C  
ANISOU 1466  CZ3 TRP A 185    13087  15754  14180   -318  -1594    597       C  
ATOM   1467  CH2 TRP A 185      47.894  63.467  44.158  1.00107.94           C  
ANISOU 1467  CH2 TRP A 185    12252  15062  13698   -311  -1771    587       C  
ATOM   1468  N   ILE A 186      54.744  60.945  47.694  1.00 90.41           N  
ANISOU 1468  N   ILE A 186     9866  12748  11737   -469   -654    655       N  
ATOM   1469  CA  ILE A 186      56.175  60.613  47.731  1.00 89.68           C  
ANISOU 1469  CA  ILE A 186     9679  12801  11591   -347   -503    638       C  
ATOM   1470  C   ILE A 186      56.436  59.316  46.957  1.00 94.51           C  
ANISOU 1470  C   ILE A 186    10475  13352  12080   -176   -466    564       C  
ATOM   1471  O   ILE A 186      57.400  59.226  46.195  1.00100.00           O  
ANISOU 1471  O   ILE A 186    11163  14178  12653    -73   -323    524       O  
ATOM   1472  CB  ILE A 186      56.731  60.551  49.187  1.00 86.90           C  
ANISOU 1472  CB  ILE A 186     9094  12603  11320   -285   -512    619       C  
ATOM   1473  CG1 ILE A 186      57.209  61.952  49.628  1.00 85.36           C  
ANISOU 1473  CG1 ILE A 186     8628  12551  11250   -438   -473    544       C  
ATOM   1474  CG2 ILE A 186      57.873  59.541  49.301  1.00 83.10           C  
ANISOU 1474  CG2 ILE A 186     8564  12248  10762    -32   -436    602       C  
ATOM   1475  CD1 ILE A 186      57.206  62.189  51.128  1.00 74.05           C  
ANISOU 1475  CD1 ILE A 186     6961  11317   9855   -416   -571    438       C  
ATOM   1476  N   VAL A 187      55.521  58.355  47.083  1.00 88.56           N  
ANISOU 1476  N   VAL A 187     9872  12381  11393   -168   -568    510       N  
ATOM   1477  CA  VAL A 187      55.562  57.143  46.259  1.00 88.89           C  
ANISOU 1477  CA  VAL A 187    10101  12272  11399    -43   -546    341       C  
ATOM   1478  C   VAL A 187      55.245  57.362  44.753  1.00 95.71           C  
ANISOU 1478  C   VAL A 187    11098  13236  12029    -58   -594    177       C  
ATOM   1479  O   VAL A 187      55.983  56.866  43.891  1.00 95.87           O  
ANISOU 1479  O   VAL A 187    11194  13348  11880    105   -491     31       O  
ATOM   1480  CB  VAL A 187      54.668  56.059  46.828  1.00 91.18           C  
ANISOU 1480  CB  VAL A 187    10491  12227  11926    -87   -596    304       C  
ATOM   1481  CG1 VAL A 187      54.872  54.751  46.073  1.00 93.81           C  
ANISOU 1481  CG1 VAL A 187    11000  12313  12327     47   -542     64       C  
ATOM   1482  CG2 VAL A 187      54.974  55.877  48.301  1.00 97.20           C  
ANISOU 1482  CG2 VAL A 187    11153  12973  12802     -6   -526    551       C  
ATOM   1483  N   VAL A 188      54.163  58.094  44.434  1.00 92.92           N  
ANISOU 1483  N   VAL A 188    10759  12922  11624   -201   -754    193       N  
ATOM   1484  CA  VAL A 188      53.852  58.373  43.011  1.00 89.68           C  
ANISOU 1484  CA  VAL A 188    10474  12714  10887   -134   -832     86       C  
ATOM   1485  C   VAL A 188      54.932  59.209  42.297  1.00 89.01           C  
ANISOU 1485  C   VAL A 188    10402  12894  10522    -30   -618    285       C  
ATOM   1486  O   VAL A 188      55.178  59.022  41.100  1.00 92.35           O  
ANISOU 1486  O   VAL A 188    10954  13544  10589    119   -569    186       O  
ATOM   1487  CB  VAL A 188      52.398  58.927  42.752  1.00 88.03           C  
ANISOU 1487  CB  VAL A 188    10253  12543  10651   -225  -1094     59       C  
ATOM   1488  CG1 VAL A 188      51.475  58.592  43.897  1.00 91.31           C  
ANISOU 1488  CG1 VAL A 188    10539  12710  11444   -409  -1193     10       C  
ATOM   1489  CG2 VAL A 188      52.392  60.425  42.469  1.00 84.21           C  
ANISOU 1489  CG2 VAL A 188     9761  12219  10014   -194  -1072    383       C  
ATOM   1490  N   ASN A 189      55.579  60.114  43.025  1.00 83.48           N  
ANISOU 1490  N   ASN A 189     9548  12183   9986   -120   -465    533       N  
ATOM   1491  CA  ASN A 189      56.635  60.902  42.436  1.00 86.40           C  
ANISOU 1491  CA  ASN A 189     9878  12741  10209    -96   -192    724       C  
ATOM   1492  C   ASN A 189      57.883  60.045  42.144  1.00 91.90           C  
ANISOU 1492  C   ASN A 189    10521  13590  10807     54     17    569       C  
ATOM   1493  O   ASN A 189      58.586  60.265  41.155  1.00 92.22           O  
ANISOU 1493  O   ASN A 189    10594  13870  10576    140    253    631       O  
ATOM   1494  CB  ASN A 189      56.986  62.083  43.327  1.00 86.85           C  
ANISOU 1494  CB  ASN A 189     9727  12700  10572   -283    -84    922       C  
ATOM   1495  CG  ASN A 189      56.007  63.227  43.194  1.00 85.61           C  
ANISOU 1495  CG  ASN A 189     9646  12413  10467   -367   -178   1132       C  
ATOM   1496  OD1 ASN A 189      55.825  64.014  44.131  1.00 89.18           O  
ANISOU 1496  OD1 ASN A 189     9945  12697  11240   -515   -201   1170       O  
ATOM   1497  ND2 ASN A 189      55.392  63.348  42.030  1.00 82.40           N  
ANISOU 1497  ND2 ASN A 189     9464  12115   9729   -229   -241   1247       N  
ATOM   1498  N   ILE A 190      58.139  59.061  43.001  1.00 92.01           N  
ANISOU 1498  N   ILE A 190    10452  13474  11031    122    -46    395       N  
ATOM   1499  CA  ILE A 190      59.227  58.133  42.768  1.00 93.52           C  
ANISOU 1499  CA  ILE A 190    10590  13771  11171    343    114    221       C  
ATOM   1500  C   ILE A 190      58.853  57.198  41.631  1.00 98.23           C  
ANISOU 1500  C   ILE A 190    11430  14379  11514    508     70    -53       C  
ATOM   1501  O   ILE A 190      59.690  56.849  40.806  1.00103.78           O  
ANISOU 1501  O   ILE A 190    12133  15306  11992    695    268   -195       O  
ATOM   1502  CB  ILE A 190      59.596  57.359  44.049  1.00 89.80           C  
ANISOU 1502  CB  ILE A 190     9984  13143  10991    450     51    182       C  
ATOM   1503  CG1 ILE A 190      60.290  58.303  45.023  1.00 88.45           C  
ANISOU 1503  CG1 ILE A 190     9492  13138  10973    344    109    335       C  
ATOM   1504  CG2 ILE A 190      60.507  56.174  43.741  1.00 89.10           C  
ANISOU 1504  CG2 ILE A 190     9896  13075  10883    769    171    -22       C  
ATOM   1505  CD1 ILE A 190      60.103  57.932  46.476  1.00 88.56           C  
ANISOU 1505  CD1 ILE A 190     9411  13056  11180    402    -52    384       C  
ATOM   1506  N   LEU A 191      57.578  56.853  41.548  1.00 98.73           N  
ANISOU 1506  N   LEU A 191    11660  14246  11604    429   -182   -180       N  
ATOM   1507  CA  LEU A 191      57.121  55.979  40.485  1.00105.58           C  
ANISOU 1507  CA  LEU A 191    12713  15142  12258    554   -276   -562       C  
ATOM   1508  C   LEU A 191      57.104  56.695  39.147  1.00106.51           C  
ANISOU 1508  C   LEU A 191    12925  15701  11841    635   -228   -532       C  
ATOM   1509  O   LEU A 191      57.591  56.177  38.156  1.00111.89           O  
ANISOU 1509  O   LEU A 191    13686  16634  12193    845   -116   -796       O  
ATOM   1510  CB  LEU A 191      55.748  55.401  40.805  1.00107.91           C  
ANISOU 1510  CB  LEU A 191    13080  15120  12799    402   -559   -767       C  
ATOM   1511  CG  LEU A 191      55.677  54.415  41.972  1.00106.65           C  
ANISOU 1511  CG  LEU A 191    12899  14484  13140    360   -548   -792       C  
ATOM   1512  CD1 LEU A 191      54.254  53.919  42.153  1.00108.23           C  
ANISOU 1512  CD1 LEU A 191    13132  14383  13604    141   -760   -997       C  
ATOM   1513  CD2 LEU A 191      56.637  53.251  41.782  1.00111.01           C  
ANISOU 1513  CD2 LEU A 191    13512  14876  13788    623   -378  -1028       C  
ATOM   1514  N   THR A 192      56.564  57.900  39.122  1.00104.03           N  
ANISOU 1514  N   THR A 192    12611  15493  11423    509   -288   -189       N  
ATOM   1515  CA  THR A 192      56.509  58.647  37.881  1.00110.26           C  
ANISOU 1515  CA  THR A 192    13528  16694  11670    638   -220    -29       C  
ATOM   1516  C   THR A 192      57.891  59.033  37.316  1.00114.12           C  
ANISOU 1516  C   THR A 192    13978  17474  11909    743    215    180       C  
ATOM   1517  O   THR A 192      57.999  59.310  36.145  1.00126.91           O  
ANISOU 1517  O   THR A 192    15734  19496  12987    921    343    259       O  
ATOM   1518  CB  THR A 192      55.567  59.864  37.967  1.00107.48           C  
ANISOU 1518  CB  THR A 192    13208  16325  11304    541   -375    342       C  
ATOM   1519  OG1 THR A 192      54.282  59.432  38.438  1.00104.34           O  
ANISOU 1519  OG1 THR A 192    12783  15727  11133    450   -759     86       O  
ATOM   1520  CG2 THR A 192      55.406  60.519  36.590  1.00107.05           C  
ANISOU 1520  CG2 THR A 192    13341  16723  10608    774   -329    559       C  
ATOM   1521  N   ILE A 193      58.944  59.018  38.133  1.00114.11           N  
ANISOU 1521  N   ILE A 193    13759  17326  12270    652    450    253       N  
ATOM   1522  CA  ILE A 193      60.301  59.208  37.569  1.00116.63           C  
ANISOU 1522  CA  ILE A 193    13957  17957  12398    743    887    349       C  
ATOM   1523  C   ILE A 193      60.861  57.900  36.963  1.00116.40           C  
ANISOU 1523  C   ILE A 193    13953  18121  12153   1032    954   -124       C  
ATOM   1524  O   ILE A 193      61.666  57.935  36.038  1.00112.68           O  
ANISOU 1524  O   ILE A 193    13461  18051  11300   1192   1285   -133       O  
ATOM   1525  CB  ILE A 193      61.306  59.859  38.562  1.00113.48           C  
ANISOU 1525  CB  ILE A 193    13224  17436  12455    536   1128    567       C  
ATOM   1526  CG1 ILE A 193      60.798  61.220  39.033  1.00111.89           C  
ANISOU 1526  CG1 ILE A 193    13004  17024  12482    257   1110    966       C  
ATOM   1527  CG2 ILE A 193      62.649  60.087  37.886  1.00120.25           C  
ANISOU 1527  CG2 ILE A 193    13896  18654  13140    592   1614    644       C  
ATOM   1528  CD1 ILE A 193      61.525  61.750  40.250  1.00106.12           C  
ANISOU 1528  CD1 ILE A 193    11915  16126  12280     24   1206   1005       C  
ATOM   1529  N   SER A 194      60.394  56.759  37.461  1.00116.39           N  
ANISOU 1529  N   SER A 194    14001  17807  12412   1101    670   -515       N  
ATOM   1530  CA  SER A 194      60.667  55.480  36.812  1.00121.15           C  
ANISOU 1530  CA  SER A 194    14684  18479  12865   1386    683  -1042       C  
ATOM   1531  C   SER A 194      59.983  55.423  35.455  1.00127.73           C  
ANISOU 1531  C   SER A 194    15746  19689  13093   1520    581  -1289       C  
ATOM   1532  O   SER A 194      60.532  54.879  34.506  1.00136.28           O  
ANISOU 1532  O   SER A 194    16869  21121  13790   1786    754  -1629       O  
ATOM   1533  CB  SER A 194      60.173  54.319  37.674  1.00126.61           C  
ANISOU 1533  CB  SER A 194    15416  18625  14065   1390    425  -1352       C  
ATOM   1534  OG  SER A 194      60.772  54.332  38.957  1.00136.89           O  
ANISOU 1534  OG  SER A 194    16520  19663  15827   1345    486  -1099       O  
ATOM   1535  N   LEU A 195      58.771  55.983  35.375  1.00127.45           N  
ANISOU 1535  N   LEU A 195    15837  19639  12950   1375    282  -1151       N  
ATOM   1536  CA  LEU A 195      57.994  56.006  34.129  1.00123.80           C  
ANISOU 1536  CA  LEU A 195    15559  19623  11855   1543     94  -1381       C  
ATOM   1537  C   LEU A 195      58.660  56.796  33.045  1.00121.44           C  
ANISOU 1537  C   LEU A 195    15331  19945  10863   1743    436  -1053       C  
ATOM   1538  O   LEU A 195      58.867  56.287  31.963  1.00133.32           O  
ANISOU 1538  O   LEU A 195    16928  21926  11801   2028    501  -1424       O  
ATOM   1539  CB  LEU A 195      56.583  56.537  34.366  1.00126.73           C  
ANISOU 1539  CB  LEU A 195    15980  19879  12289   1381   -307  -1252       C  
ATOM   1540  CG  LEU A 195      55.586  55.500  34.870  1.00126.73           C  
ANISOU 1540  CG  LEU A 195    15943  19467  12741   1242   -685  -1795       C  
ATOM   1541  CD1 LEU A 195      54.172  55.992  34.645  1.00128.72           C  
ANISOU 1541  CD1 LEU A 195    16199  19863  12842   1178  -1089  -1805       C  
ATOM   1542  CD2 LEU A 195      55.814  54.177  34.157  1.00132.35           C  
ANISOU 1542  CD2 LEU A 195    16701  20247  13336   1432   -706  -2540       C  
ATOM   1543  N   TRP A 196      59.000  58.048  33.330  1.00118.08           N  
ANISOU 1543  N   TRP A 196    16968  14003  13894   1817   1964   2726       N  
ATOM   1544  CA  TRP A 196      59.676  58.891  32.341  1.00122.85           C  
ANISOU 1544  CA  TRP A 196    18127  14335  14214   1783   2391   2582       C  
ATOM   1545  C   TRP A 196      61.130  58.461  32.079  1.00125.38           C  
ANISOU 1545  C   TRP A 196    18015  14908  14713   1167   2291   2211       C  
ATOM   1546  O   TRP A 196      61.737  58.859  31.076  1.00126.80           O  
ANISOU 1546  O   TRP A 196    18430  15081  14666    947   2580   1985       O  
ATOM   1547  CB  TRP A 196      59.589  60.355  32.732  1.00126.74           C  
ANISOU 1547  CB  TRP A 196    19849  14182  14123   1758   3165   2654       C  
ATOM   1548  CG  TRP A 196      58.213  60.901  32.567  1.00131.92           C  
ANISOU 1548  CG  TRP A 196    21011  14826  14287   3035   3400   3113       C  
ATOM   1549  CD1 TRP A 196      57.204  60.872  33.484  1.00132.48           C  
ANISOU 1549  CD1 TRP A 196    20813  15302  14221   3529   3239   3281       C  
ATOM   1550  CD2 TRP A 196      57.675  61.529  31.400  1.00138.70           C  
ANISOU 1550  CD2 TRP A 196    22543  15692  14461   4251   3836   3507       C  
ATOM   1551  NE1 TRP A 196      56.076  61.466  32.971  1.00140.29           N  
ANISOU 1551  NE1 TRP A 196    22135  16771  14395   5089   3540   3696       N  
ATOM   1552  CE2 TRP A 196      56.337  61.879  31.693  1.00144.53           C  
ANISOU 1552  CE2 TRP A 196    23286  17093  14534   5704   3916   3923       C  
ATOM   1553  CE3 TRP A 196      58.195  61.840  30.138  1.00142.07           C  
ANISOU 1553  CE3 TRP A 196    23521  15862  14594   4388   4196   3597       C  
ATOM   1554  CZ2 TRP A 196      55.512  62.521  30.771  1.00156.46           C  
ANISOU 1554  CZ2 TRP A 196    25260  19229  14956   7610   4333   4514       C  
ATOM   1555  CZ3 TRP A 196      57.379  62.487  29.224  1.00152.23           C  
ANISOU 1555  CZ3 TRP A 196    25464  17465  14909   6107   4643   4236       C  
ATOM   1556  CH2 TRP A 196      56.050  62.819  29.544  1.00161.22           C  
ANISOU 1556  CH2 TRP A 196    26525  19471  15259   7861   4704   4734       C  
ATOM   1557  N   ALA A 197      61.660  57.620  32.970  1.00127.06           N  
ANISOU 1557  N   ALA A 197    17556  15569  15149   1089   1916   2208       N  
ATOM   1558  CA  ALA A 197      62.967  56.995  32.774  1.00128.02           C  
ANISOU 1558  CA  ALA A 197    16976  16466  15200   1103   1749   1950       C  
ATOM   1559  C   ALA A 197      62.896  55.837  31.806  1.00126.49           C  
ANISOU 1559  C   ALA A 197    16640  15958  15462   1764   1553   1963       C  
ATOM   1560  O   ALA A 197      63.790  55.667  31.003  1.00130.95           O  
ANISOU 1560  O   ALA A 197    16846  17011  15898   1843   1582   1626       O  
ATOM   1561  CB  ALA A 197      63.556  56.535  34.098  1.00131.98           C  
ANISOU 1561  CB  ALA A 197    16841  17878  15426   1306   1515   2119       C  
ATOM   1562  N   VAL A 198      61.844  55.021  31.893  1.00123.00           N  
ANISOU 1562  N   VAL A 198    16508  14806  15420   2029   1482   2199       N  
ATOM   1563  CA  VAL A 198      61.663  53.956  30.908  1.00123.81           C  
ANISOU 1563  CA  VAL A 198    16752  14463  15824   2217   1591   1944       C  
ATOM   1564  C   VAL A 198      61.202  54.529  29.593  1.00122.89           C  
ANISOU 1564  C   VAL A 198    16507  14632  15553   1886   1668   1590       C  
ATOM   1565  O   VAL A 198      61.640  54.085  28.549  1.00128.38           O  
ANISOU 1565  O   VAL A 198    17058  15414  16305   1929   1757   1199       O  
ATOM   1566  CB  VAL A 198      60.699  52.829  31.358  1.00126.03           C  
ANISOU 1566  CB  VAL A 198    17612  13945  16326   2058   1809   2037       C  
ATOM   1567  CG1 VAL A 198      61.273  52.050  32.531  1.00130.15           C  
ANISOU 1567  CG1 VAL A 198    18589  13992  16869   2774   1899   2591       C  
ATOM   1568  CG2 VAL A 198      59.322  53.379  31.672  1.00126.94           C  
ANISOU 1568  CG2 VAL A 198    17601  14419  16211   1430   1756   2046       C  
ATOM   1569  N   ALA A 199      60.338  55.540  29.646  1.00123.62           N  
ANISOU 1569  N   ALA A 199    16687  14989  15293   1792   1694   1786       N  
ATOM   1570  CA  ALA A 199      59.893  56.231  28.428  1.00131.39           C  
ANISOU 1570  CA  ALA A 199    17634  16491  15795   1963   1842   1713       C  
ATOM   1571  C   ALA A 199      61.074  56.689  27.561  1.00139.57           C  
ANISOU 1571  C   ALA A 199    18777  17531  16721   1856   2009   1538       C  
ATOM   1572  O   ALA A 199      60.974  56.715  26.330  1.00150.98           O  
ANISOU 1572  O   ALA A 199    20052  19435  17876   1956   2095   1365       O  
ATOM   1573  CB  ALA A 199      58.996  57.409  28.771  1.00129.36           C  
ANISOU 1573  CB  ALA A 199    17785  16425  14938   2484   2030   2183       C  
ATOM   1574  N   TRP A 200      62.176  57.079  28.205  1.00141.89           N  
ANISOU 1574  N   TRP A 200    19211  17670  17029   1502   2100   1493       N  
ATOM   1575  CA  TRP A 200      63.405  57.382  27.485  1.00147.08           C  
ANISOU 1575  CA  TRP A 200    19731  18753  17398   1056   2304   1105       C  
ATOM   1576  C   TRP A 200      63.851  56.166  26.666  1.00146.51           C  
ANISOU 1576  C   TRP A 200    18939  19073  17654   1383   2038    701       C  
ATOM   1577  O   TRP A 200      64.173  56.299  25.501  1.00152.92           O  
ANISOU 1577  O   TRP A 200    19625  20249  18226   1226   2175    412       O  
ATOM   1578  CB  TRP A 200      64.508  57.873  28.450  1.00155.17           C  
ANISOU 1578  CB  TRP A 200    20609  20293  18054    334   2477    851       C  
ATOM   1579  CG  TRP A 200      65.911  57.382  28.132  1.00169.84           C  
ANISOU 1579  CG  TRP A 200    21450  23476  19603    147   2363    273       C  
ATOM   1580  CD1 TRP A 200      66.412  56.131  28.366  1.00176.49           C  
ANISOU 1580  CD1 TRP A 200    21410  24977  20671   1149   1926    241       C  
ATOM   1581  CD2 TRP A 200      66.993  58.148  27.575  1.00177.76           C  
ANISOU 1581  CD2 TRP A 200    22289  25477  19774  -1012   2834   -363       C  
ATOM   1582  NE1 TRP A 200      67.730  56.059  27.974  1.00182.85           N  
ANISOU 1582  NE1 TRP A 200    21237  27441  20794   1022   1964   -347       N  
ATOM   1583  CE2 TRP A 200      68.113  57.281  27.478  1.00183.64           C  
ANISOU 1583  CE2 TRP A 200    21610  27936  20228   -542   2480   -827       C  
ATOM   1584  CE3 TRP A 200      67.121  59.472  27.128  1.00179.88           C  
ANISOU 1584  CE3 TRP A 200    23681  25309  19356  -2382   3695   -589       C  
ATOM   1585  CZ2 TRP A 200      69.346  57.699  26.952  1.00188.35           C  
ANISOU 1585  CZ2 TRP A 200    21421  30326  19816  -1595   2802  -1658       C  
ATOM   1586  CZ3 TRP A 200      68.352  59.889  26.610  1.00188.39           C  
ANISOU 1586  CZ3 TRP A 200    24334  27752  19494  -3760   4174  -1423       C  
ATOM   1587  CH2 TRP A 200      69.444  59.000  26.525  1.00190.99           C  
ANISOU 1587  CH2 TRP A 200    22783  30277  19504  -3448   3644  -2021       C  
ATOM   1588  N   PHE A 201      63.791  54.977  27.255  1.00141.99           N  
ANISOU 1588  N   PHE A 201    18156  18244  17549   1894   1815    711       N  
ATOM   1589  CA  PHE A 201      64.284  53.782  26.574  1.00148.59           C  
ANISOU 1589  CA  PHE A 201    18769  19070  18617   2380   1858    301       C  
ATOM   1590  C   PHE A 201      63.372  53.265  25.476  1.00149.18           C  
ANISOU 1590  C   PHE A 201    19006  18843  18833   2071   2036    -87       C  
ATOM   1591  O   PHE A 201      63.833  52.931  24.397  1.00157.07           O  
ANISOU 1591  O   PHE A 201    19742  20183  19752   2065   2165   -607       O  
ATOM   1592  CB  PHE A 201      64.626  52.684  27.567  1.00159.42           C  
ANISOU 1592  CB  PHE A 201    20374  19989  20207   3293   1888    555       C  
ATOM   1593  CG  PHE A 201      65.899  52.929  28.299  1.00174.42           C  
ANISOU 1593  CG  PHE A 201    21551  23149  21571   3905   1707    693       C  
ATOM   1594  CD1 PHE A 201      65.925  53.772  29.410  1.00180.18           C  
ANISOU 1594  CD1 PHE A 201    22021  24473  21965   3450   1536    993       C  
ATOM   1595  CD2 PHE A 201      67.089  52.372  27.855  1.00185.43           C  
ANISOU 1595  CD2 PHE A 201    22334  25566  22555   4876   1758    383       C  
ATOM   1596  CE1 PHE A 201      67.110  54.028  30.085  1.00189.19           C  
ANISOU 1596  CE1 PHE A 201    22157  27461  22265   3701   1421    886       C  
ATOM   1597  CE2 PHE A 201      68.274  52.627  28.522  1.00199.54           C  
ANISOU 1597  CE2 PHE A 201    22993  29390  23431   5429   1573    371       C  
ATOM   1598  CZ  PHE A 201      68.282  53.458  29.639  1.00199.55           C  
ANISOU 1598  CZ  PHE A 201    22587  30237  22992   4696   1404    571       C  
ATOM   1599  N   LYS A 202      62.082  53.206  25.739  1.00148.83           N  
ANISOU 1599  N   LYS A 202    19199  18545  18801   1699   2072     32       N  
ATOM   1600  CA  LYS A 202      61.148  52.737  24.726  1.00155.53           C  
ANISOU 1600  CA  LYS A 202    19847  19843  19401   1115   2292   -555       C  
ATOM   1601  C   LYS A 202      60.015  53.745  24.520  1.00157.03           C  
ANISOU 1601  C   LYS A 202    19602  21165  18896   1065   2129   -249       C  
ATOM   1602  O   LYS A 202      59.103  53.840  25.343  1.00168.20           O  
ANISOU 1602  O   LYS A 202    21046  22697  20164    987   2079     -1       O  
ATOM   1603  CB  LYS A 202      60.602  51.335  25.083  1.00160.86           C  
ANISOU 1603  CB  LYS A 202    21167  19616  20336    543   2790  -1052       C  
ATOM   1604  CG  LYS A 202      59.773  50.666  23.980  1.00168.65           C  
ANISOU 1604  CG  LYS A 202    21904  21319  20856   -614   3267  -2104       C  
ATOM   1605  CD  LYS A 202      60.485  50.701  22.628  1.00168.30           C  
ANISOU 1605  CD  LYS A 202    21383  21886  20678   -471   3287  -2614       C  
ATOM   1606  CE  LYS A 202      59.558  50.312  21.474  1.00174.74           C  
ANISOU 1606  CE  LYS A 202    21511  24184  20697  -1737   3662  -3705       C  
ATOM   1607  NZ  LYS A 202      58.632  51.415  21.065  1.00173.67           N  
ANISOU 1607  NZ  LYS A 202    20090  26351  19545  -1578   3161  -3346       N  
ATOM   1608  N   ASN A 203      60.062  54.487  23.420  1.00155.08           N  
ANISOU 1608  N   ASN A 203    18987  21884  18049   1324   2113   -203       N  
ATOM   1609  CA  ASN A 203      61.081  54.331  22.403  1.00160.13           C  
ANISOU 1609  CA  ASN A 203    19485  22602  18756   1238   2198   -597       C  
ATOM   1610  C   ASN A 203      62.075  55.472  22.496  1.00150.62           C  
ANISOU 1610  C   ASN A 203    18707  21087  17433   1531   2216    -60       C  
ATOM   1611  O   ASN A 203      61.738  56.594  22.193  1.00147.91           O  
ANISOU 1611  O   ASN A 203    18753  21032  16414   1865   2394    503       O  
ATOM   1612  CB  ASN A 203      60.405  54.321  21.007  1.00176.75           C  
ANISOU 1612  CB  ASN A 203    20845  26305  20008   1070   2292  -1016       C  
ATOM   1613  CG  ASN A 203      61.387  54.089  19.863  1.00182.65           C  
ANISOU 1613  CG  ASN A 203    21349  27296  20752    868   2406  -1540       C  
ATOM   1614  OD1 ASN A 203      62.244  53.212  19.931  1.00182.75           O  
ANISOU 1614  OD1 ASN A 203    21525  26480  21432    645   2525  -2113       O  
ATOM   1615  ND2 ASN A 203      61.227  54.851  18.782  1.00187.34           N  
ANISOU 1615  ND2 ASN A 203    21585  29171  20425   1156   2439  -1298       N  
ATOM   1616  N   GLY A 204      63.288  55.180  22.959  1.00147.82           N  
ANISOU 1616  N   GLY A 204    18376  20270  17518   1417   2184   -266       N  
ATOM   1617  CA  GLY A 204      64.410  56.120  22.848  1.00151.13           C  
ANISOU 1617  CA  GLY A 204    18939  20945  17537   1088   2369   -214       C  
ATOM   1618  C   GLY A 204      63.989  57.568  22.938  1.00156.79           C  
ANISOU 1618  C   GLY A 204    20621  21319  17629    937   2774    420       C  
ATOM   1619  O   GLY A 204      64.471  58.407  22.177  1.00160.08           O  
ANISOU 1619  O   GLY A 204    21557  21876  17388    529   3247    463       O  
ATOM   1620  N   GLU A 205      63.084  57.867  23.877  1.00161.49           N  
ANISOU 1620  N   GLU A 205    21690  21343  18324   1317   2750    927       N  
ATOM   1621  CA  GLU A 205      62.579  59.239  24.036  1.00167.92           C  
ANISOU 1621  CA  GLU A 205    23802  21544  18453   1582   3350   1604       C  
ATOM   1622  C   GLU A 205      61.959  59.657  25.381  1.00166.41           C  
ANISOU 1622  C   GLU A 205    24192  20656  18379   1830   3429   1985       C  
ATOM   1623  O   GLU A 205      61.149  58.932  25.972  1.00165.83           O  
ANISOU 1623  O   GLU A 205    23432  20853  18719   2251   2915   2026       O  
ATOM   1624  CB  GLU A 205      61.651  59.620  22.883  1.00172.23           C  
ANISOU 1624  CB  GLU A 205    24576  22650  18212   2610   3542   2120       C  
ATOM   1625  CG  GLU A 205      62.337  60.464  21.834  1.00182.00           C  
ANISOU 1625  CG  GLU A 205    26767  23713  18671   2372   4244   2300       C  
ATOM   1626  CD  GLU A 205      63.263  61.505  22.444  1.00186.36           C  
ANISOU 1626  CD  GLU A 205    28891  22955  18959   1251   5144   2260       C  
ATOM   1627  OE1 GLU A 205      64.248  61.119  23.125  1.00179.30           O  
ANISOU 1627  OE1 GLU A 205    27314  22246  18566    -32   4928   1483       O  
ATOM   1628  OE2 GLU A 205      63.008  62.711  22.240  1.00196.50           O  
ANISOU 1628  OE2 GLU A 205    32178  23157  19326   1668   6215   2965       O  
ATOM   1629  N   THR A 206      62.305  60.884  25.803  1.00151.25           N  
ANISOU 1629  N   THR A 206    17779  24756  14932    568    283  -2961       N  
ATOM   1630  CA  THR A 206      61.695  61.538  26.983  1.00135.64           C  
ANISOU 1630  CA  THR A 206    15792  22400  13343    624     48  -2513       C  
ATOM   1631  C   THR A 206      61.855  63.063  26.954  1.00132.23           C  
ANISOU 1631  C   THR A 206    15635  21975  12628    898    132  -1728       C  
ATOM   1632  O   THR A 206      62.715  63.590  26.261  1.00131.15           O  
ANISOU 1632  O   THR A 206    15713  21932  12186    970    457  -1475       O  
ATOM   1633  CB  THR A 206      62.282  61.018  28.297  1.00124.54           C  
ANISOU 1633  CB  THR A 206    14312  20193  12812    423    155  -2543       C  
ATOM   1634  OG1 THR A 206      61.544  61.564  29.381  1.00114.08           O  
ANISOU 1634  OG1 THR A 206    12962  18601  11783    457    -92  -2204       O  
ATOM   1635  CG2 THR A 206      63.717  61.436  28.430  1.00124.61           C  
ANISOU 1635  CG2 THR A 206    14428  19888  13028    425    525  -2237       C  
ATOM   1636  N   SER A 207      61.016  63.758  27.713  1.00131.68           N  
ANISOU 1636  N   SER A 207    15587  21767  12677   1039   -105  -1358       N  
ATOM   1637  CA  SER A 207      61.092  65.219  27.801  1.00135.93           C  
ANISOU 1637  CA  SER A 207    16464  22156  13024   1306     41   -618       C  
ATOM   1638  C   SER A 207      61.775  65.621  29.084  1.00126.05           C  
ANISOU 1638  C   SER A 207    15290  20113  12490   1084    218   -371       C  
ATOM   1639  O   SER A 207      61.444  65.119  30.148  1.00123.51           O  
ANISOU 1639  O   SER A 207    14755  19472  12698    930     14   -564       O  
ATOM   1640  CB  SER A 207      59.695  65.853  27.732  1.00140.14           C  
ANISOU 1640  CB  SER A 207    16999  23108  13138   1707   -293   -336       C  
ATOM   1641  OG  SER A 207      59.002  65.684  28.958  1.00137.97           O  
ANISOU 1641  OG  SER A 207    16525  22488  13408   1606   -548   -409       O  
ATOM   1642  N   LEU A 208      62.733  66.529  28.982  1.00125.33           N  
ANISOU 1642  N   LEU A 208    15493  19743  12383   1038    624     32       N  
ATOM   1643  CA  LEU A 208      63.481  66.948  30.141  1.00118.44           C  
ANISOU 1643  CA  LEU A 208    14644  18236  12122    758    816    185       C  
ATOM   1644  C   LEU A 208      62.596  67.720  31.108  1.00115.45           C  
ANISOU 1644  C   LEU A 208    14391  17535  11939    883    643    505       C  
ATOM   1645  O   LEU A 208      62.682  67.499  32.323  1.00114.17           O  
ANISOU 1645  O   LEU A 208    14050  16995  12332    670    537    388       O  
ATOM   1646  CB  LEU A 208      64.713  67.783  29.748  1.00121.62           C  
ANISOU 1646  CB  LEU A 208    15307  18464  12438    577   1353    470       C  
ATOM   1647  CG  LEU A 208      65.891  67.733  30.736  1.00121.42           C  
ANISOU 1647  CG  LEU A 208    15073  18041  13018    150   1567    336       C  
ATOM   1648  CD1 LEU A 208      66.766  66.511  30.472  1.00122.26           C  
ANISOU 1648  CD1 LEU A 208    14793  18389  13271     27   1599   -137       C  
ATOM   1649  CD2 LEU A 208      66.720  69.006  30.688  1.00123.14           C  
ANISOU 1649  CD2 LEU A 208    15614  17971  13202    -97   2095    704       C  
ATOM   1650  N   PRO A 209      61.729  68.636  30.584  1.00112.94           N  
ANISOU 1650  N   PRO A 209    14384  17393  11133   1289    628    934       N  
ATOM   1651  CA  PRO A 209      61.033  69.467  31.558  1.00108.14           C  
ANISOU 1651  CA  PRO A 209    13938  16390  10760   1423    565   1256       C  
ATOM   1652  C   PRO A 209      60.138  68.661  32.477  1.00104.79           C  
ANISOU 1652  C   PRO A 209    13112  16018  10685   1393    104    918       C  
ATOM   1653  O   PRO A 209      60.005  68.996  33.654  1.00101.12           O  
ANISOU 1653  O   PRO A 209    12655  15104  10659   1278     86    996       O  
ATOM   1654  CB  PRO A 209      60.232  70.435  30.685  1.00107.35           C  
ANISOU 1654  CB  PRO A 209    14214  16567  10004   1999    633   1778       C  
ATOM   1655  CG  PRO A 209      61.073  70.576  29.484  1.00113.71           C  
ANISOU 1655  CG  PRO A 209    15251  17591  10362   1993    988   1901       C  
ATOM   1656  CD  PRO A 209      61.571  69.173  29.223  1.00114.57           C  
ANISOU 1656  CD  PRO A 209    14890  18050  10589   1658    792   1252       C  
ATOM   1657  N   LEU A 210      59.589  67.565  31.972  1.00108.16           N  
ANISOU 1657  N   LEU A 210    13190  16971  10932   1428   -218    496       N  
ATOM   1658  CA  LEU A 210      58.721  66.737  32.790  1.00111.01           C  
ANISOU 1658  CA  LEU A 210    13185  17368  11626   1331   -582    146       C  
ATOM   1659  C   LEU A 210      59.494  65.707  33.643  1.00108.63           C  
ANISOU 1659  C   LEU A 210    12665  16658  11948    901   -544   -233       C  
ATOM   1660  O   LEU A 210      59.061  65.361  34.763  1.00109.61           O  
ANISOU 1660  O   LEU A 210    12625  16517  12503    784   -700   -330       O  
ATOM   1661  CB  LEU A 210      57.602  66.095  31.952  1.00111.94           C  
ANISOU 1661  CB  LEU A 210    13012  18248  11269   1517   -921   -173       C  
ATOM   1662  CG  LEU A 210      56.696  67.078  31.180  1.00118.36           C  
ANISOU 1662  CG  LEU A 210    13955  19625  11390   2083  -1028    244       C  
ATOM   1663  CD1 LEU A 210      55.516  66.349  30.573  1.00125.24           C  
ANISOU 1663  CD1 LEU A 210    14374  21382  11828   2195  -1436   -185       C  
ATOM   1664  CD2 LEU A 210      56.210  68.233  32.050  1.00115.14           C  
ANISOU 1664  CD2 LEU A 210    13779  18817  11150   2380   -977    779       C  
ATOM   1665  N   LEU A 211      60.659  65.264  33.164  1.00107.18           N  
ANISOU 1665  N   LEU A 211    12491  16431  11800    720   -304   -399       N  
ATOM   1666  CA  LEU A 211      61.529  64.469  34.030  1.00104.43           C  
ANISOU 1666  CA  LEU A 211    11965  15697  12016    445   -215   -627       C  
ATOM   1667  C   LEU A 211      62.089  65.299  35.184  1.00102.90           C  
ANISOU 1667  C   LEU A 211    11854  15067  12176    327    -90   -309       C  
ATOM   1668  O   LEU A 211      62.117  64.830  36.308  1.00106.65           O  
ANISOU 1668  O   LEU A 211    12155  15286  13079    216   -191   -399       O  
ATOM   1669  CB  LEU A 211      62.634  63.743  33.268  1.00 99.15           C  
ANISOU 1669  CB  LEU A 211    11228  15139  11305    346     21   -904       C  
ATOM   1670  CG  LEU A 211      63.209  62.488  33.969  1.00 94.40           C  
ANISOU 1670  CG  LEU A 211    10388  14263  11217    217     56  -1239       C  
ATOM   1671  CD1 LEU A 211      62.287  61.882  35.025  1.00 89.40           C  
ANISOU 1671  CD1 LEU A 211     9638  13378  10949    183   -188  -1344       C  
ATOM   1672  CD2 LEU A 211      63.577  61.429  32.940  1.00101.02           C  
ANISOU 1672  CD2 LEU A 211    11164  15310  11906    220    197  -1682       C  
ATOM   1673  N   LEU A 212      62.468  66.552  34.909  1.00104.03           N  
ANISOU 1673  N   LEU A 212    12286  15131  12107    344    155     54       N  
ATOM   1674  CA  LEU A 212      62.881  67.494  35.965  1.00 99.15           C  
ANISOU 1674  CA  LEU A 212    11787  14106  11777    164    314    293       C  
ATOM   1675  C   LEU A 212      61.766  67.764  36.923  1.00 98.25           C  
ANISOU 1675  C   LEU A 212    11692  13814  11822    285     67    397       C  
ATOM   1676  O   LEU A 212      61.957  67.724  38.152  1.00 91.63           O  
ANISOU 1676  O   LEU A 212    10724  12727  11363    103     19    345       O  
ATOM   1677  CB  LEU A 212      63.338  68.814  35.364  1.00 99.87           C  
ANISOU 1677  CB  LEU A 212    12285  14068  11592    135    714    645       C  
ATOM   1678  CG  LEU A 212      64.797  68.845  34.973  1.00106.48           C  
ANISOU 1678  CG  LEU A 212    13064  14938  12453   -182   1086    553       C  
ATOM   1679  CD1 LEU A 212      65.351  70.239  35.229  1.00112.28           C  
ANISOU 1679  CD1 LEU A 212    14146  15294  13219   -455   1534    827       C  
ATOM   1680  CD2 LEU A 212      65.578  67.782  35.756  1.00100.09           C  
ANISOU 1680  CD2 LEU A 212    11767  14206  12057   -390    954    182       C  
HETATM 1681  N   MSE A 213      60.590  68.050  36.358  1.00103.85           N  
ANISOU 1681  N   MSE A 213    12530  14733  12193    623    -90    545       N  
HETATM 1682  CA  MSE A 213      59.445  68.475  37.123  1.00 99.01           C  
ANISOU 1682  CA  MSE A 213    11944  14019  11656    815   -282    689       C  
HETATM 1683  C   MSE A 213      59.127  67.433  38.159  1.00 94.10           C  
ANISOU 1683  C   MSE A 213    10963  13350  11440    642   -544    377       C  
HETATM 1684  O   MSE A 213      58.956  67.762  39.330  1.00 93.33           O  
ANISOU 1684  O   MSE A 213    10867  12962  11631    563   -562    450       O  
HETATM 1685  CB  MSE A 213      58.281  68.740  36.183  1.00107.86           C  
ANISOU 1685  CB  MSE A 213    13126  15581  12272   1269   -445    846       C  
HETATM 1686  CG  MSE A 213      57.139  69.483  36.886  1.00119.55           C  
ANISOU 1686  CG  MSE A 213    14682  16970  13772   1573   -555   1093       C  
HETATM 1687 SE   MSE A 213      55.401  69.142  35.981  1.00141.90          SE  
ANISOU 1687 SE   MSE A 213    17187  20699  16031   2116   -988   1040      SE  
HETATM 1688  CE  MSE A 213      55.167  67.204  36.251  1.00117.99           C  
ANISOU 1688  CE  MSE A 213    13545  17962  13320   1618  -1327    284       C  
ATOM   1689  N   TYR A 214      59.101  66.161  37.763  1.00 90.55           N  
ANISOU 1689  N   TYR A 214    10241  13142  11019    563   -692     21       N  
ATOM   1690  CA  TYR A 214      58.882  65.085  38.737  1.00 91.42           C  
ANISOU 1690  CA  TYR A 214    10087  13109  11540    394   -840   -241       C  
ATOM   1691  C   TYR A 214      60.019  64.869  39.788  1.00 90.83           C  
ANISOU 1691  C   TYR A 214     9956  12691  11864    188   -703   -226       C  
ATOM   1692  O   TYR A 214      59.761  64.366  40.892  1.00 89.83           O  
ANISOU 1692  O   TYR A 214     9697  12391  12044    127   -798   -269       O  
ATOM   1693  CB  TYR A 214      58.486  63.784  38.053  1.00 98.27           C  
ANISOU 1693  CB  TYR A 214    10747  14231  12358    338   -949   -655       C  
ATOM   1694  CG  TYR A 214      57.020  63.712  37.789  1.00106.67           C  
ANISOU 1694  CG  TYR A 214    11665  15662  13202    442  -1192   -779       C  
ATOM   1695  CD1 TYR A 214      56.131  63.366  38.802  1.00109.87           C  
ANISOU 1695  CD1 TYR A 214    11901  15955  13887    357  -1324   -853       C  
ATOM   1696  CD2 TYR A 214      56.502  64.051  36.545  1.00120.49           C  
ANISOU 1696  CD2 TYR A 214    13410  17959  14411    648  -1288   -805       C  
ATOM   1697  CE1 TYR A 214      54.759  63.326  38.578  1.00115.15           C  
ANISOU 1697  CE1 TYR A 214    12343  17063  14342    430  -1542  -1002       C  
ATOM   1698  CE2 TYR A 214      55.131  64.012  36.304  1.00129.96           C  
ANISOU 1698  CE2 TYR A 214    14368  19664  15344    775  -1547   -942       C  
ATOM   1699  CZ  TYR A 214      54.262  63.652  37.329  1.00126.51           C  
ANISOU 1699  CZ  TYR A 214    13711  19123  15232    646  -1672  -1060       C  
ATOM   1700  OH  TYR A 214      52.900  63.603  37.096  1.00132.91           O  
ANISOU 1700  OH  TYR A 214    14192  20532  15776    741  -1919  -1242       O  
ATOM   1701  N   VAL A 215      61.245  65.290  39.467  1.00 86.31           N  
ANISOU 1701  N   VAL A 215     9457  12093  11244     93   -473   -153       N  
ATOM   1702  CA  VAL A 215      62.300  65.387  40.490  1.00 82.08           C  
ANISOU 1702  CA  VAL A 215     8803  11395  10987    -87   -363   -121       C  
ATOM   1703  C   VAL A 215      61.994  66.555  41.446  1.00 85.45           C  
ANISOU 1703  C   VAL A 215     9380  11621  11464   -172   -347     86       C  
ATOM   1704  O   VAL A 215      61.933  66.370  42.666  1.00 87.35           O  
ANISOU 1704  O   VAL A 215     9484  11770  11935   -233   -450     71       O  
ATOM   1705  CB  VAL A 215      63.736  65.459  39.864  1.00 78.76           C  
ANISOU 1705  CB  VAL A 215     8318  11109  10496   -216   -100   -177       C  
ATOM   1706  CG1 VAL A 215      64.771  65.894  40.884  1.00 73.68           C  
ANISOU 1706  CG1 VAL A 215     7502  10452  10038   -443     10   -153       C  
ATOM   1707  CG2 VAL A 215      64.122  64.107  39.293  1.00 73.05           C  
ANISOU 1707  CG2 VAL A 215     7403  10524   9828   -103   -100   -430       C  
HETATM 1708  N   MSE A 216      61.694  67.726  40.892  1.00 90.77           N  
ANISOU 1708  N   MSE A 216    10374  12213  11901   -129   -196    289       N  
HETATM 1709  CA  MSE A 216      61.192  68.852  41.719  1.00 97.12           C  
ANISOU 1709  CA  MSE A 216    11408  12741  12752   -150   -129    469       C  
HETATM 1710  C   MSE A 216      59.909  68.543  42.473  1.00 89.36           C  
ANISOU 1710  C   MSE A 216    10336  11747  11869     44   -405    473       C  
HETATM 1711  O   MSE A 216      59.690  69.065  43.545  1.00 85.05           O  
ANISOU 1711  O   MSE A 216     9840  11007  11465    -29   -388    511       O  
HETATM 1712  CB  MSE A 216      60.973  70.059  40.859  1.00109.88           C  
ANISOU 1712  CB  MSE A 216    13458  14208  14080    -15    137    743       C  
HETATM 1713  CG  MSE A 216      62.219  70.304  40.044  1.00121.07           C  
ANISOU 1713  CG  MSE A 216    14962  15652  15384   -249    462    735       C  
HETATM 1714 SE   MSE A 216      61.815  71.735  38.777  1.00140.25          SE  
ANISOU 1714 SE   MSE A 216    18051  17866  17371     40    865   1198      SE  
HETATM 1715  CE  MSE A 216      63.644  72.451  38.651  1.00155.49           C  
ANISOU 1715  CE  MSE A 216    20114  19564  19400   -599   1463   1114       C  
ATOM   1716  N   TYR A 217      59.065  67.676  41.923  1.00 86.08           N  
ANISOU 1716  N   TYR A 217     9765  11573  11368    248   -634    384       N  
ATOM   1717  CA  TYR A 217      57.892  67.193  42.661  1.00 88.23           C  
ANISOU 1717  CA  TYR A 217     9865  11889  11768    348   -868    320       C  
ATOM   1718  C   TYR A 217      58.280  66.426  43.897  1.00 90.17           C  
ANISOU 1718  C   TYR A 217     9908  12003  12348    149   -919    200       C  
ATOM   1719  O   TYR A 217      57.662  66.606  44.955  1.00 99.15           O  
ANISOU 1719  O   TYR A 217    11017  13043  13609    154   -982    248       O  
ATOM   1720  CB  TYR A 217      56.974  66.330  41.791  1.00 84.65           C  
ANISOU 1720  CB  TYR A 217     9223  11783  11154    487  -1067    141       C  
ATOM   1721  CG  TYR A 217      55.947  67.106  41.018  1.00 84.86           C  
ANISOU 1721  CG  TYR A 217     9340  12094  10806    826  -1140    302       C  
ATOM   1722  CD1 TYR A 217      56.131  68.471  40.737  1.00 87.16           C  
ANISOU 1722  CD1 TYR A 217     9995  12234  10886   1044   -939    654       C  
ATOM   1723  CD2 TYR A 217      54.827  66.478  40.508  1.00 88.66           C  
ANISOU 1723  CD2 TYR A 217     9547  13028  11112    943  -1373    101       C  
ATOM   1724  CE1 TYR A 217      55.214  69.180  39.987  1.00 90.92           C  
ANISOU 1724  CE1 TYR A 217    10582  12994  10966   1491   -980    886       C  
ATOM   1725  CE2 TYR A 217      53.889  67.178  39.759  1.00 93.79           C  
ANISOU 1725  CE2 TYR A 217    10199  14103  11332   1346  -1477    266       C  
ATOM   1726  CZ  TYR A 217      54.079  68.531  39.503  1.00 97.38           C  
ANISOU 1726  CZ  TYR A 217    11043  14395  11560   1683  -1286    704       C  
ATOM   1727  OH  TYR A 217      53.132  69.233  38.752  1.00106.51           O  
ANISOU 1727  OH  TYR A 217    12226  16000  12243   2222  -1369    953       O  
ATOM   1728  N   LEU A 218      59.285  65.554  43.763  1.00 84.89           N  
ANISOU 1728  N   LEU A 218     9098  11361  11793     31   -873     65       N  
ATOM   1729  CA  LEU A 218      59.732  64.679  44.876  1.00 81.90           C  
ANISOU 1729  CA  LEU A 218     8527  10906  11683    -39   -904     14       C  
ATOM   1730  C   LEU A 218      60.244  65.512  46.040  1.00 77.96           C  
ANISOU 1730  C   LEU A 218     8034  10361  11226   -159   -859    125       C  
ATOM   1731  O   LEU A 218      59.842  65.312  47.208  1.00 76.19           O  
ANISOU 1731  O   LEU A 218     7737  10094  11115   -152   -940    168       O  
ATOM   1732  CB  LEU A 218      60.844  63.734  44.398  1.00 79.72           C  
ANISOU 1732  CB  LEU A 218     8118  10694  11476    -34   -811   -104       C  
ATOM   1733  CG  LEU A 218      60.956  62.310  44.926  1.00 72.40           C  
ANISOU 1733  CG  LEU A 218     7055   9661  10791     62   -805   -172       C  
ATOM   1734  CD1 LEU A 218      62.387  62.095  45.307  1.00 67.00           C  
ANISOU 1734  CD1 LEU A 218     6199   9099  10156    128   -710   -118       C  
ATOM   1735  CD2 LEU A 218      60.036  62.048  46.115  1.00 73.80           C  
ANISOU 1735  CD2 LEU A 218     7228   9693  11117     72   -893    -77       C  
ATOM   1736  N   CYS A 219      61.129  66.447  45.725  1.00 80.12           N  
ANISOU 1736  N   CYS A 219     8395  10660  11385   -310   -697    139       N  
ATOM   1737  CA  CYS A 219      61.600  67.382  46.706  1.00 85.36           C  
ANISOU 1737  CA  CYS A 219     9080  11299  12053   -526   -606    141       C  
ATOM   1738  C   CYS A 219      60.419  68.035  47.402  1.00 87.97           C  
ANISOU 1738  C   CYS A 219     9600  11436  12387   -461   -650    223       C  
ATOM   1739  O   CYS A 219      60.296  67.949  48.628  1.00 87.84           O  
ANISOU 1739  O   CYS A 219     9473  11461  12442   -511   -727    197       O  
ATOM   1740  CB  CYS A 219      62.499  68.427  46.065  1.00 92.01           C  
ANISOU 1740  CB  CYS A 219    10073  12110  12775   -775   -331    109       C  
ATOM   1741  SG  CYS A 219      63.995  67.730  45.343  1.00 99.91           S  
ANISOU 1741  SG  CYS A 219    10769  13433  13759   -872   -240    -20       S  
ATOM   1742  N   ASN A 220      59.503  68.615  46.624  1.00 84.90           N  
ANISOU 1742  N   ASN A 220     9469  10899  11887   -283   -607    337       N  
ATOM   1743  CA  ASN A 220      58.407  69.348  47.215  1.00 80.44           C  
ANISOU 1743  CA  ASN A 220     9081  10170  11311   -151   -603    428       C  
ATOM   1744  C   ASN A 220      57.430  68.478  47.982  1.00 84.60           C  
ANISOU 1744  C   ASN A 220     9381  10809  11951    -23   -830    402       C  
ATOM   1745  O   ASN A 220      56.858  68.927  48.972  1.00 93.02           O  
ANISOU 1745  O   ASN A 220    10492  11795  13055     -9   -816    417       O  
ATOM   1746  CB  ASN A 220      57.697  70.209  46.194  1.00 83.91           C  
ANISOU 1746  CB  ASN A 220     9831  10491  11557    121   -485    613       C  
ATOM   1747  CG  ASN A 220      56.339  70.684  46.674  1.00 89.46           C  
ANISOU 1747  CG  ASN A 220    10616  11135  12237    415   -533    720       C  
ATOM   1748  OD1 ASN A 220      56.204  71.777  47.245  1.00 83.42           O  
ANISOU 1748  OD1 ASN A 220    10141  10071  11482    428   -309    786       O  
ATOM   1749  ND2 ASN A 220      55.310  69.851  46.444  1.00 93.42           N  
ANISOU 1749  ND2 ASN A 220    10848  11936  12712    635   -793    697       N  
ATOM   1750  N   SER A 221      57.274  67.219  47.568  1.00 81.29           N  
ANISOU 1750  N   SER A 221     8739  10549  11596     29   -983    335       N  
ATOM   1751  CA  SER A 221      56.363  66.313  48.273  1.00 81.99           C  
ANISOU 1751  CA  SER A 221     8639  10690  11820     74  -1113    297       C  
ATOM   1752  C   SER A 221      56.834  65.971  49.701  1.00 81.95           C  
ANISOU 1752  C   SER A 221     8541  10655  11938    -39  -1103    321       C  
ATOM   1753  O   SER A 221      56.026  65.638  50.560  1.00 90.15           O  
ANISOU 1753  O   SER A 221     9511  11691  13048    -11  -1137    349       O  
ATOM   1754  CB  SER A 221      56.088  65.042  47.458  1.00 84.47           C  
ANISOU 1754  CB  SER A 221     8795  11102  12194     85  -1187    160       C  
ATOM   1755  OG  SER A 221      57.178  64.151  47.503  1.00 87.85           O  
ANISOU 1755  OG  SER A 221     9159  11472  12745      7  -1132    116       O  
ATOM   1756  N   VAL A 222      58.144  66.047  49.935  1.00 81.75           N  
ANISOU 1756  N   VAL A 222     8479  10686  11894   -156  -1052    309       N  
ATOM   1757  CA  VAL A 222      58.715  65.911  51.288  1.00 70.23           C  
ANISOU 1757  CA  VAL A 222     6894   9357  10433   -223  -1066    334       C  
ATOM   1758  C   VAL A 222      58.460  67.186  52.068  1.00 67.24           C  
ANISOU 1758  C   VAL A 222     6651   8948   9947   -353  -1000    286       C  
ATOM   1759  O   VAL A 222      57.932  67.150  53.169  1.00 65.59           O  
ANISOU 1759  O   VAL A 222     6412   8788   9721   -331  -1029    313       O  
ATOM   1760  CB  VAL A 222      60.225  65.579  51.222  1.00 69.59           C  
ANISOU 1760  CB  VAL A 222     6625   9502  10313   -277  -1051    297       C  
ATOM   1761  CG1 VAL A 222      60.958  65.957  52.509  1.00 65.71           C  
ANISOU 1761  CG1 VAL A 222     5966   9318   9681   -393  -1076    260       C  
ATOM   1762  CG2 VAL A 222      60.401  64.113  50.905  1.00 69.87           C  
ANISOU 1762  CG2 VAL A 222     6543   9520  10481    -62  -1073    374       C  
ATOM   1763  N   TYR A 223      58.767  68.328  51.478  1.00 66.93           N  
ANISOU 1763  N   TYR A 223     6812   8781   9837   -486   -854    212       N  
ATOM   1764  CA  TYR A 223      58.387  69.561  52.125  1.00 72.69           C  
ANISOU 1764  CA  TYR A 223     7768   9348  10503   -592   -704    141       C  
ATOM   1765  C   TYR A 223      56.913  69.600  52.444  1.00 77.07           C  
ANISOU 1765  C   TYR A 223     8405   9787  11091   -339   -745    241       C  
ATOM   1766  O   TYR A 223      56.526  70.132  53.469  1.00 79.29           O  
ANISOU 1766  O   TYR A 223     8753  10038  11333   -380   -676    176       O  
ATOM   1767  CB  TYR A 223      58.713  70.751  51.305  1.00 73.79           C  
ANISOU 1767  CB  TYR A 223     8226   9214  10595   -712   -446    107       C  
ATOM   1768  CG  TYR A 223      58.511  71.996  52.081  1.00 78.13           C  
ANISOU 1768  CG  TYR A 223     9055   9521  11110   -871   -204    -20       C  
ATOM   1769  CD1 TYR A 223      59.311  72.275  53.173  1.00 79.87           C  
ANISOU 1769  CD1 TYR A 223     9148   9929  11267  -1249   -151   -292       C  
ATOM   1770  CD2 TYR A 223      57.470  72.878  51.776  1.00 83.39           C  
ANISOU 1770  CD2 TYR A 223    10096   9811  11776   -607    -18    110       C  
ATOM   1771  CE1 TYR A 223      59.132  73.419  53.913  1.00 89.92           C  
ANISOU 1771  CE1 TYR A 223    10702  10958  12504  -1458    116   -499       C  
ATOM   1772  CE2 TYR A 223      57.279  74.038  52.506  1.00 86.92           C  
ANISOU 1772  CE2 TYR A 223    10866   9943  12216   -729    280    -30       C  
ATOM   1773  CZ  TYR A 223      58.120  74.298  53.578  1.00 91.78           C  
ANISOU 1773  CZ  TYR A 223    11384  10691  12794  -1200    359   -368       C  
ATOM   1774  OH  TYR A 223      57.962  75.419  54.326  1.00 99.37           O  
ANISOU 1774  OH  TYR A 223    12676  11337  13743  -1391    690   -599       O  
ATOM   1775  N   GLY A 224      56.091  69.056  51.546  1.00 80.02           N  
ANISOU 1775  N   GLY A 224     8739  10155  11508    -96   -844    354       N  
ATOM   1776  CA  GLY A 224      54.638  68.968  51.764  1.00 81.29           C  
ANISOU 1776  CA  GLY A 224     8855  10342  11689    137   -900    414       C  
ATOM   1777  C   GLY A 224      54.286  68.281  53.075  1.00 79.34           C  
ANISOU 1777  C   GLY A 224     8422  10215  11506     71   -957    396       C  
ATOM   1778  O   GLY A 224      53.626  68.864  53.940  1.00 78.97           O  
ANISOU 1778  O   GLY A 224     8435  10147  11421    121   -878    381       O  
ATOM   1779  N   TYR A 225      54.731  67.042  53.222  1.00 73.00           N  
ANISOU 1779  N   TYR A 225     7431   9518  10787     -7  -1048    418       N  
ATOM   1780  CA  TYR A 225      54.493  66.288  54.433  1.00 73.14           C  
ANISOU 1780  CA  TYR A 225     7325   9627  10836    -33  -1050    480       C  
ATOM   1781  C   TYR A 225      54.809  67.161  55.687  1.00 76.49           C  
ANISOU 1781  C   TYR A 225     7824  10143  11097   -116   -987    436       C  
ATOM   1782  O   TYR A 225      53.961  67.322  56.575  1.00 80.30           O  
ANISOU 1782  O   TYR A 225     8306  10665  11538    -75   -930    446       O  
ATOM   1783  CB  TYR A 225      55.359  65.041  54.413  1.00 72.52           C  
ANISOU 1783  CB  TYR A 225     7136   9585  10832    -45  -1083    561       C  
ATOM   1784  CG  TYR A 225      54.793  63.844  55.092  1.00 75.05           C  
ANISOU 1784  CG  TYR A 225     7388   9866  11260     -3  -1017    691       C  
ATOM   1785  CD1 TYR A 225      54.191  63.941  56.347  1.00 78.56           C  
ANISOU 1785  CD1 TYR A 225     7829  10395  11623      2   -952    778       C  
ATOM   1786  CD2 TYR A 225      54.928  62.584  54.519  1.00 80.89           C  
ANISOU 1786  CD2 TYR A 225     8108  10446  12178     19   -956    726       C  
ATOM   1787  CE1 TYR A 225      53.691  62.816  56.995  1.00 87.25           C  
ANISOU 1787  CE1 TYR A 225     8916  11417  12815     24   -814    941       C  
ATOM   1788  CE2 TYR A 225      54.442  61.448  55.152  1.00 90.10           C  
ANISOU 1788  CE2 TYR A 225     9296  11462  13475     28   -789    862       C  
ATOM   1789  CZ  TYR A 225      53.826  61.560  56.391  1.00 94.77           C  
ANISOU 1789  CZ  TYR A 225     9892  12134  13979     29   -712    995       C  
ATOM   1790  OH  TYR A 225      53.340  60.419  57.017  1.00103.31           O  
ANISOU 1790  OH  TYR A 225    11045  13020  15186     22   -471   1171       O  
ATOM   1791  N   ILE A 226      56.010  67.746  55.723  1.00 72.95           N  
ANISOU 1791  N   ILE A 226     7415   9763  10538   -270   -975    334       N  
ATOM   1792  CA  ILE A 226      56.430  68.591  56.846  1.00 76.68           C  
ANISOU 1792  CA  ILE A 226     7928  10386  10818   -445   -905    178       C  
ATOM   1793  C   ILE A 226      55.456  69.755  57.125  1.00 81.68           C  
ANISOU 1793  C   ILE A 226     8810  10788  11436   -425   -731     67       C  
ATOM   1794  O   ILE A 226      54.926  69.883  58.237  1.00 90.94           O  
ANISOU 1794  O   ILE A 226     9973  12075  12503   -415   -685     24       O  
ATOM   1795  CB  ILE A 226      57.851  69.158  56.626  1.00 76.75           C  
ANISOU 1795  CB  ILE A 226     7907  10528  10725   -715   -874    -13       C  
ATOM   1796  CG1 ILE A 226      58.887  68.060  56.764  1.00 70.55           C  
ANISOU 1796  CG1 ILE A 226     6804  10123   9877   -665  -1039     83       C  
ATOM   1797  CG2 ILE A 226      58.141  70.301  57.601  1.00 73.72           C  
ANISOU 1797  CG2 ILE A 226     7615  10242  10149  -1007   -732   -312       C  
ATOM   1798  CD1 ILE A 226      60.174  68.381  56.056  1.00 76.38           C  
ANISOU 1798  CD1 ILE A 226     7436  10995  10587   -874  -1012    -72       C  
ATOM   1799  N   ASN A 227      55.234  70.599  56.124  1.00 77.17           N  
ANISOU 1799  N   ASN A 227     8478   9898  10945   -370   -602     47       N  
ATOM   1800  CA  ASN A 227      54.347  71.732  56.276  1.00 80.65           C  
ANISOU 1800  CA  ASN A 227     9202  10063  11379   -236   -383     -7       C  
ATOM   1801  C   ASN A 227      52.907  71.360  56.595  1.00 82.71           C  
ANISOU 1801  C   ASN A 227     9341  10405  11679     72   -431    117       C  
ATOM   1802  O   ASN A 227      52.236  72.093  57.289  1.00 89.01           O  
ANISOU 1802  O   ASN A 227    10276  11115  12429    170   -258     36       O  
ATOM   1803  CB  ASN A 227      54.372  72.594  55.044  1.00 86.79           C  
ANISOU 1803  CB  ASN A 227    10286  10484  12206   -117   -212     56       C  
ATOM   1804  CG  ASN A 227      53.912  73.990  55.319  1.00 95.85           C  
ANISOU 1804  CG  ASN A 227    11847  11239  13333    -25    137    -27       C  
ATOM   1805  OD1 ASN A 227      54.560  74.728  56.058  1.00103.58           O  
ANISOU 1805  OD1 ASN A 227    13015  12077  14262   -369    360   -300       O  
ATOM   1806  ND2 ASN A 227      52.777  74.367  54.742  1.00104.31           N  
ANISOU 1806  ND2 ASN A 227    13049  12159  14422    452    209    180       N  
ATOM   1807  N   TRP A 228      52.423  70.229  56.072  1.00 82.23           N  
ANISOU 1807  N   TRP A 228     9015  10516  11710    197   -624    270       N  
ATOM   1808  CA  TRP A 228      51.068  69.761  56.419  1.00 77.90           C  
ANISOU 1808  CA  TRP A 228     8266  10127  11205    387   -645    332       C  
ATOM   1809  C   TRP A 228      50.981  69.234  57.825  1.00 77.25           C  
ANISOU 1809  C   TRP A 228     8068  10219  11064    249   -616    317       C  
ATOM   1810  O   TRP A 228      49.981  69.403  58.493  1.00 80.93           O  
ANISOU 1810  O   TRP A 228     8472  10772  11503    361   -513    302       O  
ATOM   1811  CB  TRP A 228      50.528  68.759  55.406  1.00 80.17           C  
ANISOU 1811  CB  TRP A 228     8302  10553  11602    465   -802    406       C  
ATOM   1812  CG  TRP A 228      49.786  69.454  54.292  1.00 82.31           C  
ANISOU 1812  CG  TRP A 228     8599  10846  11827    783   -809    438       C  
ATOM   1813  CD1 TRP A 228      50.290  70.367  53.445  1.00 82.79           C  
ANISOU 1813  CD1 TRP A 228     8939  10706  11808    924   -747    496       C  
ATOM   1814  CD2 TRP A 228      48.394  69.320  53.958  1.00 85.68           C  
ANISOU 1814  CD2 TRP A 228     8744  11572  12237   1037   -857    435       C  
ATOM   1815  NE1 TRP A 228      49.320  70.810  52.587  1.00 85.51           N  
ANISOU 1815  NE1 TRP A 228     9234  11200  12055   1330   -765    589       N  
ATOM   1816  CE2 TRP A 228      48.146  70.181  52.883  1.00 85.74           C  
ANISOU 1816  CE2 TRP A 228     8871  11597  12109   1409   -861    529       C  
ATOM   1817  CE3 TRP A 228      47.342  68.532  54.451  1.00 86.89           C  
ANISOU 1817  CE3 TRP A 228     8530  12026  12457    973   -874    358       C  
ATOM   1818  CZ2 TRP A 228      46.900  70.280  52.281  1.00 87.55           C  
ANISOU 1818  CZ2 TRP A 228     8807  12235  12224   1782   -941    550       C  
ATOM   1819  CZ3 TRP A 228      46.106  68.637  53.860  1.00 85.95           C  
ANISOU 1819  CZ3 TRP A 228     8091  12300  12265   1245   -934    314       C  
ATOM   1820  CH2 TRP A 228      45.892  69.507  52.788  1.00 88.40           C  
ANISOU 1820  CH2 TRP A 228     8470  12720  12397   1679   -996    410       C  
ATOM   1821  N   THR A 229      52.068  68.695  58.320  1.00 79.18           N  
ANISOU 1821  N   THR A 229     8284  10560  11240     46   -686    331       N  
ATOM   1822  CA  THR A 229      52.166  68.453  59.744  1.00 78.02           C  
ANISOU 1822  CA  THR A 229     8086  10637  10919    -37   -641    335       C  
ATOM   1823  C   THR A 229      52.041  69.724  60.605  1.00 78.01           C  
ANISOU 1823  C   THR A 229     8265  10637  10735    -86   -476    109       C  
ATOM   1824  O   THR A 229      51.201  69.772  61.483  1.00 80.13           O  
ANISOU 1824  O   THR A 229     8506  11017  10920    -13   -363    100       O  
ATOM   1825  CB  THR A 229      53.400  67.636  60.095  1.00 74.49           C  
ANISOU 1825  CB  THR A 229     7536  10402  10363   -139   -763    433       C  
ATOM   1826  OG1 THR A 229      53.262  66.332  59.517  1.00 72.47           O  
ANISOU 1826  OG1 THR A 229     7167  10068  10301    -54   -816    649       O  
ATOM   1827  CG2 THR A 229      53.534  67.510  61.574  1.00 75.02           C  
ANISOU 1827  CG2 THR A 229     7555  10804  10145   -164   -727    458       C  
ATOM   1828  N   LYS A 230      52.829  70.765  60.320  1.00 78.69           N  
ANISOU 1828  N   LYS A 230     8558  10566  10773   -235   -404   -104       N  
ATOM   1829  CA  LYS A 230      52.574  72.079  60.945  1.00 88.10           C  
ANISOU 1829  CA  LYS A 230    10016  11600  11857   -292   -147   -379       C  
ATOM   1830  C   LYS A 230      51.075  72.496  60.818  1.00 93.21           C  
ANISOU 1830  C   LYS A 230    10747  12049  12620     69     16   -302       C  
ATOM   1831  O   LYS A 230      50.479  73.088  61.738  1.00 91.45           O  
ANISOU 1831  O   LYS A 230    10625  11834  12286    124    219   -458       O  
ATOM   1832  CB  LYS A 230      53.463  73.159  60.338  1.00 87.39           C  
ANISOU 1832  CB  LYS A 230    10214  11195  11796   -514     12   -603       C  
ATOM   1833  CG  LYS A 230      54.904  73.093  60.784  1.00103.61           C  
ANISOU 1833  CG  LYS A 230    12140  13565  13662   -941    -71   -835       C  
ATOM   1834  CD  LYS A 230      55.551  74.481  60.795  1.00114.78           C  
ANISOU 1834  CD  LYS A 230    13887  14683  15042  -1316    252  -1249       C  
ATOM   1835  CE  LYS A 230      57.040  74.414  60.442  1.00116.53           C  
ANISOU 1835  CE  LYS A 230    13938  15139  15198  -1732    171  -1425       C  
ATOM   1836  NZ  LYS A 230      57.245  73.906  59.046  1.00118.66           N  
ANISOU 1836  NZ  LYS A 230    14176  15220  15687  -1550     59  -1103       N  
ATOM   1837  N   LEU A 231      50.483  72.161  59.680  1.00 89.81           N  
ANISOU 1837  N   LEU A 231    10229  11520  12374    329    -76    -86       N  
ATOM   1838  CA  LEU A 231      49.191  72.674  59.310  1.00 88.15           C  
ANISOU 1838  CA  LEU A 231    10042  11214  12236    733     51    -15       C  
ATOM   1839  C   LEU A 231      48.082  71.961  60.082  1.00 93.25           C  
ANISOU 1839  C   LEU A 231    10361  12202  12867    831     35     33       C  
ATOM   1840  O   LEU A 231      47.112  72.587  60.481  1.00102.16           O  
ANISOU 1840  O   LEU A 231    11506  13342  13966   1100    228    -19       O  
ATOM   1841  CB  LEU A 231      48.988  72.530  57.805  1.00 80.57           C  
ANISOU 1841  CB  LEU A 231     9028  10194  11388    972    -79    170       C  
ATOM   1842  CG  LEU A 231      48.372  73.698  57.051  1.00 80.14           C  
ANISOU 1842  CG  LEU A 231     9237   9882  11329   1430    119    253       C  
ATOM   1843  CD1 LEU A 231      48.947  75.048  57.479  1.00 80.05           C  
ANISOU 1843  CD1 LEU A 231     9759   9369  11284   1367    486     97       C  
ATOM   1844  CD2 LEU A 231      48.594  73.456  55.578  1.00 80.39           C  
ANISOU 1844  CD2 LEU A 231     9237   9931  11377   1565    -48    435       C  
ATOM   1845  N   VAL A 232      48.242  70.656  60.302  1.00 85.01           N  
ANISOU 1845  N   VAL A 232     9043  11409  11847    620   -139    140       N  
ATOM   1846  CA  VAL A 232      47.360  69.916  61.211  1.00 82.06           C  
ANISOU 1846  CA  VAL A 232     8416  11318  11444    598    -71    189       C  
ATOM   1847  C   VAL A 232      47.418  70.506  62.636  1.00 88.35           C  
ANISOU 1847  C   VAL A 232     9365  12195  12007    538    123     49       C  
ATOM   1848  O   VAL A 232      46.398  70.652  63.289  1.00 97.59           O  
ANISOU 1848  O   VAL A 232    10430  13520  13129    671    301     12       O  
ATOM   1849  CB  VAL A 232      47.723  68.408  61.249  1.00 75.46           C  
ANISOU 1849  CB  VAL A 232     7395  10599  10676    363   -196    363       C  
ATOM   1850  CG1 VAL A 232      46.893  67.663  62.274  1.00 70.24           C  
ANISOU 1850  CG1 VAL A 232     6556  10159   9972    293    -30    446       C  
ATOM   1851  CG2 VAL A 232      47.562  67.778  59.875  1.00 72.70           C  
ANISOU 1851  CG2 VAL A 232     6885  10192  10544    374   -347    411       C  
ATOM   1852  N   LYS A 233      48.616  70.852  63.101  1.00 90.28           N  
ANISOU 1852  N   LYS A 233     9819  12404  12079    321     95    -69       N  
ATOM   1853  CA  LYS A 233      48.784  71.371  64.458  1.00 92.66           C  
ANISOU 1853  CA  LYS A 233    10239  12882  12084    204    255   -275       C  
ATOM   1854  C   LYS A 233      48.115  72.729  64.652  1.00 92.72           C  
ANISOU 1854  C   LYS A 233    10491  12654  12085    379    549   -539       C  
ATOM   1855  O   LYS A 233      47.592  73.001  65.703  1.00 95.38           O  
ANISOU 1855  O   LYS A 233    10843  13161  12234    405    743   -679       O  
ATOM   1856  CB  LYS A 233      50.267  71.463  64.839  1.00 97.02           C  
ANISOU 1856  CB  LYS A 233    10876  13578  12408   -104    133   -421       C  
ATOM   1857  CG  LYS A 233      50.910  70.137  65.201  1.00101.73           C  
ANISOU 1857  CG  LYS A 233    11241  14541  12869   -175    -82   -147       C  
ATOM   1858  CD  LYS A 233      52.251  70.353  65.907  1.00115.26           C  
ANISOU 1858  CD  LYS A 233    12940  16634  14219   -414   -192   -342       C  
ATOM   1859  CE  LYS A 233      53.268  69.252  65.567  1.00119.81           C  
ANISOU 1859  CE  LYS A 233    13315  17429  14776   -393   -447    -59       C  
ATOM   1860  NZ  LYS A 233      54.017  69.520  64.289  1.00120.27           N  
ANISOU 1860  NZ  LYS A 233    13400  17204  15091   -495   -550   -142       N  
ATOM   1861  N   ARG A 234      48.148  73.586  63.636  1.00 94.24           N  
ANISOU 1861  N   ARG A 234    10910  12430  12464    534    625   -588       N  
ATOM   1862  CA  ARG A 234      47.560  74.928  63.765  1.00100.97           C  
ANISOU 1862  CA  ARG A 234    12090  12940  13330    785    986   -798       C  
ATOM   1863  C   ARG A 234      46.061  74.856  63.910  1.00105.76           C  
ANISOU 1863  C   ARG A 234    12477  13714  13992   1223   1103   -676       C  
ATOM   1864  O   ARG A 234      45.454  75.718  64.516  1.00109.85           O  
ANISOU 1864  O   ARG A 234    13176  14114  14444   1440   1428   -863       O  
ATOM   1865  CB  ARG A 234      47.901  75.795  62.571  1.00106.18           C  
ANISOU 1865  CB  ARG A 234    13091  13079  14170    934   1092   -770       C  
ATOM   1866  CG  ARG A 234      49.338  76.250  62.546  1.00120.80           C  
ANISOU 1866  CG  ARG A 234    15229  14702  15967    453   1136  -1015       C  
ATOM   1867  CD  ARG A 234      49.471  77.582  61.839  1.00134.55           C  
ANISOU 1867  CD  ARG A 234    17511  15766  17845    586   1520  -1105       C  
ATOM   1868  NE  ARG A 234      49.078  78.693  62.701  1.00138.76           N  
ANISOU 1868  NE  ARG A 234    18430  15973  18317    636   1986  -1441       N  
ATOM   1869  CZ  ARG A 234      47.881  79.263  62.685  1.00140.53           C  
ANISOU 1869  CZ  ARG A 234    18800  15978  18614   1226   2258  -1330       C  
ATOM   1870  NH1 ARG A 234      46.947  78.819  61.849  1.00139.10           N  
ANISOU 1870  NH1 ARG A 234    18342  15974  18535   1796   2066   -901       N  
ATOM   1871  NH2 ARG A 234      47.617  80.282  63.501  1.00143.00           N  
ANISOU 1871  NH2 ARG A 234    19512  15942  18877   1255   2735  -1682       N  
ATOM   1872  N   HIS A 235      45.470  73.815  63.345  1.00106.38           N  
ANISOU 1872  N   HIS A 235    12140  14089  14190   1330    866   -404       N  
ATOM   1873  CA  HIS A 235      44.038  73.673  63.322  1.00107.08           C  
ANISOU 1873  CA  HIS A 235    11896  14451  14336   1701    951   -316       C  
ATOM   1874  C   HIS A 235      43.635  72.420  64.108  1.00114.40           C  
ANISOU 1874  C   HIS A 235    12433  15826  15205   1430    885   -241       C  
ATOM   1875  O   HIS A 235      43.043  71.467  63.564  1.00114.78           O  
ANISOU 1875  O   HIS A 235    12087  16132  15391   1407    745    -91       O  
ATOM   1876  CB  HIS A 235      43.560  73.691  61.880  1.00104.03           C  
ANISOU 1876  CB  HIS A 235    11345  14064  14115   2060    800   -129       C  
ATOM   1877  CG  HIS A 235      44.142  74.830  61.083  1.00107.89           C  
ANISOU 1877  CG  HIS A 235    12311  14046  14636   2299    904   -115       C  
ATOM   1878  ND1 HIS A 235      44.871  74.639  59.926  1.00103.80           N  
ANISOU 1878  ND1 HIS A 235    11875  13374  14190   2226    690     26       N  
ATOM   1879  CD2 HIS A 235      44.169  76.168  61.328  1.00110.84           C  
ANISOU 1879  CD2 HIS A 235    13167  13967  14979   2564   1270   -237       C  
ATOM   1880  CE1 HIS A 235      45.282  75.813  59.468  1.00108.28           C  
ANISOU 1880  CE1 HIS A 235    12943  13434  14764   2444    924     32       C  
ATOM   1881  NE2 HIS A 235      44.869  76.756  60.300  1.00110.88           N  
ANISOU 1881  NE2 HIS A 235    13547  13533  15050   2646   1296   -130       N  
ATOM   1882  N   SER A 236      43.999  72.465  65.410  1.00120.56           N  
ANISOU 1882  N   SER A 236    13361  16692  15751   1200   1029   -371       N  
ATOM   1883  CA  SER A 236      43.827  71.384  66.422  1.00115.98           C  
ANISOU 1883  CA  SER A 236    12561  16486  15018    942   1055   -258       C  
ATOM   1884  C   SER A 236      44.505  70.050  66.108  1.00110.10           C  
ANISOU 1884  C   SER A 236    11697  15791  14344    651    812      2       C  
ATOM   1885  O   SER A 236      43.935  69.184  65.446  1.00112.96           O  
ANISOU 1885  O   SER A 236    11778  16211  14931    623    752    156       O  
ATOM   1886  CB  SER A 236      42.362  71.212  66.811  1.00121.00           C  
ANISOU 1886  CB  SER A 236    12858  17431  15683   1128   1290   -250       C  
ATOM   1887  OG  SER A 236      41.940  72.311  67.593  1.00122.69           O  
ANISOU 1887  OG  SER A 236    13244  17647  15723   1358   1584   -497       O  
TER    1888      SER A 236                                                      
ATOM   1889  N   GLY B   2     100.272  77.824  56.040  1.00137.25           N  
ANISOU 1889  N   GLY B   2    13863  16889  21396   -797   1425    620       N  
ATOM   1890  CA  GLY B   2     101.108  76.673  55.625  1.00126.53           C  
ANISOU 1890  CA  GLY B   2    12698  15957  19419   -822   1016    565       C  
ATOM   1891  C   GLY B   2     101.622  75.904  56.827  1.00126.91           C  
ANISOU 1891  C   GLY B   2    12822  16201  19194  -1038    670     51       C  
ATOM   1892  O   GLY B   2     102.024  74.750  56.700  1.00129.09           O  
ANISOU 1892  O   GLY B   2    13156  16714  19178   -992    427    130       O  
ATOM   1893  N   SER B   3     101.574  76.535  58.005  1.00122.80           N  
ANISOU 1893  N   SER B   3    12222  15619  18816  -1375    747   -424       N  
ATOM   1894  CA  SER B   3     102.203  75.988  59.195  1.00119.23           C  
ANISOU 1894  CA  SER B   3    11662  15655  17986  -1815    354   -732       C  
ATOM   1895  C   SER B   3     101.795  74.535  59.465  1.00116.92           C  
ANISOU 1895  C   SER B   3    11451  15778  17194  -1653   -125   -435       C  
ATOM   1896  O   SER B   3     100.626  74.179  59.365  1.00119.83           O  
ANISOU 1896  O   SER B   3    12072  16118  17337  -1448   -133   -399       O  
ATOM   1897  CB  SER B   3     101.888  76.852  60.403  1.00122.95           C  
ANISOU 1897  CB  SER B   3    12104  16191  18417  -2470    620  -1433       C  
ATOM   1898  OG  SER B   3     102.178  76.149  61.599  1.00133.49           O  
ANISOU 1898  OG  SER B   3    13302  18360  19058  -3045     98  -1555       O  
ATOM   1899  N   LEU B   4     102.769  73.701  59.800  1.00119.85           N  
ANISOU 1899  N   LEU B   4    11505  16490  17540  -1740   -458   -112       N  
ATOM   1900  CA  LEU B   4     102.506  72.287  60.009  1.00124.03           C  
ANISOU 1900  CA  LEU B   4    11964  17227  17934  -1531   -723    305       C  
ATOM   1901  C   LEU B   4     101.509  72.076  61.142  1.00132.56           C  
ANISOU 1901  C   LEU B   4    13143  18769  18455  -1810  -1023    139       C  
ATOM   1902  O   LEU B   4     100.627  71.219  61.053  1.00132.43           O  
ANISOU 1902  O   LEU B   4    13327  18696  18293  -1529  -1061    257       O  
ATOM   1903  CB  LEU B   4     103.800  71.524  60.297  1.00126.20           C  
ANISOU 1903  CB  LEU B   4    11615  17713  18622  -1569   -914    958       C  
ATOM   1904  CG  LEU B   4     103.646  70.135  60.939  1.00128.89           C  
ANISOU 1904  CG  LEU B   4    11587  18319  19065  -1461  -1153   1617       C  
ATOM   1905  CD1 LEU B   4     103.388  70.226  62.443  1.00134.86           C  
ANISOU 1905  CD1 LEU B   4    12054  20052  19133  -2073  -1765   1772       C  
ATOM   1906  CD2 LEU B   4     102.555  69.326  60.252  1.00121.42           C  
ANISOU 1906  CD2 LEU B   4    11128  16883  18123  -1041   -799   1393       C  
ATOM   1907  N   ALA B   5     101.681  72.835  62.222  1.00140.15           N  
ANISOU 1907  N   ALA B   5    13953  20236  19061  -2493  -1166   -210       N  
ATOM   1908  CA  ALA B   5     100.764  72.775  63.356  1.00137.02           C  
ANISOU 1908  CA  ALA B   5    13671  20343  18046  -2961  -1329   -526       C  
ATOM   1909  C   ALA B   5      99.361  73.076  62.842  1.00132.43           C  
ANISOU 1909  C   ALA B   5    13613  19112  17589  -2538   -923   -903       C  
ATOM   1910  O   ALA B   5      98.383  72.445  63.246  1.00125.67           O  
ANISOU 1910  O   ALA B   5    12926  18403  16419  -2452  -1067   -868       O  
ATOM   1911  CB  ALA B   5     101.173  73.785  64.430  1.00136.80           C  
ANISOU 1911  CB  ALA B   5    13477  20930  17571  -4037  -1251  -1167       C  
ATOM   1912  N   TRP B   6      99.292  74.034  61.926  1.00126.14           N  
ANISOU 1912  N   TRP B   6    12961  17642  17321  -2275   -426  -1092       N  
ATOM   1913  CA  TRP B   6      98.073  74.380  61.264  1.00116.17           C  
ANISOU 1913  CA  TRP B   6    11949  15849  16341  -1856    -67  -1059       C  
ATOM   1914  C   TRP B   6      97.483  73.174  60.550  1.00111.09           C  
ANISOU 1914  C   TRP B   6    11458  15316  15432  -1370   -379   -560       C  
ATOM   1915  O   TRP B   6      96.509  72.621  60.992  1.00113.41           O  
ANISOU 1915  O   TRP B   6    11898  15764  15426  -1339   -518   -574       O  
ATOM   1916  CB  TRP B   6      98.335  75.486  60.287  1.00116.70           C  
ANISOU 1916  CB  TRP B   6    11915  15328  17099  -1645    436   -951       C  
ATOM   1917  CG  TRP B   6      97.159  76.061  59.734  1.00119.79           C  
ANISOU 1917  CG  TRP B   6    12293  15267  17954  -1327    845   -647       C  
ATOM   1918  CD1 TRP B   6      96.365  77.018  60.304  1.00125.40           C  
ANISOU 1918  CD1 TRP B   6    12902  15447  19296  -1485   1509   -943       C  
ATOM   1919  CD2 TRP B   6      96.610  75.786  58.458  1.00122.77           C  
ANISOU 1919  CD2 TRP B   6    12626  15709  18312   -888    730    133       C  
ATOM   1920  NE1 TRP B   6      95.349  77.353  59.452  1.00127.54           N  
ANISOU 1920  NE1 TRP B   6    12953  15383  20123  -1015   1763   -148       N  
ATOM   1921  CE2 TRP B   6      95.474  76.609  58.307  1.00128.05           C  
ANISOU 1921  CE2 TRP B   6    13043  15970  19640   -718   1193    554       C  
ATOM   1922  CE3 TRP B   6      96.959  74.913  57.418  1.00122.89           C  
ANISOU 1922  CE3 TRP B   6    12732  16140  17818   -757    379    513       C  
ATOM   1923  CZ2 TRP B   6      94.687  76.584  57.166  1.00132.70           C  
ANISOU 1923  CZ2 TRP B   6    13376  16799  20242   -449   1101   1561       C  
ATOM   1924  CZ3 TRP B   6      96.179  74.891  56.286  1.00125.67           C  
ANISOU 1924  CZ3 TRP B   6    12972  16765  18012   -650    374   1218       C  
ATOM   1925  CH2 TRP B   6      95.052  75.718  56.166  1.00131.62           C  
ANISOU 1925  CH2 TRP B   6    13384  17348  19275   -508    624   1847       C  
ATOM   1926  N   TRP B   7      98.100  72.742  59.471  1.00108.26           N  
ANISOU 1926  N   TRP B   7    11073  14889  15172  -1109   -389   -227       N  
ATOM   1927  CA  TRP B   7      97.558  71.612  58.731  1.00106.07           C  
ANISOU 1927  CA  TRP B   7    10963  14720  14618   -897   -452     10       C  
ATOM   1928  C   TRP B   7      97.044  70.509  59.644  1.00108.28           C  
ANISOU 1928  C   TRP B   7    11291  15239  14612   -919   -724    -22       C  
ATOM   1929  O   TRP B   7      96.296  69.644  59.213  1.00115.23           O  
ANISOU 1929  O   TRP B   7    12344  16173  15263   -826   -691     32       O  
ATOM   1930  CB  TRP B   7      98.591  71.031  57.787  1.00107.00           C  
ANISOU 1930  CB  TRP B   7    11013  14730  14909   -848   -256    129       C  
ATOM   1931  CG  TRP B   7      98.700  71.785  56.585  1.00108.12           C  
ANISOU 1931  CG  TRP B   7    11185  14807  15086   -863     10    258       C  
ATOM   1932  CD1 TRP B   7      99.605  72.739  56.324  1.00113.62           C  
ANISOU 1932  CD1 TRP B   7    11707  15289  16173   -855    161    307       C  
ATOM   1933  CD2 TRP B   7      97.837  71.720  55.451  1.00110.90           C  
ANISOU 1933  CD2 TRP B   7    11667  15470  15000   -995    135    478       C  
ATOM   1934  NE1 TRP B   7      99.390  73.273  55.083  1.00118.13           N  
ANISOU 1934  NE1 TRP B   7    12275  15957  16649   -897    388    617       N  
ATOM   1935  CE2 TRP B   7      98.303  72.663  54.525  1.00115.26           C  
ANISOU 1935  CE2 TRP B   7    12063  16030  15701  -1048    335    781       C  
ATOM   1936  CE3 TRP B   7      96.721  70.945  55.120  1.00114.31           C  
ANISOU 1936  CE3 TRP B   7    12269  16303  14858  -1181     81    506       C  
ATOM   1937  CZ2 TRP B   7      97.697  72.864  53.288  1.00118.82           C  
ANISOU 1937  CZ2 TRP B   7    12448  17032  15665  -1337    416   1259       C  
ATOM   1938  CZ3 TRP B   7      96.114  71.147  53.883  1.00119.21           C  
ANISOU 1938  CZ3 TRP B   7    12850  17511  14930  -1546    160    881       C  
ATOM   1939  CH2 TRP B   7      96.606  72.100  52.987  1.00120.47           C  
ANISOU 1939  CH2 TRP B   7    12779  17818  15173  -1646    292   1325       C  
ATOM   1940  N   LYS B   8      97.483  70.520  60.897  1.00112.86           N  
ANISOU 1940  N   LYS B   8    11660  16073  15147  -1155   -982    -76       N  
ATOM   1941  CA  LYS B   8      96.980  69.577  61.891  1.00112.05           C  
ANISOU 1941  CA  LYS B   8    11500  16322  14750  -1235  -1280     49       C  
ATOM   1942  C   LYS B   8      95.541  69.949  62.267  1.00106.44           C  
ANISOU 1942  C   LYS B   8    11104  15619  13718  -1284  -1241   -272       C  
ATOM   1943  O   LYS B   8      94.653  69.101  62.226  1.00101.97           O  
ANISOU 1943  O   LYS B   8    10686  15078  12977  -1101  -1307   -167       O  
ATOM   1944  CB  LYS B   8      97.903  69.562  63.132  1.00119.86           C  
ANISOU 1944  CB  LYS B   8    12031  17911  15598  -1698  -1643    267       C  
ATOM   1945  CG  LYS B   8      97.548  68.532  64.220  1.00122.87           C  
ANISOU 1945  CG  LYS B   8    12157  18857  15668  -1855  -2021    694       C  
ATOM   1946  CD  LYS B   8      98.789  68.134  65.028  1.00135.37           C  
ANISOU 1946  CD  LYS B   8    12969  21161  17305  -2233  -2431   1493       C  
ATOM   1947  CE  LYS B   8      98.452  67.696  66.454  1.00136.76           C  
ANISOU 1947  CE  LYS B   8    12795  22360  16806  -2815  -2924   1893       C  
ATOM   1948  NZ  LYS B   8      99.687  67.579  67.304  1.00138.68           N  
ANISOU 1948  NZ  LYS B   8    12118  23692  16881  -3466  -3446   2838       N  
ATOM   1949  N   ARG B   9      95.338  71.237  62.604  1.00106.70           N  
ANISOU 1949  N   ARG B   9    11186  15520  13833  -1553   -990   -678       N  
ATOM   1950  CA  ARG B   9      94.022  71.824  62.941  1.00103.97           C  
ANISOU 1950  CA  ARG B   9    11022  14944  13538  -1597   -687   -961       C  
ATOM   1951  C   ARG B   9      93.069  71.720  61.775  1.00103.87           C  
ANISOU 1951  C   ARG B   9    11091  14647  13724  -1114   -585   -530       C  
ATOM   1952  O   ARG B   9      91.979  71.177  61.901  1.00104.92           O  
ANISOU 1952  O   ARG B   9    11339  14870  13655  -1000   -681   -420       O  
ATOM   1953  CB  ARG B   9      94.161  73.318  63.282  1.00107.92           C  
ANISOU 1953  CB  ARG B   9    11444  15047  14514  -1973    -72  -1481       C  
ATOM   1954  CG  ARG B   9      95.166  73.657  64.351  1.00125.03           C  
ANISOU 1954  CG  ARG B   9    13488  17679  16337  -2769    -82  -2039       C  
ATOM   1955  CD  ARG B   9      95.403  75.156  64.425  1.00134.48           C  
ANISOU 1955  CD  ARG B   9    14612  18304  18177  -3187    764  -2687       C  
ATOM   1956  NE  ARG B   9      95.923  75.542  65.738  1.00162.19           N  
ANISOU 1956  NE  ARG B   9    18072  22420  21131  -4344    948  -3548       N  
ATOM   1957  CZ  ARG B   9      95.205  75.540  66.875  1.00182.21           C  
ANISOU 1957  CZ  ARG B   9    20747  25292  23190  -5075   1221  -4203       C  
ATOM   1958  NH1 ARG B   9      93.914  75.160  66.869  1.00187.60           N  
ANISOU 1958  NH1 ARG B   9    21624  25608  24045  -4595   1329  -4037       N  
ATOM   1959  NH2 ARG B   9      95.771  75.925  68.024  1.00184.21           N  
ANISOU 1959  NH2 ARG B   9    20921  26360  22711  -6425   1413  -5050       N  
ATOM   1960  N   GLU B  10      93.472  72.308  60.653  1.00104.71           N  
ANISOU 1960  N   GLU B  10    11075  14534  14175   -936   -399   -225       N  
ATOM   1961  CA  GLU B  10      92.645  72.406  59.483  1.00106.23           C  
ANISOU 1961  CA  GLU B  10    11178  14752  14432   -708   -337    373       C  
ATOM   1962  C   GLU B  10      92.120  71.060  59.079  1.00107.04           C  
ANISOU 1962  C   GLU B  10    11472  15315  13882   -718   -667    484       C  
ATOM   1963  O   GLU B  10      90.927  70.909  58.817  1.00114.65           O  
ANISOU 1963  O   GLU B  10    12393  16484  14685   -701   -724    821       O  
ATOM   1964  CB  GLU B  10      93.436  72.996  58.332  1.00111.07           C  
ANISOU 1964  CB  GLU B  10    11603  15324  15273   -667   -190    733       C  
ATOM   1965  CG  GLU B  10      92.608  73.216  57.092  1.00122.07           C  
ANISOU 1965  CG  GLU B  10    12736  17055  16590   -637   -185   1583       C  
ATOM   1966  CD  GLU B  10      91.660  74.402  57.221  1.00133.96           C  
ANISOU 1966  CD  GLU B  10    13774  18152  18972   -436    194   2222       C  
ATOM   1967  OE1 GLU B  10      91.534  74.947  58.340  1.00141.80           O  
ANISOU 1967  OE1 GLU B  10    14790  18494  20592   -382    589   1710       O  
ATOM   1968  OE2 GLU B  10      91.048  74.794  56.199  1.00136.09           O  
ANISOU 1968  OE2 GLU B  10    13567  18782  19359   -422    187   3296       O  
ATOM   1969  N   LEU B  11      93.012  70.076  59.023  1.00102.49           N  
ANISOU 1969  N   LEU B  11    11028  14852  13061   -784   -778    232       N  
ATOM   1970  CA  LEU B  11      92.653  68.750  58.536  1.00102.13           C  
ANISOU 1970  CA  LEU B  11    11142  15061  12599   -892   -796    179       C  
ATOM   1971  C   LEU B  11      91.890  67.858  59.522  1.00 98.91           C  
ANISOU 1971  C   LEU B  11    10844  14695  12041   -834   -966     35       C  
ATOM   1972  O   LEU B  11      91.102  67.018  59.094  1.00100.70           O  
ANISOU 1972  O   LEU B  11    11194  15127  11938   -966   -915      3       O  
ATOM   1973  CB  LEU B  11      93.875  68.014  58.013  1.00102.63           C  
ANISOU 1973  CB  LEU B  11    11200  14979  12814   -977   -534     -3       C  
ATOM   1974  CG  LEU B  11      94.145  68.210  56.540  1.00107.82           C  
ANISOU 1974  CG  LEU B  11    11888  15847  13232  -1284   -234     30       C  
ATOM   1975  CD1 LEU B  11      95.590  67.846  56.236  1.00110.35           C  
ANISOU 1975  CD1 LEU B  11    12136  15785  14005  -1293    152   -179       C  
ATOM   1976  CD2 LEU B  11      93.180  67.367  55.712  1.00109.68           C  
ANISOU 1976  CD2 LEU B  11    12292  16580  12802  -1769    -61   -108       C  
ATOM   1977  N   PHE B  12      92.141  68.011  60.827  1.00 95.55           N  
ANISOU 1977  N   PHE B  12    10347  14187  11771   -771  -1141    -66       N  
ATOM   1978  CA  PHE B  12      91.623  67.035  61.820  1.00 93.84           C  
ANISOU 1978  CA  PHE B  12    10157  14103  11395   -759  -1318    -89       C  
ATOM   1979  C   PHE B  12      90.812  67.667  62.920  1.00 94.11           C  
ANISOU 1979  C   PHE B  12    10243  14240  11273   -870  -1434   -244       C  
ATOM   1980  O   PHE B  12      90.271  66.964  63.763  1.00 93.80           O  
ANISOU 1980  O   PHE B  12    10231  14389  11020   -910  -1591   -241       O  
ATOM   1981  CB  PHE B  12      92.758  66.210  62.443  1.00 95.82           C  
ANISOU 1981  CB  PHE B  12    10109  14392  11904   -757  -1399    132       C  
ATOM   1982  CG  PHE B  12      93.381  65.228  61.499  1.00104.21           C  
ANISOU 1982  CG  PHE B  12    11078  15120  13395   -643   -998    227       C  
ATOM   1983  CD1 PHE B  12      94.422  65.624  60.639  1.00106.86           C  
ANISOU 1983  CD1 PHE B  12    11336  15242  14024   -662   -741    197       C  
ATOM   1984  CD2 PHE B  12      92.936  63.906  61.451  1.00105.58           C  
ANISOU 1984  CD2 PHE B  12    11231  15097  13786   -582   -702    258       C  
ATOM   1985  CE1 PHE B  12      94.991  64.724  59.749  1.00105.16           C  
ANISOU 1985  CE1 PHE B  12    11049  14617  14286   -679   -131    123       C  
ATOM   1986  CE2 PHE B  12      93.512  63.000  60.566  1.00108.75           C  
ANISOU 1986  CE2 PHE B  12    11538  15010  14771   -614     -2    147       C  
ATOM   1987  CZ  PHE B  12      94.543  63.411  59.717  1.00109.37           C  
ANISOU 1987  CZ  PHE B  12    11562  14872  15120   -691    317     45       C  
ATOM   1988  N   GLY B  13      90.727  68.994  62.914  1.00 93.67           N  
ANISOU 1988  N   GLY B  13    10167  13984  11436   -959  -1216   -400       N  
ATOM   1989  CA  GLY B  13      90.177  69.733  64.048  1.00 98.58           C  
ANISOU 1989  CA  GLY B  13    10816  14550  12088  -1246  -1011   -782       C  
ATOM   1990  C   GLY B  13      88.693  70.042  63.942  1.00102.69           C  
ANISOU 1990  C   GLY B  13    11382  14773  12862  -1072   -739   -686       C  
ATOM   1991  O   GLY B  13      88.197  70.407  62.863  1.00100.88           O  
ANISOU 1991  O   GLY B  13    11008  14345  12976   -791   -617   -202       O  
ATOM   1992  N   GLY B  14      87.987  69.878  65.072  1.00102.87           N  
ANISOU 1992  N   GLY B  14    11515  14875  12695  -1310   -654  -1026       N  
ATOM   1993  CA  GLY B  14      86.570  70.268  65.206  1.00104.70           C  
ANISOU 1993  CA  GLY B  14    11721  14713  13347  -1189   -249   -971       C  
ATOM   1994  C   GLY B  14      85.559  69.580  64.287  1.00 97.07           C  
ANISOU 1994  C   GLY B  14    10687  13852  12341   -769   -540   -293       C  
ATOM   1995  O   GLY B  14      84.638  70.233  63.793  1.00 94.55           O  
ANISOU 1995  O   GLY B  14    10078  13203  12640   -569   -219    200       O  
ATOM   1996  N   TRP B  15      85.747  68.274  64.054  1.00 91.00           N  
ANISOU 1996  N   TRP B  15    10083  13555  10935   -716  -1058   -207       N  
ATOM   1997  CA  TRP B  15      84.753  67.436  63.394  1.00 89.56           C  
ANISOU 1997  CA  TRP B  15     9901  13617  10508   -587  -1270    168       C  
ATOM   1998  C   TRP B  15      83.821  66.893  64.436  1.00 91.51           C  
ANISOU 1998  C   TRP B  15    10280  13867  10621   -601  -1285    -26       C  
ATOM   1999  O   TRP B  15      84.251  66.465  65.503  1.00 94.90           O  
ANISOU 1999  O   TRP B  15    10852  14407  10796   -753  -1366   -391       O  
ATOM   2000  CB  TRP B  15      85.413  66.243  62.691  1.00 92.75           C  
ANISOU 2000  CB  TRP B  15    10428  14344  10470   -653  -1505    130       C  
ATOM   2001  CG  TRP B  15      86.323  66.600  61.545  1.00102.70           C  
ANISOU 2001  CG  TRP B  15    11597  15675  11750   -732  -1444    263       C  
ATOM   2002  CD1 TRP B  15      87.680  66.522  61.533  1.00102.03           C  
ANISOU 2002  CD1 TRP B  15    11531  15465  11769   -737  -1399     59       C  
ATOM   2003  CD2 TRP B  15      85.934  67.056  60.225  1.00105.21           C  
ANISOU 2003  CD2 TRP B  15    11708  16328  11938   -898  -1432    745       C  
ATOM   2004  NE1 TRP B  15      88.165  66.934  60.316  1.00110.00           N  
ANISOU 2004  NE1 TRP B  15    12455  16583  12756   -853  -1290    232       N  
ATOM   2005  CE2 TRP B  15      87.116  67.265  59.496  1.00106.82           C  
ANISOU 2005  CE2 TRP B  15    11905  16544  12137  -1001  -1333    677       C  
ATOM   2006  CE3 TRP B  15      84.702  67.333  59.608  1.00104.26           C  
ANISOU 2006  CE3 TRP B  15    11297  16618  11698  -1029  -1527   1388       C  
ATOM   2007  CZ2 TRP B  15      87.112  67.737  58.174  1.00109.28           C  
ANISOU 2007  CZ2 TRP B  15    11986  17322  12212  -1289  -1320   1158       C  
ATOM   2008  CZ3 TRP B  15      84.700  67.798  58.290  1.00103.11           C  
ANISOU 2008  CZ3 TRP B  15    10811  17058  11308  -1349  -1589   2039       C  
ATOM   2009  CH2 TRP B  15      85.892  67.999  57.594  1.00106.58           C  
ANISOU 2009  CH2 TRP B  15    11307  17550  11637  -1500  -1482   1886       C  
ATOM   2010  N   THR B  16      82.534  66.886  64.129  1.00 95.55           N  
ANISOU 2010  N   THR B  16    10659  14377  11268   -502  -1241    344       N  
ATOM   2011  CA  THR B  16      81.558  66.186  64.970  1.00 93.05           C  
ANISOU 2011  CA  THR B  16    10476  14093  10786   -498  -1278    198       C  
ATOM   2012  C   THR B  16      81.715  64.689  64.748  1.00 88.08           C  
ANISOU 2012  C   THR B  16    10030  13838   9599   -544  -1611    110       C  
ATOM   2013  O   THR B  16      82.291  64.271  63.731  1.00 84.70           O  
ANISOU 2013  O   THR B  16     9592  13611   8979   -638  -1689    173       O  
ATOM   2014  CB  THR B  16      80.128  66.602  64.617  1.00 95.15           C  
ANISOU 2014  CB  THR B  16    10426  14248  11476   -376  -1118    767       C  
ATOM   2015  OG1 THR B  16      79.836  66.230  63.248  1.00 99.02           O  
ANISOU 2015  OG1 THR B  16    10682  15297  11642   -475  -1448   1382       O  
ATOM   2016  CG2 THR B  16      79.956  68.125  64.806  1.00 98.83           C  
ANISOU 2016  CG2 THR B  16    10548  14053  12947   -273   -481    966       C  
ATOM   2017  N   HIS B  17      81.217  63.879  65.689  1.00 81.97           N  
ANISOU 2017  N   HIS B  17     9391  13096   8657   -536  -1665    -64       N  
ATOM   2018  CA  HIS B  17      81.260  62.428  65.518  1.00 79.32           C  
ANISOU 2018  CA  HIS B  17     9131  12912   8093   -550  -1762   -101       C  
ATOM   2019  C   HIS B  17      80.589  62.040  64.228  1.00 86.32           C  
ANISOU 2019  C   HIS B  17     9979  14028   8791   -735  -1735      5       C  
ATOM   2020  O   HIS B  17      81.094  61.188  63.499  1.00 91.04           O  
ANISOU 2020  O   HIS B  17    10623  14694   9271   -950  -1570   -202       O  
ATOM   2021  CB  HIS B  17      80.593  61.722  66.669  1.00 79.26           C  
ANISOU 2021  CB  HIS B  17     9185  12914   8014   -503  -1794   -143       C  
ATOM   2022  CG  HIS B  17      80.559  60.233  66.520  1.00 86.07           C  
ANISOU 2022  CG  HIS B  17    10033  13753   8915   -480  -1711   -124       C  
ATOM   2023  ND1 HIS B  17      79.591  59.576  65.785  1.00 86.21           N  
ANISOU 2023  ND1 HIS B  17    10105  13812   8838   -611  -1581   -223       N  
ATOM   2024  CD2 HIS B  17      81.367  59.268  67.021  1.00 90.13           C  
ANISOU 2024  CD2 HIS B  17    10379  14171   9694   -396  -1621     48       C  
ATOM   2025  CE1 HIS B  17      79.805  58.274  65.839  1.00 87.36           C  
ANISOU 2025  CE1 HIS B  17    10206  13750   9236   -624  -1285   -317       C  
ATOM   2026  NE2 HIS B  17      80.876  58.060  66.582  1.00 93.82           N  
ANISOU 2026  NE2 HIS B  17    10836  14412  10397   -417  -1281    -49       N  
ATOM   2027  N   PHE B  18      79.443  62.684  63.947  1.00 90.80           N  
ANISOU 2027  N   PHE B  18     9215  13983  11301   2465    163    621       N  
ATOM   2028  CA  PHE B  18      78.682  62.484  62.692  1.00 87.11           C  
ANISOU 2028  CA  PHE B  18     8805  13277  11014   2192     85    632       C  
ATOM   2029  C   PHE B  18      79.487  62.744  61.397  1.00 89.12           C  
ANISOU 2029  C   PHE B  18     9219  13374  11266   2025     -9    395       C  
ATOM   2030  O   PHE B  18      79.701  61.799  60.591  1.00 88.56           O  
ANISOU 2030  O   PHE B  18     9256  13111  11278   1835      7    339       O  
ATOM   2031  CB  PHE B  18      77.387  63.318  62.688  1.00 82.62           C  
ANISOU 2031  CB  PHE B  18     8097  12829  10462   2188     52    753       C  
ATOM   2032  CG  PHE B  18      76.433  62.941  61.588  1.00 77.60           C  
ANISOU 2032  CG  PHE B  18     7392  12158   9934   1893    -49    863       C  
ATOM   2033  CD1 PHE B  18      75.657  61.776  61.684  1.00 79.21           C  
ANISOU 2033  CD1 PHE B  18     7501  12312  10282   1711    -19   1030       C  
ATOM   2034  CD2 PHE B  18      76.343  63.713  60.429  1.00 77.27           C  
ANISOU 2034  CD2 PHE B  18     7332  12182   9842   1770   -161    808       C  
ATOM   2035  CE1 PHE B  18      74.797  61.409  60.653  1.00 80.53           C  
ANISOU 2035  CE1 PHE B  18     7559  12538  10498   1340   -141   1044       C  
ATOM   2036  CE2 PHE B  18      75.487  63.344  59.391  1.00 76.32           C  
ANISOU 2036  CE2 PHE B  18     7076  12219   9703   1461   -291    901       C  
ATOM   2037  CZ  PHE B  18      74.710  62.198  59.509  1.00 78.37           C  
ANISOU 2037  CZ  PHE B  18     7244  12471  10061   1210   -303    970       C  
ATOM   2038  N   GLU B  19      79.901  64.016  61.189  1.00 84.91           N  
ANISOU 2038  N   GLU B  19     8693  12897  10669   2093    -58    249       N  
ATOM   2039  CA  GLU B  19      80.738  64.401  60.037  1.00 82.28           C  
ANISOU 2039  CA  GLU B  19     8463  12461  10335   1999   -117     98       C  
ATOM   2040  C   GLU B  19      81.868  63.407  59.870  1.00 84.87           C  
ANISOU 2040  C   GLU B  19     8927  12674  10644   1987    -74     20       C  
ATOM   2041  O   GLU B  19      82.141  62.953  58.772  1.00 92.63           O  
ANISOU 2041  O   GLU B  19    10024  13540  11632   1841    -83    -55       O  
ATOM   2042  CB  GLU B  19      81.342  65.782  60.237  1.00 82.43           C  
ANISOU 2042  CB  GLU B  19     8451  12485  10384   2115    -81    -38       C  
ATOM   2043  CG  GLU B  19      80.365  66.927  60.257  1.00 90.45           C  
ANISOU 2043  CG  GLU B  19     9344  13500  11520   2178     -3     58       C  
ATOM   2044  CD  GLU B  19      80.894  68.146  61.021  1.00 96.66           C  
ANISOU 2044  CD  GLU B  19    10112  14203  12408   2288    148   -185       C  
ATOM   2045  OE1 GLU B  19      80.104  69.089  61.281  1.00105.96           O  
ANISOU 2045  OE1 GLU B  19    11209  15300  13750   2388    326   -135       O  
ATOM   2046  OE2 GLU B  19      82.087  68.166  61.366  1.00 91.23           O  
ANISOU 2046  OE2 GLU B  19     9473  13534  11655   2259    122   -436       O  
ATOM   2047  N   ALA B  20      82.537  63.090  60.975  1.00 83.45           N  
ANISOU 2047  N   ALA B  20     8703  12586  10415   2165      2     61       N  
ATOM   2048  CA  ALA B  20      83.629  62.146  60.966  1.00 84.03           C  
ANISOU 2048  CA  ALA B  20     8838  12584  10504   2240    114    119       C  
ATOM   2049  C   ALA B  20      83.186  60.796  60.464  1.00 88.73           C  
ANISOU 2049  C   ALA B  20     9543  12885  11283   2124    265    206       C  
ATOM   2050  O   ALA B  20      83.795  60.240  59.538  1.00 91.64           O  
ANISOU 2050  O   ALA B  20    10074  13021  11725   2041    363    100       O  
ATOM   2051  CB  ALA B  20      84.215  62.016  62.346  1.00 89.71           C  
ANISOU 2051  CB  ALA B  20     9380  13620  11085   2476    176    271       C  
ATOM   2052  N   VAL B  21      82.124  60.259  61.067  1.00 87.97           N  
ANISOU 2052  N   VAL B  21     9357  12774  11290   2101    325    372       N  
ATOM   2053  CA  VAL B  21      81.682  58.928  60.730  1.00 92.74           C  
ANISOU 2053  CA  VAL B  21    10035  13031  12168   1943    531    426       C  
ATOM   2054  C   VAL B  21      81.349  58.823  59.272  1.00 96.59           C  
ANISOU 2054  C   VAL B  21    10688  13345  12665   1577    453     94       C  
ATOM   2055  O   VAL B  21      81.602  57.794  58.657  1.00105.83           O  
ANISOU 2055  O   VAL B  21    12017  14167  14024   1417    672    -57       O  
ATOM   2056  CB  VAL B  21      80.489  58.466  61.562  1.00 98.89           C  
ANISOU 2056  CB  VAL B  21    10641  13831  13098   1938    601    681       C  
ATOM   2057  CG1 VAL B  21      79.635  57.483  60.764  1.00103.43           C  
ANISOU 2057  CG1 VAL B  21    11287  14045  13966   1549    708    550       C  
ATOM   2058  CG2 VAL B  21      80.977  57.806  62.846  1.00104.92           C  
ANISOU 2058  CG2 VAL B  21    11248  14670  13945   2300    857   1090       C  
ATOM   2059  N   TRP B  22      80.823  59.897  58.697  1.00 91.56           N  
ANISOU 2059  N   TRP B  22     9995  12978  11816   1458    185    -13       N  
ATOM   2060  CA  TRP B  22      80.458  59.870  57.277  1.00 95.26           C  
ANISOU 2060  CA  TRP B  22    10531  13491  12170   1118     76   -276       C  
ATOM   2061  C   TRP B  22      81.637  60.083  56.311  1.00 96.63           C  
ANISOU 2061  C   TRP B  22    10878  13637  12200   1154     97   -477       C  
ATOM   2062  O   TRP B  22      81.872  59.282  55.402  1.00 97.10           O  
ANISOU 2062  O   TRP B  22    11104  13539  12248    936    215   -753       O  
ATOM   2063  CB  TRP B  22      79.318  60.840  56.987  1.00 91.37           C  
ANISOU 2063  CB  TRP B  22     9818  13381  11515   1012   -167   -163       C  
ATOM   2064  CG  TRP B  22      78.013  60.258  57.316  1.00 91.19           C  
ANISOU 2064  CG  TRP B  22     9634  13401  11611    794   -181    -57       C  
ATOM   2065  CD1 TRP B  22      77.372  60.303  58.528  1.00 90.50           C  
ANISOU 2065  CD1 TRP B  22     9396  13319  11670    974   -130    236       C  
ATOM   2066  CD2 TRP B  22      77.196  59.480  56.457  1.00 93.34           C  
ANISOU 2066  CD2 TRP B  22     9850  13745  11867    324   -234   -259       C  
ATOM   2067  NE1 TRP B  22      76.188  59.616  58.463  1.00 92.29           N  
ANISOU 2067  NE1 TRP B  22     9461  13581  12022    668   -144    300       N  
ATOM   2068  CE2 TRP B  22      76.053  59.096  57.202  1.00 96.38           C  
ANISOU 2068  CE2 TRP B  22    10025  14142  12451    227   -220    -31       C  
ATOM   2069  CE3 TRP B  22      77.312  59.062  55.127  1.00 96.66           C  
ANISOU 2069  CE3 TRP B  22    10356  14276  12093    -54   -287   -648       C  
ATOM   2070  CZ2 TRP B  22      75.030  58.320  56.657  1.00101.16           C  
ANISOU 2070  CZ2 TRP B  22    10482  14839  13115   -281   -272   -181       C  
ATOM   2071  CZ3 TRP B  22      76.294  58.294  54.582  1.00107.03           C  
ANISOU 2071  CZ3 TRP B  22    11537  15731  13397   -580   -346   -873       C  
ATOM   2072  CH2 TRP B  22      75.162  57.933  55.348  1.00107.60           C  
ANISOU 2072  CH2 TRP B  22    11377  15785  13719   -713   -347   -639       C  
ATOM   2073  N   LEU B  23      82.362  61.166  56.496  1.00 92.22           N  
ANISOU 2073  N   LEU B  23    10270  13220  11546   1408     13   -368       N  
ATOM   2074  CA  LEU B  23      83.471  61.443  55.639  1.00 92.95           C  
ANISOU 2074  CA  LEU B  23    10474  13308  11533   1471     42   -477       C  
ATOM   2075  C   LEU B  23      84.445  60.245  55.570  1.00 94.21           C  
ANISOU 2075  C   LEU B  23    10839  13139  11815   1525    317   -576       C  
ATOM   2076  O   LEU B  23      85.021  59.973  54.516  1.00 95.46           O  
ANISOU 2076  O   LEU B  23    11149  13242  11878   1458    410   -765       O  
ATOM   2077  CB  LEU B  23      84.171  62.714  56.085  1.00 89.68           C  
ANISOU 2077  CB  LEU B  23     9944  13012  11116   1713    -32   -340       C  
ATOM   2078  CG  LEU B  23      85.612  62.936  55.692  1.00 86.58           C  
ANISOU 2078  CG  LEU B  23     9614  12570  10711   1857     43   -357       C  
ATOM   2079  CD1 LEU B  23      85.732  63.229  54.211  1.00 83.89           C  
ANISOU 2079  CD1 LEU B  23     9314  12340  10217   1766     17   -422       C  
ATOM   2080  CD2 LEU B  23      86.117  64.096  56.520  1.00 93.24           C  
ANISOU 2080  CD2 LEU B  23    10293  13504  11627   2007    -18   -281       C  
ATOM   2081  N   LEU B  24      84.590  59.508  56.670  1.00 88.71           N  
ANISOU 2081  N   LEU B  24    10125  12247  11333   1677    499   -403       N  
ATOM   2082  CA  LEU B  24      85.418  58.306  56.630  1.00 91.98           C  
ANISOU 2082  CA  LEU B  24    10694  12297  11958   1780    865   -387       C  
ATOM   2083  C   LEU B  24      84.762  57.202  55.816  1.00 93.88           C  
ANISOU 2083  C   LEU B  24    11130  12190  12350   1440   1075   -713       C  
ATOM   2084  O   LEU B  24      85.385  56.623  54.947  1.00 93.99           O  
ANISOU 2084  O   LEU B  24    11358  11961  12392   1385   1318   -955       O  
ATOM   2085  CB  LEU B  24      85.771  57.805  58.032  1.00 97.05           C  
ANISOU 2085  CB  LEU B  24    11180  12901  12791   2091   1057     13       C  
ATOM   2086  CG  LEU B  24      86.733  58.610  58.934  1.00 98.89           C  
ANISOU 2086  CG  LEU B  24    11192  13532  12846   2406    931    285       C  
ATOM   2087  CD1 LEU B  24      87.066  57.798  60.189  1.00102.11           C  
ANISOU 2087  CD1 LEU B  24    11400  14007  13389   2715   1188    736       C  
ATOM   2088  CD2 LEU B  24      88.012  59.056  58.218  1.00 87.63           C  
ANISOU 2088  CD2 LEU B  24     9817  12164  11312   2497    926    229       C  
HETATM 2089  N   MSE B  25      83.493  56.927  56.093  1.00100.27           N  
ANISOU 2089  N   MSE B  25    11852  12989  13255   1186    999   -754       N  
HETATM 2090  CA  MSE B  25      82.754  55.884  55.360  1.00107.51           C  
ANISOU 2090  CA  MSE B  25    12907  13603  14337    743   1182  -1148       C  
HETATM 2091  C   MSE B  25      82.716  56.189  53.878  1.00107.05           C  
ANISOU 2091  C   MSE B  25    12965  13811  13899    422   1016  -1615       C  
HETATM 2092  O   MSE B  25      82.660  55.278  53.056  1.00111.46           O  
ANISOU 2092  O   MSE B  25    13721  14109  14518     86   1258  -2085       O  
HETATM 2093  CB  MSE B  25      81.350  55.725  55.956  1.00110.69           C  
ANISOU 2093  CB  MSE B  25    13104  14070  14881    509   1059  -1046       C  
HETATM 2094  CG  MSE B  25      80.205  55.977  54.970  1.00116.20           C  
ANISOU 2094  CG  MSE B  25    13714  15135  15302     -7    754  -1398       C  
HETATM 2095 SE   MSE B  25      78.913  54.504  55.130  1.00129.48          SE  
ANISOU 2095 SE   MSE B  25    15336  16383  17474   -573   1012  -1639      SE  
HETATM 2096  CE  MSE B  25      80.242  53.065  54.996  1.00132.44           C  
ANISOU 2096  CE  MSE B  25    16114  15830  18377   -458   1741  -1895       C  
ATOM   2097  N   PHE B  26      82.769  57.472  53.524  1.00101.15           N  
ANISOU 2097  N   PHE B  26    12077  13592  12762    531    650  -1489       N  
ATOM   2098  CA  PHE B  26      82.769  57.860  52.122  1.00103.97           C  
ANISOU 2098  CA  PHE B  26    12462  14346  12696    308    495  -1795       C  
ATOM   2099  C   PHE B  26      84.053  57.478  51.466  1.00106.91           C  
ANISOU 2099  C   PHE B  26    13095  14491  13035    460    779  -1988       C  
ATOM   2100  O   PHE B  26      84.045  57.008  50.344  1.00118.46           O  
ANISOU 2100  O   PHE B  26    14701  16046  14259    173    873  -2444       O  
ATOM   2101  CB  PHE B  26      82.547  59.356  51.955  1.00105.53           C  
ANISOU 2101  CB  PHE B  26    12397  15104  12595    471    134  -1470       C  
ATOM   2102  CG  PHE B  26      81.113  59.751  51.963  1.00107.88           C  
ANISOU 2102  CG  PHE B  26    12410  15814  12762    225   -138  -1362       C  
ATOM   2103  CD1 PHE B  26      80.108  58.800  51.703  1.00110.78           C  
ANISOU 2103  CD1 PHE B  26    12751  16213  13127   -252   -139  -1676       C  
ATOM   2104  CD2 PHE B  26      80.747  61.067  52.212  1.00103.58           C  
ANISOU 2104  CD2 PHE B  26    11599  15614  12141    452   -349   -942       C  
ATOM   2105  CE1 PHE B  26      78.779  59.158  51.701  1.00109.17           C  
ANISOU 2105  CE1 PHE B  26    12218  16472  12789   -483   -401  -1510       C  
ATOM   2106  CE2 PHE B  26      79.417  61.434  52.199  1.00107.89           C  
ANISOU 2106  CE2 PHE B  26    11844  16564  12583    280   -549   -750       C  
ATOM   2107  CZ  PHE B  26      78.430  60.476  51.945  1.00112.50           C  
ANISOU 2107  CZ  PHE B  26    12361  17273  13107   -183   -603  -1005       C  
ATOM   2108  N   LEU B  27      85.164  57.695  52.176  1.00 99.95           N  
ANISOU 2108  N   LEU B  27    12242  13379  12355    908    920  -1642       N  
ATOM   2109  CA  LEU B  27      86.493  57.418  51.653  1.00 91.69           C  
ANISOU 2109  CA  LEU B  27    11389  12141  11309   1139   1210  -1690       C  
ATOM   2110  C   LEU B  27      86.758  55.932  51.593  1.00 92.91           C  
ANISOU 2110  C   LEU B  27    11817  11682  11800   1065   1733  -1961       C  
ATOM   2111  O   LEU B  27      87.294  55.429  50.619  1.00 95.60           O  
ANISOU 2111  O   LEU B  27    12392  11884  12045   1001   2013  -2315       O  
ATOM   2112  CB  LEU B  27      87.547  58.127  52.492  1.00 87.98           C  
ANISOU 2112  CB  LEU B  27    10774  11706  10946   1593   1174  -1201       C  
ATOM   2113  CG  LEU B  27      87.505  59.661  52.355  1.00 90.32           C  
ANISOU 2113  CG  LEU B  27    10838  12484  10994   1660    779  -1009       C  
ATOM   2114  CD1 LEU B  27      88.536  60.364  53.240  1.00 84.87           C  
ANISOU 2114  CD1 LEU B  27     9982  11830  10433   1997    745   -644       C  
ATOM   2115  CD2 LEU B  27      87.647  60.082  50.895  1.00 89.88           C  
ANISOU 2115  CD2 LEU B  27    10820  12736  10591   1563    719  -1187       C  
ATOM   2116  N   GLY B  28      86.346  55.227  52.629  1.00 96.41           N  
ANISOU 2116  N   GLY B  28    12222  11744  12666   1083   1920  -1786       N  
ATOM   2117  CA  GLY B  28      86.343  53.767  52.617  1.00106.91           C  
ANISOU 2117  CA  GLY B  28    13778  12380  14460    960   2497  -2027       C  
ATOM   2118  C   GLY B  28      85.654  53.147  51.409  1.00114.45           C  
ANISOU 2118  C   GLY B  28    14957  13241  15288    376   2601  -2808       C  
ATOM   2119  O   GLY B  28      86.219  52.269  50.766  1.00120.40           O  
ANISOU 2119  O   GLY B  28    16006  13526  16215    321   3111  -3196       O  
ATOM   2120  N   ILE B  29      84.433  53.605  51.091  1.00117.19           N  
ANISOU 2120  N   ILE B  29    15136  14078  15310    -70   2142  -3050       N  
ATOM   2121  CA  ILE B  29      83.693  53.076  49.910  1.00125.08           C  
ANISOU 2121  CA  ILE B  29    16256  15212  16054   -724   2154  -3843       C  
ATOM   2122  C   ILE B  29      84.405  53.393  48.607  1.00125.17           C  
ANISOU 2122  C   ILE B  29    16425  15616  15515   -729   2143  -4213       C  
ATOM   2123  O   ILE B  29      84.371  52.604  47.670  1.00132.24           O  
ANISOU 2123  O   ILE B  29    17560  16384  16299  -1134   2437  -4943       O  
ATOM   2124  CB  ILE B  29      82.237  53.590  49.828  1.00125.71           C  
ANISOU 2124  CB  ILE B  29    16011  15931  15821  -1178   1616  -3905       C  
ATOM   2125  CG1 ILE B  29      81.446  53.140  51.047  1.00133.81           C  
ANISOU 2125  CG1 ILE B  29    16885  16554  17403  -1219   1684  -3590       C  
ATOM   2126  CG2 ILE B  29      81.553  53.075  48.570  1.00127.62           C  
ANISOU 2126  CG2 ILE B  29    16302  16506  15683  -1895   1584  -4741       C  
ATOM   2127  CD1 ILE B  29      81.757  51.724  51.497  1.00145.37           C  
ANISOU 2127  CD1 ILE B  29    18597  17028  19608  -1251   2372  -3755       C  
ATOM   2128  N   GLN B  30      85.043  54.557  48.558  1.00116.46           N  
ANISOU 2128  N   GLN B  30    15173  14995  14079   -293   1835  -3725       N  
ATOM   2129  CA  GLN B  30      85.885  54.934  47.440  1.00114.84           C  
ANISOU 2129  CA  GLN B  30    15075  15151  13408   -158   1867  -3889       C  
ATOM   2130  C   GLN B  30      87.096  53.960  47.328  1.00117.24           C  
ANISOU 2130  C   GLN B  30    15752  14725  14067    100   2537  -4061       C  
ATOM   2131  O   GLN B  30      87.490  53.558  46.215  1.00124.69           O  
ANISOU 2131  O   GLN B  30    16930  15735  14709    -39   2803  -4599       O  
ATOM   2132  CB  GLN B  30      86.349  56.397  47.615  1.00106.45           C  
ANISOU 2132  CB  GLN B  30    13731  14603  12108    288   1469  -3217       C  
ATOM   2133  CG  GLN B  30      86.359  57.252  46.347  1.00106.76           C  
ANISOU 2133  CG  GLN B  30    13621  15464  11476    241   1199  -3276       C  
ATOM   2134  CD  GLN B  30      85.215  56.950  45.394  1.00111.91           C  
ANISOU 2134  CD  GLN B  30    14188  16712  11618   -353   1014  -3840       C  
ATOM   2135  OE1 GLN B  30      85.407  56.300  44.366  1.00122.72           O  
ANISOU 2135  OE1 GLN B  30    15758  18231  12636   -613   1237  -4454       O  
ATOM   2136  NE2 GLN B  30      84.037  57.444  45.708  1.00108.82           N  
ANISOU 2136  NE2 GLN B  30    13470  16734  11140   -576    616  -3640       N  
ATOM   2137  N   ALA B  31      87.635  53.556  48.484  1.00109.08           N  
ANISOU 2137  N   ALA B  31    14742  13051  13651    485   2842  -3584       N  
ATOM   2138  CA  ALA B  31      88.784  52.659  48.550  1.00108.00           C  
ANISOU 2138  CA  ALA B  31    14872  12218  13942    836   3529  -3533       C  
ATOM   2139  C   ALA B  31      88.427  51.248  48.143  1.00117.04           C  
ANISOU 2139  C   ALA B  31    16356  12657  15457    440   4148  -4243       C  
ATOM   2140  O   ALA B  31      89.037  50.694  47.245  1.00125.73           O  
ANISOU 2140  O   ALA B  31    17764  13512  16494    423   4617  -4717       O  
ATOM   2141  CB  ALA B  31      89.376  52.667  49.937  1.00102.29           C  
ANISOU 2141  CB  ALA B  31    13962  11191  13712   1360   3649  -2725       C  
ATOM   2142  N   VAL B  32      87.454  50.657  48.821  1.00 90.04           N  
ANISOU 2142  N   VAL B  32    10234  11617  12358   1947     40    -51       N  
ATOM   2143  CA  VAL B  32      86.888  49.355  48.415  1.00 97.09           C  
ANISOU 2143  CA  VAL B  32    11459  12024  13407   1952    -72   -260       C  
ATOM   2144  C   VAL B  32      86.624  49.243  46.890  1.00103.12           C  
ANISOU 2144  C   VAL B  32    12659  12674  13845   1949     24   -713       C  
ATOM   2145  O   VAL B  32      86.741  48.155  46.290  1.00105.52           O  
ANISOU 2145  O   VAL B  32    13337  12524  14230   2064    109  -1020       O  
ATOM   2146  CB  VAL B  32      85.572  49.095  49.151  1.00 96.23           C  
ANISOU 2146  CB  VAL B  32    11347  11842  13372   1600   -429    -74       C  
ATOM   2147  CG1 VAL B  32      85.026  47.698  48.829  1.00103.77           C  
ANISOU 2147  CG1 VAL B  32    12645  12253  14528   1532   -618   -226       C  
ATOM   2148  CG2 VAL B  32      85.758  49.291  50.643  1.00 94.19           C  
ANISOU 2148  CG2 VAL B  32    10708  11785  13292   1521   -502    344       C  
ATOM   2149  N   VAL B  33      86.244  50.366  46.285  1.00105.84           N  
ANISOU 2149  N   VAL B  33    12979  13414  13818   1777      9   -741       N  
ATOM   2150  CA  VAL B  33      86.016  50.444  44.843  1.00109.90           C  
ANISOU 2150  CA  VAL B  33    13855  13980  13919   1672     63  -1081       C  
ATOM   2151  C   VAL B  33      87.309  50.261  44.067  1.00114.04           C  
ANISOU 2151  C   VAL B  33    14497  14499  14334   2052    502  -1358       C  
ATOM   2152  O   VAL B  33      87.318  49.637  43.018  1.00122.31           O  
ANISOU 2152  O   VAL B  33    16008  15347  15116   2045    641  -1772       O  
ATOM   2153  CB  VAL B  33      85.319  51.779  44.463  1.00106.15           C  
ANISOU 2153  CB  VAL B  33    13202  13969  13159   1393    -75   -889       C  
ATOM   2154  CG1 VAL B  33      86.174  52.631  43.518  1.00100.55           C  
ANISOU 2154  CG1 VAL B  33    12443  13627  12132   1531    198   -982       C  
ATOM   2155  CG2 VAL B  33      83.929  51.509  43.906  1.00105.29           C  
ANISOU 2155  CG2 VAL B  33    13331  13802  12869    950   -438   -879       C  
ATOM   2156  N   PHE B  34      88.402  50.783  44.626  1.00113.52           N  
ANISOU 2156  N   PHE B  34    14015  14656  14461   2354    731  -1104       N  
ATOM   2157  CA  PHE B  34      89.726  50.761  44.002  1.00115.34           C  
ANISOU 2157  CA  PHE B  34    14187  14984  14651   2760   1189  -1203       C  
ATOM   2158  C   PHE B  34      90.421  49.417  44.220  1.00119.14           C  
ANISOU 2158  C   PHE B  34    14766  14938  15561   3163   1467  -1304       C  
ATOM   2159  O   PHE B  34      91.176  48.945  43.368  1.00125.65           O  
ANISOU 2159  O   PHE B  34    15789  15620  16329   3515   1929  -1588       O  
ATOM   2160  CB  PHE B  34      90.572  51.891  44.590  1.00113.12           C  
ANISOU 2160  CB  PHE B  34    13363  15170  14446   2837   1239   -764       C  
ATOM   2161  CG  PHE B  34      92.026  51.803  44.256  1.00118.11           C  
ANISOU 2161  CG  PHE B  34    13762  15930  15185   3274   1677   -657       C  
ATOM   2162  CD1 PHE B  34      92.871  50.965  44.980  1.00117.91           C  
ANISOU 2162  CD1 PHE B  34    13484  15645  15668   3614   1844   -403       C  
ATOM   2163  CD2 PHE B  34      92.563  52.579  43.237  1.00119.47           C  
ANISOU 2163  CD2 PHE B  34    13885  16521  14987   3342   1923   -707       C  
ATOM   2164  CE1 PHE B  34      94.208  50.885  44.671  1.00123.09           C  
ANISOU 2164  CE1 PHE B  34    13832  16439  16497   4052   2283   -192       C  
ATOM   2165  CE2 PHE B  34      93.902  52.506  42.929  1.00122.50           C  
ANISOU 2165  CE2 PHE B  34    13986  17073  15485   3763   2363   -534       C  
ATOM   2166  CZ  PHE B  34      94.726  51.658  43.646  1.00126.39           C  
ANISOU 2166  CZ  PHE B  34    14208  17290  16522   4138   2560   -265       C  
ATOM   2167  N   VAL B  35      90.175  48.816  45.372  1.00116.12           N  
ANISOU 2167  N   VAL B  35    14223  14264  15631   3126   1225  -1036       N  
ATOM   2168  CA  VAL B  35      90.661  47.480  45.654  1.00121.35           C  
ANISOU 2168  CA  VAL B  35    14957  14336  16814   3469   1421  -1050       C  
ATOM   2169  C   VAL B  35      89.938  46.454  44.746  1.00126.93           C  
ANISOU 2169  C   VAL B  35    16384  14457  17383   3388   1462  -1651       C  
ATOM   2170  O   VAL B  35      90.162  45.244  44.833  1.00131.99           O  
ANISOU 2170  O   VAL B  35    17240  14443  18465   3640   1634  -1778       O  
ATOM   2171  CB  VAL B  35      90.511  47.149  47.166  1.00120.04           C  
ANISOU 2171  CB  VAL B  35    14395  14079  17133   3348   1071   -517       C  
ATOM   2172  CG1 VAL B  35      90.708  45.667  47.434  1.00126.62           C  
ANISOU 2172  CG1 VAL B  35    15342  14200  18566   3617   1168   -500       C  
ATOM   2173  CG2 VAL B  35      91.508  47.966  47.980  1.00120.15           C  
ANISOU 2173  CG2 VAL B  35    13779  14603  17267   3426   1102     48       C  
ATOM   2174  N   PHE B  36      89.094  46.959  43.855  1.00128.35           N  
ANISOU 2174  N   PHE B  36    16944  14865  16958   2997   1295  -1988       N  
ATOM   2175  CA  PHE B  36      88.427  46.115  42.872  1.00134.55           C  
ANISOU 2175  CA  PHE B  36    18479  15195  17447   2775   1289  -2569       C  
ATOM   2176  C   PHE B  36      88.948  46.412  41.476  1.00141.25           C  
ANISOU 2176  C   PHE B  36    19692  16258  17718   2879   1740  -3040       C  
ATOM   2177  O   PHE B  36      89.204  45.501  40.694  1.00151.37           O  
ANISOU 2177  O   PHE B  36    21576  17044  18892   3028   2120  -3591       O  
ATOM   2178  CB  PHE B  36      86.900  46.300  42.935  1.00125.50           C  
ANISOU 2178  CB  PHE B  36    17501  14152  16032   2108    652  -2497       C  
ATOM   2179  CG  PHE B  36      86.188  45.234  43.730  1.00123.18           C  
ANISOU 2179  CG  PHE B  36    17326  13289  16186   1930    293  -2379       C  
ATOM   2180  CD1 PHE B  36      85.865  44.002  43.146  1.00127.65           C  
ANISOU 2180  CD1 PHE B  36    18594  13153  16754   1787    284  -2848       C  
ATOM   2181  CD2 PHE B  36      85.818  45.458  45.059  1.00115.47           C  
ANISOU 2181  CD2 PHE B  36    15802  12472  15597   1854    -37  -1806       C  
ATOM   2182  CE1 PHE B  36      85.196  43.014  43.873  1.00126.88           C  
ANISOU 2182  CE1 PHE B  36    18591  12511  17105   1581    -94  -2681       C  
ATOM   2183  CE2 PHE B  36      85.148  44.470  45.789  1.00115.32           C  
ANISOU 2183  CE2 PHE B  36    15851  11986  15980   1659   -385  -1629       C  
ATOM   2184  CZ  PHE B  36      84.839  43.246  45.193  1.00120.46           C  
ANISOU 2184  CZ  PHE B  36    17147  11926  16696   1525   -438  -2036       C  
ATOM   2185  N   ASN B  37      89.108  47.696  41.177  1.00141.55           N  
ANISOU 2185  N   ASN B  37    19382  17020  17380   2788   1724  -2823       N  
ATOM   2186  CA  ASN B  37      89.611  48.134  39.894  1.00152.71           C  
ANISOU 2186  CA  ASN B  37    21030  18791  18199   2840   2116  -3149       C  
ATOM   2187  C   ASN B  37      90.810  49.023  40.079  1.00152.83           C  
ANISOU 2187  C   ASN B  37    20411  19308  18349   3265   2459  -2763       C  
ATOM   2188  O   ASN B  37      90.694  50.244  39.944  1.00151.85           O  
ANISOU 2188  O   ASN B  37    19954  19798  17944   3035   2256  -2466       O  
ATOM   2189  CB  ASN B  37      88.531  48.908  39.131  1.00159.82           C  
ANISOU 2189  CB  ASN B  37    22126  20157  18439   2182   1678  -3175       C  
ATOM   2190  CG  ASN B  37      87.368  48.035  38.717  1.00176.27           C  
ANISOU 2190  CG  ASN B  37    24886  21826  20261   1648   1315  -3535       C  
ATOM   2191  OD1 ASN B  37      86.825  48.181  37.616  1.00185.54           O  
ANISOU 2191  OD1 ASN B  37    26505  23243  20747   1158   1184  -3793       O  
ATOM   2192  ND2 ASN B  37      86.975  47.115  39.596  1.00182.62           N  
ANISOU 2192  ND2 ASN B  37    25763  22029  21593   1671   1103  -3498       N  
ATOM   2193  N   PRO B  38      91.985  48.430  40.405  1.00158.93           N  
ANISOU 2193  N   PRO B  38    20968  19809  19609   3880   2968  -2688       N  
ATOM   2194  CA  PRO B  38      93.170  49.281  40.491  1.00156.20           C  
ANISOU 2194  CA  PRO B  38    19988  20001  19357   4228   3272  -2244       C  
ATOM   2195  C   PRO B  38      93.395  49.972  39.148  1.00156.99           C  
ANISOU 2195  C   PRO B  38    20272  20634  18743   4147   3559  -2494       C  
ATOM   2196  O   PRO B  38      94.067  51.009  39.076  1.00148.76           O  
ANISOU 2196  O   PRO B  38    18717  20196  17607   4211   3624  -2082       O  
ATOM   2197  CB  PRO B  38      94.301  48.279  40.788  1.00160.95           C  
ANISOU 2197  CB  PRO B  38    20422  20145  20586   4911   3852  -2162       C  
ATOM   2198  CG  PRO B  38      93.619  47.078  41.353  1.00159.98           C  
ANISOU 2198  CG  PRO B  38    20666  19240  20879   4863   3654  -2372       C  
ATOM   2199  CD  PRO B  38      92.312  47.008  40.631  1.00162.54           C  
ANISOU 2199  CD  PRO B  38    21708  19468  20580   4280   3306  -2935       C  
ATOM   2200  N   ASP B  39      92.721  49.445  38.125  1.00161.89           N  
ANISOU 2200  N   ASP B  39    21637  21057  18814   3884   3630  -3127       N  
ATOM   2201  CA  ASP B  39      92.987  49.748  36.726  1.00171.11           C  
ANISOU 2201  CA  ASP B  39    23141  22645  19228   3813   4020  -3488       C  
ATOM   2202  C   ASP B  39      92.936  51.235  36.390  1.00168.06           C  
ANISOU 2202  C   ASP B  39    22302  23111  18440   3480   3727  -3046       C  
ATOM   2203  O   ASP B  39      93.844  51.756  35.755  1.00172.34           O  
ANISOU 2203  O   ASP B  39    22604  24149  18727   3716   4156  -2928       O  
ATOM   2204  CB  ASP B  39      92.034  48.952  35.841  1.00176.18           C  
ANISOU 2204  CB  ASP B  39    24725  22931  19282   3358   3947  -4206       C  
ATOM   2205  CG  ASP B  39      91.817  47.534  36.355  1.00180.31           C  
ANISOU 2205  CG  ASP B  39    25709  22496  20302   3549   4037  -4581       C  
ATOM   2206  OD1 ASP B  39      91.518  47.374  37.563  1.00171.22           O  
ANISOU 2206  OD1 ASP B  39    24177  21050  19826   3587   3628  -4177       O  
ATOM   2207  OD2 ASP B  39      91.967  46.582  35.556  1.00189.99           O  
ANISOU 2207  OD2 ASP B  39    27697  23249  21242   3651   4542  -5278       O  
ATOM   2208  N   SER B  40      91.885  51.918  36.821  1.00168.03           N  
ANISOU 2208  N   SER B  40    22152  23258  18431   2956   3030  -2756       N  
ATOM   2209  CA  SER B  40      91.867  53.373  36.732  1.00164.86           C  
ANISOU 2209  CA  SER B  40    21233  23529  17874   2706   2748  -2237       C  
ATOM   2210  C   SER B  40      91.880  54.016  38.105  1.00153.91           C  
ANISOU 2210  C   SER B  40    19253  22100  17123   2760   2405  -1688       C  
ATOM   2211  O   SER B  40      90.846  54.485  38.597  1.00140.64           O  
ANISOU 2211  O   SER B  40    17508  20383  15543   2377   1899  -1498       O  
ATOM   2212  CB  SER B  40      90.685  53.872  35.912  1.00167.67           C  
ANISOU 2212  CB  SER B  40    21863  24190  17654   2036   2301  -2276       C  
ATOM   2213  OG  SER B  40      90.856  55.241  35.597  1.00165.37           O  
ANISOU 2213  OG  SER B  40    21084  24536  17210   1867   2160  -1782       O  
ATOM   2214  N   TRP B  41      93.056  53.994  38.731  1.00150.71           N  
ANISOU 2214  N   TRP B  41    18425  21696  17139   3223   2710  -1419       N  
ATOM   2215  CA  TRP B  41      93.322  54.759  39.934  1.00142.40           C  
ANISOU 2215  CA  TRP B  41    16817  20738  16548   3204   2429   -872       C  
ATOM   2216  C   TRP B  41      92.959  56.225  39.684  1.00134.08           C  
ANISOU 2216  C   TRP B  41    15524  20161  15258   2811   2112   -556       C  
ATOM   2217  O   TRP B  41      92.370  56.890  40.537  1.00131.87           O  
ANISOU 2217  O   TRP B  41    15077  19814  15213   2552   1730   -310       O  
ATOM   2218  CB  TRP B  41      94.809  54.647  40.298  1.00148.03           C  
ANISOU 2218  CB  TRP B  41    17069  21569  17602   3677   2817   -527       C  
ATOM   2219  CG  TRP B  41      95.703  55.166  39.218  1.00154.80           C  
ANISOU 2219  CG  TRP B  41    17751  22957  18107   3847   3217   -428       C  
ATOM   2220  CD1 TRP B  41      95.916  54.600  38.004  1.00163.18           C  
ANISOU 2220  CD1 TRP B  41    19172  24080  18746   4058   3717   -858       C  
ATOM   2221  CD2 TRP B  41      96.450  56.401  39.224  1.00155.23           C  
ANISOU 2221  CD2 TRP B  41    17260  23580  18140   3755   3142    135       C  
ATOM   2222  NE1 TRP B  41      96.771  55.380  37.256  1.00168.70           N  
ANISOU 2222  NE1 TRP B  41    19532  25408  19159   4143   3992   -565       N  
ATOM   2223  CE2 TRP B  41      97.110  56.493  37.980  1.00161.98           C  
ANISOU 2223  CE2 TRP B  41    18100  24868  18576   3955   3615     76       C  
ATOM   2224  CE3 TRP B  41      96.630  57.428  40.165  1.00152.03           C  
ANISOU 2224  CE3 TRP B  41    16422  23340  18002   3486   2729    668       C  
ATOM   2225  CZ2 TRP B  41      97.950  57.574  37.646  1.00160.77           C  
ANISOU 2225  CZ2 TRP B  41    17431  25340  18314   3907   3650    616       C  
ATOM   2226  CZ3 TRP B  41      97.457  58.507  39.832  1.00155.28           C  
ANISOU 2226  CZ3 TRP B  41    16390  24299  18309   3405   2741   1155       C  
ATOM   2227  CH2 TRP B  41      98.109  58.565  38.582  1.00158.12           C  
ANISOU 2227  CH2 TRP B  41    16665  25113  18300   3623   3181   1165       C  
ATOM   2228  N   LEU B  42      93.295  56.708  38.491  1.00131.51           N  
ANISOU 2228  N   LEU B  42    15201  20295  14472   2770   2311   -566       N  
ATOM   2229  CA  LEU B  42      93.130  58.107  38.147  1.00125.40           C  
ANISOU 2229  CA  LEU B  42    14133  19980  13532   2439   2055   -179       C  
ATOM   2230  C   LEU B  42      91.768  58.683  38.612  1.00123.28           C  
ANISOU 2230  C   LEU B  42    13913  19521  13404   2017   1547    -77       C  
ATOM   2231  O   LEU B  42      91.707  59.740  39.274  1.00116.09           O  
ANISOU 2231  O   LEU B  42    12678  18645  12785   1875   1322    302       O  
ATOM   2232  CB  LEU B  42      93.291  58.282  36.655  1.00125.12           C  
ANISOU 2232  CB  LEU B  42    14234  20433  12871   2340   2274   -286       C  
ATOM   2233  CG  LEU B  42      94.145  59.453  36.202  1.00124.72           C  
ANISOU 2233  CG  LEU B  42    13696  20978  12712   2314   2342    213       C  
ATOM   2234  CD1 LEU B  42      93.824  59.751  34.744  1.00127.77           C  
ANISOU 2234  CD1 LEU B  42    14258  21876  12412   2007   2377    153       C  
ATOM   2235  CD2 LEU B  42      93.945  60.693  37.079  1.00117.46           C  
ANISOU 2235  CD2 LEU B  42    12371  20026  12232   2073   1907    722       C  
ATOM   2236  N   ALA B  43      90.692  57.977  38.274  1.00124.34           N  
ANISOU 2236  N   ALA B  43    14462  19432  13349   1815   1395   -400       N  
ATOM   2237  CA  ALA B  43      89.354  58.355  38.704  1.00118.24           C  
ANISOU 2237  CA  ALA B  43    13691  18474  12761   1467    968   -247       C  
ATOM   2238  C   ALA B  43      89.169  58.195  40.203  1.00113.73           C  
ANISOU 2238  C   ALA B  43    13006  17477  12725   1591    866   -184       C  
ATOM   2239  O   ALA B  43      88.509  59.023  40.832  1.00117.06           O  
ANISOU 2239  O   ALA B  43    13228  17830  13419   1419    652     92       O  
ATOM   2240  CB  ALA B  43      88.309  57.546  37.961  1.00128.54           C  
ANISOU 2240  CB  ALA B  43    15443  19685  13709   1161    793   -532       C  
ATOM   2241  N   SER B  44      89.720  57.110  40.768  1.00107.57           N  
ANISOU 2241  N   SER B  44    12363  16404  12105   1884   1048   -426       N  
ATOM   2242  CA  SER B  44      89.616  56.850  42.215  1.00102.10           C  
ANISOU 2242  CA  SER B  44    11558  15373  11862   1955    939   -329       C  
ATOM   2243  C   SER B  44      90.261  57.953  43.008  1.00 95.28           C  
ANISOU 2243  C   SER B  44    10315  14679  11208   1945    927     30       C  
ATOM   2244  O   SER B  44      89.813  58.303  44.081  1.00 97.15           O  
ANISOU 2244  O   SER B  44    10478  14748  11685   1806    769    158       O  
ATOM   2245  CB  SER B  44      90.247  55.507  42.589  1.00105.64           C  
ANISOU 2245  CB  SER B  44    12142  15507  12488   2277   1140   -540       C  
ATOM   2246  OG  SER B  44      89.378  54.427  42.290  1.00115.32           O  
ANISOU 2246  OG  SER B  44    13789  16383  13642   2189   1046   -879       O  
ATOM   2247  N   VAL B  45      91.318  58.510  42.474  1.00 98.14           N  
ANISOU 2247  N   VAL B  45    10462  15381  11442   2054   1104    194       N  
ATOM   2248  CA  VAL B  45      91.944  59.627  43.115  1.00 97.97           C  
ANISOU 2248  CA  VAL B  45    10124  15524  11576   1945   1038    556       C  
ATOM   2249  C   VAL B  45      91.086  60.884  42.926  1.00 96.70           C  
ANISOU 2249  C   VAL B  45     9932  15398  11410   1638    848    699       C  
ATOM   2250  O   VAL B  45      90.871  61.635  43.877  1.00 94.76           O  
ANISOU 2250  O   VAL B  45     9631  14983  11388   1463    737    835       O  
ATOM   2251  CB  VAL B  45      93.412  59.801  42.637  1.00 99.80           C  
ANISOU 2251  CB  VAL B  45    10063  16133  11723   2146   1267    797       C  
ATOM   2252  CG1 VAL B  45      93.968  61.184  43.005  1.00 95.69           C  
ANISOU 2252  CG1 VAL B  45     9243  15831  11281   1895   1116   1216       C  
ATOM   2253  CG2 VAL B  45      94.262  58.697  43.231  1.00 94.28           C  
ANISOU 2253  CG2 VAL B  45     9273  15308  11240   2461   1450    820       C  
ATOM   2254  N   ALA B  46      90.534  61.061  41.724  1.00 99.02           N  
ANISOU 2254  N   ALA B  46    10287  15877  11456   1554    826    672       N  
ATOM   2255  CA  ALA B  46      89.650  62.212  41.432  1.00 98.77           C  
ANISOU 2255  CA  ALA B  46    10149  15865  11511   1286    649    920       C  
ATOM   2256  C   ALA B  46      88.434  62.217  42.360  1.00 98.55           C  
ANISOU 2256  C   ALA B  46    10218  15426  11798   1189    526    883       C  
ATOM   2257  O   ALA B  46      87.871  63.278  42.677  1.00 95.98           O  
ANISOU 2257  O   ALA B  46     9764  14956  11746   1057    481   1114       O  
ATOM   2258  CB  ALA B  46      89.202  62.187  39.975  1.00 99.75           C  
ANISOU 2258  CB  ALA B  46    10310  16317  11273   1147    592    960       C  
ATOM   2259  N   ALA B  47      88.025  61.023  42.783  1.00 97.73           N  
ANISOU 2259  N   ALA B  47    10333  15113  11686   1271    509    613       N  
ATOM   2260  CA  ALA B  47      86.954  60.883  43.739  1.00 99.23           C  
ANISOU 2260  CA  ALA B  47    10584  14969  12150   1200    426    604       C  
ATOM   2261  C   ALA B  47      87.420  61.243  45.174  1.00100.80           C  
ANISOU 2261  C   ALA B  47    10753  14975  12570   1223    519    606       C  
ATOM   2262  O   ALA B  47      86.876  62.169  45.789  1.00101.98           O  
ANISOU 2262  O   ALA B  47    10858  14949  12941   1117    568    723       O  
ATOM   2263  CB  ALA B  47      86.363  59.484  43.674  1.00 97.54           C  
ANISOU 2263  CB  ALA B  47    10604  14609  11845   1216    326    372       C  
ATOM   2264  N   VAL B  48      88.463  60.557  45.670  1.00100.46           N  
ANISOU 2264  N   VAL B  48    10735  14973  12462   1338    565    506       N  
ATOM   2265  CA  VAL B  48      88.977  60.795  47.036  1.00 93.81           C  
ANISOU 2265  CA  VAL B  48     9877  14033  11731   1243    581    559       C  
ATOM   2266  C   VAL B  48      89.340  62.255  47.307  1.00 96.44           C  
ANISOU 2266  C   VAL B  48    10148  14390  12103   1042    617    717       C  
ATOM   2267  O   VAL B  48      88.824  62.853  48.236  1.00 96.14           O  
ANISOU 2267  O   VAL B  48    10233  14122  12172    870    668    679       O  
ATOM   2268  CB  VAL B  48      90.160  59.889  47.392  1.00 88.43           C  
ANISOU 2268  CB  VAL B  48     9117  13462  11017   1372    587    596       C  
ATOM   2269  CG1 VAL B  48      90.716  60.277  48.751  1.00 86.10           C  
ANISOU 2269  CG1 VAL B  48     8786  13168  10760   1130    524    752       C  
ATOM   2270  CG2 VAL B  48      89.725  58.438  47.413  1.00 88.53           C  
ANISOU 2270  CG2 VAL B  48     9251  13292  11094   1545    564    424       C  
ATOM   2271  N   THR B  49      90.237  62.825  46.510  1.00102.40           N  
ANISOU 2271  N   THR B  49    10737  15401  12767   1052    617    889       N  
ATOM   2272  CA  THR B  49      90.366  64.287  46.484  1.00107.32           C  
ANISOU 2272  CA  THR B  49    11315  15982  13479    840    618   1064       C  
ATOM   2273  C   THR B  49      89.144  64.812  45.801  1.00107.85           C  
ANISOU 2273  C   THR B  49    11372  15898  13705    868    655   1094       C  
ATOM   2274  O   THR B  49      88.941  64.560  44.616  1.00124.91           O  
ANISOU 2274  O   THR B  49    13412  18289  15757    965    608   1174       O  
ATOM   2275  CB  THR B  49      91.605  64.755  45.701  1.00105.46           C  
ANISOU 2275  CB  THR B  49    10836  16114  13119    823    575   1339       C  
ATOM   2276  OG1 THR B  49      91.414  64.521  44.295  1.00101.18           O  
ANISOU 2276  OG1 THR B  49    10165  15831  12445   1003    610   1382       O  
ATOM   2277  CG2 THR B  49      92.844  64.014  46.178  1.00112.19           C  
ANISOU 2277  CG2 THR B  49    11568  17194  13862    869    551   1440       C  
ATOM   2278  N   GLY B  50      88.288  65.489  46.533  1.00101.88           N  
ANISOU 2278  N   GLY B  50    10740  14769  13201    774    760   1053       N  
ATOM   2279  CA  GLY B  50      87.039  65.922  45.934  1.00105.69           C  
ANISOU 2279  CA  GLY B  50    11116  15096  13943    838    813   1203       C  
ATOM   2280  C   GLY B  50      85.834  65.675  46.794  1.00101.35           C  
ANISOU 2280  C   GLY B  50    10680  14217  13609    895    968   1090       C  
ATOM   2281  O   GLY B  50      85.039  66.579  46.986  1.00102.59           O  
ANISOU 2281  O   GLY B  50    10799  14055  14124    913   1167   1219       O  
ATOM   2282  N   ILE B  51      85.670  64.435  47.276  1.00 94.13           N  
ANISOU 2282  N   ILE B  51     9871  13368  12523    947    904    896       N  
ATOM   2283  CA  ILE B  51      84.840  64.182  48.449  1.00 93.14           C  
ANISOU 2283  CA  ILE B  51     9881  12982  12523    950   1072    770       C  
ATOM   2284  C   ILE B  51      85.344  65.105  49.538  1.00 97.13           C  
ANISOU 2284  C   ILE B  51    10616  13259  13030    791   1292    613       C  
ATOM   2285  O   ILE B  51      84.568  65.807  50.201  1.00101.58           O  
ANISOU 2285  O   ILE B  51    11291  13482  13822    796   1606    564       O  
ATOM   2286  CB  ILE B  51      84.976  62.739  48.971  1.00 90.90           C  
ANISOU 2286  CB  ILE B  51     9690  12823  12023    962    925    607       C  
ATOM   2287  CG1 ILE B  51      84.337  61.739  48.022  1.00 96.91           C  
ANISOU 2287  CG1 ILE B  51    10349  13706  12765   1051    716    687       C  
ATOM   2288  CG2 ILE B  51      84.338  62.607  50.350  1.00 90.53           C  
ANISOU 2288  CG2 ILE B  51     9784  12580  12030    896   1111    503       C  
ATOM   2289  CD1 ILE B  51      84.498  60.301  48.492  1.00100.49           C  
ANISOU 2289  CD1 ILE B  51    10914  14181  13085   1070    571    536       C  
ATOM   2290  N   LEU B  52      86.660  65.098  49.726  1.00100.40           N  
ANISOU 2290  N   LEU B  52     9858  14265  14021    885   2150    305       N  
ATOM   2291  CA  LEU B  52      87.278  65.979  50.687  1.00 97.36           C  
ANISOU 2291  CA  LEU B  52     8976  14110  13903   1000   1870    482       C  
ATOM   2292  C   LEU B  52      87.044  67.422  50.291  1.00 98.61           C  
ANISOU 2292  C   LEU B  52     9356  14389  13721    665   1637    526       C  
ATOM   2293  O   LEU B  52      86.819  68.253  51.150  1.00107.01           O  
ANISOU 2293  O   LEU B  52    10253  15583  14823    688   1247    667       O  
ATOM   2294  CB  LEU B  52      88.782  65.692  50.861  1.00 95.11           C  
ANISOU 2294  CB  LEU B  52     8117  13821  14199   1167   2245    498       C  
ATOM   2295  CG  LEU B  52      89.247  64.418  51.596  1.00 94.72           C  
ANISOU 2295  CG  LEU B  52     7608  13606  14775   1558   2294    603       C  
ATOM   2296  CD1 LEU B  52      90.718  64.164  51.295  1.00 98.07           C  
ANISOU 2296  CD1 LEU B  52     7424  13870  15965   1667   2818    589       C  
ATOM   2297  CD2 LEU B  52      89.026  64.488  53.097  1.00 89.06           C  
ANISOU 2297  CD2 LEU B  52     6664  13028  14144   1681   1594    917       C  
ATOM   2298  N   CYS B  53      87.053  67.727  48.992  1.00 96.87           N  
ANISOU 2298  N   CYS B  53     9598  14068  13139    285   1879    405       N  
ATOM   2299  CA  CYS B  53      86.833  69.109  48.587  1.00 93.71           C  
ANISOU 2299  CA  CYS B  53     9432  13726  12446    -65   1571    506       C  
ATOM   2300  C   CYS B  53      85.528  69.585  49.167  1.00 88.79           C  
ANISOU 2300  C   CYS B  53     8837  13045  11851      2    953    690       C  
ATOM   2301  O   CYS B  53      85.495  70.553  49.923  1.00 88.39           O  
ANISOU 2301  O   CYS B  53     8536  13083  11963     59    700    792       O  
ATOM   2302  CB  CYS B  53      86.821  69.279  47.073  1.00 99.38           C  
ANISOU 2302  CB  CYS B  53    10839  14271  12650   -628   1788    406       C  
ATOM   2303  SG  CYS B  53      86.646  71.019  46.564  1.00113.41           S  
ANISOU 2303  SG  CYS B  53    12917  16064  14110  -1103   1311    607       S  
ATOM   2304  N   VAL B  54      84.457  68.859  48.856  1.00 86.55           N  
ANISOU 2304  N   VAL B  54     8836  12565  11483    -17    775    713       N  
ATOM   2305  CA  VAL B  54      83.098  69.321  49.140  1.00 81.16           C  
ANISOU 2305  CA  VAL B  54     8153  11705  10977    -25    231    896       C  
ATOM   2306  C   VAL B  54      82.777  69.156  50.618  1.00 79.45           C  
ANISOU 2306  C   VAL B  54     7491  11543  11149    368    218    862       C  
ATOM   2307  O   VAL B  54      82.102  70.018  51.229  1.00 76.80           O  
ANISOU 2307  O   VAL B  54     6978  11085  11114    385     -7    934       O  
ATOM   2308  CB  VAL B  54      82.048  68.575  48.289  1.00 76.65           C  
ANISOU 2308  CB  VAL B  54     8010  10876  10237   -255    -17    981       C  
ATOM   2309  CG1 VAL B  54      82.298  68.808  46.814  1.00 80.18           C  
ANISOU 2309  CG1 VAL B  54     9113  11204  10145   -853    -56   1037       C  
ATOM   2310  CG2 VAL B  54      82.059  67.093  48.601  1.00 72.62           C  
ANISOU 2310  CG2 VAL B  54     7494  10390   9709      5    318    807       C  
ATOM   2311  N   VAL B  55      83.272  68.072  51.213  1.00 74.40           N  
ANISOU 2311  N   VAL B  55     6709  11023  10536    630    496    749       N  
ATOM   2312  CA  VAL B  55      83.084  67.901  52.641  1.00 73.02           C  
ANISOU 2312  CA  VAL B  55     6267  10888  10588    854    462    735       C  
ATOM   2313  C   VAL B  55      83.723  69.054  53.384  1.00 75.10           C  
ANISOU 2313  C   VAL B  55     6343  11286  10904    770    425    775       C  
ATOM   2314  O   VAL B  55      83.161  69.553  54.342  1.00 79.83           O  
ANISOU 2314  O   VAL B  55     6909  11790  11630    732    365    751       O  
ATOM   2315  CB  VAL B  55      83.540  66.512  53.163  1.00 69.64           C  
ANISOU 2315  CB  VAL B  55     5751  10510  10197   1095    636    693       C  
ATOM   2316  CG1 VAL B  55      83.641  66.503  54.668  1.00 65.30           C  
ANISOU 2316  CG1 VAL B  55     5046  10013   9750   1151    526    739       C  
ATOM   2317  CG2 VAL B  55      82.544  65.455  52.739  1.00 68.56           C  
ANISOU 2317  CG2 VAL B  55     5853  10186  10010   1148    639    635       C  
ATOM   2318  N   PHE B  56      84.849  69.540  52.872  1.00 79.68           N  
ANISOU 2318  N   PHE B  56     6851  12038  11383    671    524    808       N  
ATOM   2319  CA  PHE B  56      85.527  70.688  53.470  1.00 81.81           C  
ANISOU 2319  CA  PHE B  56     6978  12446  11659    526    460    868       C  
ATOM   2320  C   PHE B  56      84.800  72.009  53.222  1.00 82.57           C  
ANISOU 2320  C   PHE B  56     7221  12380  11770    329    310    880       C  
ATOM   2321  O   PHE B  56      84.765  72.862  54.105  1.00 80.01           O  
ANISOU 2321  O   PHE B  56     6862  12025  11513    224    286    871       O  
ATOM   2322  CB  PHE B  56      86.990  70.776  53.022  1.00 84.32           C  
ANISOU 2322  CB  PHE B  56     7090  12974  11973    471    635    908       C  
ATOM   2323  CG  PHE B  56      87.916  69.905  53.810  1.00 87.41           C  
ANISOU 2323  CG  PHE B  56     7121  13466  12623    641    653   1009       C  
ATOM   2324  CD1 PHE B  56      87.508  68.648  54.262  1.00 91.51           C  
ANISOU 2324  CD1 PHE B  56     7628  13875  13266    872    627   1015       C  
ATOM   2325  CD2 PHE B  56      89.196  70.323  54.092  1.00 91.89           C  
ANISOU 2325  CD2 PHE B  56     7334  14196  13383    546    628   1152       C  
ATOM   2326  CE1 PHE B  56      88.372  67.836  54.981  1.00 92.23           C  
ANISOU 2326  CE1 PHE B  56     7367  13980  13695   1006    523   1197       C  
ATOM   2327  CE2 PHE B  56      90.067  69.514  54.803  1.00 94.31           C  
ANISOU 2327  CE2 PHE B  56     7217  14515  14100    677    500   1358       C  
ATOM   2328  CZ  PHE B  56      89.650  68.276  55.258  1.00 94.60           C  
ANISOU 2328  CZ  PHE B  56     7255  14405  14283    908    417   1399       C  
ATOM   2329  N   VAL B  57      84.200  72.185  52.040  1.00 87.16           N  
ANISOU 2329  N   VAL B  57     8008  12792  12314    219    187    926       N  
ATOM   2330  CA  VAL B  57      83.380  73.396  51.822  1.00 89.61           C  
ANISOU 2330  CA  VAL B  57     8378  12826  12841     55    -72   1026       C  
ATOM   2331  C   VAL B  57      82.168  73.403  52.757  1.00 87.55           C  
ANISOU 2331  C   VAL B  57     7953  12260  13051    205    -81    973       C  
ATOM   2332  O   VAL B  57      81.855  74.431  53.355  1.00 84.57           O  
ANISOU 2332  O   VAL B  57     7479  11671  12982    142    -27    941       O  
ATOM   2333  CB  VAL B  57      82.902  73.585  50.381  1.00 87.79           C  
ANISOU 2333  CB  VAL B  57     8448  12396  12513   -203   -392   1201       C  
ATOM   2334  CG1 VAL B  57      82.290  74.964  50.236  1.00 92.96           C  
ANISOU 2334  CG1 VAL B  57     9068  12725  13526   -368   -736   1385       C  
ATOM   2335  CG2 VAL B  57      84.042  73.431  49.419  1.00 86.86           C  
ANISOU 2335  CG2 VAL B  57     8613  12512  11878   -448   -197   1160       C  
ATOM   2336  N   GLY B  58      81.509  72.250  52.896  1.00 82.13           N  
ANISOU 2336  N   GLY B  58     7251  11509  12443    370    -55    925       N  
ATOM   2337  CA  GLY B  58      80.439  72.098  53.888  1.00 84.24           C  
ANISOU 2337  CA  GLY B  58     7364  11490  13153    479     86    807       C  
ATOM   2338  C   GLY B  58      80.843  72.732  55.201  1.00 83.72           C  
ANISOU 2338  C   GLY B  58     7298  11447  13065    392    411    632       C  
ATOM   2339  O   GLY B  58      80.097  73.562  55.770  1.00 80.83           O  
ANISOU 2339  O   GLY B  58     6846  10699  13163    310    619    519       O  
ATOM   2340  N   LYS B  59      82.070  72.400  55.638  1.00 78.90           N  
ANISOU 2340  N   LYS B  59     6788  11223  11967    348    458    629       N  
ATOM   2341  CA  LYS B  59      82.596  72.823  56.923  1.00 74.20           C  
ANISOU 2341  CA  LYS B  59     6327  10685  11178    122    639    534       C  
ATOM   2342  C   LYS B  59      83.001  74.260  56.925  1.00 78.03           C  
ANISOU 2342  C   LYS B  59     6847  11128  11671   -100    673    540       C  
ATOM   2343  O   LYS B  59      83.226  74.825  57.975  1.00 93.04           O  
ANISOU 2343  O   LYS B  59     8960  12966  13423   -396    866    433       O  
ATOM   2344  CB  LYS B  59      83.786  71.973  57.336  1.00 70.90           C  
ANISOU 2344  CB  LYS B  59     5925  10633  10380    111    494    660       C  
ATOM   2345  CG  LYS B  59      83.431  70.657  57.984  1.00 75.27           C  
ANISOU 2345  CG  LYS B  59     6571  11150  10875    196    504    632       C  
ATOM   2346  CD  LYS B  59      82.612  70.836  59.270  1.00 83.32           C  
ANISOU 2346  CD  LYS B  59     7923  11882  11852   -107    770    426       C  
ATOM   2347  CE  LYS B  59      83.500  71.099  60.472  1.00 87.93           C  
ANISOU 2347  CE  LYS B  59     8835  12571  12004   -571    662    511       C  
ATOM   2348  NZ  LYS B  59      82.713  71.328  61.718  1.00 87.37           N  
ANISOU 2348  NZ  LYS B  59     9281  12153  11760  -1038   1056    241       N  
ATOM   2349  N   GLY B  60      83.095  74.865  55.753  1.00 78.43           N  
ANISOU 2349  N   GLY B  60     6784  11179  11834    -43    483    668       N  
ATOM   2350  CA  GLY B  60      83.602  76.238  55.651  1.00 85.24           C  
ANISOU 2350  CA  GLY B  60     7698  12021  12665   -266    474    704       C  
ATOM   2351  C   GLY B  60      85.115  76.328  55.836  1.00 86.41           C  
ANISOU 2351  C   GLY B  60     7875  12616  12340   -436    402    793       C  
ATOM   2352  O   GLY B  60      85.638  77.397  56.044  1.00 89.51           O  
ANISOU 2352  O   GLY B  60     8356  13030  12623   -687    422    805       O  
ATOM   2353  N   LYS B  61      85.796  75.179  55.739  1.00 83.18           N  
ANISOU 2353  N   LYS B  61     7338  12507  11757   -295    320    874       N  
ATOM   2354  CA  LYS B  61      87.240  75.086  55.849  1.00 82.82           C  
ANISOU 2354  CA  LYS B  61     7134  12814  11520   -404    226   1018       C  
ATOM   2355  C   LYS B  61      87.925  75.579  54.580  1.00 93.77           C  
ANISOU 2355  C   LYS B  61     8418  14338  12869   -436    251   1069       C  
ATOM   2356  O   LYS B  61      87.607  75.111  53.466  1.00 96.54           O  
ANISOU 2356  O   LYS B  61     8808  14628  13242   -304    317   1034       O  
ATOM   2357  CB  LYS B  61      87.650  73.649  56.130  1.00 77.98           C  
ANISOU 2357  CB  LYS B  61     6324  12332  10970   -200    164   1104       C  
ATOM   2358  CG  LYS B  61      87.669  73.318  57.605  1.00 84.68           C  
ANISOU 2358  CG  LYS B  61     7320  13152  11701   -398      8   1174       C  
ATOM   2359  CD  LYS B  61      88.295  71.964  57.859  1.00 88.65           C  
ANISOU 2359  CD  LYS B  61     7565  13754  12361   -223   -186   1370       C  
ATOM   2360  CE  LYS B  61      87.836  71.391  59.198  1.00 93.66           C  
ANISOU 2360  CE  LYS B  61     8532  14251  12803   -442   -363   1414       C  
ATOM   2361  NZ  LYS B  61      88.560  71.991  60.359  1.00 92.88           N  
ANISOU 2361  NZ  LYS B  61     8664  14203  12422  -1002   -698   1631       N  
ATOM   2362  N   ILE B  62      88.882  76.511  54.746  1.00 95.20           N  
ANISOU 2362  N   ILE B  62     8550  14687  12934   -706    210   1148       N  
ATOM   2363  CA  ILE B  62      89.553  77.170  53.595  1.00 86.41           C  
ANISOU 2363  CA  ILE B  62     7418  13678  11733   -850    293   1165       C  
ATOM   2364  C   ILE B  62      90.525  76.251  52.836  1.00 87.55           C  
ANISOU 2364  C   ILE B  62     7266  14002  11995   -745    518   1171       C  
ATOM   2365  O   ILE B  62      90.796  76.465  51.650  1.00 85.29           O  
ANISOU 2365  O   ILE B  62     7108  13707  11589   -883    738   1095       O  
ATOM   2366  CB  ILE B  62      90.278  78.454  54.007  1.00 79.81           C  
ANISOU 2366  CB  ILE B  62     6618  12950  10755  -1200    217   1235       C  
ATOM   2367  CG1 ILE B  62      90.702  79.208  52.770  1.00 78.22           C  
ANISOU 2367  CG1 ILE B  62     6520  12782  10417  -1394    316   1223       C  
ATOM   2368  CG2 ILE B  62      91.478  78.131  54.873  1.00 78.52           C  
ANISOU 2368  CG2 ILE B  62     6119  13052  10661  -1317     99   1403       C  
ATOM   2369  CD1 ILE B  62      90.682  80.703  52.929  1.00 80.60           C  
ANISOU 2369  CD1 ILE B  62     7069  12989  10563  -1710    211   1249       C  
ATOM   2370  N   SER B  63      91.004  75.209  53.509  1.00 88.10           N  
ANISOU 2370  N   SER B  63     6983  14157  12334   -547    500   1255       N  
ATOM   2371  CA  SER B  63      91.888  74.226  52.878  1.00 93.86           C  
ANISOU 2371  CA  SER B  63     7324  14924  13411   -384    821   1239       C  
ATOM   2372  C   SER B  63      91.184  73.365  51.863  1.00 93.50           C  
ANISOU 2372  C   SER B  63     7546  14696  13284   -219   1134   1035       C  
ATOM   2373  O   SER B  63      91.795  72.456  51.291  1.00 95.71           O  
ANISOU 2373  O   SER B  63     7594  14908  13860    -98   1553    942       O  
ATOM   2374  CB  SER B  63      92.477  73.307  53.915  1.00 97.50           C  
ANISOU 2374  CB  SER B  63     7311  15416  14317   -203    603   1460       C  
ATOM   2375  OG  SER B  63      91.513  72.361  54.310  1.00 88.47           O  
ANISOU 2375  OG  SER B  63     6358  14130  13125     41    503   1422       O  
ATOM   2376  N   ASN B  64      89.880  73.575  51.704  1.00 98.02           N  
ANISOU 2376  N   ASN B  64     8575  15124  13542   -230    941    979       N  
ATOM   2377  CA  ASN B  64      89.109  72.840  50.703  1.00 99.56           C  
ANISOU 2377  CA  ASN B  64     9123  15124  13579   -199   1104    848       C  
ATOM   2378  C   ASN B  64      89.746  73.054  49.318  1.00102.85           C  
ANISOU 2378  C   ASN B  64     9803  15506  13768   -538   1515    713       C  
ATOM   2379  O   ASN B  64      89.712  72.172  48.450  1.00105.12           O  
ANISOU 2379  O   ASN B  64    10342  15641  13956   -602   1896    551       O  
ATOM   2380  CB  ASN B  64      87.642  73.304  50.702  1.00 89.06           C  
ANISOU 2380  CB  ASN B  64     8152  13595  12091   -243    715    901       C  
ATOM   2381  CG  ASN B  64      87.437  74.591  49.916  1.00 92.25           C  
ANISOU 2381  CG  ASN B  64     8884  13900  12266   -609    531    971       C  
ATOM   2382  OD1 ASN B  64      87.356  74.582  48.669  1.00 96.16           O  
ANISOU 2382  OD1 ASN B  64     9797  14276  12463   -919    575    961       O  
ATOM   2383  ND2 ASN B  64      87.377  75.710  50.629  1.00 90.42           N  
ANISOU 2383  ND2 ASN B  64     8549  13671  12136   -657    326   1049       N  
ATOM   2384  N   TYR B  65      90.354  74.217  49.146  1.00 95.80           N  
ANISOU 2384  N   TYR B  65     8920  14725  12755   -823   1499    753       N  
ATOM   2385  CA  TYR B  65      90.773  74.658  47.864  1.00105.31           C  
ANISOU 2385  CA  TYR B  65    10543  15860  13610  -1284   1829    629       C  
ATOM   2386  C   TYR B  65      91.937  73.824  47.227  1.00122.84           C  
ANISOU 2386  C   TYR B  65    12574  18047  16050  -1350   2654    374       C  
ATOM   2387  O   TYR B  65      91.969  73.635  45.993  1.00130.30           O  
ANISOU 2387  O   TYR B  65    14108  18796  16601  -1783   3116    160       O  
ATOM   2388  CB  TYR B  65      91.102  76.128  47.931  1.00103.24           C  
ANISOU 2388  CB  TYR B  65    10335  15706  13183  -1573   1591    742       C  
ATOM   2389  CG  TYR B  65      89.888  76.996  47.896  1.00101.40           C  
ANISOU 2389  CG  TYR B  65    10507  15292  12727  -1691    982    924       C  
ATOM   2390  CD1 TYR B  65      88.892  76.763  46.978  1.00106.69           C  
ANISOU 2390  CD1 TYR B  65    11730  15681  13123  -1907    751    981       C  
ATOM   2391  CD2 TYR B  65      89.745  78.077  48.765  1.00102.13           C  
ANISOU 2391  CD2 TYR B  65    10428  15421  12956  -1640    635   1061       C  
ATOM   2392  CE1 TYR B  65      87.774  77.572  46.913  1.00111.30           C  
ANISOU 2392  CE1 TYR B  65    12550  15998  13740  -2008    122   1227       C  
ATOM   2393  CE2 TYR B  65      88.624  78.898  48.713  1.00100.34           C  
ANISOU 2393  CE2 TYR B  65    10471  14900  12752  -1718    161   1221       C  
ATOM   2394  CZ  TYR B  65      87.642  78.638  47.776  1.00107.56           C  
ANISOU 2394  CZ  TYR B  65    11797  15510  13560  -1871   -127   1332       C  
ATOM   2395  OH  TYR B  65      86.504  79.424  47.693  1.00111.90           O  
ANISOU 2395  OH  TYR B  65    12478  15668  14369  -1932   -678   1573       O  
ATOM   2396  N   LEU B  66      92.865  73.318  48.054  1.00126.67           N  
ANISOU 2396  N   LEU B  66    12274  18645  17209   -989   2847    409       N  
ATOM   2397  CA  LEU B  66      93.934  72.441  47.538  1.00134.61           C  
ANISOU 2397  CA  LEU B  66    12910  19490  18743   -957   3693    177       C  
ATOM   2398  C   LEU B  66      93.341  71.150  47.021  1.00132.56           C  
ANISOU 2398  C   LEU B  66    12984  18950  18431   -839   4061    -27       C  
ATOM   2399  O   LEU B  66      93.608  70.745  45.871  1.00134.41           O  
ANISOU 2399  O   LEU B  66    13656  18920  18491  -1193   4861   -367       O  
ATOM   2400  CB  LEU B  66      94.998  72.111  48.597  1.00141.38           C  
ANISOU 2400  CB  LEU B  66    12730  20434  20550   -573   3642    387       C  
ATOM   2401  CG  LEU B  66      95.440  73.019  49.753  1.00143.82           C  
ANISOU 2401  CG  LEU B  66    12567  21036  21042   -553   2952    751       C  
ATOM   2402  CD1 LEU B  66      96.812  72.536  50.178  1.00145.27           C  
ANISOU 2402  CD1 LEU B  66    11745  21151  22300   -377   3168    913       C  
ATOM   2403  CD2 LEU B  66      95.461  74.526  49.443  1.00138.53           C  
ANISOU 2403  CD2 LEU B  66    12301  20556  19778  -1004   2787    749       C  
ATOM   2404  N   PHE B  67      92.529  70.499  47.862  1.00122.87           N  
ANISOU 2404  N   PHE B  67    15511  19155  12018    868   3644   -478       N  
ATOM   2405  CA  PHE B  67      91.865  69.265  47.468  1.00120.38           C  
ANISOU 2405  CA  PHE B  67    15131  18796  11810    799   3732   -405       C  
ATOM   2406  C   PHE B  67      91.085  69.455  46.170  1.00118.95           C  
ANISOU 2406  C   PHE B  67    14424  18739  12031    924   3892   -504       C  
ATOM   2407  O   PHE B  67      91.142  68.605  45.271  1.00119.66           O  
ANISOU 2407  O   PHE B  67    14327  18823  12315   1009   3736   -454       O  
ATOM   2408  CB  PHE B  67      90.947  68.772  48.556  1.00126.61           C  
ANISOU 2408  CB  PHE B  67    16310  19500  12296    482   4074   -373       C  
ATOM   2409  CG  PHE B  67      91.657  68.371  49.813  1.00136.30           C  
ANISOU 2409  CG  PHE B  67    18194  20544  13049    277   3836   -218       C  
ATOM   2410  CD1 PHE B  67      92.117  67.064  49.988  1.00135.65           C  
ANISOU 2410  CD1 PHE B  67    18417  20240  12884    187   3440      0       C  
ATOM   2411  CD2 PHE B  67      91.829  69.288  50.854  1.00142.14           C  
ANISOU 2411  CD2 PHE B  67    19302  21282  13422    154   3952   -299       C  
ATOM   2412  CE1 PHE B  67      92.750  66.689  51.164  1.00138.47           C  
ANISOU 2412  CE1 PHE B  67    19454  20350  12806    -40   3107    173       C  
ATOM   2413  CE2 PHE B  67      92.456  68.916  52.034  1.00144.46           C  
ANISOU 2413  CE2 PHE B  67    20301  21362  13224    -82   3672   -137       C  
ATOM   2414  CZ  PHE B  67      92.921  67.615  52.187  1.00144.24           C  
ANISOU 2414  CZ  PHE B  67    20595  21086  13122   -191   3221    117       C  
ATOM   2415  N   GLY B  68      90.396  70.595  46.058  1.00114.62           N  
ANISOU 2415  N   GLY B  68    13658  18264  11625    941   4136   -664       N  
ATOM   2416  CA  GLY B  68      89.657  70.949  44.834  1.00109.59           C  
ANISOU 2416  CA  GLY B  68    12568  17672  11397   1043   4168   -750       C  
ATOM   2417  C   GLY B  68      90.544  71.021  43.611  1.00108.75           C  
ANISOU 2417  C   GLY B  68    12274  17651  11393   1190   3820   -679       C  
ATOM   2418  O   GLY B  68      90.248  70.403  42.581  1.00113.47           O  
ANISOU 2418  O   GLY B  68    12681  18256  12173   1225   3745   -656       O  
ATOM   2419  N   LEU B  69      91.649  71.758  43.738  1.00103.45           N  
ANISOU 2419  N   LEU B  69    11672  17049  10586   1244   3621   -658       N  
ATOM   2420  CA  LEU B  69      92.597  71.936  42.652  1.00 97.23           C  
ANISOU 2420  CA  LEU B  69    10698  16390   9853   1312   3372   -622       C  
ATOM   2421  C   LEU B  69      93.056  70.609  42.063  1.00 96.23           C  
ANISOU 2421  C   LEU B  69    10521  16296   9745   1369   3272   -602       C  
ATOM   2422  O   LEU B  69      93.036  70.429  40.850  1.00 90.74           O  
ANISOU 2422  O   LEU B  69     9624  15696   9154   1383   3230   -635       O  
ATOM   2423  CB  LEU B  69      93.798  72.724  43.127  1.00 98.49           C  
ANISOU 2423  CB  LEU B  69    10947  16597   9876   1325   3189   -599       C  
ATOM   2424  CG  LEU B  69      94.501  73.646  42.130  1.00 96.60           C  
ANISOU 2424  CG  LEU B  69    10493  16506   9704   1292   3027   -582       C  
ATOM   2425  CD1 LEU B  69      95.976  73.679  42.463  1.00 97.21           C  
ANISOU 2425  CD1 LEU B  69    10579  16646   9708   1314   2832   -564       C  
ATOM   2426  CD2 LEU B  69      94.283  73.253  40.670  1.00 96.90           C  
ANISOU 2426  CD2 LEU B  69    10316  16664   9835   1251   3038   -587       C  
ATOM   2427  N   ILE B  70      93.479  69.683  42.917  1.00 99.86           N  
ANISOU 2427  N   ILE B  70    11200  16644  10095   1388   3192   -564       N  
ATOM   2428  CA  ILE B  70      93.778  68.330  42.451  1.00103.41           C  
ANISOU 2428  CA  ILE B  70    11606  17045  10637   1467   3045   -584       C  
ATOM   2429  C   ILE B  70      92.540  67.754  41.784  1.00106.29           C  
ANISOU 2429  C   ILE B  70    11876  17371  11135   1428   3199   -582       C  
ATOM   2430  O   ILE B  70      92.553  67.444  40.576  1.00104.09           O  
ANISOU 2430  O   ILE B  70    11389  17177  10982   1492   3147   -661       O  
ATOM   2431  CB  ILE B  70      94.212  67.393  43.605  1.00105.39           C  
ANISOU 2431  CB  ILE B  70    12193  17071  10779   1451   2837   -504       C  
ATOM   2432  CG1 ILE B  70      95.502  67.902  44.257  1.00104.24           C  
ANISOU 2432  CG1 ILE B  70    12141  16899  10567   1502   2575   -509       C  
ATOM   2433  CG2 ILE B  70      94.374  65.950  43.103  1.00102.88           C  
ANISOU 2433  CG2 ILE B  70    11822  16632  10634   1549   2620   -546       C  
ATOM   2434  CD1 ILE B  70      95.648  67.510  45.711  1.00103.79           C  
ANISOU 2434  CD1 ILE B  70    12585  16571  10276   1384   2375   -371       C  
ATOM   2435  N   SER B  71      91.451  67.674  42.565  1.00111.42           N  
ANISOU 2435  N   SER B  71    12680  17898  11754   1294   3409   -514       N  
ATOM   2436  CA  SER B  71      90.214  66.988  42.159  1.00112.55           C  
ANISOU 2436  CA  SER B  71    12729  17949  12084   1225   3541   -501       C  
ATOM   2437  C   SER B  71      89.699  67.381  40.788  1.00111.15           C  
ANISOU 2437  C   SER B  71    12245  17838  12145   1285   3515   -576       C  
ATOM   2438  O   SER B  71      89.481  66.511  39.939  1.00111.82           O  
ANISOU 2438  O   SER B  71    12256  17875  12356   1326   3390   -587       O  
ATOM   2439  CB  SER B  71      89.125  67.235  43.164  1.00118.03           C  
ANISOU 2439  CB  SER B  71    13526  18568  12752   1032   3877   -487       C  
ATOM   2440  OG  SER B  71      87.915  66.653  42.724  1.00130.08           O  
ANISOU 2440  OG  SER B  71    14874  20002  14548    952   4007   -492       O  
ATOM   2441  N   VAL B  72      89.490  68.691  40.586  1.00105.85           N  
ANISOU 2441  N   VAL B  72    11446  17236  11534   1274   3574   -624       N  
ATOM   2442  CA  VAL B  72      88.872  69.213  39.354  1.00104.56           C  
ANISOU 2442  CA  VAL B  72    11071  17058  11597   1271   3462   -660       C  
ATOM   2443  C   VAL B  72      89.712  68.947  38.092  1.00103.15           C  
ANISOU 2443  C   VAL B  72    10883  17013  11294   1304   3245   -668       C  
ATOM   2444  O   VAL B  72      89.165  68.688  37.000  1.00101.40           O  
ANISOU 2444  O   VAL B  72    10604  16734  11187   1273   3114   -680       O  
ATOM   2445  CB  VAL B  72      88.510  70.735  39.452  1.00104.40           C  
ANISOU 2445  CB  VAL B  72    10950  17011  11706   1241   3463   -709       C  
ATOM   2446  CG1 VAL B  72      87.601  71.009  40.640  1.00103.95           C  
ANISOU 2446  CG1 VAL B  72    10851  16842  11801   1208   3755   -809       C  
ATOM   2447  CG2 VAL B  72      89.755  71.601  39.513  1.00104.41           C  
ANISOU 2447  CG2 VAL B  72    11045  17171  11452   1248   3351   -678       C  
ATOM   2448  N   SER B  73      91.030  69.019  38.240  1.00105.15           N  
ANISOU 2448  N   SER B  73    11192  17438  11322   1347   3214   -690       N  
ATOM   2449  CA  SER B  73      91.933  68.811  37.115  1.00108.41           C  
ANISOU 2449  CA  SER B  73    11550  18035  11605   1345   3119   -774       C  
ATOM   2450  C   SER B  73      91.873  67.364  36.696  1.00107.12           C  
ANISOU 2450  C   SER B  73    11387  17811  11499   1442   3070   -870       C  
ATOM   2451  O   SER B  73      91.452  67.050  35.584  1.00105.81           O  
ANISOU 2451  O   SER B  73    11215  17644  11344   1399   3003   -924       O  
ATOM   2452  CB  SER B  73      93.355  69.206  37.483  1.00109.49           C  
ANISOU 2452  CB  SER B  73    11653  18353  11595   1368   3122   -823       C  
ATOM   2453  OG  SER B  73      93.357  70.414  38.231  1.00112.82           O  
ANISOU 2453  OG  SER B  73    12121  18755  11987   1308   3132   -722       O  
ATOM   2454  N   LEU B  74      92.212  66.467  37.606  1.00106.85           N  
ANISOU 2454  N   LEU B  74    11413  17674  11508   1556   3042   -882       N  
ATOM   2455  CA  LEU B  74      92.056  65.069  37.304  1.00112.89           C  
ANISOU 2455  CA  LEU B  74    12200  18307  12385   1653   2920   -962       C  
ATOM   2456  C   LEU B  74      90.663  64.799  36.725  1.00114.65           C  
ANISOU 2456  C   LEU B  74    12432  18380  12748   1573   2916   -890       C  
ATOM   2457  O   LEU B  74      90.556  64.196  35.655  1.00110.28           O  
ANISOU 2457  O   LEU B  74    11858  17819  12222   1606   2805  -1006       O  
ATOM   2458  CB  LEU B  74      92.340  64.189  38.519  1.00113.80           C  
ANISOU 2458  CB  LEU B  74    12467  18221  12549   1719   2797   -902       C  
ATOM   2459  CG  LEU B  74      93.713  64.333  39.178  1.00114.97           C  
ANISOU 2459  CG  LEU B  74    12616  18418  12649   1814   2674   -973       C  
ATOM   2460  CD1 LEU B  74      93.960  63.146  40.087  1.00117.16           C  
ANISOU 2460  CD1 LEU B  74    13100  18397  13015   1876   2383   -927       C  
ATOM   2461  CD2 LEU B  74      94.839  64.478  38.151  1.00109.34           C  
ANISOU 2461  CD2 LEU B  74    11626  17945  11970   1923   2669  -1246       C  
ATOM   2462  N   TYR B  75      89.606  65.308  37.393  1.00113.69           N  
ANISOU 2462  N   TYR B  75    12321  18137  12740   1462   3039   -740       N  
ATOM   2463  CA  TYR B  75      88.202  65.078  36.931  1.00108.64           C  
ANISOU 2463  CA  TYR B  75    11607  17308  12363   1383   3014   -692       C  
ATOM   2464  C   TYR B  75      87.997  65.559  35.503  1.00105.39           C  
ANISOU 2464  C   TYR B  75    11144  16931  11966   1353   2846   -749       C  
ATOM   2465  O   TYR B  75      87.440  64.827  34.669  1.00106.71           O  
ANISOU 2465  O   TYR B  75    11329  16962  12254   1351   2670   -777       O  
ATOM   2466  CB  TYR B  75      87.174  65.737  37.870  1.00110.47           C  
ANISOU 2466  CB  TYR B  75    11756  17437  12780   1267   3237   -617       C  
ATOM   2467  CG  TYR B  75      85.692  65.578  37.451  1.00112.03           C  
ANISOU 2467  CG  TYR B  75    11764  17414  13386   1185   3213   -610       C  
ATOM   2468  CD1 TYR B  75      84.937  64.462  37.853  1.00115.12           C  
ANISOU 2468  CD1 TYR B  75    12147  17631  13962   1099   3272   -551       C  
ATOM   2469  CD2 TYR B  75      85.046  66.569  36.714  1.00108.73           C  
ANISOU 2469  CD2 TYR B  75    11173  16920  13216   1167   3083   -657       C  
ATOM   2470  CE1 TYR B  75      83.596  64.329  37.491  1.00116.55           C  
ANISOU 2470  CE1 TYR B  75    12090  17597  14596   1012   3245   -561       C  
ATOM   2471  CE2 TYR B  75      83.713  66.448  36.352  1.00115.90           C  
ANISOU 2471  CE2 TYR B  75    11860  17574  14602   1109   2989   -678       C  
ATOM   2472  CZ  TYR B  75      82.986  65.334  36.736  1.00118.26           C  
ANISOU 2472  CZ  TYR B  75    12089  17729  15115   1037   3095   -642       C  
ATOM   2473  OH  TYR B  75      81.655  65.231  36.350  1.00117.26           O  
ANISOU 2473  OH  TYR B  75    11676  17331  15546    970   2985   -679       O  
ATOM   2474  N   ALA B  76      88.460  66.780  35.215  1.00 98.60           N  
ANISOU 2474  N   ALA B  76    10278  16227  10957   1294   2853   -749       N  
ATOM   2475  CA  ALA B  76      88.394  67.318  33.860  1.00100.00           C  
ANISOU 2475  CA  ALA B  76    10519  16435  11039   1178   2651   -764       C  
ATOM   2476  C   ALA B  76      88.959  66.320  32.834  1.00100.60           C  
ANISOU 2476  C   ALA B  76    10710  16611  10901   1199   2577   -908       C  
ATOM   2477  O   ALA B  76      88.362  66.083  31.781  1.00101.76           O  
ANISOU 2477  O   ALA B  76    10970  16636  11055   1113   2365   -921       O  
ATOM   2478  CB  ALA B  76      89.112  68.661  33.771  1.00 98.38           C  
ANISOU 2478  CB  ALA B  76    10347  16412  10622   1064   2663   -724       C  
ATOM   2479  N   TYR B  77      90.088  65.712  33.150  1.00101.96           N  
ANISOU 2479  N   TYR B  77    10852  16969  10918   1322   2718  -1051       N  
ATOM   2480  CA  TYR B  77      90.627  64.729  32.254  1.00105.32           C  
ANISOU 2480  CA  TYR B  77    11328  17479  11210   1382   2679  -1283       C  
ATOM   2481  C   TYR B  77      89.695  63.521  32.146  1.00103.08           C  
ANISOU 2481  C   TYR B  77    11091  16901  11172   1479   2489  -1284       C  
ATOM   2482  O   TYR B  77      89.325  63.127  31.049  1.00105.07           O  
ANISOU 2482  O   TYR B  77    11471  17090  11358   1425   2333  -1376       O  
ATOM   2483  CB  TYR B  77      92.052  64.309  32.648  1.00110.16           C  
ANISOU 2483  CB  TYR B  77    11808  18301  11747   1534   2822  -1506       C  
ATOM   2484  CG  TYR B  77      92.554  63.156  31.824  1.00114.47           C  
ANISOU 2484  CG  TYR B  77    12339  18890  12263   1655   2786  -1842       C  
ATOM   2485  CD1 TYR B  77      92.985  63.350  30.523  1.00115.07           C  
ANISOU 2485  CD1 TYR B  77    12479  19214  12026   1503   2906  -2071       C  
ATOM   2486  CD2 TYR B  77      92.514  61.860  32.317  1.00115.72           C  
ANISOU 2486  CD2 TYR B  77    12463  18813  12692   1888   2611  -1939       C  
ATOM   2487  CE1 TYR B  77      93.390  62.294  29.748  1.00120.64           C  
ANISOU 2487  CE1 TYR B  77    13174  19962  12699   1619   2911  -2453       C  
ATOM   2488  CE2 TYR B  77      92.930  60.799  31.553  1.00120.80           C  
ANISOU 2488  CE2 TYR B  77    13080  19450  13366   2035   2533  -2299       C  
ATOM   2489  CZ  TYR B  77      93.364  61.023  30.267  1.00124.36           C  
ANISOU 2489  CZ  TYR B  77    13557  20177  13514   1917   2711  -2586       C  
ATOM   2490  OH  TYR B  77      93.765  59.969  29.489  1.00137.53           O  
ANISOU 2490  OH  TYR B  77    15200  21852  15203   2067   2676  -3022       O  
ATOM   2491  N   VAL B  78      89.291  62.962  33.286  1.00118.25           N  
ANISOU 2491  N   VAL B  78    13851  16073  15003   1811   -223    490       N  
ATOM   2492  CA  VAL B  78      88.570  61.679  33.295  1.00115.41           C  
ANISOU 2492  CA  VAL B  78    13716  16034  14099   2018    282     55       C  
ATOM   2493  C   VAL B  78      87.220  61.745  32.564  1.00118.27           C  
ANISOU 2493  C   VAL B  78    14217  16680  14037   2191    717   -260       C  
ATOM   2494  O   VAL B  78      86.783  60.759  31.952  1.00114.43           O  
ANISOU 2494  O   VAL B  78    13746  16445  13284   2337   1045   -388       O  
ATOM   2495  CB  VAL B  78      88.344  61.148  34.718  1.00111.93           C  
ANISOU 2495  CB  VAL B  78    13948  15250  13330   1930    -46   -296       C  
ATOM   2496  CG1 VAL B  78      87.972  59.667  34.674  1.00106.96           C  
ANISOU 2496  CG1 VAL B  78    13293  14942  12405   2113    420   -559       C  
ATOM   2497  CG2 VAL B  78      89.581  61.367  35.569  1.00115.51           C  
ANISOU 2497  CG2 VAL B  78    14509  15130  14250   1606   -965     81       C  
ATOM   2498  N   SER B  79      86.567  62.901  32.633  1.00123.13           N  
ANISOU 2498  N   SER B  79    14967  17122  14692   2142    594   -309       N  
ATOM   2499  CA  SER B  79      85.285  63.094  31.964  1.00126.14           C  
ANISOU 2499  CA  SER B  79    15299  17593  15035   2238    811   -414       C  
ATOM   2500  C   SER B  79      85.490  63.259  30.464  1.00129.84           C  
ANISOU 2500  C   SER B  79    15579  18299  15453   2242    820   -147       C  
ATOM   2501  O   SER B  79      84.591  62.997  29.680  1.00135.47           O  
ANISOU 2501  O   SER B  79    16398  19013  16058   2253    743   -166       O  
ATOM   2502  CB  SER B  79      84.556  64.310  32.539  1.00125.67           C  
ANISOU 2502  CB  SER B  79    15428  17145  15174   2243    810   -450       C  
ATOM   2503  OG  SER B  79      85.410  65.433  32.574  1.00128.57           O  
ANISOU 2503  OG  SER B  79    15837  17371  15642   2094    452   -255       O  
ATOM   2504  N   TYR B  80      86.688  63.700  30.083  1.00133.74           N  
ANISOU 2504  N   TYR B  80    15886  18829  16099   2228    872    199       N  
ATOM   2505  CA  TYR B  80      87.083  63.846  28.676  1.00135.03           C  
ANISOU 2505  CA  TYR B  80    16128  19061  16115   2350   1185    543       C  
ATOM   2506  C   TYR B  80      87.222  62.485  27.990  1.00128.52           C  
ANISOU 2506  C   TYR B  80    15779  18282  14771   2574   1627    514       C  
ATOM   2507  O   TYR B  80      86.761  62.298  26.862  1.00128.07           O  
ANISOU 2507  O   TYR B  80    16417  18102  14139   2663   1687    530       O  
ATOM   2508  CB  TYR B  80      88.386  64.657  28.598  1.00144.55           C  
ANISOU 2508  CB  TYR B  80    16852  20140  17931   2342   1324   1103       C  
ATOM   2509  CG  TYR B  80      89.246  64.442  27.369  1.00154.05           C  
ANISOU 2509  CG  TYR B  80    18139  21254  19138   2646   2142   1651       C  
ATOM   2510  CD1 TYR B  80      88.854  64.933  26.120  1.00157.72           C  
ANISOU 2510  CD1 TYR B  80    19200  21642  19084   2772   2410   1760       C  
ATOM   2511  CD2 TYR B  80      90.504  63.834  27.475  1.00160.44           C  
ANISOU 2511  CD2 TYR B  80    18485  21886  20586   2842   2721   2189       C  
ATOM   2512  CE1 TYR B  80      89.663  64.775  25.005  1.00166.24           C  
ANISOU 2512  CE1 TYR B  80    20702  22441  20020   3164   3425   2314       C  
ATOM   2513  CE2 TYR B  80      91.315  63.665  26.365  1.00168.56           C  
ANISOU 2513  CE2 TYR B  80    19655  22644  21746   3272   3861   2839       C  
ATOM   2514  CZ  TYR B  80      90.894  64.138  25.134  1.00172.09           C  
ANISOU 2514  CZ  TYR B  80    20971  22983  21430   3469   4304   2874       C  
ATOM   2515  OH  TYR B  80      91.702  63.981  24.036  1.00182.87           O  
ANISOU 2515  OH  TYR B  80    22817  23896  22767   4006   5689   3559       O  
ATOM   2516  N   THR B  81      87.806  61.524  28.696  1.00122.76           N  
ANISOU 2516  N   THR B  81    14867  17604  14169   2643   1821    464       N  
ATOM   2517  CA  THR B  81      87.881  60.157  28.189  1.00124.51           C  
ANISOU 2517  CA  THR B  81    15619  17814  13874   2877   2256    383       C  
ATOM   2518  C   THR B  81      86.494  59.475  28.074  1.00125.07           C  
ANISOU 2518  C   THR B  81    16233  17878  13411   2767   1754    -77       C  
ATOM   2519  O   THR B  81      86.375  58.415  27.480  1.00125.41           O  
ANISOU 2519  O   THR B  81    16988  17782  12879   2907   1886   -163       O  
ATOM   2520  CB  THR B  81      88.867  59.267  29.009  1.00123.11           C  
ANISOU 2520  CB  THR B  81    14996  17649  14130   2964   2547    513       C  
ATOM   2521  OG1 THR B  81      88.202  58.695  30.142  1.00115.54           O  
ANISOU 2521  OG1 THR B  81    13987  16813  13097   2774   2037     32       O  
ATOM   2522  CG2 THR B  81      90.081  60.072  29.475  1.00126.22           C  
ANISOU 2522  CG2 THR B  81    14549  17866  15542   2882   2531   1104       C  
ATOM   2523  N   PHE B  82      85.454  60.106  28.627  1.00127.57           N  
ANISOU 2523  N   PHE B  82    16221  18198  14051   2534   1199   -261       N  
ATOM   2524  CA  PHE B  82      84.089  59.530  28.595  1.00125.40           C  
ANISOU 2524  CA  PHE B  82    16105  17749  13793   2406    687   -444       C  
ATOM   2525  C   PHE B  82      83.102  60.347  27.748  1.00125.47           C  
ANISOU 2525  C   PHE B  82    16238  17452  13982   2218     72   -244       C  
ATOM   2526  O   PHE B  82      81.877  60.204  27.874  1.00126.36           O  
ANISOU 2526  O   PHE B  82    16086  17266  14658   2051   -470   -169       O  
ATOM   2527  CB  PHE B  82      83.549  59.351  30.011  1.00121.29           C  
ANISOU 2527  CB  PHE B  82    15049  17242  13792   2381    754   -638       C  
ATOM   2528  CG  PHE B  82      84.027  58.104  30.687  1.00118.17           C  
ANISOU 2528  CG  PHE B  82    14736  16985  13176   2482   1016   -847       C  
ATOM   2529  CD1 PHE B  82      83.324  56.909  30.555  1.00119.67           C  
ANISOU 2529  CD1 PHE B  82    15098  17067  13304   2472    814   -943       C  
ATOM   2530  CD2 PHE B  82      85.165  58.123  31.476  1.00114.79           C  
ANISOU 2530  CD2 PHE B  82    14196  16690  12728   2534   1295   -875       C  
ATOM   2531  CE1 PHE B  82      83.761  55.755  31.189  1.00117.13           C  
ANISOU 2531  CE1 PHE B  82    14846  16876  12783   2568   1065  -1138       C  
ATOM   2532  CE2 PHE B  82      85.600  56.975  32.119  1.00114.63           C  
ANISOU 2532  CE2 PHE B  82    14232  16736  12584   2595   1441  -1020       C  
ATOM   2533  CZ  PHE B  82      84.900  55.787  31.971  1.00113.33           C  
ANISOU 2533  CZ  PHE B  82    14248  16571  12240   2640   1416  -1190       C  
ATOM   2534  N   LYS B  83      83.636  61.209  26.898  1.00125.66           N  
ANISOU 2534  N   LYS B  83    16578  17454  13712   2244    153    -43       N  
ATOM   2535  CA  LYS B  83      82.821  61.934  25.937  1.00130.10           C  
ANISOU 2535  CA  LYS B  83    17470  17647  14313   2039   -544    183       C  
ATOM   2536  C   LYS B  83      81.808  62.896  26.614  1.00124.54           C  
ANISOU 2536  C   LYS B  83    15806  16844  14667   1866   -866    297       C  
ATOM   2537  O   LYS B  83      80.898  63.413  25.975  1.00127.41           O  
ANISOU 2537  O   LYS B  83    16167  16799  15443   1642  -1600    581       O  
ATOM   2538  CB  LYS B  83      82.122  60.945  24.967  1.00140.56           C  
ANISOU 2538  CB  LYS B  83    19861  18431  15112   1888  -1369    230       C  
ATOM   2539  CG  LYS B  83      83.077  59.959  24.268  1.00143.97           C  
ANISOU 2539  CG  LYS B  83    21603  18757  14340   2176   -829    126       C  
ATOM   2540  CD  LYS B  83      82.347  58.709  23.785  1.00147.67           C  
ANISOU 2540  CD  LYS B  83    23125  18649  14332   2012  -1719     55       C  
ATOM   2541  CE  LYS B  83      81.401  59.037  22.639  1.00157.51           C  
ANISOU 2541  CE  LYS B  83    25480  19043  15323   1631  -3142    336       C  
ATOM   2542  NZ  LYS B  83      80.036  58.481  22.859  1.00159.27           N  
ANISOU 2542  NZ  LYS B  83    25250  18757  16506   1161  -4616    526       N  
ATOM   2543  N   LEU B  84      82.000  63.141  27.901  1.00118.54           N  
ANISOU 2543  N   LEU B  84    14391  16311  14334   1995   -294    134       N  
ATOM   2544  CA  LEU B  84      81.263  64.182  28.593  1.00119.88           C  
ANISOU 2544  CA  LEU B  84    13953  16262  15330   1993   -194    257       C  
ATOM   2545  C   LEU B  84      81.958  65.527  28.431  1.00118.38           C  
ANISOU 2545  C   LEU B  84    13761  16195  15022   1985    -81    324       C  
ATOM   2546  O   LEU B  84      82.467  66.096  29.404  1.00112.94           O  
ANISOU 2546  O   LEU B  84    13006  15532  14373   2080    295    195       O  
ATOM   2547  CB  LEU B  84      81.134  63.845  30.076  1.00119.30           C  
ANISOU 2547  CB  LEU B  84    13683  16126  15517   2195    440     51       C  
ATOM   2548  CG  LEU B  84      80.539  62.498  30.470  1.00120.86           C  
ANISOU 2548  CG  LEU B  84    13792  16209  15920   2251    510      5       C  
ATOM   2549  CD1 LEU B  84      80.699  62.318  31.964  1.00120.68           C  
ANISOU 2549  CD1 LEU B  84    13923  16085  15845   2502   1281   -229       C  
ATOM   2550  CD2 LEU B  84      79.067  62.401  30.083  1.00127.76           C  
ANISOU 2550  CD2 LEU B  84    14085  16535  17923   2150    105    484       C  
ATOM   2551  N   TYR B  85      81.973  66.043  27.205  1.00123.43           N  
ANISOU 2551  N   TYR B  85    14636  16781  15477   1849   -511    558       N  
ATOM   2552  CA  TYR B  85      82.787  67.225  26.897  1.00129.41           C  
ANISOU 2552  CA  TYR B  85    15395  17670  16102   1849   -372    689       C  
ATOM   2553  C   TYR B  85      82.270  68.509  27.544  1.00130.16           C  
ANISOU 2553  C   TYR B  85    15015  17558  16878   1826   -358    760       C  
ATOM   2554  O   TYR B  85      82.994  69.494  27.635  1.00128.74           O  
ANISOU 2554  O   TYR B  85    14792  17444  16676   1815   -269    830       O  
ATOM   2555  CB  TYR B  85      82.975  67.408  25.375  1.00136.94           C  
ANISOU 2555  CB  TYR B  85    16988  18517  16523   1775   -677    948       C  
ATOM   2556  CG  TYR B  85      83.343  66.132  24.646  1.00138.74           C  
ANISOU 2556  CG  TYR B  85    18118  18688  15907   1881   -586    898       C  
ATOM   2557  CD1 TYR B  85      84.650  65.629  24.676  1.00138.29           C  
ANISOU 2557  CD1 TYR B  85    18263  18856  15424   2159    248    917       C  
ATOM   2558  CD2 TYR B  85      82.380  65.418  23.946  1.00143.90           C  
ANISOU 2558  CD2 TYR B  85    19460  18902  16312   1701  -1385    925       C  
ATOM   2559  CE1 TYR B  85      84.974  64.448  24.020  1.00145.42           C  
ANISOU 2559  CE1 TYR B  85    20143  19583  15526   2356    548    895       C  
ATOM   2560  CE2 TYR B  85      82.692  64.246  23.278  1.00149.67           C  
ANISOU 2560  CE2 TYR B  85    21362  19414  16092   1814  -1351    849       C  
ATOM   2561  CZ  TYR B  85      83.981  63.759  23.315  1.00149.83           C  
ANISOU 2561  CZ  TYR B  85    21685  19697  15545   2192   -251    796       C  
ATOM   2562  OH  TYR B  85      84.265  62.582  22.655  1.00153.60           O  
ANISOU 2562  OH  TYR B  85    23477  19836  15046   2393    -29    740       O  
ATOM   2563  N   GLY B  86      81.020  68.488  28.001  1.00137.09           N  
ANISOU 2563  N   GLY B  86    15538  18068  18482   1852   -376    832       N  
ATOM   2564  CA  GLY B  86      80.462  69.609  28.758  1.00136.35           C  
ANISOU 2564  CA  GLY B  86    15149  17598  19060   1977    -23    933       C  
ATOM   2565  C   GLY B  86      81.188  69.801  30.075  1.00135.25           C  
ANISOU 2565  C   GLY B  86    15458  17417  18515   2168    534    605       C  
ATOM   2566  O   GLY B  86      81.585  70.924  30.416  1.00126.86           O  
ANISOU 2566  O   GLY B  86    14636  16174  17389   2177    563    598       O  
ATOM   2567  N   GLU B  87      81.399  68.684  30.788  1.00139.20           N  
ANISOU 2567  N   GLU B  87    16215  17990  18684   2272    805    354       N  
ATOM   2568  CA  GLU B  87      81.993  68.680  32.137  1.00143.66           C  
ANISOU 2568  CA  GLU B  87    17500  18299  18783   2411   1144     60       C  
ATOM   2569  C   GLU B  87      83.504  68.962  32.135  1.00139.23           C  
ANISOU 2569  C   GLU B  87    17199  17972  17730   2177    583     11       C  
ATOM   2570  O   GLU B  87      84.011  69.712  32.986  1.00135.01           O  
ANISOU 2570  O   GLU B  87    17325  16984  16990   2139    392    -51       O  
ATOM   2571  CB  GLU B  87      81.707  67.340  32.849  1.00148.16           C  
ANISOU 2571  CB  GLU B  87    18257  18823  19213   2573   1547   -128       C  
ATOM   2572  CG  GLU B  87      80.250  67.138  33.287  1.00161.19           C  
ANISOU 2572  CG  GLU B  87    19681  19926  21637   2896   2333     82       C  
ATOM   2573  CD  GLU B  87      79.880  67.895  34.576  1.00170.91           C  
ANISOU 2573  CD  GLU B  87    21835  20297  22804   3300   3277     47       C  
ATOM   2574  OE1 GLU B  87      80.295  67.445  35.688  1.00176.86           O  
ANISOU 2574  OE1 GLU B  87    23663  20728  22804   3458   3617   -259       O  
ATOM   2575  OE2 GLU B  87      79.142  68.916  34.479  1.00165.94           O  
ANISOU 2575  OE2 GLU B  87    21021  19184  22843   3491   3718    361       O  
HETATM 2576  N   MSE B  88      84.214  68.343  31.192  1.00156.21           N  
ANISOU 2576  N   MSE B  88    20968  20970  17413  -1081  -1961  -1834       N  
HETATM 2577  CA  MSE B  88      85.667  68.495  31.086  1.00154.65           C  
ANISOU 2577  CA  MSE B  88    20905  20750  17103   -619  -1625  -1854       C  
HETATM 2578  C   MSE B  88      86.069  69.940  30.839  1.00146.96           C  
ANISOU 2578  C   MSE B  88    19619  20341  15876   -381  -1506  -1313       C  
HETATM 2579  O   MSE B  88      87.130  70.385  31.287  1.00143.42           O  
ANISOU 2579  O   MSE B  88    19147  19794  15551    -77  -1246  -1047       O  
HETATM 2580  CB  MSE B  88      86.232  67.542  30.013  1.00166.08           C  
ANISOU 2580  CB  MSE B  88    22701  22233  18167   -496  -1580  -2539       C  
HETATM 2581  CG  MSE B  88      85.836  67.934  28.589  1.00180.65           C  
ANISOU 2581  CG  MSE B  88    24444  24901  19291   -572  -1767  -2727       C  
HETATM 2582 SE   MSE B  88      87.405  68.076  27.389  1.00193.23          SE  
ANISOU 2582 SE   MSE B  88    26159  27053  20206     43  -1416  -2935      SE  
HETATM 2583  CE  MSE B  88      88.116  69.813  28.014  1.00172.92           C  
ANISOU 2583  CE  MSE B  88    23090  24791  17818    340  -1183  -1883       C  
HETATM 2584  N   MSE B  89      85.231  70.685  30.126  1.00145.39           N  
ANISOU 2584  N   MSE B  89    19152  20741  15348   -536  -1698  -1103       N  
HETATM 2585  CA  MSE B  89      85.540  72.082  29.858  1.00140.78           C  
ANISOU 2585  CA  MSE B  89    18251  20638  14599   -319  -1577   -530       C  
HETATM 2586  C   MSE B  89      85.153  72.899  31.029  1.00129.82           C  
ANISOU 2586  C   MSE B  89    16687  18940  13696   -357  -1527    -22       C  
HETATM 2587  O   MSE B  89      85.749  73.916  31.276  1.00123.16           O  
ANISOU 2587  O   MSE B  89    15704  18139  12950   -152  -1350    393       O  
HETATM 2588  CB  MSE B  89      84.922  72.643  28.580  1.00155.30           C  
ANISOU 2588  CB  MSE B  89    19818  23308  15881   -386  -1743   -399       C  
HETATM 2589  CG  MSE B  89      83.441  72.327  28.455  1.00172.36           C  
ANISOU 2589  CG  MSE B  89    21859  25627  18000   -803  -2077   -473       C  
HETATM 2590 SE   MSE B  89      82.783  72.851  26.677  1.00208.93          SE  
ANISOU 2590 SE   MSE B  89    26117  31492  21772   -892  -2309   -350      SE  
HETATM 2591  CE  MSE B  89      83.536  71.411  25.550  1.00201.73           C  
ANISOU 2591  CE  MSE B  89    25679  30740  20227   -878  -2369  -1391       C  
ATOM   2592  N   LEU B  90      84.162  72.436  31.786  1.00128.35           N  
ANISOU 2592  N   LEU B  90    16514  18424  13827   -623  -1679    -63       N  
ATOM   2593  CA  LEU B  90      83.693  73.154  32.974  1.00122.31           C  
ANISOU 2593  CA  LEU B  90    15597  17386  13486   -624  -1612    382       C  
ATOM   2594  C   LEU B  90      84.788  73.184  34.018  1.00119.85           C  
ANISOU 2594  C   LEU B  90    15445  16598  13492   -424  -1377    412       C  
ATOM   2595  O   LEU B  90      85.149  74.245  34.534  1.00112.65           O  
ANISOU 2595  O   LEU B  90    14431  15651  12718   -276  -1229    770       O  
ATOM   2596  CB  LEU B  90      82.453  72.462  33.555  1.00122.97           C  
ANISOU 2596  CB  LEU B  90    15641  17268  13813   -933  -1816    337       C  
ATOM   2597  CG  LEU B  90      81.405  73.238  34.380  1.00118.66           C  
ANISOU 2597  CG  LEU B  90    14825  16734  13524   -964  -1815    842       C  
ATOM   2598  CD1 LEU B  90      80.858  72.343  35.475  1.00117.72           C  
ANISOU 2598  CD1 LEU B  90    14757  16181  13790  -1143  -1879    785       C  
ATOM   2599  CD2 LEU B  90      81.939  74.529  34.972  1.00113.38           C  
ANISOU 2599  CD2 LEU B  90    14097  15982  12998   -657  -1552   1220       C  
ATOM   2600  N   ASN B  91      85.306  72.000  34.333  1.00125.04           N  
ANISOU 2600  N   ASN B  91    16349  16881  14279   -435  -1347     39       N  
ATOM   2601  CA  ASN B  91      86.380  71.847  35.298  1.00124.86           C  
ANISOU 2601  CA  ASN B  91    16438  16482  14520   -255  -1135     87       C  
ATOM   2602  C   ASN B  91      87.635  72.604  34.894  1.00127.56           C  
ANISOU 2602  C   ASN B  91    16742  17056  14668      3   -953    249       C  
ATOM   2603  O   ASN B  91      88.234  73.301  35.714  1.00129.66           O  
ANISOU 2603  O   ASN B  91    16940  17205  15118     82   -832    534       O  
ATOM   2604  CB  ASN B  91      86.712  70.371  35.484  1.00128.20           C  
ANISOU 2604  CB  ASN B  91    17104  16498  15107   -269  -1108   -299       C  
ATOM   2605  CG  ASN B  91      85.563  69.587  36.078  1.00130.30           C  
ANISOU 2605  CG  ASN B  91    17372  16450  15682   -558  -1283   -370       C  
ATOM   2606  OD1 ASN B  91      85.478  69.410  37.295  1.00130.16           O  
ANISOU 2606  OD1 ASN B  91    17299  16128  16026   -570  -1221   -155       O  
ATOM   2607  ND2 ASN B  91      84.677  69.109  35.226  1.00132.46           N  
ANISOU 2607  ND2 ASN B  91    17679  16851  15798   -812  -1516   -643       N  
ATOM   2608  N   LEU B  92      88.011  72.472  33.616  1.00131.55           N  
ANISOU 2608  N   LEU B  92    17274  17933  14775    113   -948     72       N  
ATOM   2609  CA  LEU B  92      89.275  73.011  33.082  1.00130.17           C  
ANISOU 2609  CA  LEU B  92    17030  18048  14379    384   -763    250       C  
ATOM   2610  C   LEU B  92      89.280  74.547  32.977  1.00126.22           C  
ANISOU 2610  C   LEU B  92    16255  17830  13872    393   -750    769       C  
ATOM   2611  O   LEU B  92      90.097  75.223  33.615  1.00124.70           O  
ANISOU 2611  O   LEU B  92    15990  17505  13883    454   -631   1069       O  
ATOM   2612  CB  LEU B  92      89.566  72.383  31.714  1.00135.17           C  
ANISOU 2612  CB  LEU B  92    17760  19068  14528    534   -748    -98       C  
ATOM   2613  CG  LEU B  92      90.956  71.813  31.380  1.00137.99           C  
ANISOU 2613  CG  LEU B  92    18237  19469  14721    881   -498   -229       C  
ATOM   2614  CD1 LEU B  92      91.813  71.549  32.620  1.00131.10           C  
ANISOU 2614  CD1 LEU B  92    17407  18128  14276    971   -327    -60       C  
ATOM   2615  CD2 LEU B  92      90.814  70.550  30.519  1.00141.55           C  
ANISOU 2615  CD2 LEU B  92    18987  19927  14869    957   -507   -876       C  
ATOM   2616  N   LEU B  93      88.364  75.091  32.186  1.00126.32           N  
ANISOU 2616  N   LEU B  93    16102  18219  13672    312   -878    893       N  
ATOM   2617  CA  LEU B  93      88.298  76.538  31.984  1.00127.49           C  
ANISOU 2617  CA  LEU B  93    15978  18597  13866    351   -837   1430       C  
ATOM   2618  C   LEU B  93      87.716  77.271  33.185  1.00126.89           C  
ANISOU 2618  C   LEU B  93    15885  18082  14243    236   -832   1661       C  
ATOM   2619  O   LEU B  93      88.048  78.428  33.421  1.00129.78           O  
ANISOU 2619  O   LEU B  93    16133  18370  14807    283   -735   2042       O  
ATOM   2620  CB  LEU B  93      87.515  76.889  30.710  1.00128.82           C  
ANISOU 2620  CB  LEU B  93    15913  19387  13642    346   -947   1577       C  
ATOM   2621  CG  LEU B  93      87.732  75.937  29.525  1.00135.02           C  
ANISOU 2621  CG  LEU B  93    16773  20654  13872    413  -1008   1171       C  
ATOM   2622  CD1 LEU B  93      86.742  76.203  28.397  1.00135.23           C  
ANISOU 2622  CD1 LEU B  93    16548  21363  13469    330  -1179   1286       C  
ATOM   2623  CD2 LEU B  93      89.175  75.968  29.020  1.00136.88           C  
ANISOU 2623  CD2 LEU B  93    17000  21118  13890    703   -804   1234       C  
ATOM   2624  N   VAL B  94      86.870  76.593  33.961  1.00124.84           N  
ANISOU 2624  N   VAL B  94    15750  17523  14157     93   -924   1426       N  
ATOM   2625  CA  VAL B  94      86.150  77.262  35.047  1.00119.75           C  
ANISOU 2625  CA  VAL B  94    15077  16560  13862     37   -900   1634       C  
ATOM   2626  C   VAL B  94      86.733  76.973  36.432  1.00113.15           C  
ANISOU 2626  C   VAL B  94    14419  15262  13310     20   -820   1502       C  
ATOM   2627  O   VAL B  94      87.124  77.890  37.143  1.00104.96           O  
ANISOU 2627  O   VAL B  94    13388  14019  12470     51   -721   1683       O  
ATOM   2628  CB  VAL B  94      84.633  76.940  35.033  1.00121.08           C  
ANISOU 2628  CB  VAL B  94    15149  16828  14026    -93  -1047   1636       C  
ATOM   2629  CG1 VAL B  94      83.903  77.778  36.069  1.00118.96           C  
ANISOU 2629  CG1 VAL B  94    14820  16305  14073    -49   -957   1915       C  
ATOM   2630  CG2 VAL B  94      84.046  77.179  33.654  1.00122.82           C  
ANISOU 2630  CG2 VAL B  94    15144  17621  13900   -110  -1157   1789       C  
ATOM   2631  N   TYR B  95      86.768  75.701  36.814  1.00115.35           N  
ANISOU 2631  N   TYR B  95    14833  15381  13612    -41   -869   1194       N  
ATOM   2632  CA  TYR B  95      87.067  75.340  38.203  1.00115.58           C  
ANISOU 2632  CA  TYR B  95    14960  15056  13897    -60   -806   1142       C  
ATOM   2633  C   TYR B  95      88.532  75.519  38.541  1.00114.80           C  
ANISOU 2633  C   TYR B  95    14905  14901  13811     21   -686   1182       C  
ATOM   2634  O   TYR B  95      88.859  76.025  39.614  1.00119.86           O  
ANISOU 2634  O   TYR B  95    15554  15380  14605     -6   -635   1283       O  
ATOM   2635  CB  TYR B  95      86.631  73.889  38.534  1.00118.87           C  
ANISOU 2635  CB  TYR B  95    15461  15292  14411   -150   -879    897       C  
ATOM   2636  CG  TYR B  95      85.114  73.650  38.667  1.00118.33           C  
ANISOU 2636  CG  TYR B  95    15299  15230  14428   -303  -1020    936       C  
ATOM   2637  CD1 TYR B  95      84.209  74.717  38.888  1.00114.30           C  
ANISOU 2637  CD1 TYR B  95    14638  14846  13945   -286  -1016   1221       C  
ATOM   2638  CD2 TYR B  95      84.599  72.355  38.604  1.00118.81           C  
ANISOU 2638  CD2 TYR B  95    15410  15149  14582   -461  -1143    726       C  
ATOM   2639  CE1 TYR B  95      82.848  74.488  39.001  1.00114.89           C  
ANISOU 2639  CE1 TYR B  95    14565  15003  14085   -402  -1131   1342       C  
ATOM   2640  CE2 TYR B  95      83.243  72.117  38.717  1.00122.92           C  
ANISOU 2640  CE2 TYR B  95    15791  15718  15194   -649  -1299    826       C  
ATOM   2641  CZ  TYR B  95      82.366  73.177  38.912  1.00121.55           C  
ANISOU 2641  CZ  TYR B  95    15418  15765  14997   -611  -1293   1159       C  
ATOM   2642  OH  TYR B  95      81.010  72.908  39.026  1.00123.32           O  
ANISOU 2642  OH  TYR B  95    15444  16106  15304   -783  -1440   1338       O  
ATOM   2643  N   VAL B  96      89.416  75.079  37.637  1.00117.23           N  
ANISOU 2643  N   VAL B  96    15229  15388  13925    124   -644   1104       N  
ATOM   2644  CA  VAL B  96      90.874  75.088  37.896  1.00112.99           C  
ANISOU 2644  CA  VAL B  96    14675  14872  13383    219   -523   1209       C  
ATOM   2645  C   VAL B  96      91.428  76.498  38.214  1.00109.67           C  
ANISOU 2645  C   VAL B  96    14142  14488  13040    149   -505   1519       C  
ATOM   2646  O   VAL B  96      92.222  76.649  39.163  1.00111.74           O  
ANISOU 2646  O   VAL B  96    14389  14649  13416     84   -475   1607       O  
ATOM   2647  CB  VAL B  96      91.693  74.403  36.760  1.00111.42           C  
ANISOU 2647  CB  VAL B  96    14491  14919  12922    417   -436   1106       C  
ATOM   2648  CG1 VAL B  96      93.174  74.641  36.960  1.00111.01           C  
ANISOU 2648  CG1 VAL B  96    14329  14991  12856    528   -303   1359       C  
ATOM   2649  CG2 VAL B  96      91.413  72.904  36.727  1.00111.28           C  
ANISOU 2649  CG2 VAL B  96    14655  14697  12927    476   -421    739       C  
ATOM   2650  N   PRO B  97      91.011  77.533  37.429  1.00104.28           N  
ANISOU 2650  N   PRO B  97    13364  13947  12310    140   -532   1705       N  
ATOM   2651  CA  PRO B  97      91.394  78.915  37.813  1.00102.82           C  
ANISOU 2651  CA  PRO B  97    13111  13646  12311     36   -518   1983       C  
ATOM   2652  C   PRO B  97      90.676  79.395  39.056  1.00104.54           C  
ANISOU 2652  C   PRO B  97    13449  13508  12762    -77   -537   1893       C  
ATOM   2653  O   PRO B  97      91.207  80.232  39.787  1.00104.26           O  
ANISOU 2653  O   PRO B  97    13448  13279  12887   -205   -533   1963       O  
ATOM   2654  CB  PRO B  97      90.977  79.770  36.615  1.00102.14           C  
ANISOU 2654  CB  PRO B  97    12870  13781  12156    102   -511   2250       C  
ATOM   2655  CG  PRO B  97      90.286  78.867  35.664  1.00104.54           C  
ANISOU 2655  CG  PRO B  97    13158  14392  12170    215   -552   2079       C  
ATOM   2656  CD  PRO B  97      90.500  77.444  36.053  1.00103.28           C  
ANISOU 2656  CD  PRO B  97    13160  14152  11930    236   -561   1708       C  
ATOM   2657  N   VAL B  98      89.482  78.858  39.309  1.00109.55           N  
ANISOU 2657  N   VAL B  98    14145  14079  13400    -39   -563   1730       N  
ATOM   2658  CA  VAL B  98      88.631  79.382  40.391  1.00111.49           C  
ANISOU 2658  CA  VAL B  98    14476  14063  13821    -68   -540   1688       C  
ATOM   2659  C   VAL B  98      89.100  79.046  41.812  1.00108.25           C  
ANISOU 2659  C   VAL B  98    14164  13507  13456   -148   -535   1527       C  
ATOM   2660  O   VAL B  98      89.047  79.909  42.685  1.00109.20           O  
ANISOU 2660  O   VAL B  98    14376  13437  13675   -199   -502   1493       O  
ATOM   2661  CB  VAL B  98      87.114  79.084  40.187  1.00113.34           C  
ANISOU 2661  CB  VAL B  98    14662  14352  14047      6   -561   1692       C  
ATOM   2662  CG1 VAL B  98      86.641  77.925  41.071  1.00109.76           C  
ANISOU 2662  CG1 VAL B  98    14248  13849  13606    -21   -599   1514       C  
ATOM   2663  CG2 VAL B  98      86.301  80.343  40.471  1.00111.74           C  
ANISOU 2663  CG2 VAL B  98    14461  13982  14010     88   -466   1865       C  
ATOM   2664  N   GLN B  99      89.572  77.808  42.036  1.00101.64           N  
ANISOU 2664  N   GLN B  99    13306  12770  12541   -145   -556   1433       N  
ATOM   2665  CA  GLN B  99      90.220  77.466  43.297  1.00100.76           C  
ANISOU 2665  CA  GLN B  99    13208  12640  12435   -213   -548   1382       C  
ATOM   2666  C   GLN B  99      91.091  78.624  43.771  1.00105.92           C  
ANISOU 2666  C   GLN B  99    13891  13250  13100   -366   -567   1424       C  
ATOM   2667  O   GLN B  99      91.212  78.866  44.968  1.00112.52           O  
ANISOU 2667  O   GLN B  99    14778  14058  13914   -461   -582   1329       O  
ATOM   2668  CB  GLN B  99      91.093  76.232  43.159  1.00101.26           C  
ANISOU 2668  CB  GLN B  99    13198  12830  12444   -162   -527   1403       C  
ATOM   2669  CG  GLN B  99      90.465  75.097  42.419  1.00107.03           C  
ANISOU 2669  CG  GLN B  99    13946  13531  13190    -54   -522   1305       C  
ATOM   2670  CD  GLN B  99      89.180  74.694  43.032  1.00114.23           C  
ANISOU 2670  CD  GLN B  99    14866  14323  14210    -74   -556   1250       C  
ATOM   2671  OE1 GLN B  99      89.140  74.206  44.160  1.00130.73           O  
ANISOU 2671  OE1 GLN B  99    16911  16384  16375    -80   -530   1295       O  
ATOM   2672  NE2 GLN B  99      88.105  74.928  42.325  1.00121.12           N  
ANISOU 2672  NE2 GLN B  99    15747  15194  15077    -83   -615   1218       N  
ATOM   2673  N   PHE B 100      91.726  79.320  42.827  1.00109.04           N  
ANISOU 2673  N   PHE B 100    14239  13672  13518   -411   -578   1574       N  
ATOM   2674  CA  PHE B 100      92.660  80.374  43.177  1.00111.43           C  
ANISOU 2674  CA  PHE B 100    14544  13904  13887   -626   -630   1651       C  
ATOM   2675  C   PHE B 100      91.901  81.609  43.545  1.00112.88           C  
ANISOU 2675  C   PHE B 100    14897  13749  14240   -680   -611   1549       C  
ATOM   2676  O   PHE B 100      92.105  82.159  44.630  1.00122.30           O  
ANISOU 2676  O   PHE B 100    16221  14793  15451   -847   -650   1368       O  
ATOM   2677  CB  PHE B 100      93.692  80.636  42.050  1.00112.34           C  
ANISOU 2677  CB  PHE B 100    14487  14197  13996   -656   -640   1944       C  
ATOM   2678  CG  PHE B 100      94.720  79.532  41.902  1.00111.74           C  
ANISOU 2678  CG  PHE B 100    14251  14452  13750   -583   -620   2056       C  
ATOM   2679  CD1 PHE B 100      94.487  78.451  41.050  1.00110.03           C  
ANISOU 2679  CD1 PHE B 100    14006  14394  13406   -320   -531   2027       C  
ATOM   2680  CD2 PHE B 100      95.893  79.541  42.658  1.00114.09           C  
ANISOU 2680  CD2 PHE B 100    14432  14904  14012   -771   -681   2178       C  
ATOM   2681  CE1 PHE B 100      95.404  77.419  40.940  1.00107.40           C  
ANISOU 2681  CE1 PHE B 100    13562  14291  12952   -182   -455   2113       C  
ATOM   2682  CE2 PHE B 100      96.817  78.507  42.547  1.00112.20           C  
ANISOU 2682  CE2 PHE B 100    14012  14980  13635   -637   -613   2352       C  
ATOM   2683  CZ  PHE B 100      96.569  77.450  41.687  1.00109.63           C  
ANISOU 2683  CZ  PHE B 100    13694  14735  13225   -310   -475   2315       C  
ATOM   2684  N   VAL B 101      90.964  82.019  42.693  1.00108.04           N  
ANISOU 2684  N   VAL B 101    14288  13031  13731   -517   -537   1651       N  
ATOM   2685  CA  VAL B 101      90.163  83.205  43.016  1.00109.61           C  
ANISOU 2685  CA  VAL B 101    14645  12862  14137   -485   -455   1601       C  
ATOM   2686  C   VAL B 101      89.466  83.033  44.366  1.00112.20           C  
ANISOU 2686  C   VAL B 101    15145  13091  14394   -428   -411   1298       C  
ATOM   2687  O   VAL B 101      89.467  83.941  45.191  1.00113.81           O  
ANISOU 2687  O   VAL B 101    15552  13001  14687   -502   -375   1100       O  
ATOM   2688  CB  VAL B 101      89.113  83.523  41.958  1.00106.37           C  
ANISOU 2688  CB  VAL B 101    14142  12450  13820   -262   -359   1837       C  
ATOM   2689  CG1 VAL B 101      88.792  85.003  41.995  1.00106.87           C  
ANISOU 2689  CG1 VAL B 101    14322  12082  14200   -238   -244   1937       C  
ATOM   2690  CG2 VAL B 101      89.602  83.112  40.586  1.00106.39           C  
ANISOU 2690  CG2 VAL B 101    13916  12796  13708   -241   -409   2104       C  
ATOM   2691  N   GLY B 102      88.901  81.844  44.585  1.00109.91           N  
ANISOU 2691  N   GLY B 102    14768  13051  13938   -300   -412   1261       N  
ATOM   2692  CA  GLY B 102      88.173  81.533  45.806  1.00106.02           C  
ANISOU 2692  CA  GLY B 102    14354  12578  13349   -203   -356   1077       C  
ATOM   2693  C   GLY B 102      89.028  81.631  47.043  1.00105.11           C  
ANISOU 2693  C   GLY B 102    14335  12508  13094   -385   -415    853       C  
ATOM   2694  O   GLY B 102      88.651  82.293  48.021  1.00106.31           O  
ANISOU 2694  O   GLY B 102    14667  12531  13195   -351   -347    622       O  
ATOM   2695  N   PHE B 103      90.173  80.953  47.012  1.00102.71           N  
ANISOU 2695  N   PHE B 103    13899  12434  12692   -558   -531    925       N  
ATOM   2696  CA  PHE B 103      91.140  81.031  48.095  1.00103.10           C  
ANISOU 2696  CA  PHE B 103    13961  12640  12570   -784   -626    789       C  
ATOM   2697  C   PHE B 103      91.456  82.475  48.457  1.00106.01           C  
ANISOU 2697  C   PHE B 103    14560  12710  13008   -999   -669    559       C  
ATOM   2698  O   PHE B 103      91.639  82.810  49.640  1.00107.09           O  
ANISOU 2698  O   PHE B 103    14823  12908  12957  -1136   -716    278       O  
ATOM   2699  CB  PHE B 103      92.433  80.312  47.732  1.00102.59           C  
ANISOU 2699  CB  PHE B 103    13677  12853  12449   -926   -724   1014       C  
ATOM   2700  CG  PHE B 103      93.402  80.250  48.860  1.00108.06           C  
ANISOU 2700  CG  PHE B 103    14293  13836  12926  -1164   -837    966       C  
ATOM   2701  CD1 PHE B 103      93.311  79.237  49.807  1.00112.61           C  
ANISOU 2701  CD1 PHE B 103    14726  14751  13306  -1069   -812   1010       C  
ATOM   2702  CD2 PHE B 103      94.343  81.247  49.041  1.00110.64           C  
ANISOU 2702  CD2 PHE B 103    14669  14120  13247  -1509   -982    899       C  
ATOM   2703  CE1 PHE B 103      94.185  79.179  50.885  1.00114.37           C  
ANISOU 2703  CE1 PHE B 103    14823  15358  13271  -1289   -924   1015       C  
ATOM   2704  CE2 PHE B 103      95.205  81.211  50.116  1.00116.22           C  
ANISOU 2704  CE2 PHE B 103    15279  15178  13701  -1783  -1127    848       C  
ATOM   2705  CZ  PHE B 103      95.127  80.171  51.044  1.00118.39           C  
ANISOU 2705  CZ  PHE B 103    15382  15880  13719  -1659  -1095    912       C  
ATOM   2706  N   ALA B 104      91.556  83.316  47.424  1.00106.09           N  
ANISOU 2706  N   ALA B 104    14616  12405  13285  -1042   -657    684       N  
ATOM   2707  CA  ALA B 104      91.812  84.732  47.590  1.00111.53           C  
ANISOU 2707  CA  ALA B 104    15536  12668  14172  -1253   -682    509       C  
ATOM   2708  C   ALA B 104      90.776  85.346  48.502  1.00118.27           C  
ANISOU 2708  C   ALA B 104    16689  13243  15005  -1077   -536    143       C  
ATOM   2709  O   ALA B 104      91.121  85.897  49.548  1.00124.06           O  
ANISOU 2709  O   ALA B 104    17640  13883  15613  -1284   -602   -234       O  
ATOM   2710  CB  ALA B 104      91.815  85.434  46.240  1.00110.19           C  
ANISOU 2710  CB  ALA B 104    15308  12215  14343  -1224   -633    824       C  
HETATM 2711  N   MSE B 105      89.496  85.176  48.138  1.00120.34           N  
ANISOU 2711  N   MSE B 105    16941  13444  15337   -687   -340    255       N  
HETATM 2712  CA  MSE B 105      88.395  85.899  48.774  1.00121.92           C  
ANISOU 2712  CA  MSE B 105    17399  13346  15578   -414   -127     12       C  
HETATM 2713  C   MSE B 105      88.001  85.312  50.079  1.00117.96           C  
ANISOU 2713  C   MSE B 105    16939  13175  14703   -295    -91   -252       C  
HETATM 2714  O   MSE B 105      87.572  86.034  50.965  1.00123.15           O  
ANISOU 2714  O   MSE B 105    17878  13635  15277   -176     40   -612       O  
HETATM 2715  CB  MSE B 105      87.174  85.849  47.905  1.00129.10           C  
ANISOU 2715  CB  MSE B 105    18184  14201  16666    -38     61    342       C  
HETATM 2716  CG  MSE B 105      87.167  86.996  46.924  1.00144.40           C  
ANISOU 2716  CG  MSE B 105    20186  15668  19011    -24    148    544       C  
HETATM 2717 SE   MSE B 105      86.212  86.393  45.309  1.00175.92          SE  
ANISOU 2717 SE   MSE B 105    23776  19975  23090    258    211   1161      SE  
HETATM 2718  CE  MSE B 105      86.640  84.469  45.336  1.00151.51           C  
ANISOU 2718  CE  MSE B 105    20421  17545  19598    108    -24   1158       C  
ATOM   2719  N   TRP B 106      88.094  83.994  50.212  1.00109.49           N  
ANISOU 2719  N   TRP B 106    15584  12607  13407   -287   -179    -63       N  
ATOM   2720  CA  TRP B 106      87.733  83.358  51.474  1.00109.55           C  
ANISOU 2720  CA  TRP B 106    15552  13009  13061   -164   -139   -206       C  
ATOM   2721  C   TRP B 106      88.680  83.798  52.600  1.00117.98           C  
ANISOU 2721  C   TRP B 106    16788  14198  13840   -457   -268   -604       C  
ATOM   2722  O   TRP B 106      88.239  84.168  53.696  1.00120.26           O  
ANISOU 2722  O   TRP B 106    17262  14575  13856   -327   -167   -943       O  
ATOM   2723  CB  TRP B 106      87.726  81.841  51.341  1.00101.35           C  
ANISOU 2723  CB  TRP B 106    14157  12413  11935   -127   -208    138       C  
ATOM   2724  CG  TRP B 106      86.386  81.230  50.958  1.00 98.60           C  
ANISOU 2724  CG  TRP B 106    13648  12121  11693    195    -71    414       C  
ATOM   2725  CD1 TRP B 106      85.470  81.732  50.073  1.00 98.57           C  
ANISOU 2725  CD1 TRP B 106    13675  11851  11925    385     43    553       C  
ATOM   2726  CD2 TRP B 106      85.860  79.971  51.397  1.00 95.59           C  
ANISOU 2726  CD2 TRP B 106    12996  12111  11210    315    -61    656       C  
ATOM   2727  NE1 TRP B 106      84.416  80.868  49.941  1.00 94.98           N  
ANISOU 2727  NE1 TRP B 106    12984  11616  11488    579     94    839       N  
ATOM   2728  CE2 TRP B 106      84.636  79.776  50.739  1.00 93.76           C  
ANISOU 2728  CE2 TRP B 106    12653  11810  11159    527     28    900       C  
ATOM   2729  CE3 TRP B 106      86.318  78.980  52.267  1.00 96.35           C  
ANISOU 2729  CE3 TRP B 106    12895  12602  11108    250   -123    747       C  
ATOM   2730  CZ2 TRP B 106      83.856  78.638  50.938  1.00 92.31           C  
ANISOU 2730  CZ2 TRP B 106    12191  11891  10988    629     34   1198       C  
ATOM   2731  CZ3 TRP B 106      85.529  77.859  52.476  1.00 94.81           C  
ANISOU 2731  CZ3 TRP B 106    12427  12639  10957    401    -80   1070       C  
ATOM   2732  CH2 TRP B 106      84.318  77.696  51.808  1.00 92.17           C  
ANISOU 2732  CH2 TRP B 106    12010  12179  10831    563    -15   1276       C  
ATOM   2733  N   ARG B 107      89.976  83.791  52.298  1.00104.43           N  
ANISOU 2733  N   ARG B 107     8875  17271  13533   -942   1305    780       N  
ATOM   2734  CA  ARG B 107      91.029  84.107  53.267  1.00107.88           C  
ANISOU 2734  CA  ARG B 107     9130  17709  14151  -1153   1172    895       C  
ATOM   2735  C   ARG B 107      90.776  85.398  54.059  1.00108.67           C  
ANISOU 2735  C   ARG B 107     9502  17000  14787  -1742    861   1254       C  
ATOM   2736  O   ARG B 107      91.032  85.455  55.257  1.00108.77           O  
ANISOU 2736  O   ARG B 107     9732  16511  15081  -1728    685   1052       O  
ATOM   2737  CB  ARG B 107      92.391  84.147  52.578  1.00119.07           C  
ANISOU 2737  CB  ARG B 107     9723  20417  15098  -1210   1275   1217       C  
ATOM   2738  CG  ARG B 107      93.495  83.506  53.409  1.00133.81           C  
ANISOU 2738  CG  ARG B 107    11384  22548  16907   -896   1237    893       C  
ATOM   2739  CD  ARG B 107      94.803  83.397  52.650  1.00145.09           C  
ANISOU 2739  CD  ARG B 107    11872  25532  17721   -797   1375   1131       C  
ATOM   2740  NE  ARG B 107      95.551  84.654  52.643  1.00155.73           N  
ANISOU 2740  NE  ARG B 107    12691  27305  19175  -1684   1233   2044       N  
ATOM   2741  CZ  ARG B 107      95.741  85.413  51.563  1.00165.41           C  
ANISOU 2741  CZ  ARG B 107    13294  29483  20070  -2223   1269   2845       C  
ATOM   2742  NH1 ARG B 107      96.443  86.537  51.655  1.00168.54           N  
ANISOU 2742  NH1 ARG B 107    13237  30134  20663  -3152    967   3789       N  
ATOM   2743  NH2 ARG B 107      95.234  85.049  50.390  1.00170.80           N  
ANISOU 2743  NH2 ARG B 107    13795  30874  20226  -1875   1528   2759       N  
ATOM   2744  N   LYS B 108      90.242  86.416  53.394  1.00113.06           N  
ANISOU 2744  N   LYS B 108    10077  17400  15478  -2190    707   1730       N  
ATOM   2745  CA  LYS B 108      89.907  87.682  54.059  1.00114.94           C  
ANISOU 2745  CA  LYS B 108    10655  16746  16269  -2629    209   1963       C  
ATOM   2746  C   LYS B 108      88.700  87.595  55.042  1.00108.17           C  
ANISOU 2746  C   LYS B 108    10454  14971  15673  -2232    127   1362       C  
ATOM   2747  O   LYS B 108      88.477  88.520  55.833  1.00102.51           O  
ANISOU 2747  O   LYS B 108    10035  13562  15352  -2346   -344   1304       O  
ATOM   2748  CB  LYS B 108      89.672  88.793  53.017  1.00125.37           C  
ANISOU 2748  CB  LYS B 108    11834  18104  17694  -3219    -84   2682       C  
ATOM   2749  CG  LYS B 108      90.815  89.819  52.883  1.00135.84           C  
ANISOU 2749  CG  LYS B 108    12708  19687  19216  -4013   -576   3528       C  
ATOM   2750  CD  LYS B 108      90.649  90.728  51.642  1.00143.62           C  
ANISOU 2750  CD  LYS B 108    13427  20951  20187  -4686   -864   4435       C  
ATOM   2751  CE  LYS B 108      89.359  91.573  51.660  1.00143.65           C  
ANISOU 2751  CE  LYS B 108    14119  19767  20693  -4715  -1357   4338       C  
ATOM   2752  NZ  LYS B 108      88.144  90.886  51.081  1.00132.11           N  
ANISOU 2752  NZ  LYS B 108    12911  18367  18918  -4139   -833   3842       N  
ATOM   2753  N   HIS B 109      87.943  86.484  55.000  1.00104.59           N  
ANISOU 2753  N   HIS B 109    10177  14593  14967  -1750    504    927       N  
ATOM   2754  CA  HIS B 109      86.689  86.371  55.792  1.00100.59           C  
ANISOU 2754  CA  HIS B 109    10127  13516  14577  -1446    467    519       C  
ATOM   2755  C   HIS B 109      86.570  85.093  56.621  1.00102.57           C  
ANISOU 2755  C   HIS B 109    10485  13827  14658  -1066    671    131       C  
ATOM   2756  O   HIS B 109      85.483  84.562  56.795  1.00112.31           O  
ANISOU 2756  O   HIS B 109    11927  14937  15807   -866    761    -38       O  
ATOM   2757  CB  HIS B 109      85.456  86.522  54.894  1.00 95.63           C  
ANISOU 2757  CB  HIS B 109     9649  12792  13894  -1416    545    576       C  
ATOM   2758  CG  HIS B 109      85.462  87.764  54.079  1.00 98.60           C  
ANISOU 2758  CG  HIS B 109     9965  13036  14460  -1820    247   1024       C  
ATOM   2759  ND1 HIS B 109      85.679  87.756  52.719  1.00102.82           N  
ANISOU 2759  ND1 HIS B 109    10203  14085  14776  -2060    400   1451       N  
ATOM   2760  CD2 HIS B 109      85.342  89.063  54.433  1.00104.86           C  
ANISOU 2760  CD2 HIS B 109    10949  13245  15646  -2035   -310   1147       C  
ATOM   2761  CE1 HIS B 109      85.683  88.998  52.266  1.00110.25           C  
ANISOU 2761  CE1 HIS B 109    11136  14775  15978  -2520    -26   1946       C  
ATOM   2762  NE2 HIS B 109      85.493  89.811  53.288  1.00112.34           N  
ANISOU 2762  NE2 HIS B 109    11735  14275  16671  -2511   -526   1754       N  
HETATM 2763  N   MSE B 110      87.679  84.616  57.146  1.00101.49           N  
ANISOU 2763  N   MSE B 110    10183  13896  14483  -1019    674     65       N  
HETATM 2764  CA  MSE B 110      87.658  83.482  58.037  1.00 94.46           C  
ANISOU 2764  CA  MSE B 110     9421  12973  13496   -728    719   -216       C  
HETATM 2765  C   MSE B 110      87.366  83.929  59.418  1.00 97.55           C  
ANISOU 2765  C   MSE B 110     9986  13087  13989   -692    547   -359       C  
HETATM 2766  O   MSE B 110      87.663  85.050  59.785  1.00121.97           O  
ANISOU 2766  O   MSE B 110    13078  15994  17268   -821    313   -348       O  
HETATM 2767  CB  MSE B 110      89.012  82.899  57.939  1.00 93.08           C  
ANISOU 2767  CB  MSE B 110     8966  13175  13224   -640    738   -250       C  
HETATM 2768  CG  MSE B 110      89.162  82.623  56.465  1.00100.58           C  
ANISOU 2768  CG  MSE B 110     9665  14606  13942   -568    896   -165       C  
HETATM 2769 SE   MSE B 110      88.257  80.915  56.128  1.00101.08          SE  
ANISOU 2769 SE   MSE B 110    10055  14485  13864    -85    843   -539      SE  
HETATM 2770  CE  MSE B 110      87.715  81.260  54.287  1.00102.33           C  
ANISOU 2770  CE  MSE B 110    10035  15071  13772    -81   1027   -409       C  
ATOM   2771  N   ALA B 111      86.737  83.062  60.194  1.00 98.92           N  
ANISOU 2771  N   ALA B 111    10298  13267  14020   -513    577   -473       N  
ATOM   2772  CA  ALA B 111      86.367  83.377  61.570  1.00 95.41           C  
ANISOU 2772  CA  ALA B 111     9921  12834  13495   -394    448   -615       C  
ATOM   2773  C   ALA B 111      86.694  82.186  62.434  1.00 95.16           C  
ANISOU 2773  C   ALA B 111     9883  12948  13322   -330    422   -583       C  
ATOM   2774  O   ALA B 111      87.083  81.135  61.927  1.00 94.93           O  
ANISOU 2774  O   ALA B 111     9871  12874  13324   -339    418   -503       O  
ATOM   2775  CB  ALA B 111      84.877  83.718  61.665  1.00 86.41           C  
ANISOU 2775  CB  ALA B 111     8846  11793  12192   -285    480   -644       C  
ATOM   2776  N   LEU B 112      86.522  82.339  63.736  1.00 92.93           N  
ANISOU 2776  N   LEU B 112     9580  12865  12863   -216    322   -665       N  
ATOM   2777  CA  LEU B 112      86.884  81.296  64.664  1.00 88.77           C  
ANISOU 2777  CA  LEU B 112     9032  12499  12196   -219    227   -541       C  
ATOM   2778  C   LEU B 112      85.960  80.006  64.626  1.00 91.83           C  
ANISOU 2778  C   LEU B 112     9457  12996  12437   -385    173   -152       C  
ATOM   2779  O   LEU B 112      86.403  78.946  64.256  1.00 97.46           O  
ANISOU 2779  O   LEU B 112    10286  13431  13312   -455     -9    -32       O  
ATOM   2780  CB  LEU B 112      87.044  81.878  66.069  1.00 84.67           C  
ANISOU 2780  CB  LEU B 112     8425  12287  11456    -36    110   -725       C  
ATOM   2781  CG  LEU B 112      88.279  81.439  66.866  1.00 83.83           C  
ANISOU 2781  CG  LEU B 112     8301  12152  11398    -20    -46   -763       C  
ATOM   2782  CD1 LEU B 112      89.416  80.984  65.961  1.00 82.87           C  
ANISOU 2782  CD1 LEU B 112     8204  11672  11608   -113    -55   -759       C  
ATOM   2783  CD2 LEU B 112      88.742  82.538  67.810  1.00 82.32           C  
ANISOU 2783  CD2 LEU B 112     8065  12059  11152    205   -220  -1126       C  
ATOM   2784  N   GLY B 113      84.706  80.106  65.001  1.00 94.06           N  
ANISOU 2784  N   GLY B 113     9620  13696  12422   -436    234     46       N  
ATOM   2785  CA  GLY B 113      83.898  78.880  65.108  1.00104.81           C  
ANISOU 2785  CA  GLY B 113    10954  15202  13665   -745     56    586       C  
ATOM   2786  C   GLY B 113      83.991  78.278  66.497  1.00108.60           C  
ANISOU 2786  C   GLY B 113    11268  16150  13842   -879   -141    942       C  
ATOM   2787  O   GLY B 113      84.898  78.593  67.241  1.00114.21           O  
ANISOU 2787  O   GLY B 113    11964  16917  14511   -687   -150    692       O  
ATOM   2788  N   GLU B 114      83.056  77.388  66.826  1.00114.71           N  
ANISOU 2788  N   GLU B 114    11890  17287  14405  -1272   -355   1610       N  
ATOM   2789  CA  GLU B 114      82.612  77.185  68.218  1.00117.18           C  
ANISOU 2789  CA  GLU B 114    11805  18567  14148  -1436   -420   2100       C  
ATOM   2790  C   GLU B 114      83.634  76.630  69.190  1.00116.36           C  
ANISOU 2790  C   GLU B 114    11759  18410  14042  -1490   -696   2235       C  
ATOM   2791  O   GLU B 114      83.712  77.066  70.338  1.00123.15           O  
ANISOU 2791  O   GLU B 114    12310  20084  14397  -1310   -578   2206       O  
ATOM   2792  CB  GLU B 114      81.341  76.344  68.263  1.00130.29           C  
ANISOU 2792  CB  GLU B 114    13191  20738  15573  -2003   -647   2988       C  
ATOM   2793  CG  GLU B 114      80.108  77.145  68.616  1.00142.48           C  
ANISOU 2793  CG  GLU B 114    14177  23516  16442  -1850   -270   3046       C  
ATOM   2794  CD  GLU B 114      78.840  76.339  68.503  1.00160.15           C  
ANISOU 2794  CD  GLU B 114    16066  26315  18466  -2491   -494   4001       C  
ATOM   2795  OE1 GLU B 114      78.399  76.089  67.358  1.00164.70           O  
ANISOU 2795  OE1 GLU B 114    16900  26198  19481  -2680   -599   4036       O  
ATOM   2796  OE2 GLU B 114      78.270  75.970  69.558  1.00170.18           O  
ANISOU 2796  OE2 GLU B 114    16753  28816  19092  -2828   -589   4764       O  
ATOM   2797  N   THR B 115      84.382  75.634  68.777  1.00117.91           N  
ANISOU 2797  N   THR B 115    12331  17716  14754  -1677  -1129   2361       N  
ATOM   2798  CA  THR B 115      85.300  75.030  69.714  1.00124.96           C  
ANISOU 2798  CA  THR B 115    13283  18539  15656  -1736  -1473   2537       C  
ATOM   2799  C   THR B 115      86.621  75.774  69.810  1.00122.97           C  
ANISOU 2799  C   THR B 115    13155  18011  15556  -1224  -1243   1752       C  
ATOM   2800  O   THR B 115      87.415  75.474  70.679  1.00134.65           O  
ANISOU 2800  O   THR B 115    14636  19542  16982  -1193  -1454   1802       O  
ATOM   2801  CB  THR B 115      85.527  73.511  69.469  1.00127.86           C  
ANISOU 2801  CB  THR B 115    13995  18095  16489  -2133  -2269   3067       C  
ATOM   2802  OG1 THR B 115      85.362  73.200  68.081  1.00124.80           O  
ANISOU 2802  OG1 THR B 115    13936  16904  16576  -2059  -2432   2805       O  
ATOM   2803  CG2 THR B 115      84.555  72.685  70.286  1.00130.00           C  
ANISOU 2803  CG2 THR B 115    13995  18948  16448  -2843  -2717   4195       C  
ATOM   2804  N   ALA B 116      86.814  76.784  68.943  1.00114.42           N  
ANISOU 2804  N   ALA B 116    12134  16694  14644   -884   -852   1111       N  
ATOM   2805  CA  ALA B 116      88.126  77.482  68.751  1.00105.78           C  
ANISOU 2805  CA  ALA B 116    11134  15254  13803   -525   -721    473       C  
ATOM   2806  C   ALA B 116      89.236  76.548  68.278  1.00102.42           C  
ANISOU 2806  C   ALA B 116    10934  14201  13780   -462  -1054    379       C  
ATOM   2807  O   ALA B 116      90.399  76.929  68.240  1.00101.99           O  
ANISOU 2807  O   ALA B 116    10855  14023  13873   -219  -1001    -21       O  
ATOM   2808  CB  ALA B 116      88.549  78.225  70.015  1.00109.92           C  
ANISOU 2808  CB  ALA B 116    11472  16286  14006   -326   -651    269       C  
ATOM   2809  N   GLU B 117      88.855  75.320  67.939  1.00105.29           N  
ANISOU 2809  N   GLU B 117    11493  14198  14311   -659  -1490    747       N  
ATOM   2810  CA  GLU B 117      89.784  74.290  67.513  1.00109.59           C  
ANISOU 2810  CA  GLU B 117    12291  14131  15217   -460  -2000    577       C  
ATOM   2811  C   GLU B 117      90.260  74.535  66.104  1.00105.53           C  
ANISOU 2811  C   GLU B 117    11809  13380  14904    -81  -1824     14       C  
ATOM   2812  O   GLU B 117      91.292  74.042  65.709  1.00117.17           O  
ANISOU 2812  O   GLU B 117    13341  14631  16545    304  -2088   -368       O  
ATOM   2813  CB  GLU B 117      89.110  72.930  67.563  1.00121.89           C  
ANISOU 2813  CB  GLU B 117    14111  15250  16951   -789  -2734   1147       C  
ATOM   2814  CG  GLU B 117      89.416  72.094  68.788  1.00133.08           C  
ANISOU 2814  CG  GLU B 117    15593  16617  18352  -1041  -3316   1655       C  
ATOM   2815  CD  GLU B 117      88.624  70.789  68.792  1.00155.01           C  
ANISOU 2815  CD  GLU B 117    18635  18886  21374  -1538  -4211   2407       C  
ATOM   2816  OE1 GLU B 117      88.679  70.032  67.784  1.00156.50           O  
ANISOU 2816  OE1 GLU B 117    19193  18263  22005  -1334  -4798   2153       O  
ATOM   2817  OE2 GLU B 117      87.922  70.530  69.791  1.00170.18           O  
ANISOU 2817  OE2 GLU B 117    20362  21278  23019  -2140  -4394   3281       O  
ATOM   2818  N   THR B 118      89.473  75.269  65.340  1.00 98.82           N  
ANISOU 2818  N   THR B 118    10877  12689  13978   -161  -1408    -19       N  
ATOM   2819  CA  THR B 118      89.763  75.539  63.950  1.00 99.67           C  
ANISOU 2819  CA  THR B 118    10952  12735  14181    127  -1219   -429       C  
ATOM   2820  C   THR B 118      88.871  76.660  63.494  1.00 97.13           C  
ANISOU 2820  C   THR B 118    10502  12668  13733    -62   -716   -359       C  
ATOM   2821  O   THR B 118      87.946  77.008  64.182  1.00112.86           O  
ANISOU 2821  O   THR B 118    12463  14847  15571   -326   -602    -58       O  
ATOM   2822  CB  THR B 118      89.489  74.306  63.063  1.00107.09           C  
ANISOU 2822  CB  THR B 118    12176  13196  15318    312  -1774   -505       C  
ATOM   2823  OG1 THR B 118      89.551  74.694  61.689  1.00111.89           O  
ANISOU 2823  OG1 THR B 118    12676  13961  15874    600  -1503   -877       O  
ATOM   2824  CG2 THR B 118      88.088  73.684  63.360  1.00 99.16           C  
ANISOU 2824  CG2 THR B 118    11385  11914  14376   -164  -2122     87       C  
ATOM   2825  N   GLU B 119      89.116  77.182  62.301  1.00 94.69           N  
ANISOU 2825  N   GLU B 119    10084  12448  13444    104   -464   -622       N  
ATOM   2826  CA  GLU B 119      88.415  78.381  61.813  1.00 93.65           C  
ANISOU 2826  CA  GLU B 119     9843  12495  13244    -66    -60   -564       C  
ATOM   2827  C   GLU B 119      87.473  78.062  60.633  1.00 95.61           C  
ANISOU 2827  C   GLU B 119    10203  12621  13500    -68    -57   -523       C  
ATOM   2828  O   GLU B 119      87.666  77.071  59.936  1.00112.68           O  
ANISOU 2828  O   GLU B 119    12482  14610  15719    164   -350   -678       O  
ATOM   2829  CB  GLU B 119      89.434  79.458  61.418  1.00 99.53           C  
ANISOU 2829  CB  GLU B 119    10319  13493  14005    -29    178   -727       C  
ATOM   2830  CG  GLU B 119      90.658  79.551  62.346  1.00103.86           C  
ANISOU 2830  CG  GLU B 119    10730  14148  14585     28     77   -826       C  
ATOM   2831  CD  GLU B 119      91.791  78.608  61.939  1.00111.47           C  
ANISOU 2831  CD  GLU B 119    11563  15263  15526    361    -97  -1047       C  
ATOM   2832  OE1 GLU B 119      92.097  78.519  60.722  1.00114.27           O  
ANISOU 2832  OE1 GLU B 119    11720  15918  15778    555    -10  -1177       O  
ATOM   2833  OE2 GLU B 119      92.384  77.963  62.836  1.00117.24           O  
ANISOU 2833  OE2 GLU B 119    12355  15899  16291    491   -353  -1121       O  
ATOM   2834  N   GLU B 120      86.428  78.871  60.443  1.00 91.39           N  
ANISOU 2834  N   GLU B 120     9652  12163  12907   -262    185   -372       N  
ATOM   2835  CA  GLU B 120      85.451  78.631  59.352  1.00 90.92           C  
ANISOU 2835  CA  GLU B 120     9690  12003  12850   -291    190   -309       C  
ATOM   2836  C   GLU B 120      85.314  79.902  58.574  1.00 89.16           C  
ANISOU 2836  C   GLU B 120     9330  11948  12596   -329    523   -356       C  
ATOM   2837  O   GLU B 120      85.426  80.971  59.136  1.00 91.11           O  
ANISOU 2837  O   GLU B 120     9488  12275  12853   -415    645   -349       O  
ATOM   2838  CB  GLU B 120      84.043  78.307  59.892  1.00 96.60           C  
ANISOU 2838  CB  GLU B 120    10489  12709  13506   -553     86     42       C  
ATOM   2839  CG  GLU B 120      83.911  77.270  60.992  1.00102.56           C  
ANISOU 2839  CG  GLU B 120    11306  13409  14250   -738   -292    366       C  
ATOM   2840  CD  GLU B 120      82.828  77.662  61.991  1.00109.41           C  
ANISOU 2840  CD  GLU B 120    11961  14778  14831   -993   -158    744       C  
ATOM   2841  OE1 GLU B 120      82.444  78.871  62.001  1.00109.55           O  
ANISOU 2841  OE1 GLU B 120    11821  15120  14683   -863    208    555       O  
ATOM   2842  OE2 GLU B 120      82.374  76.786  62.775  1.00111.13           O  
ANISOU 2842  OE2 GLU B 120    12132  15133  14956  -1299   -485   1238       O  
ATOM   2843  N   VAL B 121      84.950  79.795  57.303  1.00 88.02           N  
ANISOU 2843  N   VAL B 121     9201  11816  12424   -267    570   -389       N  
ATOM   2844  CA  VAL B 121      84.541  80.962  56.530  1.00 87.95           C  
ANISOU 2844  CA  VAL B 121     9097  11923  12395   -387    806   -305       C  
ATOM   2845  C   VAL B 121      83.303  81.615  57.164  1.00 90.13           C  
ANISOU 2845  C   VAL B 121     9457  12103  12683   -528    844   -182       C  
ATOM   2846  O   VAL B 121      82.509  80.948  57.835  1.00 94.37           O  
ANISOU 2846  O   VAL B 121    10062  12639  13153   -566    746    -78       O  
ATOM   2847  CB  VAL B 121      84.239  80.574  55.082  1.00 93.02           C  
ANISOU 2847  CB  VAL B 121     9738  12669  12934   -264    824   -352       C  
ATOM   2848  CG1 VAL B 121      82.963  79.755  55.016  1.00107.00           C  
ANISOU 2848  CG1 VAL B 121    11748  14164  14743   -287    639   -298       C  
ATOM   2849  CG2 VAL B 121      84.134  81.810  54.202  1.00 96.78           C  
ANISOU 2849  CG2 VAL B 121    10055  13344  13370   -430   1029   -182       C  
ATOM   2850  N   LYS B 122      83.166  82.919  56.985  1.00 90.11           N  
ANISOU 2850  N   LYS B 122     9409  12083  12743   -594    904   -170       N  
ATOM   2851  CA  LYS B 122      81.961  83.621  57.409  1.00 93.36           C  
ANISOU 2851  CA  LYS B 122     9872  12483  13115   -551    875   -192       C  
ATOM   2852  C   LYS B 122      80.899  83.583  56.309  1.00 97.66           C  
ANISOU 2852  C   LYS B 122    10462  13019  13624   -587    950    -84       C  
ATOM   2853  O   LYS B 122      81.068  84.215  55.249  1.00104.84           O  
ANISOU 2853  O   LYS B 122    11374  13839  14622   -669    964    -12       O  
ATOM   2854  CB  LYS B 122      82.286  85.064  57.761  1.00 91.15           C  
ANISOU 2854  CB  LYS B 122     9607  12030  12994   -515    686   -319       C  
ATOM   2855  CG  LYS B 122      83.290  85.211  58.878  1.00 89.57           C  
ANISOU 2855  CG  LYS B 122     9372  11814  12843   -465    545   -459       C  
ATOM   2856  CD  LYS B 122      83.157  86.555  59.565  1.00 91.57           C  
ANISOU 2856  CD  LYS B 122     9715  11851  13224   -285    172   -720       C  
ATOM   2857  CE  LYS B 122      83.352  87.682  58.571  1.00 96.82           C  
ANISOU 2857  CE  LYS B 122    10467  12095  14222   -512   -117   -557       C  
ATOM   2858  NZ  LYS B 122      83.724  88.946  59.254  1.00110.22           N  
ANISOU 2858  NZ  LYS B 122    12314  13355  16209   -415   -733   -784       N  
ATOM   2859  N   ALA B 123      79.807  82.849  56.571  1.00 98.09           N  
ANISOU 2859  N   ALA B 123    10510  13230  13529   -584    957      6       N  
ATOM   2860  CA  ALA B 123      78.714  82.626  55.589  1.00 90.75           C  
ANISOU 2860  CA  ALA B 123     9612  12304  12564   -640    984    128       C  
ATOM   2861  C   ALA B 123      77.702  83.782  55.550  1.00 90.24           C  
ANISOU 2861  C   ALA B 123     9495  12346  12446   -513    996     55       C  
ATOM   2862  O   ALA B 123      77.411  84.408  56.577  1.00 96.13           O  
ANISOU 2862  O   ALA B 123    10137  13317  13070   -309    936   -107       O  
ATOM   2863  CB  ALA B 123      78.002  81.314  55.891  1.00 85.45           C  
ANISOU 2863  CB  ALA B 123     8921  11741  11803   -792    853    365       C  
ATOM   2864  N   LYS B 124      77.145  84.045  54.377  1.00 87.90           N  
ANISOU 2864  N   LYS B 124     9262  11934  12201   -550   1016    116       N  
ATOM   2865  CA  LYS B 124      76.124  85.085  54.257  1.00 93.82           C  
ANISOU 2865  CA  LYS B 124     9986  12738  12921   -377    943     19       C  
ATOM   2866  C   LYS B 124      74.872  84.573  53.597  1.00 95.22           C  
ANISOU 2866  C   LYS B 124    10099  13101  12976   -432    996    175       C  
ATOM   2867  O   LYS B 124      74.900  83.553  52.910  1.00 95.74           O  
ANISOU 2867  O   LYS B 124    10224  13088  13063   -632   1022    350       O  
ATOM   2868  CB  LYS B 124      76.662  86.286  53.497  1.00 99.94           C  
ANISOU 2868  CB  LYS B 124    10907  13124  13938   -399    781     -3       C  
ATOM   2869  CG  LYS B 124      77.500  87.236  54.349  1.00106.00           C  
ANISOU 2869  CG  LYS B 124    11733  13661  14879   -302    516   -184       C  
ATOM   2870  CD  LYS B 124      78.056  88.376  53.513  1.00107.40           C  
ANISOU 2870  CD  LYS B 124    12044  13395  15368   -509    196     -1       C  
ATOM   2871  CE  LYS B 124      78.497  87.885  52.143  1.00105.73           C  
ANISOU 2871  CE  LYS B 124    11748  13324  15100   -860    438    397       C  
ATOM   2872  NZ  LYS B 124      78.887  89.008  51.249  1.00119.35           N  
ANISOU 2872  NZ  LYS B 124    13506  14792  17048  -1174    105    770       N  
ATOM   2873  N   ALA B 125      73.764  85.280  53.808  1.00 99.70           N  
ANISOU 2873  N   ALA B 125    10539  13929  13411   -195    933     61       N  
ATOM   2874  CA  ALA B 125      72.476  84.871  53.234  1.00 98.26           C  
ANISOU 2874  CA  ALA B 125    10224  14017  13090   -256    966    237       C  
ATOM   2875  C   ALA B 125      71.934  85.887  52.216  1.00 99.35           C  
ANISOU 2875  C   ALA B 125    10489  13913  13346    -96    858    122       C  
ATOM   2876  O   ALA B 125      71.861  87.088  52.496  1.00104.25           O  
ANISOU 2876  O   ALA B 125    11159  14427  14025    241    647   -167       O  
ATOM   2877  CB  ALA B 125      71.460  84.606  54.335  1.00 94.71           C  
ANISOU 2877  CB  ALA B 125     9362  14363  12258   -134    990    305       C  
ATOM   2878  N   LEU B 126      71.572  85.399  51.028  1.00100.38           N  
ANISOU 2878  N   LEU B 126    10704  13905  13530   -311    899    329       N  
ATOM   2879  CA  LEU B 126      70.897  86.228  50.027  1.00100.29           C  
ANISOU 2879  CA  LEU B 126    10780  13740  13585   -201    786    302       C  
ATOM   2880  C   LEU B 126      69.503  86.556  50.536  1.00107.33           C  
ANISOU 2880  C   LEU B 126    11398  15125  14257    102    718    174       C  
ATOM   2881  O   LEU B 126      68.960  85.813  51.353  1.00124.70           O  
ANISOU 2881  O   LEU B 126    13276  17907  16196     63    821    284       O  
ATOM   2882  CB  LEU B 126      70.794  85.471  48.708  1.00 97.11           C  
ANISOU 2882  CB  LEU B 126    10482  13217  13198   -454    846    521       C  
ATOM   2883  CG  LEU B 126      72.066  85.292  47.874  1.00100.85           C  
ANISOU 2883  CG  LEU B 126    11122  13455  13740   -607    899    594       C  
ATOM   2884  CD1 LEU B 126      71.774  84.450  46.638  1.00101.62           C  
ANISOU 2884  CD1 LEU B 126    11276  13601  13732   -675    891    666       C  
ATOM   2885  CD2 LEU B 126      72.667  86.637  47.475  1.00 97.02           C  
ANISOU 2885  CD2 LEU B 126    10722  12750  13389   -624    782    670       C  
ATOM   2886  N   THR B 127      68.919  87.665  50.083  1.00104.67           N  
ANISOU 2886  N   THR B 127    11135  14645  13989    406    491    -18       N  
ATOM   2887  CA  THR B 127      67.495  87.908  50.351  1.00103.97           C  
ANISOU 2887  CA  THR B 127    10720  15159  13624    775    421   -173       C  
ATOM   2888  C   THR B 127      66.640  87.403  49.184  1.00110.43           C  
ANISOU 2888  C   THR B 127    11512  16010  14436    519    485    117       C  
ATOM   2889  O   THR B 127      67.174  87.007  48.140  1.00110.85           O  
ANISOU 2889  O   THR B 127    11843  15587  14687    158    536    349       O  
ATOM   2890  CB  THR B 127      67.188  89.382  50.623  1.00104.96           C  
ANISOU 2890  CB  THR B 127    10928  15141  13807   1418     -8   -677       C  
ATOM   2891  OG1 THR B 127      67.144  90.102  49.387  1.00105.74           O  
ANISOU 2891  OG1 THR B 127    11377  14562  14236   1339   -287   -590       O  
ATOM   2892  CG2 THR B 127      68.226  89.985  51.539  1.00105.60           C  
ANISOU 2892  CG2 THR B 127    11185  14909  14029   1632   -233   -984       C  
ATOM   2893  N   VAL B 128      65.317  87.401  49.365  1.00115.26           N  
ANISOU 2893  N   VAL B 128    11733  17299  14760    749    463     87       N  
ATOM   2894  CA  VAL B 128      64.417  86.867  48.338  1.00105.99           C  
ANISOU 2894  CA  VAL B 128    10490  16204  13575    486    477    380       C  
ATOM   2895  C   VAL B 128      64.522  87.698  47.084  1.00105.59           C  
ANISOU 2895  C   VAL B 128    10847  15472  13799    569    288    289       C  
ATOM   2896  O   VAL B 128      64.568  87.163  45.977  1.00 99.12           O  
ANISOU 2896  O   VAL B 128    10213  14360  13085    224    325    544       O  
ATOM   2897  CB  VAL B 128      62.961  86.841  48.795  1.00102.48           C  
ANISOU 2897  CB  VAL B 128     9450  16755  12730    730    463    398       C  
ATOM   2898  CG1 VAL B 128      62.292  85.588  48.281  1.00 95.99           C  
ANISOU 2898  CG1 VAL B 128     8426  16173  11871    133    503    951       C  
ATOM   2899  CG2 VAL B 128      62.882  86.905  50.307  1.00109.54           C  
ANISOU 2899  CG2 VAL B 128     9860  18548  13212   1049    547    247       C  
ATOM   2900  N   ARG B 129      64.581  89.015  47.270  1.00113.15           N  
ANISOU 2900  N   ARG B 129    11949  16176  14867   1045    -11    -72       N  
ATOM   2901  CA  ARG B 129      64.833  89.941  46.174  1.00119.59           C  
ANISOU 2901  CA  ARG B 129    13174  16269  15995   1034   -327    -33       C  
ATOM   2902  C   ARG B 129      66.106  89.548  45.406  1.00113.74           C  
ANISOU 2902  C   ARG B 129    12728  15051  15435    480   -171    343       C  
ATOM   2903  O   ARG B 129      66.042  89.201  44.220  1.00108.06           O  
ANISOU 2903  O   ARG B 129    12101  14255  14699    199    -95    624       O  
ATOM   2904  CB  ARG B 129      64.926  91.391  46.702  1.00130.39           C  
ANISOU 2904  CB  ARG B 129    14729  17250  17563   1588   -891   -464       C  
ATOM   2905  CG  ARG B 129      63.593  92.160  46.698  1.00146.14           C  
ANISOU 2905  CG  ARG B 129    16572  19509  19445   2259  -1282   -868       C  
ATOM   2906  CD  ARG B 129      62.726  91.865  47.931  1.00153.41           C  
ANISOU 2906  CD  ARG B 129    16905  21525  19858   2836  -1116  -1291       C  
ATOM   2907  NE  ARG B 129      61.388  92.475  47.845  1.00150.15           N  
ANISOU 2907  NE  ARG B 129    16216  21614  19218   3535  -1434  -1689       N  
ATOM   2908  CZ  ARG B 129      60.931  93.415  48.677  1.00159.87           C  
ANISOU 2908  CZ  ARG B 129    17295  23182  20265   4517  -1930  -2438       C  
ATOM   2909  NH1 ARG B 129      61.693  93.867  49.664  1.00161.40           N  
ANISOU 2909  NH1 ARG B 129    17623  23201  20498   4886  -2190  -2864       N  
ATOM   2910  NH2 ARG B 129      59.709  93.906  48.522  1.00169.02           N  
ANISOU 2910  NH2 ARG B 129    18157  24887  21173   5211  -2225  -2828       N  
ATOM   2911  N   GLN B 130      67.245  89.561  46.106  1.00109.07           N  
ANISOU 2911  N   GLN B 130    12218  14281  14940    380   -123    314       N  
ATOM   2912  CA  GLN B 130      68.545  89.237  45.509  1.00102.67           C  
ANISOU 2912  CA  GLN B 130    11568  13225  14215    -60     23    634       C  
ATOM   2913  C   GLN B 130      68.548  87.885  44.812  1.00101.73           C  
ANISOU 2913  C   GLN B 130    11367  13397  13886   -313    363    802       C  
ATOM   2914  O   GLN B 130      69.054  87.753  43.698  1.00104.77           O  
ANISOU 2914  O   GLN B 130    11834  13765  14207   -516    404   1029       O  
ATOM   2915  CB  GLN B 130      69.625  89.253  46.563  1.00 98.80           C  
ANISOU 2915  CB  GLN B 130    11087  12642  13811    -83     56    530       C  
ATOM   2916  CG  GLN B 130      69.794  90.581  47.262  1.00107.31           C  
ANISOU 2916  CG  GLN B 130    12314  13310  15146    196   -441    297       C  
ATOM   2917  CD  GLN B 130      70.575  90.444  48.557  1.00114.69           C  
ANISOU 2917  CD  GLN B 130    13197  14292  16088    296   -393     65       C  
ATOM   2918  OE1 GLN B 130      70.874  89.323  49.004  1.00116.08           O  
ANISOU 2918  OE1 GLN B 130    13196  14850  16056    159     38    100       O  
ATOM   2919  NE2 GLN B 130      70.913  91.581  49.175  1.00117.75           N  
ANISOU 2919  NE2 GLN B 130    13768  14228  16743    549   -944   -182       N  
ATOM   2920  N   TRP B 131      67.991  86.875  45.477  1.00103.22           N  
ANISOU 2920  N   TRP B 131    11372  13901  13944   -289    517    706       N  
ATOM   2921  CA  TRP B 131      67.955  85.519  44.919  1.00 97.94           C  
ANISOU 2921  CA  TRP B 131    10699  13336  13174   -506    609    818       C  
ATOM   2922  C   TRP B 131      67.173  85.456  43.611  1.00 98.84           C  
ANISOU 2922  C   TRP B 131    10870  13461  13222   -521    507    905       C  
ATOM   2923  O   TRP B 131      67.638  84.885  42.635  1.00102.31           O  
ANISOU 2923  O   TRP B 131    11432  13870  13571   -585    498    926       O  
ATOM   2924  CB  TRP B 131      67.388  84.526  45.917  1.00 93.05           C  
ANISOU 2924  CB  TRP B 131     9862  12994  12496   -606    611    864       C  
ATOM   2925  CG  TRP B 131      67.249  83.179  45.344  1.00 88.69           C  
ANISOU 2925  CG  TRP B 131     9385  12355  11958   -840    452    985       C  
ATOM   2926  CD1 TRP B 131      66.098  82.547  45.046  1.00 92.64           C  
ANISOU 2926  CD1 TRP B 131     9764  12990  12444  -1007    240   1167       C  
ATOM   2927  CD2 TRP B 131      68.301  82.294  44.972  1.00 88.88           C  
ANISOU 2927  CD2 TRP B 131     9633  12109  12028   -880    362    887       C  
ATOM   2928  NE1 TRP B 131      66.352  81.315  44.517  1.00 93.42           N  
ANISOU 2928  NE1 TRP B 131    10068  12781  12645  -1171    -72   1184       N  
ATOM   2929  CE2 TRP B 131      67.701  81.129  44.459  1.00 91.39           C  
ANISOU 2929  CE2 TRP B 131    10030  12290  12404  -1024     -8    951       C  
ATOM   2930  CE3 TRP B 131      69.695  82.365  45.033  1.00 89.96           C  
ANISOU 2930  CE3 TRP B 131     9883  12144  12152   -771    491    729       C  
ATOM   2931  CZ2 TRP B 131      68.445  80.031  43.999  1.00 93.63           C  
ANISOU 2931  CZ2 TRP B 131    10565  12266  12742   -946   -334    745       C  
ATOM   2932  CZ3 TRP B 131      70.437  81.278  44.570  1.00 94.98           C  
ANISOU 2932  CZ3 TRP B 131    10680  12642  12766   -687    285    548       C  
ATOM   2933  CH2 TRP B 131      69.802  80.123  44.060  1.00 92.48           C  
ANISOU 2933  CH2 TRP B 131    10500  12120  12516   -719   -161    502       C  
ATOM   2934  N   LEU B 132      65.988  86.056  43.604  1.00100.67           N  
ANISOU 2934  N   LEU B 132    10982  13818  13447   -380    403    898       N  
ATOM   2935  CA  LEU B 132      65.238  86.287  42.369  1.00100.96           C  
ANISOU 2935  CA  LEU B 132    11083  13836  13439   -359    276    980       C  
ATOM   2936  C   LEU B 132      66.124  86.921  41.286  1.00104.38           C  
ANISOU 2936  C   LEU B 132    11734  14068  13856   -416    253   1114       C  
ATOM   2937  O   LEU B 132      66.101  86.499  40.115  1.00102.94           O  
ANISOU 2937  O   LEU B 132    11612  13991  13506   -474    237   1197       O  
ATOM   2938  CB  LEU B 132      64.020  87.180  42.659  1.00 97.15           C  
ANISOU 2938  CB  LEU B 132    10432  13517  12963    -83    124    891       C  
ATOM   2939  CG  LEU B 132      63.136  87.665  41.517  1.00 92.80           C  
ANISOU 2939  CG  LEU B 132     9937  12926  12394      2    -63    958       C  
ATOM   2940  CD1 LEU B 132      62.562  86.504  40.712  1.00 88.20           C  
ANISOU 2940  CD1 LEU B 132     9308  12505  11698   -222    -56   1088       C  
ATOM   2941  CD2 LEU B 132      62.031  88.524  42.100  1.00 92.80           C  
ANISOU 2941  CD2 LEU B 132     9715  13165  12379    417   -255    746       C  
ATOM   2942  N   LEU B 133      66.915  87.920  41.678  1.00104.89           N  
ANISOU 2942  N   LEU B 133    11875  13917  14060   -418    191   1176       N  
ATOM   2943  CA  LEU B 133      67.841  88.537  40.740  1.00106.52           C  
ANISOU 2943  CA  LEU B 133    12174  14075  14222   -625    122   1504       C  
ATOM   2944  C   LEU B 133      68.925  87.553  40.259  1.00102.70           C  
ANISOU 2944  C   LEU B 133    11606  13960  13454   -743    388   1545       C  
ATOM   2945  O   LEU B 133      69.104  87.367  39.060  1.00100.35           O  
ANISOU 2945  O   LEU B 133    11255  14016  12856   -779    415   1705       O  
ATOM   2946  CB  LEU B 133      68.434  89.826  41.304  1.00107.07           C  
ANISOU 2946  CB  LEU B 133    12348  13749  14585   -695   -177   1649       C  
ATOM   2947  CG  LEU B 133      67.742  91.095  40.774  1.00111.20           C  
ANISOU 2947  CG  LEU B 133    13032  13900  15319   -655   -682   1834       C  
ATOM   2948  CD1 LEU B 133      66.225  90.939  40.774  1.00110.05           C  
ANISOU 2948  CD1 LEU B 133    12850  13831  15131   -280   -719   1502       C  
ATOM   2949  CD2 LEU B 133      68.167  92.345  41.545  1.00114.45           C  
ANISOU 2949  CD2 LEU B 133    13633  13710  16142   -625  -1232   1842       C  
ATOM   2950  N   VAL B 134      69.567  86.869  41.198  1.00 96.67           N  
ANISOU 2950  N   VAL B 134    10804  13193  12731   -715    545   1338       N  
ATOM   2951  CA  VAL B 134      70.519  85.821  40.870  1.00 94.80           C  
ANISOU 2951  CA  VAL B 134    10496  13287  12234   -670    703   1222       C  
ATOM   2952  C   VAL B 134      69.923  84.814  39.889  1.00 96.62           C  
ANISOU 2952  C   VAL B 134    10765  13718  12227   -485    621   1023       C  
ATOM   2953  O   VAL B 134      70.587  84.401  38.938  1.00103.58           O  
ANISOU 2953  O   VAL B 134    11560  15059  12736   -327    645    955       O  
ATOM   2954  CB  VAL B 134      71.011  85.091  42.141  1.00 94.41           C  
ANISOU 2954  CB  VAL B 134    10454  13083  12333   -632    777    984       C  
ATOM   2955  CG1 VAL B 134      71.818  83.842  41.789  1.00 94.94           C  
ANISOU 2955  CG1 VAL B 134    10504  13400  12168   -453    785    733       C  
ATOM   2956  CG2 VAL B 134      71.830  86.034  43.003  1.00 94.56           C  
ANISOU 2956  CG2 VAL B 134    10434  12960  12532   -767    817   1125       C  
ATOM   2957  N   VAL B 135      68.678  84.413  40.114  1.00 94.44           N  
ANISOU 2957  N   VAL B 135    10571  13189  12121   -472    471    918       N  
ATOM   2958  CA  VAL B 135      68.055  83.435  39.226  1.00 97.76           C  
ANISOU 2958  CA  VAL B 135    11071  13671  12401   -333    246    731       C  
ATOM   2959  C   VAL B 135      67.801  84.054  37.851  1.00102.79           C  
ANISOU 2959  C   VAL B 135    11681  14619  12753   -258    239    868       C  
ATOM   2960  O   VAL B 135      68.087  83.435  36.833  1.00104.28           O  
ANISOU 2960  O   VAL B 135    11874  15150  12596    -15    134    668       O  
ATOM   2961  CB  VAL B 135      66.740  82.827  39.806  1.00 97.08           C  
ANISOU 2961  CB  VAL B 135    11001  13307  12576   -469     13    734       C  
ATOM   2962  CG1 VAL B 135      66.148  81.807  38.834  1.00 94.22           C  
ANISOU 2962  CG1 VAL B 135    10768  12888  12140   -371   -380    558       C  
ATOM   2963  CG2 VAL B 135      67.000  82.163  41.148  1.00 95.39           C  
ANISOU 2963  CG2 VAL B 135    10752  12919  12572   -616    -21    730       C  
ATOM   2964  N   ALA B 136      67.292  85.290  37.835  1.00105.07           N  
ANISOU 2964  N   ALA B 136    11941  14817  13165   -413    280   1181       N  
ATOM   2965  CA  ALA B 136      67.021  86.016  36.583  1.00110.29           C  
ANISOU 2965  CA  ALA B 136    12578  15735  13591   -426    211   1443       C  
ATOM   2966  C   ALA B 136      68.277  86.135  35.701  1.00117.48           C  
ANISOU 2966  C   ALA B 136    13313  17286  14035   -426    340   1642       C  
ATOM   2967  O   ALA B 136      68.241  85.832  34.496  1.00118.62           O  
ANISOU 2967  O   ALA B 136    13370  17970  13729   -252    298   1621       O  
ATOM   2968  CB  ALA B 136      66.452  87.394  36.884  1.00105.97           C  
ANISOU 2968  CB  ALA B 136    12074  14847  13339   -575     82   1744       C  
ATOM   2969  N   ALA B 137      69.378  86.583  36.312  1.00118.11           N  
ANISOU 2969  N   ALA B 137    13280  17427  14168   -607    477   1850       N  
ATOM   2970  CA  ALA B 137      70.706  86.519  35.697  1.00118.00           C  
ANISOU 2970  CA  ALA B 137    12955  18230  13649   -612    639   2046       C  
ATOM   2971  C   ALA B 137      70.950  85.191  34.973  1.00118.36           C  
ANISOU 2971  C   ALA B 137    12908  18885  13177    -93    666   1501       C  
ATOM   2972  O   ALA B 137      71.320  85.184  33.803  1.00124.16           O  
ANISOU 2972  O   ALA B 137    13360  20534  13281     76    704   1612       O  
ATOM   2973  CB  ALA B 137      71.783  86.754  36.745  1.00116.37           C  
ANISOU 2973  CB  ALA B 137    12660  17907  13646   -802    757   2150       C  
ATOM   2974  N   SER B 138      70.708  84.079  35.672  1.00116.17           N  
ANISOU 2974  N   SER B 138    12863  18117  13157    176    550    920       N  
ATOM   2975  CA  SER B 138      70.981  82.730  35.147  1.00124.73           C  
ANISOU 2975  CA  SER B 138    13973  19530  13888    752    340    273       C  
ATOM   2976  C   SER B 138      70.258  82.386  33.861  1.00129.17           C  
ANISOU 2976  C   SER B 138    14571  20427  14079   1080     96     51       C  
ATOM   2977  O   SER B 138      70.794  81.651  33.050  1.00142.22           O  
ANISOU 2977  O   SER B 138    16095  22774  15167   1663    -60   -425       O  
ATOM   2978  CB  SER B 138      70.692  81.657  36.193  1.00129.17           C  
ANISOU 2978  CB  SER B 138    14854  19275  14949    830     55   -155       C  
ATOM   2979  OG  SER B 138      71.417  81.903  37.382  1.00137.51           O  
ANISOU 2979  OG  SER B 138    15861  20108  16278    592    274      0       O  
ATOM   2980  N   VAL B 139      69.038  82.889  33.671  1.00121.97           N  
ANISOU 2980  N   VAL B 139    13818  19078  13445    795     15    319       N  
ATOM   2981  CA  VAL B 139      68.372  82.724  32.359  1.00124.90           C  
ANISOU 2981  CA  VAL B 139    14192  19843  13420   1071   -199    184       C  
ATOM   2982  C   VAL B 139      68.919  83.681  31.296  1.00129.18           C  
ANISOU 2982  C   VAL B 139    14343  21432  13307   1016     63    681       C  
ATOM   2983  O   VAL B 139      69.175  83.268  30.156  1.00140.41           O  
ANISOU 2983  O   VAL B 139    15560  23771  14016   1496    -25    415       O  
ATOM   2984  CB  VAL B 139      66.830  82.834  32.424  1.00122.53           C  
ANISOU 2984  CB  VAL B 139    14151  18811  13592    826   -432    281       C  
ATOM   2985  CG1 VAL B 139      66.180  81.512  32.015  1.00119.20           C  
ANISOU 2985  CG1 VAL B 139    13979  18105  13206   1200   -985   -323       C  
ATOM   2986  CG2 VAL B 139      66.372  83.292  33.802  1.00118.22           C  
ANISOU 2986  CG2 VAL B 139    13697  17517  13703    374   -313    561       C  
ATOM   2987  N   VAL B 140      69.107  84.953  31.668  1.00157.22           N  
ANISOU 2987  N   VAL B 140    20192  25635  13908   7101  -2698    825       N  
ATOM   2988  CA  VAL B 140      69.683  85.941  30.746  1.00157.20           C  
ANISOU 2988  CA  VAL B 140    21813  24810  13106   7571  -2440   1177       C  
ATOM   2989  C   VAL B 140      71.056  85.466  30.332  1.00150.47           C  
ANISOU 2989  C   VAL B 140    21170  23555  12445   6663  -1786   1617       C  
ATOM   2990  O   VAL B 140      71.378  85.403  29.154  1.00150.79           O  
ANISOU 2990  O   VAL B 140    21980  23314  11999   6954  -1692   1684       O  
ATOM   2991  CB  VAL B 140      69.795  87.350  31.385  1.00160.44           C  
ANISOU 2991  CB  VAL B 140    23164  24618  13175   7675  -2159   1389       C  
ATOM   2992  CG1 VAL B 140      70.616  88.270  30.496  1.00166.72           C  
ANISOU 2992  CG1 VAL B 140    25757  24361  13226   7807  -1598   1849       C  
ATOM   2993  CG2 VAL B 140      68.417  87.951  31.611  1.00167.24           C  
ANISOU 2993  CG2 VAL B 140    23984  25822  13736   8818  -2875    844       C  
ATOM   2994  N   GLY B 141      71.840  85.076  31.322  1.00144.24           N  
ANISOU 2994  N   GLY B 141    19603  22855  12347   5600  -1377   1832       N  
ATOM   2995  CA  GLY B 141      73.158  84.558  31.096  1.00141.24           C  
ANISOU 2995  CA  GLY B 141    19141  22252  12269   4749   -824   2075       C  
ATOM   2996  C   GLY B 141      73.211  83.266  30.312  1.00141.53           C  
ANISOU 2996  C   GLY B 141    18539  22591  12645   4740  -1035   1903       C  
ATOM   2997  O   GLY B 141      74.276  82.837  29.920  1.00153.62           O  
ANISOU 2997  O   GLY B 141    20052  23943  14374   4179   -625   1986       O  
ATOM   2998  N   THR B 142      72.084  82.627  30.071  1.00139.44           N  
ANISOU 2998  N   THR B 142    17672  22819  12490   5324  -1639   1530       N  
ATOM   2999  CA  THR B 142      72.148  81.369  29.338  1.00139.18           C  
ANISOU 2999  CA  THR B 142    16978  23037  12865   5240  -1771   1265       C  
ATOM   3000  C   THR B 142      72.209  81.582  27.845  1.00147.61           C  
ANISOU 3000  C   THR B 142    18939  23951  13193   5841  -1799   1091       C  
ATOM   3001  O   THR B 142      72.870  80.831  27.136  1.00151.01           O  
ANISOU 3001  O   THR B 142    19177  24361  13839   5521  -1598    994       O  
ATOM   3002  CB  THR B 142      71.020  80.416  29.699  1.00138.04           C  
ANISOU 3002  CB  THR B 142    15667  23502  13278   5378  -2246    794       C  
ATOM   3003  OG1 THR B 142      71.012  80.231  31.108  1.00136.90           O  
ANISOU 3003  OG1 THR B 142    14854  23468  13691   4755  -2130   1045       O  
ATOM   3004  CG2 THR B 142      71.230  79.070  29.039  1.00135.48           C  
ANISOU 3004  CG2 THR B 142    14646  23297  13532   5124  -2246    505       C  
ATOM   3005  N   SER B 143      71.550  82.634  27.374  1.00156.55           N  
ANISOU 3005  N   SER B 143    21125  24962  13395   6759  -2048   1055       N  
ATOM   3006  CA  SER B 143      71.567  83.000  25.945  1.00164.07           C  
ANISOU 3006  CA  SER B 143    23242  25735  13362   7489  -2090    997       C  
ATOM   3007  C   SER B 143      72.995  83.390  25.483  1.00162.05           C  
ANISOU 3007  C   SER B 143    23998  24771  12802   6739  -1216   1459       C  
ATOM   3008  O   SER B 143      73.338  83.265  24.300  1.00163.91           O  
ANISOU 3008  O   SER B 143    24893  24936  12450   6905  -1047   1392       O  
ATOM   3009  CB  SER B 143      70.583  84.151  25.694  1.00171.68           C  
ANISOU 3009  CB  SER B 143    25302  26599  13326   8763  -2574    956       C  
ATOM   3010  OG  SER B 143      69.493  84.098  26.617  1.00168.07           O  
ANISOU 3010  OG  SER B 143    23853  26695  13310   9114  -3146    539       O  
ATOM   3011  N   VAL B 144      73.798  83.836  26.462  1.00155.21           N  
ANISOU 3011  N   VAL B 144    23131  23495  12345   5867   -645   1804       N  
ATOM   3012  CA  VAL B 144      75.201  84.233  26.314  1.00150.21           C  
ANISOU 3012  CA  VAL B 144    23162  22294  11615   4925    292   2037       C  
ATOM   3013  C   VAL B 144      76.094  83.001  26.225  1.00143.48           C  
ANISOU 3013  C   VAL B 144    21134  21798  11583   4125    485   1778       C  
ATOM   3014  O   VAL B 144      77.082  82.974  25.484  1.00145.42           O  
ANISOU 3014  O   VAL B 144    21815  21826  11612   3597   1104   1676       O  
ATOM   3015  CB  VAL B 144      75.627  85.074  27.551  1.00146.47           C  
ANISOU 3015  CB  VAL B 144    22767  21476  11408   4322    724   2266       C  
ATOM   3016  CG1 VAL B 144      77.140  85.201  27.659  1.00146.49           C  
ANISOU 3016  CG1 VAL B 144    22829  21187  11643   3139   1670   2220       C  
ATOM   3017  CG2 VAL B 144      74.951  86.437  27.528  1.00153.18           C  
ANISOU 3017  CG2 VAL B 144    25048  21737  11416   5055    712   2502       C  
ATOM   3018  N   TYR B 145      75.747  81.989  26.999  1.00136.24           N  
ANISOU 3018  N   TYR B 145    18772  21391  11599   4031     -4   1641       N  
ATOM   3019  CA  TYR B 145      76.442  80.732  26.950  1.00134.39           C  
ANISOU 3019  CA  TYR B 145    17440  21420  12199   3490     38   1399       C  
ATOM   3020  C   TYR B 145      76.046  79.944  25.714  1.00139.02           C  
ANISOU 3020  C   TYR B 145    17896  22263  12660   3940   -246    997       C  
ATOM   3021  O   TYR B 145      76.730  79.015  25.339  1.00138.03           O  
ANISOU 3021  O   TYR B 145    17121  22246  13077   3539   -105    708       O  
ATOM   3022  CB  TYR B 145      76.169  79.923  28.220  1.00128.99           C  
ANISOU 3022  CB  TYR B 145    15492  21044  12475   3273   -335   1484       C  
ATOM   3023  CG  TYR B 145      76.650  78.493  28.161  1.00126.86           C  
ANISOU 3023  CG  TYR B 145    14158  20936  13104   2957   -433   1262       C  
ATOM   3024  CD1 TYR B 145      77.978  78.170  28.406  1.00128.17           C  
ANISOU 3024  CD1 TYR B 145    13956  21021  13718   2352    -71   1223       C  
ATOM   3025  CD2 TYR B 145      75.776  77.466  27.858  1.00128.14           C  
ANISOU 3025  CD2 TYR B 145    13663  21328  13695   3289   -877    981       C  
ATOM   3026  CE1 TYR B 145      78.417  76.850  28.352  1.00129.58           C  
ANISOU 3026  CE1 TYR B 145    13221  21266  14745   2212   -226   1001       C  
ATOM   3027  CE2 TYR B 145      76.200  76.149  27.794  1.00127.17           C  
ANISOU 3027  CE2 TYR B 145    12677  21190  14452   3020   -921    771       C  
ATOM   3028  CZ  TYR B 145      77.514  75.843  28.041  1.00128.34           C  
ANISOU 3028  CZ  TYR B 145    12561  21175  15028   2544   -632    828       C  
ATOM   3029  OH  TYR B 145      77.928  74.529  27.990  1.00128.39           O  
ANISOU 3029  OH  TYR B 145    11767  21085  15930   2419   -738    608       O  
ATOM   3030  N   ILE B 146      74.931  80.321  25.088  1.00148.57           N  
ANISOU 3030  N   ILE B 146    19673  23630  13144   4844   -690    886       N  
ATOM   3031  CA  ILE B 146      74.509  79.687  23.824  1.00162.73           C  
ANISOU 3031  CA  ILE B 146    21399  25800  14629   5375   -988    389       C  
ATOM   3032  C   ILE B 146      75.120  80.361  22.580  1.00177.12           C  
ANISOU 3032  C   ILE B 146    24616  27343  15336   5484   -516    459       C  
ATOM   3033  O   ILE B 146      75.540  79.674  21.644  1.00182.74           O  
ANISOU 3033  O   ILE B 146    25107  28286  16040   5329   -377     65       O  
ATOM   3034  CB  ILE B 146      72.962  79.592  23.690  1.00164.73           C  
ANISOU 3034  CB  ILE B 146    21348  26600  14642   6392  -1796     -7       C  
ATOM   3035  CG1 ILE B 146      72.376  78.743  24.826  1.00157.77           C  
ANISOU 3035  CG1 ILE B 146    19036  26012  14895   6070  -2091   -196       C  
ATOM   3036  CG2 ILE B 146      72.564  79.004  22.331  1.00169.17           C  
ANISOU 3036  CG2 ILE B 146    21827  27676  14770   6987  -2109   -651       C  
ATOM   3037  CD1 ILE B 146      72.989  77.363  24.951  1.00152.85           C  
ANISOU 3037  CD1 ILE B 146    17289  25391  15394   5304  -1891   -396       C  
ATOM   3038  N   GLU B 147      75.166  81.698  22.578  1.00184.91           N  
ANISOU 3038  N   GLU B 147    27094  27789  15375   5713   -208    942       N  
ATOM   3039  CA  GLU B 147      75.819  82.446  21.497  1.00191.01           C  
ANISOU 3039  CA  GLU B 147    29476  28100  14996   5657    448   1134       C  
ATOM   3040  C   GLU B 147      77.307  82.108  21.438  1.00190.84           C  
ANISOU 3040  C   GLU B 147    29147  27896  15466   4357   1356    988       C  
ATOM   3041  O   GLU B 147      77.788  81.613  20.429  1.00197.92           O  
ANISOU 3041  O   GLU B 147    30083  29007  16108   4149   1624    636       O  
ATOM   3042  CB  GLU B 147      75.614  83.944  21.673  1.00196.81           C  
ANISOU 3042  CB  GLU B 147    31940  28075  14760   6053    715   1719       C  
ATOM   3043  CG  GLU B 147      74.158  84.346  21.808  1.00201.35           C  
ANISOU 3043  CG  GLU B 147    32755  28868  14880   7449   -247   1748       C  
ATOM   3044  CD  GLU B 147      73.903  85.770  21.369  1.00214.47           C  
ANISOU 3044  CD  GLU B 147    36595  29724  15168   8248    -66   2276       C  
ATOM   3045  OE1 GLU B 147      73.293  86.529  22.149  1.00218.09           O  
ANISOU 3045  OE1 GLU B 147    37351  29885  15628   8752   -358   2474       O  
ATOM   3046  OE2 GLU B 147      74.313  86.132  20.243  1.00221.99           O  
ANISOU 3046  OE2 GLU B 147    39036  30298  15011   8382    395   2493       O  
ATOM   3047  N   TRP B 148      78.025  82.367  22.536  1.00182.47           N  
ANISOU 3047  N   TRP B 148    27676  26548  15103   3517   1796   1136       N  
ATOM   3048  CA  TRP B 148      79.326  81.723  22.791  1.00176.41           C  
ANISOU 3048  CA  TRP B 148    25919  25913  15192   2412   2351    752       C  
ATOM   3049  C   TRP B 148      79.112  80.224  22.650  1.00170.52           C  
ANISOU 3049  C   TRP B 148    23639  25787  15361   2596   1713    308       C  
ATOM   3050  O   TRP B 148      78.040  79.739  22.932  1.00174.21           O  
ANISOU 3050  O   TRP B 148    23518  26536  16137   3276    935    349       O  
ATOM   3051  CB  TRP B 148      79.788  82.053  24.219  1.00170.15           C  
ANISOU 3051  CB  TRP B 148    24550  24989  15109   1826   2529    904       C  
ATOM   3052  CG  TRP B 148      81.223  81.651  24.568  1.00169.45           C  
ANISOU 3052  CG  TRP B 148    23573  25066  15742    774   3124    423       C  
ATOM   3053  CD1 TRP B 148      82.297  82.493  24.724  1.00173.96           C  
ANISOU 3053  CD1 TRP B 148    24659  25349  16086   -139   4098    200       C  
ATOM   3054  CD2 TRP B 148      81.709  80.324  24.876  1.00163.35           C  
ANISOU 3054  CD2 TRP B 148    21201  24804  16061    599   2749      6       C  
ATOM   3055  NE1 TRP B 148      83.419  81.771  25.080  1.00172.88           N  
ANISOU 3055  NE1 TRP B 148    23220  25667  16799   -817   4286   -434       N  
ATOM   3056  CE2 TRP B 148      83.088  80.442  25.179  1.00165.73           C  
ANISOU 3056  CE2 TRP B 148    21070  25204  16693   -303   3427   -501       C  
ATOM   3057  CE3 TRP B 148      81.115  79.054  24.920  1.00155.49           C  
ANISOU 3057  CE3 TRP B 148    19133  24142  15801   1121   1947    -50       C  
ATOM   3058  CZ2 TRP B 148      83.885  79.329  25.516  1.00161.01           C  
ANISOU 3058  CZ2 TRP B 148    19017  25063  17093   -512   3189  -1028       C  
ATOM   3059  CZ3 TRP B 148      81.915  77.945  25.247  1.00150.71           C  
ANISOU 3059  CZ3 TRP B 148    17236  23814  16212    827   1812   -469       C  
ATOM   3060  CH2 TRP B 148      83.278  78.096  25.543  1.00152.55           C  
ANISOU 3060  CH2 TRP B 148    17083  24169  16707    110   2362   -929       C  
ATOM   3061  N   LEU B 149      80.115  79.497  22.182  1.00166.33           N  
ANISOU 3061  N   LEU B 149    22475  25448  15272   1970   2095   -212       N  
ATOM   3062  CA  LEU B 149      79.976  78.043  21.992  1.00161.04           C  
ANISOU 3062  CA  LEU B 149    20420  25229  15538   2134   1560   -691       C  
ATOM   3063  C   LEU B 149      79.165  77.673  20.754  1.00167.99           C  
ANISOU 3063  C   LEU B 149    21563  26435  15831   2815   1209   -993       C  
ATOM   3064  O   LEU B 149      79.143  76.509  20.355  1.00172.49           O  
ANISOU 3064  O   LEU B 149    21097  27350  17090   2856    930  -1550       O  
ATOM   3065  CB  LEU B 149      79.405  77.353  23.258  1.00150.65           C  
ANISOU 3065  CB  LEU B 149    17963  23987  15288   2342    893   -467       C  
ATOM   3066  CG  LEU B 149      78.229  76.374  23.131  1.00146.32           C  
ANISOU 3066  CG  LEU B 149    16666  23724  15204   2970    160   -658       C  
ATOM   3067  CD1 LEU B 149      78.496  75.078  23.881  1.00139.61           C  
ANISOU 3067  CD1 LEU B 149    14480  22858  15707   2704    -85   -806       C  
ATOM   3068  CD2 LEU B 149      76.922  77.020  23.586  1.00146.69           C  
ANISOU 3068  CD2 LEU B 149    17138  23819  14778   3611   -296   -290       C  
ATOM   3069  N   HIS B 150      78.491  78.654  20.156  1.00175.32           N  
ANISOU 3069  N   HIS B 150    23879  27258  15476   3421   1193   -674       N  
ATOM   3070  CA  HIS B 150      78.105  78.554  18.754  1.00186.20           C  
ANISOU 3070  CA  HIS B 150    25863  28988  15895   3976   1092  -1011       C  
ATOM   3071  C   HIS B 150      79.419  78.476  18.010  1.00189.04           C  
ANISOU 3071  C   HIS B 150    26468  29297  16059   3079   1982  -1372       C  
ATOM   3072  O   HIS B 150      79.566  77.736  17.032  1.00189.65           O  
ANISOU 3072  O   HIS B 150    26140  29842  16074   3086   1980  -1995       O  
ATOM   3073  CB  HIS B 150      77.348  79.816  18.325  1.00200.65           C  
ANISOU 3073  CB  HIS B 150    29460  30569  16207   4833    995   -475       C  
ATOM   3074  CG  HIS B 150      76.212  79.560  17.378  1.00216.87           C  
ANISOU 3074  CG  HIS B 150    31658  33253  17489   6023    225   -813       C  
ATOM   3075  ND1 HIS B 150      75.010  79.020  17.784  1.00215.94           N  
ANISOU 3075  ND1 HIS B 150    30475  33657  17913   6794   -712  -1136       N  
ATOM   3076  CD2 HIS B 150      76.078  79.819  16.052  1.00230.99           C  
ANISOU 3076  CD2 HIS B 150    34553  35304  17908   6600    264   -949       C  
ATOM   3077  CE1 HIS B 150      74.194  78.933  16.747  1.00226.81           C  
ANISOU 3077  CE1 HIS B 150    32145  35672  18359   7819  -1264  -1575       C  
ATOM   3078  NE2 HIS B 150      74.819  79.409  15.683  1.00233.58           N  
ANISOU 3078  NE2 HIS B 150    34350  36393  18004   7784   -733  -1418       N  
ATOM   3079  N   HIS B 151      80.400  79.190  18.553  1.00190.60           N  
ANISOU 3079  N   HIS B 151    27142  28997  16278   2222   2770  -1125       N  
ATOM   3080  CA  HIS B 151      81.722  79.285  17.985  1.00197.43           C  
ANISOU 3080  CA  HIS B 151    28245  29814  16953   1194   3781  -1579       C  
ATOM   3081  C   HIS B 151      82.617  78.139  18.456  1.00195.40           C  
ANISOU 3081  C   HIS B 151    26150  29910  18180    557   3756  -2296       C  
ATOM   3082  O   HIS B 151      82.722  77.857  19.657  1.00185.06           O  
ANISOU 3082  O   HIS B 151    23875  28528  17910    475   3417  -2162       O  
ATOM   3083  CB  HIS B 151      82.352  80.640  18.339  1.00201.59           C  
ANISOU 3083  CB  HIS B 151    30134  29656  16802    504   4741  -1159       C  
ATOM   3084  CG  HIS B 151      81.371  81.775  18.372  1.00204.48           C  
ANISOU 3084  CG  HIS B 151    32158  29466  16067   1306   4558   -305       C  
ATOM   3085  ND1 HIS B 151      80.258  81.825  17.557  1.00207.36           N  
ANISOU 3085  ND1 HIS B 151    33325  29994  15468   2490   3899    -45       N  
ATOM   3086  CD2 HIS B 151      81.340  82.906  19.118  1.00204.84           C  
ANISOU 3086  CD2 HIS B 151    33181  28819  15828   1170   4915    253       C  
ATOM   3087  CE1 HIS B 151      79.581  82.932  17.806  1.00210.65           C  
ANISOU 3087  CE1 HIS B 151    35167  29816  15051   3138   3800    665       C  
ATOM   3088  NE2 HIS B 151      80.217  83.606  18.747  1.00208.59           N  
ANISOU 3088  NE2 HIS B 151    35066  28973  15213   2318   4444    877       N  
ATOM   3089  N   LEU B 152      83.287  77.513  17.490  1.00207.86           N  
ANISOU 3089  N   LEU B 152    27332  31875  19767    152   4124  -3076       N  
ATOM   3090  CA  LEU B 152      84.038  76.262  17.693  1.00212.16           C  
ANISOU 3090  CA  LEU B 152    26117  32795  21698   -198   3959  -3903       C  
ATOM   3091  C   LEU B 152      83.116  75.025  17.772  1.00206.64           C  
ANISOU 3091  C   LEU B 152    24269  32330  21913    612   2932  -4019       C  
ATOM   3092  O   LEU B 152      83.558  73.934  18.132  1.00209.16           O  
ANISOU 3092  O   LEU B 152    23202  32757  23511    514   2650  -4534       O  
ATOM   3093  CB  LEU B 152      85.037  76.350  18.896  1.00211.03           C  
ANISOU 3093  CB  LEU B 152    25192  32512  22477   -838   4209  -4024       C  
ATOM   3094  CG  LEU B 152      86.528  76.695  18.582  1.00216.32           C  
ANISOU 3094  CG  LEU B 152    25798  33364  23029  -1967   5291  -4879       C  
ATOM   3095  CD1 LEU B 152      86.848  78.164  18.838  1.00217.31           C  
ANISOU 3095  CD1 LEU B 152    27297  33060  22208  -2632   6210  -4495       C  
ATOM   3096  CD2 LEU B 152      87.497  75.806  19.358  1.00210.51           C  
ANISOU 3096  CD2 LEU B 152    23317  32960  23708  -2192   5044  -5637       C  
ATOM   3097  N   GLY B 153      81.851  75.202  17.381  1.00203.53           N  
ANISOU 3097  N   GLY B 153    24495  32010  20825   1422   2419  -3637       N  
ATOM   3098  CA  GLY B 153      80.916  74.079  17.232  1.00199.61           C  
ANISOU 3098  CA  GLY B 153    22978  31822  21042   2076   1614  -3979       C  
ATOM   3099  C   GLY B 153      80.449  73.498  18.559  1.00193.23           C  
ANISOU 3099  C   GLY B 153    21211  30725  21482   2266   1024  -3634       C  
ATOM   3100  O   GLY B 153      81.075  73.713  19.599  1.00187.10           O  
ANISOU 3100  O   GLY B 153    20255  29608  21225   1876   1176  -3261       O  
ATOM   3101  N   SER B 154      79.337  72.763  18.525  1.00193.42           N  
ANISOU 3101  N   SER B 154    20626  30930  21933   2836    393  -3822       N  
ATOM   3102  CA  SER B 154      78.733  72.236  19.752  1.00186.67           C  
ANISOU 3102  CA  SER B 154    19039  29772  22112   2966    -70  -3467       C  
ATOM   3103  C   SER B 154      77.703  71.140  19.495  1.00187.63           C  
ANISOU 3103  C   SER B 154    18266  30107  22915   3331   -540  -4050       C  
ATOM   3104  O   SER B 154      76.599  71.401  19.009  1.00189.37           O  
ANISOU 3104  O   SER B 154    18726  30767  22457   3889   -865  -4256       O  
ATOM   3105  CB  SER B 154      78.079  73.362  20.570  1.00187.20           C  
ANISOU 3105  CB  SER B 154    19931  29687  21506   3230   -214  -2634       C  
ATOM   3106  OG  SER B 154      78.443  74.652  20.098  1.00192.39           O  
ANISOU 3106  OG  SER B 154    21901  30323  20875   3208    206  -2314       O  
ATOM   3107  N   ALA B 155      78.052  69.918  19.848  1.00205.08           N  
ANISOU 3107  N   ALA B 155    30156  33390  14375  -3305   3880  -2214       N  
ATOM   3108  CA  ALA B 155      77.045  68.949  20.179  1.00204.48           C  
ANISOU 3108  CA  ALA B 155    29720  33169  14804  -2880   3096  -2512       C  
ATOM   3109  C   ALA B 155      76.835  69.051  21.653  1.00197.77           C  
ANISOU 3109  C   ALA B 155    27931  31973  15239  -2416   2743  -2215       C  
ATOM   3110  O   ALA B 155      77.290  68.204  22.413  1.00196.85           O  
ANISOU 3110  O   ALA B 155    26985  31744  16063  -2159   3057  -2655       O  
ATOM   3111  CB  ALA B 155      77.488  67.566  19.805  1.00211.53           C  
ANISOU 3111  CB  ALA B 155    30330  34214  15825  -2874   3637  -3468       C  
ATOM   3112  N   LEU B 156      76.218  70.152  22.058  1.00201.85           N  
ANISOU 3112  N   LEU B 156    28605  32302  15785  -2348   2125  -1455       N  
ATOM   3113  CA  LEU B 156      75.931  70.438  23.454  1.00190.77           C  
ANISOU 3113  CA  LEU B 156    26432  30573  15478  -1959   1773  -1114       C  
ATOM   3114  C   LEU B 156      74.611  69.779  23.806  1.00178.27           C  
ANISOU 3114  C   LEU B 156    24614  28773  14347  -1588    887  -1203       C  
ATOM   3115  O   LEU B 156      73.557  70.385  23.628  1.00187.25           O  
ANISOU 3115  O   LEU B 156    26112  29758  15276  -1546     84   -776       O  
ATOM   3116  CB  LEU B 156      75.824  71.967  23.656  1.00197.88           C  
ANISOU 3116  CB  LEU B 156    27620  31348  16216  -2082   1526   -311       C  
ATOM   3117  CG  LEU B 156      74.780  72.711  22.771  1.00211.33           C  
ANISOU 3117  CG  LEU B 156    30195  33015  17085  -2247    701    172       C  
ATOM   3118  CD1 LEU B 156      74.577  74.153  23.208  1.00213.15           C  
ANISOU 3118  CD1 LEU B 156    30496  33007  17483  -2276    348    946       C  
ATOM   3119  CD2 LEU B 156      75.085  72.632  21.272  1.00215.49           C  
ANISOU 3119  CD2 LEU B 156    31705  33873  16298  -2715    986     14       C  
ATOM   3120  N   PRO B 157      74.645  68.509  24.250  1.00165.14           N  
ANISOU 3120  N   PRO B 157    22343  27054  13347  -1334   1008  -1776       N  
ATOM   3121  CA  PRO B 157      73.362  67.974  24.633  1.00162.93           C  
ANISOU 3121  CA  PRO B 157    21821  26523  13562  -1005    195  -1805       C  
ATOM   3122  C   PRO B 157      72.805  68.821  25.778  1.00160.46           C  
ANISOU 3122  C   PRO B 157    21142  25900  13926   -789   -220  -1216       C  
ATOM   3123  O   PRO B 157      73.579  69.364  26.577  1.00168.52           O  
ANISOU 3123  O   PRO B 157    21831  26886  15313   -791    213   -979       O  
ATOM   3124  CB  PRO B 157      73.696  66.548  25.103  1.00154.45           C  
ANISOU 3124  CB  PRO B 157    20069  25396  13216   -788    512  -2447       C  
ATOM   3125  CG  PRO B 157      75.066  66.279  24.592  1.00156.05           C  
ANISOU 3125  CG  PRO B 157    20315  25867  13108  -1048   1423  -2865       C  
ATOM   3126  CD  PRO B 157      75.737  67.608  24.626  1.00159.44           C  
ANISOU 3126  CD  PRO B 157    21023  26385  13172  -1292   1773  -2331       C  
ATOM   3127  N   THR B 158      71.488  68.994  25.819  1.00155.25           N  
ANISOU 3127  N   THR B 158    20554  24998  13434   -626  -1052  -1008       N  
ATOM   3128  CA  THR B 158      70.878  69.936  26.750  1.00142.98           C  
ANISOU 3128  CA  THR B 158    18733  23141  12448   -477  -1441   -480       C  
ATOM   3129  C   THR B 158      71.234  69.642  28.190  1.00133.14           C  
ANISOU 3129  C   THR B 158    16722  21742  12123   -255  -1076   -513       C  
ATOM   3130  O   THR B 158      71.605  70.548  28.936  1.00131.54           O  
ANISOU 3130  O   THR B 158    16358  21464  12156   -268   -901   -133       O  
ATOM   3131  CB  THR B 158      69.363  69.986  26.600  1.00143.51           C  
ANISOU 3131  CB  THR B 158    18862  22902  12761   -315  -2370   -386       C  
ATOM   3132  OG1 THR B 158      68.953  69.015  25.632  1.00154.77           O  
ANISOU 3132  OG1 THR B 158    20578  24421  13805   -326  -2656   -844       O  
ATOM   3133  CG2 THR B 158      68.953  71.330  26.126  1.00148.37           C  
ANISOU 3133  CG2 THR B 158    19991  23412  12970   -473  -2875    168       C  
ATOM   3134  N   LEU B 159      71.158  68.366  28.567  1.00126.96           N  
ANISOU 3134  N   LEU B 159    15502  20901  11836    -71   -977   -966       N  
ATOM   3135  CA  LEU B 159      71.414  67.959  29.940  1.00119.91           C  
ANISOU 3135  CA  LEU B 159    13956  19823  11779    121   -722   -982       C  
ATOM   3136  C   LEU B 159      72.765  68.454  30.395  1.00121.54           C  
ANISOU 3136  C   LEU B 159    14053  20158  11967      5   -108   -846       C  
ATOM   3137  O   LEU B 159      72.858  69.179  31.393  1.00116.19           O  
ANISOU 3137  O   LEU B 159    13156  19336  11655     58    -82   -495       O  
ATOM   3138  CB  LEU B 159      71.334  66.445  30.080  1.00117.95           C  
ANISOU 3138  CB  LEU B 159    13334  19504  11976    277   -665  -1497       C  
ATOM   3139  CG  LEU B 159      71.455  65.893  31.504  1.00112.17           C  
ANISOU 3139  CG  LEU B 159    12000  18522  12095    460   -513  -1479       C  
ATOM   3140  CD1 LEU B 159      70.262  66.257  32.357  1.00109.09           C  
ANISOU 3140  CD1 LEU B 159    11432  17827  12189    594   -921  -1183       C  
ATOM   3141  CD2 LEU B 159      71.620  64.389  31.454  1.00117.58           C  
ANISOU 3141  CD2 LEU B 159    12366  19146  13161    564   -412  -1990       C  
ATOM   3142  N   ASP B 160      73.814  68.070  29.647  1.00128.10           N  
ANISOU 3142  N   ASP B 160    15025  21243  12403   -164    398  -1169       N  
ATOM   3143  CA  ASP B 160      75.193  68.566  29.869  1.00130.54           C  
ANISOU 3143  CA  ASP B 160    15234  21661  12705   -315   1024  -1104       C  
ATOM   3144  C   ASP B 160      75.241  70.071  29.941  1.00122.97           C  
ANISOU 3144  C   ASP B 160    14558  20707  11455   -453    974   -537       C  
ATOM   3145  O   ASP B 160      75.983  70.627  30.732  1.00118.73           O  
ANISOU 3145  O   ASP B 160    13750  20093  11267   -452   1247   -339       O  
ATOM   3146  CB  ASP B 160      76.126  68.127  28.738  1.00152.56           C  
ANISOU 3146  CB  ASP B 160    18260  24728  14977   -556   1590  -1550       C  
ATOM   3147  CG  ASP B 160      76.147  66.638  28.542  1.00171.24           C  
ANISOU 3147  CG  ASP B 160    20334  27082  17648   -438   1667  -2186       C  
ATOM   3148  OD1 ASP B 160      75.065  66.047  28.289  1.00176.73           O  
ANISOU 3148  OD1 ASP B 160    21120  27716  18311   -306   1156  -2315       O  
ATOM   3149  OD2 ASP B 160      77.254  66.057  28.602  1.00185.01           O  
ANISOU 3149  OD2 ASP B 160    21726  28840  19726   -482   2226  -2588       O  
ATOM   3150  N   GLY B 161      74.470  70.720  29.075  1.00122.21           N  
ANISOU 3150  N   GLY B 161    15022  20675  10737   -579    581   -287       N  
ATOM   3151  CA  GLY B 161      74.507  72.156  28.936  1.00123.26           C  
ANISOU 3151  CA  GLY B 161    15494  20792  10545   -749    492    257       C  
ATOM   3152  C   GLY B 161      73.907  72.864  30.122  1.00122.33           C  
ANISOU 3152  C   GLY B 161    15021  20379  11080   -547    123    630       C  
ATOM   3153  O   GLY B 161      74.475  73.834  30.624  1.00119.40           O  
ANISOU 3153  O   GLY B 161    14563  19953  10850   -615    324    950       O  
ATOM   3154  N   VAL B 162      72.753  72.374  30.580  1.00128.56           N  
ANISOU 3154  N   VAL B 162    15584  20957  12305   -312   -382    548       N  
ATOM   3155  CA  VAL B 162      72.019  73.016  31.678  1.00128.16           C  
ANISOU 3155  CA  VAL B 162    15209  20605  12879   -146   -706    829       C  
ATOM   3156  C   VAL B 162      72.806  72.948  32.971  1.00125.63           C  
ANISOU 3156  C   VAL B 162    14416  20228  13087    -57   -281    808       C  
ATOM   3157  O   VAL B 162      73.011  73.973  33.640  1.00133.41           O  
ANISOU 3157  O   VAL B 162    15307  21106  14275    -78   -242   1117       O  
ATOM   3158  CB  VAL B 162      70.612  72.403  31.880  1.00128.36           C  
ANISOU 3158  CB  VAL B 162    15052  20388  13331     57  -1246    672       C  
ATOM   3159  CG1 VAL B 162      69.977  72.936  33.158  1.00123.71           C  
ANISOU 3159  CG1 VAL B 162    14054  19490  13459    200  -1380    852       C  
ATOM   3160  CG2 VAL B 162      69.722  72.716  30.685  1.00133.07           C  
ANISOU 3160  CG2 VAL B 162    16121  20943  13497    -17  -1856    765       C  
ATOM   3161  N   THR B 163      73.271  71.742  33.312  1.00124.42           N  
ANISOU 3161  N   THR B 163    13980  20122  13172     34     -6    439       N  
ATOM   3162  CA  THR B 163      74.137  71.550  34.491  1.00115.85           C  
ANISOU 3162  CA  THR B 163    12498  18958  12559    103    326    408       C  
ATOM   3163  C   THR B 163      75.406  72.428  34.475  1.00111.42           C  
ANISOU 3163  C   THR B 163    11976  18500  11856    -54    721    575       C  
ATOM   3164  O   THR B 163      75.958  72.718  35.519  1.00112.25           O  
ANISOU 3164  O   THR B 163    11813  18482  12356     -4    838    673       O  
ATOM   3165  CB  THR B 163      74.533  70.060  34.729  1.00112.68           C  
ANISOU 3165  CB  THR B 163    11801  18542  12467    207    499    -10       C  
ATOM   3166  OG1 THR B 163      75.952  69.968  34.866  1.00125.54           O  
ANISOU 3166  OG1 THR B 163    13264  20237  14196    136    936   -129       O  
ATOM   3167  CG2 THR B 163      74.112  69.178  33.584  1.00115.34           C  
ANISOU 3167  CG2 THR B 163    12314  19008  12501    195    409   -351       C  
ATOM   3168  N   VAL B 164      75.856  72.839  33.292  1.00110.91           N  
ANISOU 3168  N   VAL B 164    12271  18644  11224   -264    924    601       N  
ATOM   3169  CA  VAL B 164      77.035  73.695  33.195  1.00113.02           C  
ANISOU 3169  CA  VAL B 164    12567  18980  11394   -448   1353    757       C  
ATOM   3170  C   VAL B 164      76.720  75.121  33.599  1.00116.36           C  
ANISOU 3170  C   VAL B 164    13082  19267  11862   -483   1121   1243       C  
ATOM   3171  O   VAL B 164      77.555  75.803  34.202  1.00120.64           O  
ANISOU 3171  O   VAL B 164    13424  19732  12682   -521   1355   1381       O  
ATOM   3172  CB  VAL B 164      77.666  73.670  31.786  1.00115.96           C  
ANISOU 3172  CB  VAL B 164    13336  19615  11108   -726   1763    618       C  
ATOM   3173  CG1 VAL B 164      78.589  74.864  31.584  1.00113.27           C  
ANISOU 3173  CG1 VAL B 164    13120  19300  10615   -965   2143    916       C  
ATOM   3174  CG2 VAL B 164      78.432  72.377  31.582  1.00117.16           C  
ANISOU 3174  CG2 VAL B 164    13228  19860  11425   -711   2188     52       C  
ATOM   3175  N   VAL B 165      75.515  75.578  33.272  1.00122.45           N  
ANISOU 3175  N   VAL B 165    14118  19964  12443   -463    621   1475       N  
ATOM   3176  CA  VAL B 165      75.101  76.921  33.669  1.00124.78           C  
ANISOU 3176  CA  VAL B 165    14442  20066  12902   -479    339   1899       C  
ATOM   3177  C   VAL B 165      74.857  76.967  35.163  1.00116.05           C  
ANISOU 3177  C   VAL B 165    12878  18742  12470   -272    251   1867       C  
ATOM   3178  O   VAL B 165      75.358  77.853  35.844  1.00119.43           O  
ANISOU 3178  O   VAL B 165    13152  19065  13158   -295    357   2051       O  
ATOM   3179  CB  VAL B 165      73.835  77.416  32.932  1.00131.94           C  
ANISOU 3179  CB  VAL B 165    15704  20865  13562   -505   -259   2138       C  
ATOM   3180  CG1 VAL B 165      73.767  78.939  32.996  1.00134.70           C  
ANISOU 3180  CG1 VAL B 165    16154  21027  13996   -610   -458   2604       C  
ATOM   3181  CG2 VAL B 165      73.821  76.942  31.484  1.00137.63           C  
ANISOU 3181  CG2 VAL B 165    16952  21811  13529   -682   -282   2059       C  
ATOM   3182  N   VAL B 166      74.106  75.987  35.665  1.00108.37           N  
ANISOU 3182  N   VAL B 166    11715  17697  11761    -94     79   1618       N  
ATOM   3183  CA  VAL B 166      73.774  75.904  37.083  1.00103.88           C  
ANISOU 3183  CA  VAL B 166    10802  16928  11737     54     34   1568       C  
ATOM   3184  C   VAL B 166      75.051  75.869  37.929  1.00104.54           C  
ANISOU 3184  C   VAL B 166    10676  17032  12012     47    386   1520       C  
ATOM   3185  O   VAL B 166      75.216  76.679  38.847  1.00114.06           O  
ANISOU 3185  O   VAL B 166    11756  18101  13481     55    382   1662       O  
ATOM   3186  CB  VAL B 166      72.832  74.695  37.370  1.00 99.63           C  
ANISOU 3186  CB  VAL B 166    10130  16309  11415    199   -128   1300       C  
ATOM   3187  CG1 VAL B 166      72.841  74.308  38.829  1.00 94.77           C  
ANISOU 3187  CG1 VAL B 166     9237  15539  11229    288    -13   1216       C  
ATOM   3188  CG2 VAL B 166      71.414  75.037  36.957  1.00101.09           C  
ANISOU 3188  CG2 VAL B 166    10391  16329  11688    236   -567   1366       C  
ATOM   3189  N   SER B 167      75.971  74.980  37.560  1.00102.93           N  
ANISOU 3189  N   SER B 167    10426  16969  11710     25    663   1293       N  
ATOM   3190  CA  SER B 167      77.283  74.852  38.208  1.00 98.51           C  
ANISOU 3190  CA  SER B 167     9630  16377  11419     19    940   1203       C  
ATOM   3191  C   SER B 167      78.074  76.145  38.305  1.00 96.60           C  
ANISOU 3191  C   SER B 167     9380  16105  11219    -94   1087   1437       C  
ATOM   3192  O   SER B 167      78.757  76.391  39.309  1.00 92.04           O  
ANISOU 3192  O   SER B 167     8581  15384  11002    -53   1111   1442       O  
ATOM   3193  CB  SER B 167      78.126  73.830  37.467  1.00101.70           C  
ANISOU 3193  CB  SER B 167     9968  16915  11758    -19   1237    882       C  
ATOM   3194  OG  SER B 167      78.216  72.632  38.196  1.00106.16           O  
ANISOU 3194  OG  SER B 167    10286  17359  12691    119   1161    641       O  
ATOM   3195  N   ILE B 168      78.054  76.937  37.237  1.00 98.12           N  
ANISOU 3195  N   ILE B 168     9832  16409  11038   -255   1169   1630       N  
ATOM   3196  CA  ILE B 168      78.778  78.196  37.243  1.00 98.64           C  
ANISOU 3196  CA  ILE B 168     9892  16416  11170   -388   1323   1882       C  
ATOM   3197  C   ILE B 168      78.196  79.131  38.275  1.00 99.86           C  
ANISOU 3197  C   ILE B 168     9943  16360  11640   -299   1009   2092       C  
ATOM   3198  O   ILE B 168      78.931  79.754  39.023  1.00103.05           O  
ANISOU 3198  O   ILE B 168    10143  16637  12373   -301   1087   2138       O  
ATOM   3199  CB  ILE B 168      78.821  78.875  35.863  1.00100.04           C  
ANISOU 3199  CB  ILE B 168    10453  16729  10829   -626   1463   2112       C  
ATOM   3200  CG1 ILE B 168      79.897  78.217  34.999  1.00101.27           C  
ANISOU 3200  CG1 ILE B 168    10647  17074  10755   -790   2002   1853       C  
ATOM   3201  CG2 ILE B 168      79.130  80.365  36.018  1.00 99.98           C  
ANISOU 3201  CG2 ILE B 168    10452  16571  10964   -742   1455   2482       C  
ATOM   3202  CD1 ILE B 168      79.693  78.378  33.516  1.00105.89           C  
ANISOU 3202  CD1 ILE B 168    11757  17863  10610  -1042   2140   1970       C  
ATOM   3203  N   VAL B 169      76.868  79.181  38.362  1.00105.38           N  
ANISOU 3203  N   VAL B 169    10743  16991  12304   -218    656   2159       N  
ATOM   3204  CA  VAL B 169      76.210  80.097  39.301  1.00101.62           C  
ANISOU 3204  CA  VAL B 169    10144  16292  12172   -154    408   2287       C  
ATOM   3205  C   VAL B 169      76.463  79.688  40.765  1.00102.13           C  
ANISOU 3205  C   VAL B 169     9969  16257  12575    -40    453   2084       C  
ATOM   3206  O   VAL B 169      76.781  80.537  41.597  1.00102.87           O  
ANISOU 3206  O   VAL B 169     9942  16213  12931    -46    439   2142       O  
ATOM   3207  CB  VAL B 169      74.705  80.269  39.007  1.00 94.99           C  
ANISOU 3207  CB  VAL B 169     9405  15341  11345   -106     34   2354       C  
ATOM   3208  CG1 VAL B 169      74.190  81.550  39.638  1.00 93.81           C  
ANISOU 3208  CG1 VAL B 169     9121  14934  11586   -102   -166   2506       C  
ATOM   3209  CG2 VAL B 169      74.465  80.303  37.515  1.00 91.86           C  
ANISOU 3209  CG2 VAL B 169     9343  15057  10500   -219    -98   2518       C  
ATOM   3210  N   ALA B 170      76.391  78.382  41.048  1.00 99.19           N  
ANISOU 3210  N   ALA B 170     9565  15945  12178     43    490   1854       N  
ATOM   3211  CA  ALA B 170      76.707  77.854  42.388  1.00 98.82           C  
ANISOU 3211  CA  ALA B 170     9392  15791  12362    112    492   1707       C  
ATOM   3212  C   ALA B 170      78.137  78.215  42.823  1.00 97.08           C  
ANISOU 3212  C   ALA B 170     9041  15524  12321     80    597   1710       C  
ATOM   3213  O   ALA B 170      78.343  78.799  43.888  1.00 92.51           O  
ANISOU 3213  O   ALA B 170     8414  14801  11932     86    504   1728       O  
ATOM   3214  CB  ALA B 170      76.498  76.347  42.432  1.00102.63           C  
ANISOU 3214  CB  ALA B 170     9873  16313  12806    183    491   1507       C  
ATOM   3215  N   GLN B 171      79.106  77.865  41.979  1.00 94.27           N  
ANISOU 3215  N   GLN B 171     8618  15269  11931     36    801   1650       N  
ATOM   3216  CA  GLN B 171      80.504  78.267  42.146  1.00 93.86           C  
ANISOU 3216  CA  GLN B 171     8369  15135  12159     -9    941   1625       C  
ATOM   3217  C   GLN B 171      80.726  79.780  42.465  1.00 91.86           C  
ANISOU 3217  C   GLN B 171     8076  14766  12059    -74    908   1830       C  
ATOM   3218  O   GLN B 171      81.570  80.127  43.314  1.00 96.89           O  
ANISOU 3218  O   GLN B 171     8538  15232  13041    -54    835   1779       O  
ATOM   3219  CB  GLN B 171      81.309  77.857  40.900  1.00 96.78           C  
ANISOU 3219  CB  GLN B 171     8679  15641  12449   -105   1294   1512       C  
ATOM   3220  CG  GLN B 171      82.816  77.847  41.093  1.00 98.77           C  
ANISOU 3220  CG  GLN B 171     8614  15752  13159   -137   1482   1353       C  
ATOM   3221  CD  GLN B 171      83.245  76.858  42.145  1.00 99.63           C  
ANISOU 3221  CD  GLN B 171     8526  15669  13657      4   1221   1140       C  
ATOM   3222  OE1 GLN B 171      82.996  75.661  42.022  1.00100.02           O  
ANISOU 3222  OE1 GLN B 171     8575  15756  13671     72   1181    964       O  
ATOM   3223  NE2 GLN B 171      83.881  77.352  43.197  1.00 97.38           N  
ANISOU 3223  NE2 GLN B 171     8095  15150  13753     44    988   1166       N  
ATOM   3224  N   VAL B 172      80.014  80.659  41.753  1.00 84.43           N  
ANISOU 3224  N   VAL B 172     7289  13880  10911   -152    914   2054       N  
ATOM   3225  CA  VAL B 172      80.075  82.113  42.009  1.00 85.41           C  
ANISOU 3225  CA  VAL B 172     7359  13854  11236   -212    844   2259       C  
ATOM   3226  C   VAL B 172      79.569  82.462  43.410  1.00 90.15           C  
ANISOU 3226  C   VAL B 172     7899  14288  12065   -116    589   2175       C  
ATOM   3227  O   VAL B 172      80.134  83.355  44.090  1.00 89.40           O  
ANISOU 3227  O   VAL B 172     7663  14029  12275   -130    532   2186       O  
ATOM   3228  CB  VAL B 172      79.228  82.910  40.996  1.00 84.74           C  
ANISOU 3228  CB  VAL B 172     7478  13798  10920   -310    781   2541       C  
ATOM   3229  CG1 VAL B 172      79.165  84.383  41.385  1.00 79.38           C  
ANISOU 3229  CG1 VAL B 172     6700  12900  10560   -352    641   2738       C  
ATOM   3230  CG2 VAL B 172      79.766  82.731  39.588  1.00 87.62           C  
ANISOU 3230  CG2 VAL B 172     8018  14334  10938   -473   1066   2654       C  
ATOM   3231  N   LEU B 173      78.481  81.795  43.827  1.00 88.18           N  
ANISOU 3231  N   LEU B 173     7763  14067  11674    -41    464   2068       N  
ATOM   3232  CA  LEU B 173      77.896  82.048  45.142  1.00 85.58           C  
ANISOU 3232  CA  LEU B 173     7437  13596  11481     -2    324   1945       C  
ATOM   3233  C   LEU B 173      78.819  81.497  46.214  1.00 89.47           C  
ANISOU 3233  C   LEU B 173     7922  14028  12043     25    270   1791       C  
ATOM   3234  O   LEU B 173      79.056  82.150  47.242  1.00 93.88           O  
ANISOU 3234  O   LEU B 173     8473  14445  12750     10    159   1721       O  
ATOM   3235  CB  LEU B 173      76.488  81.439  45.269  1.00 80.77           C  
ANISOU 3235  CB  LEU B 173     6935  13002  10751     31    286   1853       C  
ATOM   3236  CG  LEU B 173      75.374  81.972  44.359  1.00 80.96           C  
ANISOU 3236  CG  LEU B 173     6953  12995  10810     22    201   1970       C  
ATOM   3237  CD1 LEU B 173      74.200  81.016  44.372  1.00 77.52           C  
ANISOU 3237  CD1 LEU B 173     6569  12567  10316     69    176   1826       C  
ATOM   3238  CD2 LEU B 173      74.932  83.367  44.768  1.00 81.80           C  
ANISOU 3238  CD2 LEU B 173     6935  12890  11254    -10    103   2004       C  
HETATM 3239  N   MSE B 174      79.376  80.316  45.953  1.00 88.23           N  
ANISOU 3239  N   MSE B 174     7766  13949  11808     61    302   1725       N  
HETATM 3240  CA  MSE B 174      80.272  79.666  46.887  1.00 90.93           C  
ANISOU 3240  CA  MSE B 174     8100  14174  12276     93    143   1603       C  
HETATM 3241  C   MSE B 174      81.507  80.525  47.140  1.00 93.37           C  
ANISOU 3241  C   MSE B 174     8214  14333  12928     77     70   1601       C  
HETATM 3242  O   MSE B 174      81.862  80.771  48.288  1.00 92.01           O  
ANISOU 3242  O   MSE B 174     8101  13995  12861     80   -176   1529       O  
HETATM 3243  CB  MSE B 174      80.613  78.286  46.336  1.00 99.81           C  
ANISOU 3243  CB  MSE B 174     9179  15364  13380    139    187   1520       C  
HETATM 3244  CG  MSE B 174      81.452  77.465  47.305  1.00108.31           C  
ANISOU 3244  CG  MSE B 174    10250  16249  14651    178    -85   1416       C  
HETATM 3245 SE   MSE B 174      83.266  77.267  46.570  1.00116.41          SE  
ANISOU 3245 SE   MSE B 174    10840  17153  16235    205    -17   1274      SE  
HETATM 3246  CE  MSE B 174      84.299  77.057  48.227  1.00120.27           C  
ANISOU 3246  CE  MSE B 174    11337  17250  17108    251   -612   1205       C  
ATOM   3247  N   ILE B 175      82.155  81.019  46.083  1.00 94.24           N  
ANISOU 3247  N   ILE B 175     8115  14481  13208     36    289   1675       N  
ATOM   3248  CA  ILE B 175      83.325  81.895  46.297  1.00100.15           C  
ANISOU 3248  CA  ILE B 175     8621  15044  14387      8    258   1664       C  
ATOM   3249  C   ILE B 175      82.919  83.169  47.049  1.00 95.00           C  
ANISOU 3249  C   ILE B 175     8014  14277  13803    -11    103   1720       C  
ATOM   3250  O   ILE B 175      83.665  83.666  47.923  1.00 93.31           O  
ANISOU 3250  O   ILE B 175     7695  13855  13902      3   -120   1620       O  
ATOM   3251  CB  ILE B 175      84.129  82.223  44.993  1.00100.21           C  
ANISOU 3251  CB  ILE B 175     8402  15094  14578    -86    630   1735       C  
ATOM   3252  CG1 ILE B 175      83.344  83.139  44.068  1.00102.96           C  
ANISOU 3252  CG1 ILE B 175     8889  15572  14659   -190    825   1994       C  
ATOM   3253  CG2 ILE B 175      84.559  80.952  44.274  1.00 98.52           C  
ANISOU 3253  CG2 ILE B 175     8114  14981  14335    -81    836   1581       C  
ATOM   3254  CD1 ILE B 175      84.197  83.754  42.979  1.00106.72           C  
ANISOU 3254  CD1 ILE B 175     9221  16039  15287   -349   1194   2120       C  
ATOM   3255  N   LEU B 176      81.705  83.633  46.778  1.00 86.82           N  
ANISOU 3255  N   LEU B 176     7123  13341  12521    -38    174   1831       N  
ATOM   3256  CA  LEU B 176      81.170  84.817  47.438  1.00 91.94           C  
ANISOU 3256  CA  LEU B 176     7773  13860  13297    -59     59   1827       C  
ATOM   3257  C   LEU B 176      80.551  84.574  48.850  1.00 93.43           C  
ANISOU 3257  C   LEU B 176     8178  13996  13324    -40   -118   1609       C  
ATOM   3258  O   LEU B 176      80.110  85.539  49.518  1.00 91.90           O  
ANISOU 3258  O   LEU B 176     7982  13683  13250    -72   -175   1511       O  
ATOM   3259  CB  LEU B 176      80.169  85.476  46.547  1.00 94.36           C  
ANISOU 3259  CB  LEU B 176     8090  14214  13545   -102    165   2015       C  
ATOM   3260  CG  LEU B 176      80.727  86.536  45.650  1.00 97.59           C  
ANISOU 3260  CG  LEU B 176     8333  14540  14205   -186    257   2254       C  
ATOM   3261  CD1 LEU B 176      80.260  86.253  44.237  1.00 97.93           C  
ANISOU 3261  CD1 LEU B 176     8515  14746  13948   -251    403   2493       C  
ATOM   3262  CD2 LEU B 176      80.215  87.875  46.146  1.00101.47           C  
ANISOU 3262  CD2 LEU B 176     8715  14816  15022   -201    105   2264       C  
ATOM   3263  N   ARG B 177      80.515  83.295  49.271  1.00 89.84           N  
ANISOU 3263  N   ARG B 177     7922  13613  12600    -15   -177   1527       N  
ATOM   3264  CA  ARG B 177      80.242  82.887  50.674  1.00 86.11           C  
ANISOU 3264  CA  ARG B 177     7749  13072  11895    -50   -348   1355       C  
ATOM   3265  C   ARG B 177      78.768  82.999  51.024  1.00 86.36           C  
ANISOU 3265  C   ARG B 177     7954  13155  11702   -115   -161   1266       C  
ATOM   3266  O   ARG B 177      78.394  83.223  52.188  1.00 90.92           O  
ANISOU 3266  O   ARG B 177     8766  13658  12120   -204   -182   1083       O  
ATOM   3267  CB  ARG B 177      81.106  83.677  51.656  1.00 85.43           C  
ANISOU 3267  CB  ARG B 177     7664  12792  12000    -71   -614   1231       C  
ATOM   3268  CG  ARG B 177      82.598  83.460  51.478  1.00 95.02           C  
ANISOU 3268  CG  ARG B 177     8666  13875  13560     -7   -845   1259       C  
ATOM   3269  CD  ARG B 177      83.366  84.724  51.791  1.00 94.49           C  
ANISOU 3269  CD  ARG B 177     8379  13611  13910     -9   -997   1184       C  
ATOM   3270  NE  ARG B 177      82.696  85.471  52.846  1.00 95.89           N  
ANISOU 3270  NE  ARG B 177     8792  13740  13902    -77  -1077   1012       N  
ATOM   3271  CZ  ARG B 177      82.347  86.750  52.758  1.00 96.40           C  
ANISOU 3271  CZ  ARG B 177     8674  13744  14209   -102   -959    965       C  
ATOM   3272  NH1 ARG B 177      82.650  87.451  51.666  1.00 97.28           N  
ANISOU 3272  NH1 ARG B 177     8409  13824  14728    -75   -798   1145       N  
ATOM   3273  NH2 ARG B 177      81.734  87.344  53.781  1.00 93.04           N  
ANISOU 3273  NH2 ARG B 177     8455  13262  13632   -175   -998    723       N  
ATOM   3274  N   TYR B 178      77.929  82.840  50.013  1.00 83.10           N  
ANISOU 3274  N   TYR B 178     7431  12848  11294    -87     26   1364       N  
ATOM   3275  CA  TYR B 178      76.484  82.824  50.200  1.00 84.81           C  
ANISOU 3275  CA  TYR B 178     7720  13063  11441   -135    204   1253       C  
ATOM   3276  C   TYR B 178      75.942  81.407  50.454  1.00 83.86           C  
ANISOU 3276  C   TYR B 178     7825  13017  11018   -157    287   1215       C  
ATOM   3277  O   TYR B 178      76.324  80.463  49.766  1.00 81.49           O  
ANISOU 3277  O   TYR B 178     7509  12815  10639    -89    235   1335       O  
ATOM   3278  CB  TYR B 178      75.804  83.459  48.997  1.00 83.31           C  
ANISOU 3278  CB  TYR B 178     7286  12872  11495    -93    252   1378       C  
ATOM   3279  CG  TYR B 178      75.853  84.951  49.041  1.00 86.86           C  
ANISOU 3279  CG  TYR B 178     7537  13162  12303   -113    195   1373       C  
ATOM   3280  CD1 TYR B 178      75.186  85.648  50.051  1.00 89.97           C  
ANISOU 3280  CD1 TYR B 178     7915  13399  12867   -179    268   1101       C  
ATOM   3281  CD2 TYR B 178      76.588  85.682  48.098  1.00 83.76           C  
ANISOU 3281  CD2 TYR B 178     6971  12750  12104    -91    101   1618       C  
ATOM   3282  CE1 TYR B 178      75.227  87.033  50.119  1.00 95.12           C  
ANISOU 3282  CE1 TYR B 178     8339  13864  13937   -190    195   1056       C  
ATOM   3283  CE2 TYR B 178      76.652  87.076  48.160  1.00 87.61           C  
ANISOU 3283  CE2 TYR B 178     7259  13043  12986   -117     22   1638       C  
ATOM   3284  CZ  TYR B 178      75.961  87.751  49.174  1.00 92.80           C  
ANISOU 3284  CZ  TYR B 178     7857  13529  13874   -151     40   1347       C  
ATOM   3285  OH  TYR B 178      75.981  89.136  49.262  1.00 90.97           O  
ANISOU 3285  OH  TYR B 178     7380  13063  14119   -169    -55   1321       O  
ATOM   3286  N   ARG B 179      75.060  81.275  51.457  1.00 88.89           N  
ANISOU 3286  N   ARG B 179     8668  13589  11516   -275    454   1024       N  
ATOM   3287  CA  ARG B 179      74.493  79.975  51.837  1.00 87.89           C  
ANISOU 3287  CA  ARG B 179     8784  13487  11122   -341    574   1000       C  
ATOM   3288  C   ARG B 179      73.800  79.306  50.676  1.00 89.70           C  
ANISOU 3288  C   ARG B 179     8812  13783  11483   -246    640   1078       C  
ATOM   3289  O   ARG B 179      73.880  78.086  50.525  1.00 95.77           O  
ANISOU 3289  O   ARG B 179     9682  14598  12105   -226    607   1148       O  
ATOM   3290  CB  ARG B 179      73.504  80.109  52.987  1.00 87.78           C  
ANISOU 3290  CB  ARG B 179     8999  13376  10974   -533    874    756       C  
ATOM   3291  CG  ARG B 179      72.462  78.989  52.996  1.00 91.36           C  
ANISOU 3291  CG  ARG B 179     9544  13815  11353   -605   1127    722       C  
ATOM   3292  CD  ARG B 179      71.828  78.755  54.357  1.00 99.95           C  
ANISOU 3292  CD  ARG B 179    11023  14813  12138   -869   1464    524       C  
ATOM   3293  NE  ARG B 179      71.220  79.971  54.922  1.00115.26           N  
ANISOU 3293  NE  ARG B 179    12880  16661  14253   -985   1752    202       N  
ATOM   3294  CZ  ARG B 179      70.149  80.602  54.431  1.00113.44           C  
ANISOU 3294  CZ  ARG B 179    12232  16319  14549   -954   1991    -12       C  
ATOM   3295  NH1 ARG B 179      69.529  80.146  53.335  1.00121.01           N  
ANISOU 3295  NH1 ARG B 179    12859  17256  15862   -809   1940     81       N  
ATOM   3296  NH2 ARG B 179      69.701  81.695  55.036  1.00110.55           N  
ANISOU 3296  NH2 ARG B 179    11772  15830  14402  -1066   2240   -349       N  
ATOM   3297  N   GLU B 180      73.130  80.109  49.852  1.00 89.47           N  
ANISOU 3297  N   GLU B 180     8505  13728  11761   -189    675   1063       N  
ATOM   3298  CA  GLU B 180      72.206  79.603  48.830  1.00 93.05           C  
ANISOU 3298  CA  GLU B 180     8798  14193  12363   -119    689   1085       C  
ATOM   3299  C   GLU B 180      72.865  78.787  47.698  1.00 89.66           C  
ANISOU 3299  C   GLU B 180     8352  13929  11784     -8    527   1266       C  
ATOM   3300  O   GLU B 180      72.178  78.086  46.954  1.00 89.20           O  
ANISOU 3300  O   GLU B 180     8235  13894  11763     41    510   1253       O  
ATOM   3301  CB  GLU B 180      71.354  80.745  48.262  1.00 99.88           C  
ANISOU 3301  CB  GLU B 180     9394  14920  13635    -94    646   1042       C  
ATOM   3302  CG  GLU B 180      70.269  81.250  49.220  1.00111.63           C  
ANISOU 3302  CG  GLU B 180    10797  16194  15422   -205    896    738       C  
ATOM   3303  CD  GLU B 180      70.800  82.183  50.323  1.00118.19           C  
ANISOU 3303  CD  GLU B 180    11716  16974  16215   -305    999    604       C  
ATOM   3304  OE1 GLU B 180      71.902  82.757  50.158  1.00113.35           O  
ANISOU 3304  OE1 GLU B 180    11119  16432  15513   -256    796    772       O  
ATOM   3305  OE2 GLU B 180      70.101  82.345  51.358  1.00121.21           O  
ANISOU 3305  OE2 GLU B 180    12149  17229  16674   -451   1311    296       O  
ATOM   3306  N   GLN B 181      74.189  78.872  47.581  1.00 89.66           N  
ANISOU 3306  N   GLN B 181     8383  14018  11663     18    423   1385       N  
ATOM   3307  CA  GLN B 181      74.942  77.959  46.717  1.00 84.18           C  
ANISOU 3307  CA  GLN B 181     7671  13461  10853     89    361   1463       C  
ATOM   3308  C   GLN B 181      74.457  76.508  46.885  1.00 81.83           C  
ANISOU 3308  C   GLN B 181     7459  13160  10470    103    390   1376       C  
ATOM   3309  O   GLN B 181      74.306  75.775  45.912  1.00 79.66           O  
ANISOU 3309  O   GLN B 181     7119  12975  10173    168    373   1361       O  
ATOM   3310  CB  GLN B 181      76.419  78.032  47.045  1.00 82.66           C  
ANISOU 3310  CB  GLN B 181     7472  13268  10664     92    283   1505       C  
ATOM   3311  CG  GLN B 181      76.713  77.728  48.490  1.00 90.66           C  
ANISOU 3311  CG  GLN B 181     8676  14153  11615     36    190   1442       C  
ATOM   3312  CD  GLN B 181      78.169  77.424  48.754  1.00 98.32           C  
ANISOU 3312  CD  GLN B 181     9615  15060  12680     66     -7   1461       C  
ATOM   3313  OE1 GLN B 181      78.690  76.376  48.346  1.00104.49           O  
ANISOU 3313  OE1 GLN B 181    10326  15848  13526    122    -68   1446       O  
ATOM   3314  NE2 GLN B 181      78.826  78.312  49.488  1.00 97.00           N  
ANISOU 3314  NE2 GLN B 181     9469  14787  12598     32   -138   1453       N  
ATOM   3315  N   TRP B 182      74.202  76.117  48.128  1.00 80.83           N  
ANISOU 3315  N   TRP B 182     7512  12919  10281     20    437   1316       N  
ATOM   3316  CA  TRP B 182      73.879  74.731  48.459  1.00 84.12           C  
ANISOU 3316  CA  TRP B 182     8045  13281  10633      0    454   1283       C  
ATOM   3317  C   TRP B 182      72.610  74.224  47.828  1.00 81.57           C  
ANISOU 3317  C   TRP B 182     7605  12945  10441     25    567   1192       C  
ATOM   3318  O   TRP B 182      72.489  73.032  47.525  1.00 78.53           O  
ANISOU 3318  O   TRP B 182     7205  12549  10084     64    534   1167       O  
ATOM   3319  CB  TRP B 182      73.862  74.530  49.970  1.00 86.36           C  
ANISOU 3319  CB  TRP B 182     8646  13427  10740   -155    492   1285       C  
ATOM   3320  CG  TRP B 182      75.228  74.511  50.493  1.00 93.54           C  
ANISOU 3320  CG  TRP B 182     9681  14299  11559   -151    226   1378       C  
ATOM   3321  CD1 TRP B 182      75.857  75.506  51.161  1.00 95.13           C  
ANISOU 3321  CD1 TRP B 182     9979  14466  11697   -198    128   1379       C  
ATOM   3322  CD2 TRP B 182      76.216  73.484  50.270  1.00 97.90           C  
ANISOU 3322  CD2 TRP B 182    10194  14804  12200    -73    -31   1446       C  
ATOM   3323  NE1 TRP B 182      77.167  75.147  51.418  1.00101.43           N  
ANISOU 3323  NE1 TRP B 182    10816  15182  12540   -156   -206   1455       N  
ATOM   3324  CE2 TRP B 182      77.400  73.905  50.884  1.00 98.29           C  
ANISOU 3324  CE2 TRP B 182    10319  14760  12265    -80   -303   1493       C  
ATOM   3325  CE3 TRP B 182      76.190  72.225  49.641  1.00 95.88           C  
ANISOU 3325  CE3 TRP B 182     9816  14533  12079      2    -77   1435       C  
ATOM   3326  CZ2 TRP B 182      78.542  73.124  50.895  1.00 98.95           C  
ANISOU 3326  CZ2 TRP B 182    10333  14707  12555    -13   -633   1529       C  
ATOM   3327  CZ3 TRP B 182      77.320  71.457  49.653  1.00 89.12           C  
ANISOU 3327  CZ3 TRP B 182     8893  13559  11407     63   -365   1459       C  
ATOM   3328  CH2 TRP B 182      78.479  71.900  50.276  1.00 95.58           C  
ANISOU 3328  CH2 TRP B 182     9762  14257  12296     56   -647   1507       C  
ATOM   3329  N   ALA B 183      71.669  75.131  47.612  1.00 82.65           N  
ANISOU 3329  N   ALA B 183     7622  13039  10742     12    657   1122       N  
ATOM   3330  CA  ALA B 183      70.458  74.802  46.908  1.00 81.04           C  
ANISOU 3330  CA  ALA B 183     7248  12769  10773     56    673   1016       C  
ATOM   3331  C   ALA B 183      70.813  74.451  45.471  1.00 83.16           C  
ANISOU 3331  C   ALA B 183     7428  13191  10978    188    455   1072       C  
ATOM   3332  O   ALA B 183      70.539  73.338  45.009  1.00 89.42           O  
ANISOU 3332  O   ALA B 183     8186  13991  11796    240    413    995       O  
ATOM   3333  CB  ALA B 183      69.478  75.960  46.970  1.00 77.65           C  
ANISOU 3333  CB  ALA B 183     6658  12194  10650     22    734    915       C  
ATOM   3334  N   LEU B 184      71.487  75.375  44.790  1.00 84.93           N  
ANISOU 3334  N   LEU B 184     7640  13534  11095    218    344   1196       N  
ATOM   3335  CA  LEU B 184      72.043  75.098  43.463  1.00 84.95           C  
ANISOU 3335  CA  LEU B 184     7651  13715  10908    282    223   1247       C  
ATOM   3336  C   LEU B 184      72.914  73.813  43.420  1.00 85.93           C  
ANISOU 3336  C   LEU B 184     7795  13933  10918    316    277   1168       C  
ATOM   3337  O   LEU B 184      72.767  73.013  42.511  1.00 84.87           O  
ANISOU 3337  O   LEU B 184     7640  13880  10727    369    225   1063       O  
ATOM   3338  CB  LEU B 184      72.820  76.305  42.936  1.00 82.89           C  
ANISOU 3338  CB  LEU B 184     7420  13546  10527    249    189   1424       C  
ATOM   3339  CG  LEU B 184      72.148  77.189  41.881  1.00 83.97           C  
ANISOU 3339  CG  LEU B 184     7580  13662  10662    239    -10   1546       C  
ATOM   3340  CD1 LEU B 184      70.652  76.973  41.859  1.00 88.21           C  
ANISOU 3340  CD1 LEU B 184     8023  14013  11478    284   -177   1423       C  
ATOM   3341  CD2 LEU B 184      72.474  78.660  42.106  1.00 83.63           C  
ANISOU 3341  CD2 LEU B 184     7510  13539  10724    179    -33   1727       C  
ATOM   3342  N   TRP B 185      73.779  73.603  44.422  1.00 85.55           N  
ANISOU 3342  N   TRP B 185     7784  13836  10885    285    334   1194       N  
ATOM   3343  CA  TRP B 185      74.622  72.389  44.436  1.00 88.40           C  
ANISOU 3343  CA  TRP B 185     8110  14199  11278    324    310   1113       C  
ATOM   3344  C   TRP B 185      73.794  71.111  44.397  1.00 89.99           C  
ANISOU 3344  C   TRP B 185     8288  14317  11584    358    285    991       C  
ATOM   3345  O   TRP B 185      74.130  70.171  43.644  1.00 88.84           O  
ANISOU 3345  O   TRP B 185     8041  14225  11489    423    253    851       O  
ATOM   3346  CB  TRP B 185      75.601  72.356  45.625  1.00 84.47           C  
ANISOU 3346  CB  TRP B 185     7679  13574  10841    283    242   1184       C  
ATOM   3347  CG  TRP B 185      76.727  73.338  45.511  1.00 85.48           C  
ANISOU 3347  CG  TRP B 185     7739  13752  10984    275    241   1245       C  
ATOM   3348  CD1 TRP B 185      77.103  74.275  46.444  1.00 90.57           C  
ANISOU 3348  CD1 TRP B 185     8467  14312  11634    219    182   1338       C  
ATOM   3349  CD2 TRP B 185      77.601  73.508  44.404  1.00 83.82           C  
ANISOU 3349  CD2 TRP B 185     7367  13672  10808    300    338   1190       C  
ATOM   3350  NE1 TRP B 185      78.163  75.010  45.978  1.00 86.86           N  
ANISOU 3350  NE1 TRP B 185     7848  13885  11268    228    205   1360       N  
ATOM   3351  CE2 TRP B 185      78.485  74.567  44.723  1.00 89.71           C  
ANISOU 3351  CE2 TRP B 185     8065  14380  11641    261    340   1278       C  
ATOM   3352  CE3 TRP B 185      77.729  72.878  43.174  1.00 85.97           C  
ANISOU 3352  CE3 TRP B 185     7544  14083  11036    328    459   1047       C  
ATOM   3353  CZ2 TRP B 185      79.478  75.002  43.846  1.00 95.85           C  
ANISOU 3353  CZ2 TRP B 185     8682  15237  12500    236    504   1250       C  
ATOM   3354  CZ3 TRP B 185      78.725  73.306  42.308  1.00 93.55           C  
ANISOU 3354  CZ3 TRP B 185     8394  15150  11998    285    649    999       C  
ATOM   3355  CH2 TRP B 185      79.583  74.360  42.650  1.00 94.87           C  
ANISOU 3355  CH2 TRP B 185     8496  15260  12289    233    691   1112       C  
ATOM   3356  N   ILE B 186      72.712  71.067  45.197  1.00 82.33           N  
ANISOU 3356  N   ILE B 186     7390  13199  10694    298    337   1007       N  
ATOM   3357  CA  ILE B 186      71.863  69.874  45.252  1.00 82.09           C  
ANISOU 3357  CA  ILE B 186     7315  13037  10837    306    347    902       C  
ATOM   3358  C   ILE B 186      71.326  69.539  43.857  1.00 90.32           C  
ANISOU 3358  C   ILE B 186     8201  14174  11940    413    254    739       C  
ATOM   3359  O   ILE B 186      71.184  68.375  43.515  1.00 98.02           O  
ANISOU 3359  O   ILE B 186     9087  15099  13056    466    199    603       O  
ATOM   3360  CB  ILE B 186      70.660  70.035  46.186  1.00 82.48           C  
ANISOU 3360  CB  ILE B 186     7431  12900  11008    189    520    902       C  
ATOM   3361  CG1 ILE B 186      71.090  70.228  47.631  1.00 81.09           C  
ANISOU 3361  CG1 ILE B 186     7517  12627  10666     36    624   1038       C  
ATOM   3362  CG2 ILE B 186      69.743  68.827  46.073  1.00 82.62           C  
ANISOU 3362  CG2 ILE B 186     7346  12758  11288    194    553    782       C  
ATOM   3363  CD1 ILE B 186      69.984  70.854  48.490  1.00 80.84           C  
ANISOU 3363  CD1 ILE B 186     7564  12462  10687   -120    913    980       C  
ATOM   3364  N   VAL B 187      71.019  70.564  43.061  1.00 90.10           N  
ANISOU 3364  N   VAL B 187     8166  14259  11809    434    193    758       N  
ATOM   3365  CA  VAL B 187      70.492  70.336  41.719  1.00 92.26           C  
ANISOU 3365  CA  VAL B 187     8391  14613  12048    509     23    625       C  
ATOM   3366  C   VAL B 187      71.582  69.898  40.755  1.00 95.46           C  
ANISOU 3366  C   VAL B 187     8838  15239  12193    540     27    540       C  
ATOM   3367  O   VAL B 187      71.365  68.942  39.996  1.00101.73           O  
ANISOU 3367  O   VAL B 187     9584  16064  13004    598    -52    326       O  
ATOM   3368  CB  VAL B 187      69.722  71.559  41.154  1.00 95.23           C  
ANISOU 3368  CB  VAL B 187     8796  14974  12413    501   -139    708       C  
ATOM   3369  CG1 VAL B 187      69.400  71.357  39.681  1.00 95.21           C  
ANISOU 3369  CG1 VAL B 187     8864  15074  12235    553   -404    613       C  
ATOM   3370  CG2 VAL B 187      68.443  71.791  41.941  1.00 91.77           C  
ANISOU 3370  CG2 VAL B 187     8212  14258  12398    478   -121    658       C  
ATOM   3371  N   VAL B 188      72.766  70.562  40.794  1.00 91.32           N  
ANISOU 3371  N   VAL B 188     8373  14844  11479    491    152    658       N  
ATOM   3372  CA  VAL B 188      73.886  70.149  39.893  1.00 88.43           C  
ANISOU 3372  CA  VAL B 188     7998  14662  10936    485    269    513       C  
ATOM   3373  C   VAL B 188      74.322  68.741  40.181  1.00 85.10           C  
ANISOU 3373  C   VAL B 188     7403  14144  10784    546    294    295       C  
ATOM   3374  O   VAL B 188      74.792  68.045  39.289  1.00 93.78           O  
ANISOU 3374  O   VAL B 188     8439  15350  11843    563    371     39       O  
ATOM   3375  CB  VAL B 188      75.153  71.074  39.880  1.00 82.69           C  
ANISOU 3375  CB  VAL B 188     7294  14038  10084    406    452    640       C  
ATOM   3376  CG1 VAL B 188      74.807  72.522  40.070  1.00 90.05           C  
ANISOU 3376  CG1 VAL B 188     8347  14963  10903    347    400    914       C  
ATOM   3377  CG2 VAL B 188      76.144  70.630  40.903  1.00 84.55           C  
ANISOU 3377  CG2 VAL B 188     7366  14133  10625    427    501    616       C  
ATOM   3378  N   ASN B 189      74.172  68.309  41.420  1.00 78.71           N  
ANISOU 3378  N   ASN B 189     6539  13116  10251    559    231    385       N  
ATOM   3379  CA  ASN B 189      74.513  66.935  41.745  1.00 84.68           C  
ANISOU 3379  CA  ASN B 189     7141  13709  11322    608    174    231       C  
ATOM   3380  C   ASN B 189      73.543  65.912  41.145  1.00 85.05           C  
ANISOU 3380  C   ASN B 189     7105  13708  11500    672     93     14       C  
ATOM   3381  O   ASN B 189      73.963  64.813  40.736  1.00 83.35           O  
ANISOU 3381  O   ASN B 189     6717  13444  11507    729     69   -237       O  
ATOM   3382  CB  ASN B 189      74.668  66.747  43.247  1.00 83.00           C  
ANISOU 3382  CB  ASN B 189     6990  13250  11297    562     86    444       C  
ATOM   3383  CG  ASN B 189      75.871  67.476  43.796  1.00 83.68           C  
ANISOU 3383  CG  ASN B 189     7106  13332  11357    524     76    575       C  
ATOM   3384  OD1 ASN B 189      75.961  67.725  45.001  1.00 84.98           O  
ANISOU 3384  OD1 ASN B 189     7427  13341  11520    457    -21    781       O  
ATOM   3385  ND2 ASN B 189      76.822  67.813  42.912  1.00 78.22           N  
ANISOU 3385  ND2 ASN B 189     6276  12795  10647    546    190    435       N  
ATOM   3386  N   ILE B 190      72.258  66.286  41.077  1.00 81.27           N  
ANISOU 3386  N   ILE B 190     6704  13207  10967    667     33     71       N  
ATOM   3387  CA  ILE B 190      71.215  65.395  40.583  1.00 81.80           C  
ANISOU 3387  CA  ILE B 190     6664  13173  11243    730    -88   -137       C  
ATOM   3388  C   ILE B 190      71.344  65.329  39.073  1.00 87.06           C  
ANISOU 3388  C   ILE B 190     7360  14068  11649    777   -158   -397       C  
ATOM   3389  O   ILE B 190      71.236  64.256  38.469  1.00 89.85           O  
ANISOU 3389  O   ILE B 190     7588  14393  12154    841   -230   -697       O  
ATOM   3390  CB  ILE B 190      69.783  65.878  41.003  1.00 81.11           C  
ANISOU 3390  CB  ILE B 190     6589  12924  11303    702   -136    -36       C  
ATOM   3391  CG1 ILE B 190      69.658  65.919  42.525  1.00 78.79           C  
ANISOU 3391  CG1 ILE B 190     6338  12421  11176    597     29    181       C  
ATOM   3392  CG2 ILE B 190      68.683  64.965  40.433  1.00 76.27           C  
ANISOU 3392  CG2 ILE B 190     5810  12159  11010    775   -301   -287       C  
ATOM   3393  CD1 ILE B 190      68.563  66.844  43.021  1.00 80.15           C  
ANISOU 3393  CD1 ILE B 190     6530  12480  11442    525    116    266       C  
ATOM   3394  N   LEU B 191      71.635  66.475  38.473  1.00 89.62           N  
ANISOU 3394  N   LEU B 191     7878  14612  11559    721   -125   -284       N  
ATOM   3395  CA  LEU B 191      71.876  66.559  37.035  1.00 93.80           C  
ANISOU 3395  CA  LEU B 191     8570  15390  11679    697   -144   -480       C  
ATOM   3396  C   LEU B 191      73.101  65.761  36.614  1.00 95.74           C  
ANISOU 3396  C   LEU B 191     8709  15750  11916    685     98   -770       C  
ATOM   3397  O   LEU B 191      73.058  65.006  35.629  1.00 98.26           O  
ANISOU 3397  O   LEU B 191     9040  16165  12128    699     85  -1126       O  
ATOM   3398  CB  LEU B 191      72.036  68.019  36.614  1.00 93.34           C  
ANISOU 3398  CB  LEU B 191     8781  15499  11183    594   -132   -213       C  
ATOM   3399  CG  LEU B 191      70.741  68.823  36.667  1.00 89.68           C  
ANISOU 3399  CG  LEU B 191     8403  14899  10770    609   -448    -14       C  
ATOM   3400  CD1 LEU B 191      70.905  70.110  35.879  1.00 86.69           C  
ANISOU 3400  CD1 LEU B 191     8335  14675   9926    499   -530    216       C  
ATOM   3401  CD2 LEU B 191      69.582  67.981  36.137  1.00 87.49           C  
ANISOU 3401  CD2 LEU B 191     8066  14492  10683    700   -765   -262       C  
ATOM   3402  N   THR B 192      74.190  65.921  37.369  1.00 95.80           N  
ANISOU 3402  N   THR B 192     8590  15713  12094    657    302   -663       N  
ATOM   3403  CA  THR B 192      75.438  65.247  37.056  1.00 95.92           C  
ANISOU 3403  CA  THR B 192     8413  15763  12269    645    540   -965       C  
ATOM   3404  C   THR B 192      75.388  63.744  37.341  1.00 91.25           C  
ANISOU 3404  C   THR B 192     7522  14938  12209    753    426  -1247       C  
ATOM   3405  O   THR B 192      75.991  62.958  36.603  1.00 93.76           O  
ANISOU 3405  O   THR B 192     7673  15298  12652    759    574  -1666       O  
ATOM   3406  CB  THR B 192      76.666  65.913  37.726  1.00 96.23           C  
ANISOU 3406  CB  THR B 192     8359  15765  12438    588    724   -791       C  
ATOM   3407  OG1 THR B 192      76.734  67.294  37.345  1.00 93.77           O  
ANISOU 3407  OG1 THR B 192     8306  15655  11666    476    847   -548       O  
ATOM   3408  CG2 THR B 192      77.958  65.230  37.272  1.00104.53           C  
ANISOU 3408  CG2 THR B 192     9133  16803  13778    568    992  -1184       C  
ATOM   3409  N   ILE B 193      74.650  63.323  38.366  1.00 91.54           N  
ANISOU 3409  N   ILE B 193    11006  14193   9582    865    549    840       N  
ATOM   3410  CA  ILE B 193      74.437  61.887  38.512  1.00 95.23           C  
ANISOU 3410  CA  ILE B 193    11621  14254  10306    853    837   1028       C  
ATOM   3411  C   ILE B 193      73.838  61.331  37.211  1.00104.10           C  
ANISOU 3411  C   ILE B 193    12972  14902  11678    677    767    639       C  
ATOM   3412  O   ILE B 193      74.155  60.208  36.805  1.00112.92           O  
ANISOU 3412  O   ILE B 193    14300  15590  13014    741    978    666       O  
ATOM   3413  CB  ILE B 193      73.571  61.501  39.715  1.00 93.77           C  
ANISOU 3413  CB  ILE B 193    11311  14119  10198    644   1068   1237       C  
ATOM   3414  CG1 ILE B 193      74.287  61.832  41.026  1.00 95.74           C  
ANISOU 3414  CG1 ILE B 193    11483  14845  10049    893   1116   1653       C  
ATOM   3415  CG2 ILE B 193      73.296  60.007  39.686  1.00 96.88           C  
ANISOU 3415  CG2 ILE B 193    12032  13871  10907    511   1418   1436       C  
ATOM   3416  CD1 ILE B 193      73.646  61.206  42.266  1.00102.05           C  
ANISOU 3416  CD1 ILE B 193    12436  15642  10695    661   1488   2016       C  
ATOM   3417  N   SER B 194      73.034  62.154  36.526  1.00105.13           N  
ANISOU 3417  N   SER B 194    13086  15095  11763    535    374    219       N  
ATOM   3418  CA  SER B 194      72.360  61.743  35.285  1.00106.46           C  
ANISOU 3418  CA  SER B 194    13480  14899  12070    431    132   -258       C  
ATOM   3419  C   SER B 194      73.327  61.603  34.112  1.00108.55           C  
ANISOU 3419  C   SER B 194    14230  15032  11981    536    172   -307       C  
ATOM   3420  O   SER B 194      73.248  60.625  33.354  1.00110.15           O  
ANISOU 3420  O   SER B 194    14606  14893  12350    501    272   -579       O  
ATOM   3421  CB  SER B 194      71.234  62.716  34.931  1.00109.81           C  
ANISOU 3421  CB  SER B 194    13792  15422  12506    401   -499   -740       C  
ATOM   3422  OG  SER B 194      70.141  62.590  35.825  1.00113.12           O  
ANISOU 3422  OG  SER B 194    13622  15944  13413    208   -437  -1004       O  
ATOM   3423  N   LEU B 195      74.221  62.593  33.951  1.00110.35           N  
ANISOU 3423  N   LEU B 195    14658  15531  11737    592    164   -137       N  
ATOM   3424  CA  LEU B 195      75.332  62.538  32.944  1.00109.07           C  
ANISOU 3424  CA  LEU B 195    14914  15349  11178    555    446   -232       C  
ATOM   3425  C   LEU B 195      76.090  61.221  32.945  1.00112.93           C  
ANISOU 3425  C   LEU B 195    15227  15676  12005    694    908   -294       C  
ATOM   3426  O   LEU B 195      76.267  60.607  31.897  1.00122.21           O  
ANISOU 3426  O   LEU B 195    16690  16652  13092    635   1042   -661       O  
ATOM   3427  CB  LEU B 195      76.326  63.682  33.155  1.00100.77           C  
ANISOU 3427  CB  LEU B 195    13900  14622   9766    479    618    -49       C  
ATOM   3428  CG  LEU B 195      75.786  65.046  32.816  1.00 98.38           C  
ANISOU 3428  CG  LEU B 195    14036  14287   9056    334    159    -18       C  
ATOM   3429  CD1 LEU B 195      76.905  66.012  32.481  1.00102.19           C  
ANISOU 3429  CD1 LEU B 195    14855  14881   9090     58    518     54       C  
ATOM   3430  CD2 LEU B 195      74.865  64.882  31.642  1.00102.92           C  
ANISOU 3430  CD2 LEU B 195    15230  14532   9341    313   -312   -285       C  
ATOM   3431  N   TRP B 196      76.557  60.802  34.120  1.00108.87           N  
ANISOU 3431  N   TRP B 196    14291  15230  11844    931   1090     26       N  
ATOM   3432  CA  TRP B 196      77.268  59.539  34.243  1.00114.24           C  
ANISOU 3432  CA  TRP B 196    14854  15623  12929   1213   1364     -4       C  
ATOM   3433  C   TRP B 196      76.333  58.330  34.143  1.00115.00           C  
ANISOU 3433  C   TRP B 196    15084  15122  13488   1157   1350    -57       C  
ATOM   3434  O   TRP B 196      76.777  57.226  33.856  1.00123.20           O  
ANISOU 3434  O   TRP B 196    16171  15735  14904   1350   1526   -230       O  
ATOM   3435  CB  TRP B 196      78.116  59.490  35.539  1.00116.86           C  
ANISOU 3435  CB  TRP B 196    14834  16165  13402   1606   1392    372       C  
ATOM   3436  CG  TRP B 196      79.245  60.489  35.546  1.00113.29           C  
ANISOU 3436  CG  TRP B 196    14092  16266  12684   1655   1487    188       C  
ATOM   3437  CD1 TRP B 196      79.206  61.761  36.033  1.00110.41           C  
ANISOU 3437  CD1 TRP B 196    13590  16348  12011   1491   1373    319       C  
ATOM   3438  CD2 TRP B 196      80.555  60.309  35.005  1.00116.42           C  
ANISOU 3438  CD2 TRP B 196    14235  16806  13193   1804   1782   -306       C  
ATOM   3439  NE1 TRP B 196      80.412  62.385  35.834  1.00111.11           N  
ANISOU 3439  NE1 TRP B 196    13392  16805  12019   1469   1611    -22       N  
ATOM   3440  CE2 TRP B 196      81.259  61.516  35.205  1.00114.64           C  
ANISOU 3440  CE2 TRP B 196    13717  17119  12719   1638   1898   -447       C  
ATOM   3441  CE3 TRP B 196      81.206  59.244  34.367  1.00125.75           C  
ANISOU 3441  CE3 TRP B 196    15332  17706  14738   2040   1995   -767       C  
ATOM   3442  CZ2 TRP B 196      82.582  61.689  34.796  1.00120.48           C  
ANISOU 3442  CZ2 TRP B 196    14038  18168  13570   1619   2299  -1068       C  
ATOM   3443  CZ3 TRP B 196      82.533  59.415  33.965  1.00127.78           C  
ANISOU 3443  CZ3 TRP B 196    15132  18316  15100   2103   2346  -1424       C  
ATOM   3444  CH2 TRP B 196      83.200  60.629  34.176  1.00125.50           C  
ANISOU 3444  CH2 TRP B 196    14516  18606  14561   1850   2536  -1584       C  
ATOM   3445  N   ALA B 197      75.042  58.544  34.359  1.00112.13           N  
ANISOU 3445  N   ALA B 197    14718  14697  13186    874   1156    -30       N  
ATOM   3446  CA  ALA B 197      74.078  57.462  34.214  1.00117.64           C  
ANISOU 3446  CA  ALA B 197    15459  14830  14406    670   1225   -239       C  
ATOM   3447  C   ALA B 197      73.742  57.200  32.738  1.00122.24           C  
ANISOU 3447  C   ALA B 197    16235  15243  14968    552   1058   -936       C  
ATOM   3448  O   ALA B 197      73.518  56.040  32.344  1.00124.35           O  
ANISOU 3448  O   ALA B 197    16550  14967  15727    495   1211  -1257       O  
ATOM   3449  CB  ALA B 197      72.825  57.751  35.011  1.00117.37           C  
ANISOU 3449  CB  ALA B 197    15189  14861  14542    345   1172   -167       C  
ATOM   3450  N   VAL B 198      73.709  58.277  31.929  1.00119.08           N  
ANISOU 3450  N   VAL B 198    16036  15254  13955    516    720  -1169       N  
ATOM   3451  CA  VAL B 198      73.610  58.142  30.459  1.00122.34           C  
ANISOU 3451  CA  VAL B 198    16842  15607  14033    459    526  -1780       C  
ATOM   3452  C   VAL B 198      74.917  57.603  29.864  1.00128.82           C  
ANISOU 3452  C   VAL B 198    17830  16411  14703    572    993  -1934       C  
ATOM   3453  O   VAL B 198      74.904  56.693  29.036  1.00137.50           O  
ANISOU 3453  O   VAL B 198    19041  17232  15971    561   1088  -2483       O  
ATOM   3454  CB  VAL B 198      73.200  59.471  29.731  1.00117.64           C  
ANISOU 3454  CB  VAL B 198    16689  15347  12659    412    -38  -1894       C  
ATOM   3455  CG1 VAL B 198      72.086  60.175  30.467  1.00113.41           C  
ANISOU 3455  CG1 VAL B 198    15826  14897  12365    413   -528  -1821       C  
ATOM   3456  CG2 VAL B 198      74.392  60.402  29.534  1.00115.88           C  
ANISOU 3456  CG2 VAL B 198    16844  15455  11729    384    228  -1560       C  
ATOM   3457  N   ALA B 199      76.045  58.148  30.315  1.00128.15           N  
ANISOU 3457  N   ALA B 199    17652  16648  14392    679   1294  -1589       N  
ATOM   3458  CA  ALA B 199      77.343  57.773  29.769  1.00130.22           C  
ANISOU 3458  CA  ALA B 199    17897  17008  14572    766   1778  -1926       C  
ATOM   3459  C   ALA B 199      77.516  56.267  29.622  1.00132.24           C  
ANISOU 3459  C   ALA B 199    17953  16744  15547   1000   1961  -2319       C  
ATOM   3460  O   ALA B 199      78.347  55.831  28.855  1.00144.62           O  
ANISOU 3460  O   ALA B 199    19505  18357  17085   1049   2307  -2894       O  
ATOM   3461  CB  ALA B 199      78.480  58.370  30.594  1.00127.86           C  
ANISOU 3461  CB  ALA B 199    17232  17079  14268    918   2041  -1616       C  
ATOM   3462  N   TRP B 200      76.718  55.475  30.332  1.00127.74           N  
ANISOU 3462  N   TRP B 200    17255  15638  15642   1089   1783  -2073       N  
ATOM   3463  CA  TRP B 200      76.791  54.030  30.167  1.00139.15           C  
ANISOU 3463  CA  TRP B 200    18637  16391  17841   1273   1929  -2429       C  
ATOM   3464  C   TRP B 200      75.686  53.428  29.246  1.00149.34           C  
ANISOU 3464  C   TRP B 200    20102  17327  19312    967   1779  -3053       C  
ATOM   3465  O   TRP B 200      75.513  52.202  29.178  1.00159.87           O  
ANISOU 3465  O   TRP B 200    21387  17948  21406   1026   1889  -3367       O  
ATOM   3466  CB  TRP B 200      76.913  53.319  31.525  1.00140.00           C  
ANISOU 3466  CB  TRP B 200    18631  15944  18618   1581   1944  -1781       C  
ATOM   3467  CG  TRP B 200      75.762  52.503  31.907  1.00145.21           C  
ANISOU 3467  CG  TRP B 200    19439  15887  19847   1315   1934  -1634       C  
ATOM   3468  CD1 TRP B 200      74.625  52.936  32.510  1.00145.64           C  
ANISOU 3468  CD1 TRP B 200    19484  16019  19831    904   1869  -1296       C  
ATOM   3469  CD2 TRP B 200      75.624  51.081  31.752  1.00154.24           C  
ANISOU 3469  CD2 TRP B 200    20723  16063  21819   1368   2074  -1908       C  
ATOM   3470  NE1 TRP B 200      73.772  51.877  32.730  1.00154.34           N  
ANISOU 3470  NE1 TRP B 200    20690  16304  21645    596   2057  -1367       N  
ATOM   3471  CE2 TRP B 200      74.360  50.727  32.271  1.00158.34           C  
ANISOU 3471  CE2 TRP B 200    21349  16098  22712    867   2171  -1689       C  
ATOM   3472  CE3 TRP B 200      76.439  50.077  31.209  1.00160.28           C  
ANISOU 3472  CE3 TRP B 200    21494  16291  23115   1767   2154  -2420       C  
ATOM   3473  CZ2 TRP B 200      73.887  49.405  32.271  1.00166.79           C  
ANISOU 3473  CZ2 TRP B 200    22622  16092  24657    671   2395  -1881       C  
ATOM   3474  CZ3 TRP B 200      75.968  48.763  31.203  1.00170.46           C  
ANISOU 3474  CZ3 TRP B 200    22995  16478  25292   1688   2261  -2606       C  
ATOM   3475  CH2 TRP B 200      74.702  48.441  31.734  1.00173.01           C  
ANISOU 3475  CH2 TRP B 200    23512  16265  25957   1105   2404  -2294       C  
ATOM   3476  N   PHE B 201      74.995  54.296  28.499  1.00150.10           N  
ANISOU 3476  N   PHE B 201    20429  17881  18718    689   1465  -3301       N  
ATOM   3477  CA  PHE B 201      74.175  53.862  27.352  1.00152.47           C  
ANISOU 3477  CA  PHE B 201    20913  18048  18969    504   1201  -4126       C  
ATOM   3478  C   PHE B 201      74.739  54.392  26.052  1.00155.99           C  
ANISOU 3478  C   PHE B 201    21844  19019  18403    457   1207  -4610       C  
ATOM   3479  O   PHE B 201      74.533  53.807  25.002  1.00163.32           O  
ANISOU 3479  O   PHE B 201    22966  19875  19212    399   1140  -5410       O  
ATOM   3480  CB  PHE B 201      72.736  54.317  27.502  1.00152.80           C  
ANISOU 3480  CB  PHE B 201    20876  18123  19058    292    657  -4176       C  
ATOM   3481  CG  PHE B 201      72.083  53.839  28.758  1.00159.01           C  
ANISOU 3481  CG  PHE B 201    21226  18452  20739    147    820  -3781       C  
ATOM   3482  CD1 PHE B 201      71.697  52.508  28.895  1.00164.90           C  
ANISOU 3482  CD1 PHE B 201    21783  18433  22436    -17   1100  -4110       C  
ATOM   3483  CD2 PHE B 201      71.849  54.724  29.823  1.00156.24           C  
ANISOU 3483  CD2 PHE B 201    20713  18399  20251    108    762  -3100       C  
ATOM   3484  CE1 PHE B 201      71.098  52.067  30.063  1.00167.55           C  
ANISOU 3484  CE1 PHE B 201    21894  18287  23479   -295   1400  -3681       C  
ATOM   3485  CE2 PHE B 201      71.246  54.286  30.994  1.00154.42           C  
ANISOU 3485  CE2 PHE B 201    20176  17805  20690   -127   1041  -2751       C  
ATOM   3486  CZ  PHE B 201      70.869  52.959  31.115  1.00162.71           C  
ANISOU 3486  CZ  PHE B 201    21157  18072  22593   -370   1399  -2998       C  
ATOM   3487  N   LYS B 202      75.463  55.502  26.129  1.00155.40           N  
ANISOU 3487  N   LYS B 202    22014  19465  17563    423   1347  -4154       N  
ATOM   3488  CA  LYS B 202      76.165  56.033  24.963  1.00165.60           C  
ANISOU 3488  CA  LYS B 202    23900  21225  17794    229   1594  -4522       C  
ATOM   3489  C   LYS B 202      77.701  56.226  25.192  1.00166.38           C  
ANISOU 3489  C   LYS B 202    23764  21624  17828    212   2365  -4443       C  
ATOM   3490  O   LYS B 202      78.160  57.348  25.395  1.00172.33           O  
ANISOU 3490  O   LYS B 202    24729  22752  17997     21   2515  -3994       O  
ATOM   3491  CB  LYS B 202      75.499  57.349  24.494  1.00165.03           C  
ANISOU 3491  CB  LYS B 202    24584  21463  16654     52   1023  -4232       C  
ATOM   3492  CG  LYS B 202      76.245  58.094  23.376  1.00174.83           C  
ANISOU 3492  CG  LYS B 202    26737  23125  16563   -279   1365  -4374       C  
ATOM   3493  CD  LYS B 202      76.262  57.316  22.055  1.00185.49           C  
ANISOU 3493  CD  LYS B 202    28524  24552  17402   -385   1487  -5284       C  
ATOM   3494  CE  LYS B 202      77.363  56.261  22.018  1.00186.88           C  
ANISOU 3494  CE  LYS B 202    28052  24737  18217   -389   2381  -5889       C  
ATOM   3495  NZ  LYS B 202      77.330  55.454  20.763  1.00192.50           N  
ANISOU 3495  NZ  LYS B 202    29097  25534  18507   -483   2508  -6913       N  
ATOM   3496  N   ASN B 203      78.488  55.145  25.139  1.00164.99           N  
ANISOU 3496  N   ASN B 203    23101  21255  18330    419   2825  -4999       N  
ATOM   3497  CA  ASN B 203      77.997  53.794  24.941  1.00170.50           C  
ANISOU 3497  CA  ASN B 203    23571  21367  19843    633   2676  -5543       C  
ATOM   3498  C   ASN B 203      78.586  52.875  26.002  1.00170.27           C  
ANISOU 3498  C   ASN B 203    22881  20794  21017   1102   2820  -5365       C  
ATOM   3499  O   ASN B 203      79.811  52.834  26.199  1.00169.78           O  
ANISOU 3499  O   ASN B 203    22436  20925  21146   1338   3218  -5553       O  
ATOM   3500  CB  ASN B 203      78.365  53.292  23.524  1.00182.41           C  
ANISOU 3500  CB  ASN B 203    25345  23076  20884    463   3024  -6627       C  
ATOM   3501  CG  ASN B 203      77.722  51.937  23.173  1.00187.94           C  
ANISOU 3501  CG  ASN B 203    25853  23141  22414    630   2805  -7343       C  
ATOM   3502  OD1 ASN B 203      77.077  51.292  24.004  1.00187.70           O  
ANISOU 3502  OD1 ASN B 203    25501  22424  23391    823   2500  -7011       O  
ATOM   3503  ND2 ASN B 203      77.911  51.508  21.927  1.00193.68           N  
ANISOU 3503  ND2 ASN B 203    26819  24085  22683    484   3034  -8376       N  
ATOM   3504  N   GLY B 204      77.699  52.213  26.743  1.00171.36           N  
ANISOU 3504  N   GLY B 204    22922  20249  21935   1227   2470  -4988       N  
ATOM   3505  CA  GLY B 204      78.043  51.030  27.532  1.00178.85           C  
ANISOU 3505  CA  GLY B 204    23555  20382  24016   1665   2520  -4889       C  
ATOM   3506  C   GLY B 204      79.030  51.214  28.674  1.00180.22           C  
ANISOU 3506  C   GLY B 204    23440  20587  24447   2132   2552  -4267       C  
ATOM   3507  O   GLY B 204      79.123  50.357  29.550  1.00185.25           O  
ANISOU 3507  O   GLY B 204    24041  20461  25884   2539   2405  -3894       O  
ATOM   3508  N   GLU B 205      79.771  52.320  28.675  1.00178.54           N  
ANISOU 3508  N   GLU B 205    23083  21205  23547   2076   2712  -4174       N  
ATOM   3509  CA  GLU B 205      80.872  52.473  29.628  1.00176.80           C  
ANISOU 3509  CA  GLU B 205    22432  21127  23616   2583   2706  -3889       C  
ATOM   3510  C   GLU B 205      80.924  53.784  30.405  1.00158.44           C  
ANISOU 3510  C   GLU B 205    20067  19443  20687   2431   2614  -3174       C  
ATOM   3511  O   GLU B 205      81.011  54.869  29.819  1.00149.49           O  
ANISOU 3511  O   GLU B 205    19039  18978  18780   1965   2850  -3307       O  
ATOM   3512  CB  GLU B 205      82.224  52.154  28.970  1.00195.63           C  
ANISOU 3512  CB  GLU B 205    24303  23772  26256   2867   3088  -4921       C  
ATOM   3513  CG  GLU B 205      82.730  50.750  29.281  1.00210.45           C  
ANISOU 3513  CG  GLU B 205    25896  24795  29269   3628   2864  -5297       C  
ATOM   3514  CD  GLU B 205      82.588  50.401  30.759  1.00218.61           C  
ANISOU 3514  CD  GLU B 205    27084  25194  30784   4193   2292  -4274       C  
ATOM   3515  OE1 GLU B 205      81.445  50.179  31.222  1.00220.98           O  
ANISOU 3515  OE1 GLU B 205    27944  24953  31062   3927   2108  -3486       O  
ATOM   3516  OE2 GLU B 205      83.615  50.368  31.463  1.00226.44           O  
ANISOU 3516  OE2 GLU B 205    27646  26259  32128   4881   2032  -4313       O  
ATOM   3517  N   THR B 206      80.870  53.662  31.733  1.00152.17           N  
ANISOU 3517  N   THR B 206    19216  18384  20215   2817   2269  -2414       N  
ATOM   3518  CA  THR B 206      81.005  54.810  32.646  1.00146.03           C  
ANISOU 3518  CA  THR B 206    18308  18199  18975   2781   2135  -1810       C  
ATOM   3519  C   THR B 206      81.955  54.479  33.778  1.00151.49           C  
ANISOU 3519  C   THR B 206    18651  18812  20094   3527   1840  -1590       C  
ATOM   3520  O   THR B 206      82.219  53.307  34.046  1.00161.09           O  
ANISOU 3520  O   THR B 206    19930  19316  21959   4092   1616  -1624       O  
ATOM   3521  CB  THR B 206      79.651  55.248  33.260  1.00137.14           C  
ANISOU 3521  CB  THR B 206    17562  16995  17549   2405   1918  -1045       C  
ATOM   3522  OG1 THR B 206      79.854  56.412  34.063  1.00126.42           O  
ANISOU 3522  OG1 THR B 206    16021  16258  15751   2378   1807   -624       O  
ATOM   3523  CG2 THR B 206      79.064  54.146  34.147  1.00138.62           C  
ANISOU 3523  CG2 THR B 206    18026  16369  18275   2634   1739   -507       C  
ATOM   3524  N   SER B 207      82.462  55.517  34.448  1.00139.03           N  
ANISOU 3524  N   SER B 207    18658  18972  15193    975   2551  -3785       N  
ATOM   3525  CA  SER B 207      83.385  55.331  35.569  1.00138.43           C  
ANISOU 3525  CA  SER B 207    17956  18808  15832   1461   2593  -3826       C  
ATOM   3526  C   SER B 207      82.625  55.174  36.883  1.00129.64           C  
ANISOU 3526  C   SER B 207    16761  17447  15050   1595   1983  -3427       C  
ATOM   3527  O   SER B 207      81.799  56.009  37.234  1.00129.88           O  
ANISOU 3527  O   SER B 207    16767  17620  14960   1310   1658  -2999       O  
ATOM   3528  CB  SER B 207      84.405  56.490  35.645  1.00139.29           C  
ANISOU 3528  CB  SER B 207    17490  19313  16120   1443   2972  -3796       C  
ATOM   3529  OG  SER B 207      84.144  57.366  36.729  1.00128.88           O  
ANISOU 3529  OG  SER B 207    15802  18099  15066   1443   2563  -3323       O  
ATOM   3530  N   LEU B 208      82.896  54.089  37.592  1.00128.55           N  
ANISOU 3530  N   LEU B 208    16651  16887  15302   2034   1862  -3585       N  
ATOM   3531  CA  LEU B 208      82.284  53.871  38.883  1.00122.60           C  
ANISOU 3531  CA  LEU B 208    15961  15822  14798   2152   1396  -3222       C  
ATOM   3532  C   LEU B 208      82.706  54.863  39.980  1.00115.56           C  
ANISOU 3532  C   LEU B 208    14546  15164  14198   2323   1189  -2883       C  
ATOM   3533  O   LEU B 208      81.860  55.389  40.669  1.00112.47           O  
ANISOU 3533  O   LEU B 208    14195  14777  13759   2084    901  -2482       O  
ATOM   3534  CB  LEU B 208      82.490  52.449  39.355  1.00128.78           C  
ANISOU 3534  CB  LEU B 208    17107  15990  15833   2593   1322  -3438       C  
ATOM   3535  CG  LEU B 208      81.320  52.014  40.212  1.00129.62           C  
ANISOU 3535  CG  LEU B 208    17672  15662  15915   2376    998  -3106       C  
ATOM   3536  CD1 LEU B 208      80.224  51.454  39.316  1.00136.82           C  
ANISOU 3536  CD1 LEU B 208    19049  16421  16515   1846   1073  -3290       C  
ATOM   3537  CD2 LEU B 208      81.751  50.996  41.245  1.00135.05           C  
ANISOU 3537  CD2 LEU B 208    18706  15714  16891   2934    831  -3094       C  
ATOM   3538  N   PRO B 209      84.019  55.122  40.144  1.00119.40           N  
ANISOU 3538  N   PRO B 209    14494  15847  15024   2724   1345  -3115       N  
ATOM   3539  CA  PRO B 209      84.341  56.032  41.240  1.00117.80           C  
ANISOU 3539  CA  PRO B 209    13831  15841  15087   2851   1069  -2831       C  
ATOM   3540  C   PRO B 209      83.647  57.398  41.101  1.00114.52           C  
ANISOU 3540  C   PRO B 209    13312  15795  14404   2287   1082  -2449       C  
ATOM   3541  O   PRO B 209      83.343  58.031  42.105  1.00112.46           O  
ANISOU 3541  O   PRO B 209    12923  15561  14244   2265    774  -2110       O  
ATOM   3542  CB  PRO B 209      85.877  56.191  41.139  1.00118.78           C  
ANISOU 3542  CB  PRO B 209    13260  16217  15653   3260   1304  -3289       C  
ATOM   3543  CG  PRO B 209      86.332  55.012  40.370  1.00125.06           C  
ANISOU 3543  CG  PRO B 209    14234  16765  16515   3559   1590  -3788       C  
ATOM   3544  CD  PRO B 209      85.225  54.709  39.404  1.00126.37           C  
ANISOU 3544  CD  PRO B 209    15082  16818  16114   3038   1780  -3685       C  
ATOM   3545  N   LEU B 210      83.398  57.845  39.875  1.00116.16           N  
ANISOU 3545  N   LEU B 210    13655  16240  14238   1866   1417  -2509       N  
ATOM   3546  CA  LEU B 210      82.887  59.199  39.684  1.00114.49           C  
ANISOU 3546  CA  LEU B 210    13389  16327  13782   1429   1407  -2161       C  
ATOM   3547  C   LEU B 210      81.374  59.246  39.677  1.00111.53           C  
ANISOU 3547  C   LEU B 210    13429  15827  13119   1125   1041  -1840       C  
ATOM   3548  O   LEU B 210      80.775  60.250  40.070  1.00108.62           O  
ANISOU 3548  O   LEU B 210    12959  15581  12728    925    831  -1494       O  
ATOM   3549  CB  LEU B 210      83.489  59.860  38.437  1.00116.50           C  
ANISOU 3549  CB  LEU B 210    13649  16876  13738   1142   1949  -2347       C  
ATOM   3550  CG  LEU B 210      84.975  60.217  38.560  1.00116.62           C  
ANISOU 3550  CG  LEU B 210    13032  17108  14169   1305   2394  -2685       C  
ATOM   3551  CD1 LEU B 210      85.316  61.411  37.691  1.00114.86           C  
ANISOU 3551  CD1 LEU B 210    12845  17156  13641    824   2927  -2651       C  
ATOM   3552  CD2 LEU B 210      85.341  60.494  40.019  1.00116.19           C  
ANISOU 3552  CD2 LEU B 210    12427  17055  14664   1628   1993  -2566       C  
ATOM   3553  N   LEU B 211      80.759  58.139  39.275  1.00109.99           N  
ANISOU 3553  N   LEU B 211    13647  15367  12776   1102    963  -2015       N  
ATOM   3554  CA  LEU B 211      79.352  57.910  39.540  1.00106.44           C  
ANISOU 3554  CA  LEU B 211    13445  14733  12261    855    600  -1839       C  
ATOM   3555  C   LEU B 211      79.042  57.912  41.045  1.00103.67           C  
ANISOU 3555  C   LEU B 211    12941  14173  12274    977    378  -1578       C  
ATOM   3556  O   LEU B 211      78.132  58.618  41.491  1.00103.98           O  
ANISOU 3556  O   LEU B 211    12875  14284  12348    740    169  -1318       O  
ATOM   3557  CB  LEU B 211      78.913  56.599  38.931  1.00110.90           C  
ANISOU 3557  CB  LEU B 211    14451  14994  12688    792    618  -2170       C  
ATOM   3558  CG  LEU B 211      77.414  56.357  38.935  1.00115.42           C  
ANISOU 3558  CG  LEU B 211    15212  15427  13215    420    293  -2136       C  
ATOM   3559  CD1 LEU B 211      76.675  57.538  38.312  1.00112.84           C  
ANISOU 3559  CD1 LEU B 211    14774  15474  12623    139     23  -1960       C  
ATOM   3560  CD2 LEU B 211      77.106  55.065  38.192  1.00123.12           C  
ANISOU 3560  CD2 LEU B 211    16632  16104  14042    307    353  -2554       C  
ATOM   3561  N   LEU B 212      79.791  57.102  41.812  1.00103.73           N  
ANISOU 3561  N   LEU B 212    12993  13891  12527   1374    416  -1672       N  
ATOM   3562  CA  LEU B 212      79.708  57.089  43.292  1.00 97.72           C  
ANISOU 3562  CA  LEU B 212    12243  12892  11993   1553    214  -1419       C  
ATOM   3563  C   LEU B 212      80.011  58.416  43.927  1.00 99.07           C  
ANISOU 3563  C   LEU B 212    11974  13400  12266   1558    117  -1168       C  
ATOM   3564  O   LEU B 212      79.250  58.889  44.752  1.00102.91           O  
ANISOU 3564  O   LEU B 212    12484  13835  12781   1377    -17   -907       O  
ATOM   3565  CB  LEU B 212      80.618  56.038  43.875  1.00 94.20           C  
ANISOU 3565  CB  LEU B 212    12009  12065  11718   2092    172  -1574       C  
ATOM   3566  CG  LEU B 212      79.794  54.849  44.262  1.00 96.17           C  
ANISOU 3566  CG  LEU B 212    12914  11716  11907   2003    155  -1558       C  
ATOM   3567  CD1 LEU B 212      80.658  53.678  44.684  1.00100.03           C  
ANISOU 3567  CD1 LEU B 212    13790  11701  12513   2599     81  -1717       C  
ATOM   3568  CD2 LEU B 212      78.874  55.286  45.380  1.00 95.26           C  
ANISOU 3568  CD2 LEU B 212    12935  11479  11777   1722     53  -1205       C  
HETATM 3569  N   MSE B 213      81.131  59.018  43.532  1.00104.92           N  
ANISOU 3569  N   MSE B 213    12306  14469  13087   1725    250  -1304       N  
HETATM 3570  CA  MSE B 213      81.522  60.353  43.985  1.00103.96           C  
ANISOU 3570  CA  MSE B 213    11746  14671  13081   1663    216  -1135       C  
HETATM 3571  C   MSE B 213      80.363  61.296  44.055  1.00 98.69           C  
ANISOU 3571  C   MSE B 213    11127  14094  12275   1257    124   -816       C  
HETATM 3572  O   MSE B 213      80.173  61.987  45.061  1.00 91.04           O  
ANISOU 3572  O   MSE B 213    10026  13135  11428   1244    -28   -604       O  
HETATM 3573  CB  MSE B 213      82.538  60.946  43.022  1.00109.80           C  
ANISOU 3573  CB  MSE B 213    12121  15758  13839   1616    562  -1372       C  
HETATM 3574  CG  MSE B 213      83.341  61.981  43.797  1.00117.03           C  
ANISOU 3574  CG  MSE B 213    12521  16901  15043   1686    518  -1343       C  
HETATM 3575 SE   MSE B 213      84.149  63.368  42.647  1.00123.13          SE  
ANISOU 3575 SE   MSE B 213    12925  18089  15769   1261   1095  -1478      SE  
HETATM 3576  CE  MSE B 213      83.105  63.131  40.995  1.00129.59           C  
ANISOU 3576  CE  MSE B 213    14454  18850  15934    881   1323  -1364       C  
ATOM   3577  N   TYR B 214      79.573  61.336  42.986  1.00103.84           N  
ANISOU 3577  N   TYR B 214    11977  14803  12671    958    178   -818       N  
ATOM   3578  CA  TYR B 214      78.457  62.280  42.894  1.00100.79           C  
ANISOU 3578  CA  TYR B 214    11582  14513  12198    651     11   -573       C  
ATOM   3579  C   TYR B 214      77.232  61.963  43.752  1.00 94.86           C  
ANISOU 3579  C   TYR B 214    10908  13531  11601    531   -185   -476       C  
ATOM   3580  O   TYR B 214      76.564  62.876  44.201  1.00 96.14           O  
ANISOU 3580  O   TYR B 214    10897  13760  11870    397   -302   -294       O  
ATOM   3581  CB  TYR B 214      78.074  62.553  41.442  1.00101.14           C  
ANISOU 3581  CB  TYR B 214    11838  14708  11879    435     19   -622       C  
ATOM   3582  CG  TYR B 214      78.825  63.719  40.887  1.00101.77           C  
ANISOU 3582  CG  TYR B 214    11851  15020  11796    365    227   -515       C  
ATOM   3583  CD1 TYR B 214      78.522  65.013  41.294  1.00103.88           C  
ANISOU 3583  CD1 TYR B 214    11975  15353  12141    269    108   -228       C  
ATOM   3584  CD2 TYR B 214      79.882  63.537  40.003  1.00101.74           C  
ANISOU 3584  CD2 TYR B 214    11940  15126  11591    367    626   -735       C  
ATOM   3585  CE1 TYR B 214      79.233  66.099  40.815  1.00105.82           C  
ANISOU 3585  CE1 TYR B 214    12244  15723  12238    144    369   -126       C  
ATOM   3586  CE2 TYR B 214      80.604  64.617  39.522  1.00103.50           C  
ANISOU 3586  CE2 TYR B 214    12143  15511  11672    204    955   -664       C  
ATOM   3587  CZ  TYR B 214      80.280  65.893  39.941  1.00104.88           C  
ANISOU 3587  CZ  TYR B 214    12239  15703  11906     80    819   -341       C  
ATOM   3588  OH  TYR B 214      80.977  66.971  39.470  1.00112.05           O  
ANISOU 3588  OH  TYR B 214    13220  16687  12668   -142   1198   -265       O  
ATOM   3589  N   VAL B 215      76.950  60.673  43.972  1.00 92.87           N  
ANISOU 3589  N   VAL B 215    10934  12969  11382    554   -157   -634       N  
ATOM   3590  CA  VAL B 215      75.943  60.232  44.978  1.00 89.83           C  
ANISOU 3590  CA  VAL B 215    10686  12278  11166    385   -173   -583       C  
ATOM   3591  C   VAL B 215      76.330  60.771  46.360  1.00 90.05           C  
ANISOU 3591  C   VAL B 215    10659  12248  11305    543   -166   -361       C  
ATOM   3592  O   VAL B 215      75.520  61.361  47.064  1.00 94.26           O  
ANISOU 3592  O   VAL B 215    11090  12765  11957    342   -154   -245       O  
ATOM   3593  CB  VAL B 215      75.813  58.662  45.005  1.00 89.80           C  
ANISOU 3593  CB  VAL B 215    11144  11834  11139    382    -52   -789       C  
ATOM   3594  CG1 VAL B 215      75.076  58.148  46.256  1.00 81.66           C  
ANISOU 3594  CG1 VAL B 215    10414  10379  10232    206     84   -710       C  
ATOM   3595  CG2 VAL B 215      75.149  58.161  43.734  1.00 87.07           C  
ANISOU 3595  CG2 VAL B 215    10857  11529  10695    121    -93  -1066       C  
HETATM 3596  N   MSE B 216      77.587  60.589  46.718  1.00 94.93           N  
ANISOU 3596  N   MSE B 216    11316  12853  11899    923   -192   -361       N  
HETATM 3597  CA  MSE B 216      78.106  61.124  47.950  1.00 94.08           C  
ANISOU 3597  CA  MSE B 216    11167  12732  11844   1120   -293   -205       C  
HETATM 3598  C   MSE B 216      78.061  62.648  47.948  1.00 85.20           C  
ANISOU 3598  C   MSE B 216     9599  11967  10802    967   -319    -81       C  
HETATM 3599  O   MSE B 216      77.845  63.247  48.983  1.00 82.58           O  
ANISOU 3599  O   MSE B 216     9267  11597  10510    931   -360     52       O  
HETATM 3600  CB  MSE B 216      79.521  60.590  48.151  1.00103.41           C  
ANISOU 3600  CB  MSE B 216    12368  13872  13052   1620   -430   -338       C  
HETATM 3601  CG  MSE B 216      79.547  59.051  48.123  1.00113.20           C  
ANISOU 3601  CG  MSE B 216    14143  14653  14213   1834   -421   -455       C  
HETATM 3602 SE   MSE B 216      81.419  58.375  48.138  1.00123.34          SE  
ANISOU 3602 SE   MSE B 216    15287  15911  15664   2621   -672   -751      SE  
HETATM 3603  CE  MSE B 216      81.112  56.429  48.145  1.00112.36           C  
ANISOU 3603  CE  MSE B 216    14797  13753  14139   2859   -647   -832       C  
ATOM   3604  N   TYR B 217      78.248  63.275  46.783  1.00 78.79           N  
ANISOU 3604  N   TYR B 217     8512  11452   9971    862   -266   -126       N  
ATOM   3605  CA  TYR B 217      78.227  64.745  46.691  1.00 80.30           C  
ANISOU 3605  CA  TYR B 217     8402  11890  10216    713   -269     13       C  
ATOM   3606  C   TYR B 217      76.872  65.274  47.088  1.00 88.60           C  
ANISOU 3606  C   TYR B 217     9455  12860  11349    485   -334    149       C  
ATOM   3607  O   TYR B 217      76.778  66.293  47.792  1.00 98.03           O  
ANISOU 3607  O   TYR B 217    10494  14093  12658    445   -350    267       O  
ATOM   3608  CB  TYR B 217      78.514  65.198  45.269  1.00 83.16           C  
ANISOU 3608  CB  TYR B 217     8701  12469  10425    601   -159    -25       C  
ATOM   3609  CG  TYR B 217      79.945  65.602  44.966  1.00 84.35           C  
ANISOU 3609  CG  TYR B 217     8621  12815  10611    688     48   -152       C  
ATOM   3610  CD1 TYR B 217      81.009  65.111  45.709  1.00 85.97           C  
ANISOU 3610  CD1 TYR B 217     8620  13021  11021    977     32   -342       C  
ATOM   3611  CD2 TYR B 217      80.223  66.444  43.896  1.00 87.02           C  
ANISOU 3611  CD2 TYR B 217     8971  13312  10778    476    268   -121       C  
ATOM   3612  CE1 TYR B 217      82.315  65.469  45.411  1.00 96.25           C  
ANISOU 3612  CE1 TYR B 217     9551  14537  12480   1032    244   -580       C  
ATOM   3613  CE2 TYR B 217      81.515  66.808  43.574  1.00 94.79           C  
ANISOU 3613  CE2 TYR B 217     9712  14463  11841    448    602   -310       C  
ATOM   3614  CZ  TYR B 217      82.573  66.321  44.328  1.00100.88           C  
ANISOU 3614  CZ  TYR B 217    10093  15293  12941    715    603   -585       C  
ATOM   3615  OH  TYR B 217      83.898  66.680  43.998  1.00100.74           O  
ANISOU 3615  OH  TYR B 217     9665  15480  13132    665    967   -899       O  
ATOM   3616  N   LEU B 218      75.817  64.591  46.588  1.00 90.16           N  
ANISOU 3616  N   LEU B 218     9776  12946  11532    325   -364     64       N  
ATOM   3617  CA  LEU B 218      74.376  64.861  46.918  1.00 80.34           C  
ANISOU 3617  CA  LEU B 218     8416  11617  10490     95   -406     50       C  
ATOM   3618  C   LEU B 218      74.070  64.727  48.407  1.00 77.49           C  
ANISOU 3618  C   LEU B 218     8153  11029  10260     36   -220     79       C  
ATOM   3619  O   LEU B 218      73.558  65.659  49.004  1.00 74.32           O  
ANISOU 3619  O   LEU B 218     7552  10657  10029    -39   -188    132       O  
ATOM   3620  CB  LEU B 218      73.464  63.900  46.152  1.00 81.26           C  
ANISOU 3620  CB  LEU B 218     8602  11649  10621    -86   -465   -170       C  
ATOM   3621  CG  LEU B 218      72.151  64.349  45.505  1.00 84.72           C  
ANISOU 3621  CG  LEU B 218     8747  12192  11249   -260   -714   -306       C  
ATOM   3622  CD1 LEU B 218      71.067  63.381  45.910  1.00 84.31           C  
ANISOU 3622  CD1 LEU B 218     8641  11922  11471   -555   -571   -594       C  
ATOM   3623  CD2 LEU B 218      71.741  65.788  45.818  1.00 83.12           C  
ANISOU 3623  CD2 LEU B 218     8228  12105  11249   -196   -845   -165       C  
ATOM   3624  N   CYS B 219      74.372  63.562  49.005  1.00 73.83           N  
ANISOU 3624  N   CYS B 219     8087  10288   9675     81    -82     39       N  
ATOM   3625  CA  CYS B 219      74.318  63.425  50.476  1.00 76.30           C  
ANISOU 3625  CA  CYS B 219     8724  10331   9936     64     96    117       C  
ATOM   3626  C   CYS B 219      74.919  64.674  51.165  1.00 77.31           C  
ANISOU 3626  C   CYS B 219     8670  10644  10057    214     -5    253       C  
ATOM   3627  O   CYS B 219      74.250  65.391  51.913  1.00 80.07           O  
ANISOU 3627  O   CYS B 219     8947  10961  10513     46    140    266       O  
ATOM   3628  CB  CYS B 219      75.087  62.198  50.926  1.00 78.97           C  
ANISOU 3628  CB  CYS B 219     9636  10345  10022    294     94    141       C  
ATOM   3629  SG  CYS B 219      74.379  60.629  50.415  1.00 93.11           S  
ANISOU 3629  SG  CYS B 219    11828  11745  11802     64    306    -32       S  
ATOM   3630  N   ASN B 220      76.169  64.941  50.859  1.00 72.68           N  
ANISOU 3630  N   ASN B 220     7966  10255   9393    499   -217    287       N  
ATOM   3631  CA  ASN B 220      76.892  65.982  51.495  1.00 75.60           C  
ANISOU 3631  CA  ASN B 220     8170  10779   9776    616   -327    342       C  
ATOM   3632  C   ASN B 220      76.321  67.362  51.180  1.00 71.66           C  
ANISOU 3632  C   ASN B 220     7294  10457   9474    416   -276    391       C  
ATOM   3633  O   ASN B 220      76.379  68.257  51.999  1.00 75.63           O  
ANISOU 3633  O   ASN B 220     7748  10965  10022    390   -265    418       O  
ATOM   3634  CB  ASN B 220      78.408  65.862  51.141  1.00 83.22           C  
ANISOU 3634  CB  ASN B 220     8972  11925  10720    931   -528    253       C  
ATOM   3635  CG  ASN B 220      79.157  67.166  51.303  1.00 80.65           C  
ANISOU 3635  CG  ASN B 220     8264  11853  10527    924   -598    225       C  
ATOM   3636  OD1 ASN B 220      79.637  67.475  52.374  1.00 74.13           O  
ANISOU 3636  OD1 ASN B 220     7495  11002   9667   1043   -759    188       O  
ATOM   3637  ND2 ASN B 220      79.228  67.956  50.222  1.00 83.29           N  
ANISOU 3637  ND2 ASN B 220     8282  12391  10972    754   -472    236       N  
ATOM   3638  N   SER B 221      75.734  67.527  50.013  1.00 78.25           N  
ANISOU 3638  N   SER B 221     7934  11394  10402    303   -283    390       N  
ATOM   3639  CA  SER B 221      75.208  68.849  49.651  1.00 84.07           C  
ANISOU 3639  CA  SER B 221     8409  12227  11307    207   -322    461       C  
ATOM   3640  C   SER B 221      74.008  69.247  50.498  1.00 83.58           C  
ANISOU 3640  C   SER B 221     8268  12017  11470     77   -210    408       C  
ATOM   3641  O   SER B 221      73.687  70.446  50.591  1.00 83.06           O  
ANISOU 3641  O   SER B 221     8014  11961  11584     72   -236    446       O  
ATOM   3642  CB  SER B 221      74.887  68.953  48.155  1.00 85.96           C  
ANISOU 3642  CB  SER B 221     8581  12577  11499    184   -463    486       C  
ATOM   3643  OG  SER B 221      73.743  68.208  47.823  1.00 87.74           O  
ANISOU 3643  OG  SER B 221     8789  12734  11813     92   -530    357       O  
ATOM   3644  N   VAL B 222      73.361  68.245  51.126  1.00 76.33           N  
ANISOU 3644  N   VAL B 222     7526  10918  10558    -45    -23    292       N  
ATOM   3645  CA  VAL B 222      72.313  68.496  52.112  1.00 72.89           C  
ANISOU 3645  CA  VAL B 222     7047  10317  10330   -234    253    167       C  
ATOM   3646  C   VAL B 222      72.936  68.931  53.424  1.00 76.74           C  
ANISOU 3646  C   VAL B 222     7825  10709  10623   -191    382    230       C  
ATOM   3647  O   VAL B 222      72.623  70.016  53.944  1.00 75.12           O  
ANISOU 3647  O   VAL B 222     7457  10501  10581   -223    471    188       O  
ATOM   3648  CB  VAL B 222      71.398  67.265  52.338  1.00 72.50           C  
ANISOU 3648  CB  VAL B 222     7151  10054  10342   -496    543    -18       C  
ATOM   3649  CG1 VAL B 222      70.410  67.541  53.450  1.00 70.07           C  
ANISOU 3649  CG1 VAL B 222     6819   9562  10243   -757    987   -201       C  
ATOM   3650  CG2 VAL B 222      70.638  66.920  51.076  1.00 70.98           C  
ANISOU 3650  CG2 VAL B 222     6595   9975  10397   -571    354   -179       C  
ATOM   3651  N   TYR B 223      73.847  68.110  53.955  1.00 82.57           N  
ANISOU 3651  N   TYR B 223     9019  11351  11002    -72    334    307       N  
ATOM   3652  CA  TYR B 223      74.642  68.537  55.114  1.00 81.58           C  
ANISOU 3652  CA  TYR B 223     9198  11177  10621     47    272    347       C  
ATOM   3653  C   TYR B 223      75.182  69.933  54.920  1.00 75.19           C  
ANISOU 3653  C   TYR B 223     7994  10592   9981    117     97    352       C  
ATOM   3654  O   TYR B 223      75.207  70.725  55.845  1.00 78.45           O  
ANISOU 3654  O   TYR B 223     8498  10953  10356     73    162    298       O  
ATOM   3655  CB  TYR B 223      75.806  67.609  55.395  1.00 81.86           C  
ANISOU 3655  CB  TYR B 223     9642  11150  10311    329      0    409       C  
ATOM   3656  CG  TYR B 223      76.396  67.878  56.757  1.00 95.10           C  
ANISOU 3656  CG  TYR B 223    11758  12718  11658    454   -129    405       C  
ATOM   3657  CD1 TYR B 223      75.757  67.414  57.900  1.00 99.03           C  
ANISOU 3657  CD1 TYR B 223    12948  12862  11814    306    155    426       C  
ATOM   3658  CD2 TYR B 223      77.554  68.681  56.916  1.00101.44           C  
ANISOU 3658  CD2 TYR B 223    12299  13762  12482    665   -506    336       C  
ATOM   3659  CE1 TYR B 223      76.253  67.682  59.160  1.00111.94           C  
ANISOU 3659  CE1 TYR B 223    15119  14376  13033    421      2    419       C  
ATOM   3660  CE2 TYR B 223      78.057  68.966  58.180  1.00104.79           C  
ANISOU 3660  CE2 TYR B 223    13128  14102  12585    780   -715    274       C  
ATOM   3661  CZ  TYR B 223      77.392  68.459  59.308  1.00115.52           C  
ANISOU 3661  CZ  TYR B 223    15287  15099  13504    682   -490    335       C  
ATOM   3662  OH  TYR B 223      77.858  68.693  60.599  1.00124.85           O  
ANISOU 3662  OH  TYR B 223    17047  16160  14226    805   -729    279       O  
ATOM   3663  N   GLY B 224      75.638  70.215  53.715  1.00 70.03           N  
ANISOU 3663  N   GLY B 224     6985  10147   9474    193    -83    403       N  
ATOM   3664  CA  GLY B 224      76.154  71.518  53.382  1.00 75.88           C  
ANISOU 3664  CA  GLY B 224     7434  11028  10369    190   -170    423       C  
ATOM   3665  C   GLY B 224      75.161  72.605  53.685  1.00 79.11           C  
ANISOU 3665  C   GLY B 224     7722  11319  11016     68    -17    400       C  
ATOM   3666  O   GLY B 224      75.462  73.541  54.465  1.00 77.27           O  
ANISOU 3666  O   GLY B 224     7514  11036  10809     34     17    339       O  
ATOM   3667  N   TYR B 225      73.976  72.489  53.068  1.00 77.61           N  
ANISOU 3667  N   TYR B 225     7370  11079  11039     23     42    392       N  
ATOM   3668  CA  TYR B 225      72.909  73.437  53.289  1.00 76.74           C  
ANISOU 3668  CA  TYR B 225     7050  10842  11263    -10    152    300       C  
ATOM   3669  C   TYR B 225      72.728  73.603  54.791  1.00 77.29           C  
ANISOU 3669  C   TYR B 225     7319  10765  11283   -120    456    145       C  
ATOM   3670  O   TYR B 225      72.811  74.717  55.310  1.00 78.55           O  
ANISOU 3670  O   TYR B 225     7457  10841  11546   -114    513     90       O  
ATOM   3671  CB  TYR B 225      71.567  72.982  52.609  1.00 78.51           C  
ANISOU 3671  CB  TYR B 225     6992  11053  11783    -25    131    181       C  
ATOM   3672  CG  TYR B 225      70.643  74.150  52.266  1.00 80.99           C  
ANISOU 3672  CG  TYR B 225     6963  11282  12527    107     10    100       C  
ATOM   3673  CD1 TYR B 225      70.379  75.145  53.205  1.00 86.80           C  
ANISOU 3673  CD1 TYR B 225     7647  11855  13477    114    227    -20       C  
ATOM   3674  CD2 TYR B 225      70.081  74.283  50.998  1.00 86.32           C  
ANISOU 3674  CD2 TYR B 225     7430  12007  13361    276   -377    135       C  
ATOM   3675  CE1 TYR B 225      69.588  76.238  52.902  1.00 92.92           C  
ANISOU 3675  CE1 TYR B 225     8131  12491  14682    319     83   -108       C  
ATOM   3676  CE2 TYR B 225      69.277  75.385  50.675  1.00 89.58           C  
ANISOU 3676  CE2 TYR B 225     7591  12286  14159    514   -612     72       C  
ATOM   3677  CZ  TYR B 225      69.038  76.364  51.641  1.00 94.91           C  
ANISOU 3677  CZ  TYR B 225     8178  12770  15111    551   -368    -50       C  
ATOM   3678  OH  TYR B 225      68.257  77.484  51.366  1.00 99.85           O  
ANISOU 3678  OH  TYR B 225     8571  13198  16169    859   -614   -135       O  
ATOM   3679  N   ILE B 226      72.521  72.483  55.491  1.00 73.74           N  
ANISOU 3679  N   ILE B 226     7169  10235  10614   -236    674     75       N  
ATOM   3680  CA  ILE B 226      72.253  72.517  56.924  1.00 75.82           C  
ANISOU 3680  CA  ILE B 226     7798  10306  10701   -383   1034    -68       C  
ATOM   3681  C   ILE B 226      73.335  73.307  57.642  1.00 82.81           C  
ANISOU 3681  C   ILE B 226     8916  11218  11329   -291    853    -40       C  
ATOM   3682  O   ILE B 226      73.047  74.199  58.455  1.00 85.30           O  
ANISOU 3682  O   ILE B 226     9294  11418  11696   -370   1062   -195       O  
ATOM   3683  CB  ILE B 226      72.205  71.106  57.518  1.00 73.27           C  
ANISOU 3683  CB  ILE B 226     8018   9822   9996   -508   1245    -55       C  
ATOM   3684  CG1 ILE B 226      70.943  70.378  57.059  1.00 75.05           C  
ANISOU 3684  CG1 ILE B 226     8007   9962  10544   -739   1576   -209       C  
ATOM   3685  CG2 ILE B 226      72.244  71.179  59.031  1.00 71.48           C  
ANISOU 3685  CG2 ILE B 226     8418   9372   9368   -631   1551   -139       C  
ATOM   3686  CD1 ILE B 226      70.905  68.912  57.434  1.00 78.24           C  
ANISOU 3686  CD1 ILE B 226     9003  10131  10594   -909   1814   -173       C  
ATOM   3687  N   ASN B 227      74.592  72.992  57.323  1.00 86.52           N  
ANISOU 3687  N   ASN B 227     9461  11844  11569   -127    464     90       N  
ATOM   3688  CA  ASN B 227      75.693  73.509  58.083  1.00 80.60           C  
ANISOU 3688  CA  ASN B 227     8898  11141  10581    -51    228     27       C  
ATOM   3689  C   ASN B 227      75.957  74.965  57.812  1.00 76.30           C  
ANISOU 3689  C   ASN B 227     7995  10649  10343   -104    183    -38       C  
ATOM   3690  O   ASN B 227      76.323  75.717  58.712  1.00 74.26           O  
ANISOU 3690  O   ASN B 227     7893  10334   9986   -159    164   -197       O  
ATOM   3691  CB  ASN B 227      76.940  72.692  57.870  1.00 81.67           C  
ANISOU 3691  CB  ASN B 227     9110  11431  10488    166   -178     81       C  
ATOM   3692  CG  ASN B 227      77.920  72.870  58.988  1.00 91.10           C  
ANISOU 3692  CG  ASN B 227    10612  12639  11362    286   -496    -64       C  
ATOM   3693  OD1 ASN B 227      77.632  72.522  60.123  1.00102.42           O  
ANISOU 3693  OD1 ASN B 227    12661  13869  12385    284   -436    -94       O  
ATOM   3694  ND2 ASN B 227      79.053  73.492  58.696  1.00 94.39           N  
ANISOU 3694  ND2 ASN B 227    10624  13279  11958    351   -812   -196       N  
ATOM   3695  N   TRP B 228      75.750  75.380  56.581  1.00 70.27           N  
ANISOU 3695  N   TRP B 228     6843   9945   9910    -98    168     78       N  
ATOM   3696  CA  TRP B 228      75.869  76.776  56.277  1.00 73.49           C  
ANISOU 3696  CA  TRP B 228     7051  10279  10589   -162    183     58       C  
ATOM   3697  C   TRP B 228      74.764  77.640  56.901  1.00 80.84           C  
ANISOU 3697  C   TRP B 228     8005  10959  11750   -204    453    -75       C  
ATOM   3698  O   TRP B 228      74.996  78.810  57.199  1.00 83.60           O  
ANISOU 3698  O   TRP B 228     8361  11165  12235   -265    491   -172       O  
ATOM   3699  CB  TRP B 228      76.019  77.008  54.779  1.00 73.91           C  
ANISOU 3699  CB  TRP B 228     6874  10393  10815   -133     83    255       C  
ATOM   3700  CG  TRP B 228      77.453  76.795  54.304  1.00 79.31           C  
ANISOU 3700  CG  TRP B 228     7471  11287  11373   -177    -58    258       C  
ATOM   3701  CD1 TRP B 228      78.220  75.660  54.462  1.00 77.17           C  
ANISOU 3701  CD1 TRP B 228     7201  11225  10895    -80   -212    193       C  
ATOM   3702  CD2 TRP B 228      78.283  77.747  53.635  1.00 78.03           C  
ANISOU 3702  CD2 TRP B 228     7197  11111  11338   -339     -8    269       C  
ATOM   3703  NE1 TRP B 228      79.452  75.856  53.924  1.00 79.72           N  
ANISOU 3703  NE1 TRP B 228     7293  11714  11279   -146   -266    107       N  
ATOM   3704  CE2 TRP B 228      79.523  77.128  53.408  1.00 79.84           C  
ANISOU 3704  CE2 TRP B 228     7246  11600  11488   -362    -89    148       C  
ATOM   3705  CE3 TRP B 228      78.092  79.062  53.194  1.00 82.19           C  
ANISOU 3705  CE3 TRP B 228     7797  11380  12051   -470    129    354       C  
ATOM   3706  CZ2 TRP B 228      80.575  77.780  52.769  1.00 82.64           C  
ANISOU 3706  CZ2 TRP B 228     7415  12007  11975   -594     53     58       C  
ATOM   3707  CZ3 TRP B 228      79.135  79.709  52.549  1.00 87.29           C  
ANISOU 3707  CZ3 TRP B 228     8404  12012  12747   -716    267    339       C  
ATOM   3708  CH2 TRP B 228      80.359  79.072  52.348  1.00 86.53           C  
ANISOU 3708  CH2 TRP B 228     8054  12220  12601   -816    273    168       C  
ATOM   3709  N   THR B 229      73.582  77.064  57.164  1.00 84.85           N  
ANISOU 3709  N   THR B 229     8510  11390  12336   -200    692   -146       N  
ATOM   3710  CA  THR B 229      72.606  77.821  57.950  1.00 89.19           C  
ANISOU 3710  CA  THR B 229     9044  11714  13130   -246   1035   -387       C  
ATOM   3711  C   THR B 229      73.161  78.087  59.350  1.00 91.32           C  
ANISOU 3711  C   THR B 229     9754  11907  13033   -380   1177   -572       C  
ATOM   3712  O   THR B 229      73.062  79.205  59.843  1.00 95.22           O  
ANISOU 3712  O   THR B 229    10270  12226  13683   -412   1309   -753       O  
ATOM   3713  CB  THR B 229      71.158  77.217  58.022  1.00 90.66           C  
ANISOU 3713  CB  THR B 229     9025  11832  13588   -284   1381   -558       C  
ATOM   3714  OG1 THR B 229      70.846  76.485  56.830  1.00 83.92           O  
ANISOU 3714  OG1 THR B 229     7879  11122  12885   -196   1147   -408       O  
ATOM   3715  CG2 THR B 229      70.128  78.370  58.192  1.00 89.54           C  
ANISOU 3715  CG2 THR B 229     8556  11470  13992   -195   1611   -825       C  
ATOM   3716  N   LYS B 230      73.808  77.081  59.955  1.00 86.89           N  
ANISOU 3716  N   LYS B 230     9604  11450  11958   -421   1079   -531       N  
ATOM   3717  CA  LYS B 230      74.499  77.299  61.236  1.00 87.48           C  
ANISOU 3717  CA  LYS B 230    10191  11473  11574   -489   1029   -699       C  
ATOM   3718  C   LYS B 230      75.580  78.375  61.114  1.00 86.02           C  
ANISOU 3718  C   LYS B 230     9823  11361  11498   -481    685   -773       C  
ATOM   3719  O   LYS B 230      75.725  79.186  61.999  1.00 88.28           O  
ANISOU 3719  O   LYS B 230    10338  11523  11680   -583    752  -1016       O  
ATOM   3720  CB  LYS B 230      75.107  76.010  61.798  1.00 89.59           C  
ANISOU 3720  CB  LYS B 230    10997  11800  11241   -423    813   -606       C  
ATOM   3721  CG  LYS B 230      74.111  74.934  62.166  1.00 96.95           C  
ANISOU 3721  CG  LYS B 230    12325  12554  11958   -538   1259   -566       C  
ATOM   3722  CD  LYS B 230      74.701  73.989  63.210  1.00110.56           C  
ANISOU 3722  CD  LYS B 230    14936  14159  12911   -482   1093   -516       C  
ATOM   3723  CE  LYS B 230      73.951  72.656  63.260  1.00119.11           C  
ANISOU 3723  CE  LYS B 230    16455  15027  13773   -603   1482   -384       C  
ATOM   3724  NZ  LYS B 230      74.467  71.661  62.269  1.00117.23           N  
ANISOU 3724  NZ  LYS B 230    16009  14912  13620   -385   1088   -148       N  
ATOM   3725  N   LEU B 231      76.324  78.381  60.006  1.00 82.14           N  
ANISOU 3725  N   LEU B 231     8939  11050  11219   -412    380   -607       N  
ATOM   3726  CA  LEU B 231      77.374  79.397  59.804  1.00 86.77           C  
ANISOU 3726  CA  LEU B 231     9313  11680  11974   -509    167   -721       C  
ATOM   3727  C   LEU B 231      76.793  80.801  59.673  1.00 88.60           C  
ANISOU 3727  C   LEU B 231     9455  11618  12589   -619    439   -795       C  
ATOM   3728  O   LEU B 231      77.385  81.779  60.170  1.00 91.80           O  
ANISOU 3728  O   LEU B 231     9919  11916  13043   -781    407  -1028       O  
ATOM   3729  CB  LEU B 231      78.246  79.074  58.584  1.00 85.46           C  
ANISOU 3729  CB  LEU B 231     8774  11739  11958   -478    -55   -559       C  
ATOM   3730  CG  LEU B 231      79.624  78.393  58.765  1.00 90.38           C  
ANISOU 3730  CG  LEU B 231     9293  12656  12391   -409   -458   -701       C  
ATOM   3731  CD1 LEU B 231      79.730  77.545  60.033  1.00 92.15           C  
ANISOU 3731  CD1 LEU B 231     9970  12910  12132   -233   -718   -822       C  
ATOM   3732  CD2 LEU B 231      79.964  77.552  57.535  1.00 85.82           C  
ANISOU 3732  CD2 LEU B 231     8428  12271  11905   -301   -511   -505       C  
ATOM   3733  N   VAL B 232      75.636  80.914  59.015  1.00 82.22           N  
ANISOU 3733  N   VAL B 232     8504  10653  12081   -509    663   -639       N  
ATOM   3734  CA  VAL B 232      75.013  82.221  58.860  1.00 79.05           C  
ANISOU 3734  CA  VAL B 232     8048   9905  12080   -497    855   -706       C  
ATOM   3735  C   VAL B 232      74.579  82.780  60.196  1.00 83.71           C  
ANISOU 3735  C   VAL B 232     8892  10289  12622   -572   1137  -1057       C  
ATOM   3736  O   VAL B 232      74.656  83.977  60.408  1.00 91.36           O  
ANISOU 3736  O   VAL B 232     9931  10973  13807   -638   1230  -1220       O  
ATOM   3737  CB  VAL B 232      73.828  82.235  57.888  1.00 72.57           C  
ANISOU 3737  CB  VAL B 232     6984   8957  11633   -261    903   -525       C  
ATOM   3738  CG1 VAL B 232      73.253  83.628  57.834  1.00 73.29           C  
ANISOU 3738  CG1 VAL B 232     7081   8622  12142   -154   1021   -622       C  
ATOM   3739  CG2 VAL B 232      74.269  81.832  56.496  1.00 70.81           C  
ANISOU 3739  CG2 VAL B 232     6634   8887  11380   -204    629   -186       C  
ATOM   3740  N   LYS B 233      74.158  81.909  61.106  1.00 85.43           N  
ANISOU 3740  N   LYS B 233     9339  10609  12511   -594   1315  -1186       N  
ATOM   3741  CA  LYS B 233      73.711  82.349  62.419  1.00 95.71           C  
ANISOU 3741  CA  LYS B 233    10997  11710  13657   -704   1676  -1546       C  
ATOM   3742  C   LYS B 233      74.856  82.806  63.263  1.00102.12           C  
ANISOU 3742  C   LYS B 233    12169  12547  14083   -872   1437  -1754       C  
ATOM   3743  O   LYS B 233      74.748  83.828  63.938  1.00109.75           O  
ANISOU 3743  O   LYS B 233    13320  13262  15119   -976   1636  -2063       O  
ATOM   3744  CB  LYS B 233      72.932  81.245  63.136  1.00105.75           C  
ANISOU 3744  CB  LYS B 233    12547  13029  14602   -754   2035  -1616       C  
ATOM   3745  CG  LYS B 233      71.428  81.438  63.073  1.00121.11           C  
ANISOU 3745  CG  LYS B 233    14183  14778  17052   -709   2583  -1805       C  
ATOM   3746  CD  LYS B 233      70.732  80.227  62.481  1.00132.38           C  
ANISOU 3746  CD  LYS B 233    15357  16358  18582   -687   2681  -1647       C  
ATOM   3747  CE  LYS B 233      69.554  80.648  61.617  1.00142.73           C  
ANISOU 3747  CE  LYS B 233    15966  17576  20687   -489   2798  -1747       C  
ATOM   3748  NZ  LYS B 233      68.447  79.653  61.672  1.00146.86           N  
ANISOU 3748  NZ  LYS B 233    16260  18149  21390   -611   3233  -1918       N  
ATOM   3749  N   ARG B 234      75.965  82.047  63.217  1.00105.12           N  
ANISOU 3749  N   ARG B 234    12615  13228  14096   -875    974  -1637       N  
ATOM   3750  CA  ARG B 234      77.140  82.304  64.038  1.00101.36           C  
ANISOU 3750  CA  ARG B 234    12404  12853  13254   -990    590  -1902       C  
ATOM   3751  C   ARG B 234      77.724  83.668  63.723  1.00102.73           C  
ANISOU 3751  C   ARG B 234    12300  12882  13850  -1175    536  -2090       C  
ATOM   3752  O   ARG B 234      78.151  84.391  64.632  1.00113.29           O  
ANISOU 3752  O   ARG B 234    13902  14115  15028  -1347    465  -2469       O  
ATOM   3753  CB  ARG B 234      78.194  81.218  63.815  1.00106.39           C  
ANISOU 3753  CB  ARG B 234    12976  13844  13603   -859     40  -1767       C  
ATOM   3754  CG  ARG B 234      78.678  80.511  65.093  1.00118.84           C  
ANISOU 3754  CG  ARG B 234    15201  15505  14448   -774   -314  -1944       C  
ATOM   3755  CD  ARG B 234      79.584  79.315  64.784  1.00127.85           C  
ANISOU 3755  CD  ARG B 234    16259  16937  15378   -513   -886  -1788       C  
ATOM   3756  NE  ARG B 234      78.801  78.127  64.380  1.00145.28           N  
ANISOU 3756  NE  ARG B 234    18641  19101  17458   -365   -631  -1420       N  
ATOM   3757  CZ  ARG B 234      79.321  76.961  63.977  1.00152.43           C  
ANISOU 3757  CZ  ARG B 234    19524  20167  18224   -109   -993  -1228       C  
ATOM   3758  NH1 ARG B 234      80.638  76.795  63.919  1.00164.11           N  
ANISOU 3758  NH1 ARG B 234    20742  21898  19712     83  -1651  -1387       N  
ATOM   3759  NH2 ARG B 234      78.514  75.952  63.637  1.00138.09           N  
ANISOU 3759  NH2 ARG B 234    17912  18243  16313    -49   -685   -935       N  
ATOM   3760  N   HIS B 235      77.763  84.028  62.443  1.00 98.80           N  
ANISOU 3760  N   HIS B 235    11355  12338  13844  -1171    578  -1840       N  
ATOM   3761  CA  HIS B 235      78.420  85.287  62.048  1.00110.47           C  
ANISOU 3761  CA  HIS B 235    12665  13608  15699  -1415    585  -1981       C  
ATOM   3762  C   HIS B 235      77.428  86.284  61.437  1.00117.52           C  
ANISOU 3762  C   HIS B 235    13565  14034  17052  -1349    968  -1840       C  
ATOM   3763  O   HIS B 235      77.380  86.465  60.225  1.00121.52           O  
ANISOU 3763  O   HIS B 235    13886  14441  17843  -1300    987  -1520       O  
ATOM   3764  CB  HIS B 235      79.623  85.022  61.124  1.00105.38           C  
ANISOU 3764  CB  HIS B 235    11620  13237  15182  -1544    311  -1881       C  
ATOM   3765  CG  HIS B 235      80.401  83.787  61.485  1.00105.19           C  
ANISOU 3765  CG  HIS B 235    11497  13676  14793  -1419   -125  -1949       C  
ATOM   3766  ND1 HIS B 235      80.376  82.635  60.717  1.00102.09           N  
ANISOU 3766  ND1 HIS B 235    10921  13538  14331  -1197   -225  -1627       N  
ATOM   3767  CD2 HIS B 235      81.193  83.510  62.550  1.00106.13           C  
ANISOU 3767  CD2 HIS B 235    11736  14008  14579  -1427   -548  -2316       C  
ATOM   3768  CE1 HIS B 235      81.127  81.708  61.288  1.00 99.44           C  
ANISOU 3768  CE1 HIS B 235    10593  13516  13671  -1051   -664  -1778       C  
ATOM   3769  NE2 HIS B 235      81.628  82.210  62.404  1.00108.09           N  
ANISOU 3769  NE2 HIS B 235    11881  14601  14587  -1161   -911  -2186       N  
ATOM   3770  N   SER B 236      76.644  86.927  62.314  1.00129.20           N  
ANISOU 3770  N   SER B 236    15318  15201  18571  -1318   1255  -2110       N  
ATOM   3771  CA  SER B 236      75.454  87.739  61.932  1.00129.71           C  
ANISOU 3771  CA  SER B 236    15375  14803  19104  -1100   1590  -2052       C  
ATOM   3772  C   SER B 236      74.312  86.907  61.340  1.00125.37           C  
ANISOU 3772  C   SER B 236    14573  14367  18693   -755   1663  -1780       C  
ATOM   3773  O   SER B 236      74.125  86.866  60.123  1.00127.41           O  
ANISOU 3773  O   SER B 236    14619  14590  19201   -581   1507  -1427       O  
ATOM   3774  CB  SER B 236      75.828  88.911  61.005  1.00130.83           C  
ANISOU 3774  CB  SER B 236    15527  14526  19653  -1186   1580  -1912       C  
ATOM   3775  OG  SER B 236      75.625  90.158  61.651  1.00132.36           O  
ANISOU 3775  OG  SER B 236    16002  14213  20073  -1269   1828  -2258       O  
TER    3776      SER B 236                                                      
ATOM   3777  N   GLY C   2      57.714  33.479  72.476  1.00164.82           N  
ANISOU 3777  N   GLY C   2    25662  17030  19929   2527   -689   3776       N  
ATOM   3778  CA  GLY C   2      56.850  32.273  72.659  1.00176.23           C  
ANISOU 3778  CA  GLY C   2    28011  17484  21463   2218   -325   4109       C  
ATOM   3779  C   GLY C   2      55.361  32.584  72.703  1.00176.76           C  
ANISOU 3779  C   GLY C   2    28001  17399  21759   1207    141   4050       C  
ATOM   3780  O   GLY C   2      54.608  32.170  71.823  1.00174.53           O  
ANISOU 3780  O   GLY C   2    27753  16630  21928    716    356   3818       O  
ATOM   3781  N   SER C   3      54.945  33.336  73.723  1.00179.62           N  
ANISOU 3781  N   SER C   3    28218  18225  21805    908    287   4218       N  
ATOM   3782  CA  SER C   3      53.516  33.549  74.022  1.00180.03           C  
ANISOU 3782  CA  SER C   3    28259  18136  22007      1    787   4234       C  
ATOM   3783  C   SER C   3      52.781  34.356  72.954  1.00176.88           C  
ANISOU 3783  C   SER C   3    27040  18034  22132   -574    853   3693       C  
ATOM   3784  O   SER C   3      53.308  35.345  72.427  1.00169.88           O  
ANISOU 3784  O   SER C   3    25439  17796  21310   -367    556   3351       O  
ATOM   3785  CB  SER C   3      53.354  34.243  75.369  1.00176.09           C  
ANISOU 3785  CB  SER C   3    27761  18144  20998    -91    917   4495       C  
ATOM   3786  OG  SER C   3      54.598  34.383  76.011  1.00173.62           O  
ANISOU 3786  OG  SER C   3    27550  18243  20175    703    494   4683       O  
ATOM   3787  N   LEU C   4      51.555  33.924  72.651  1.00178.73           N  
ANISOU 3787  N   LEU C   4    27392  17790  22727  -1303   1247   3624       N  
ATOM   3788  CA  LEU C   4      50.641  34.689  71.813  1.00173.87           C  
ANISOU 3788  CA  LEU C   4    26019  17480  22561  -1899   1337   3159       C  
ATOM   3789  C   LEU C   4      50.497  36.085  72.372  1.00168.86           C  
ANISOU 3789  C   LEU C   4    24745  17662  21751  -1990   1340   3062       C  
ATOM   3790  O   LEU C   4      50.504  37.063  71.628  1.00167.89           O  
ANISOU 3790  O   LEU C   4    23905  18038  21846  -2013   1149   2677       O  
ATOM   3791  CB  LEU C   4      49.262  34.010  71.765  1.00178.67           C  
ANISOU 3791  CB  LEU C   4    26855  17524  23506  -2719   1808   3155       C  
ATOM   3792  CG  LEU C   4      48.155  34.547  70.824  1.00174.91           C  
ANISOU 3792  CG  LEU C   4    25642  17263  23549  -3370   1893   2661       C  
ATOM   3793  CD1 LEU C   4      48.118  36.074  70.730  1.00164.12           C  
ANISOU 3793  CD1 LEU C   4    23409  16776  22171  -3313   1727   2398       C  
ATOM   3794  CD2 LEU C   4      48.230  33.907  69.435  1.00173.48           C  
ANISOU 3794  CD2 LEU C   4    25473  16688  23755  -3368   1665   2310       C  
ATOM   3795  N   ALA C   5      50.343  36.169  73.691  1.00166.07           N  
ANISOU 3795  N   ALA C   5    24705  17411  20982  -2047   1583   3415       N  
ATOM   3796  CA  ALA C   5      50.360  37.451  74.377  1.00156.72           C  
ANISOU 3796  CA  ALA C   5    23026  16978  19542  -2046   1578   3331       C  
ATOM   3797  C   ALA C   5      51.637  38.179  74.028  1.00150.42           C  
ANISOU 3797  C   ALA C   5    21836  16711  18607  -1412   1065   3141       C  
ATOM   3798  O   ALA C   5      51.628  39.382  73.788  1.00139.32           O  
ANISOU 3798  O   ALA C   5    19762  15875  17297  -1482    969   2821       O  
ATOM   3799  CB  ALA C   5      50.249  37.261  75.879  1.00160.30           C  
ANISOU 3799  CB  ALA C   5    24030  17433  19442  -2065   1861   3771       C  
ATOM   3800  N   TRP C   6      52.735  37.428  73.965  1.00157.08           N  
ANISOU 3800  N   TRP C   6    23092  17338  19253   -794    753   3325       N  
ATOM   3801  CA  TRP C   6      54.005  37.981  73.543  1.00152.40           C  
ANISOU 3801  CA  TRP C   6    22093  17232  18579   -198    284   3115       C  
ATOM   3802  C   TRP C   6      53.955  38.412  72.102  1.00142.24           C  
ANISOU 3802  C   TRP C   6    20224  16034  17786   -321    164   2668       C  
ATOM   3803  O   TRP C   6      54.378  39.514  71.764  1.00139.24           O  
ANISOU 3803  O   TRP C   6    19226  16232  17447   -246    -15   2377       O  
ATOM   3804  CB  TRP C   6      55.146  36.986  73.731  1.00161.47           C  
ANISOU 3804  CB  TRP C   6    23780  18117  19454    533    -13   3390       C  
ATOM   3805  CG  TRP C   6      56.479  37.608  73.431  1.00165.19           C  
ANISOU 3805  CG  TRP C   6    23741  19201  19821   1129   -472   3153       C  
ATOM   3806  CD1 TRP C   6      57.205  38.422  74.255  1.00167.01           C  
ANISOU 3806  CD1 TRP C   6    23687  20118  19651   1404   -705   3141       C  
ATOM   3807  CD2 TRP C   6      57.217  37.528  72.198  1.00163.74           C  
ANISOU 3807  CD2 TRP C   6    23216  19046  19951   1455   -720   2839       C  
ATOM   3808  NE1 TRP C   6      58.361  38.828  73.628  1.00165.03           N  
ANISOU 3808  NE1 TRP C   6    22913  20313  19476   1859  -1078   2845       N  
ATOM   3809  CE2 TRP C   6      58.395  38.295  72.366  1.00160.17           C  
ANISOU 3809  CE2 TRP C   6    22258  19310  19287   1911  -1072   2670       C  
ATOM   3810  CE3 TRP C   6      57.009  36.867  70.979  1.00162.03           C  
ANISOU 3810  CE3 TRP C   6    23080  18331  20152   1396   -667   2662       C  
ATOM   3811  CZ2 TRP C   6      59.355  38.423  71.361  1.00150.85           C  
ANISOU 3811  CZ2 TRP C   6    20635  18367  18312   2291  -1320   2354       C  
ATOM   3812  CZ3 TRP C   6      57.969  36.998  69.976  1.00154.55           C  
ANISOU 3812  CZ3 TRP C   6    21736  17620  19363   1815   -930   2348       C  
ATOM   3813  CH2 TRP C   6      59.130  37.764  70.182  1.00149.92           C  
ANISOU 3813  CH2 TRP C   6    20636  17755  18570   2255  -1230   2212       C  
ATOM   3814  N   TRP C   7      53.455  37.536  71.243  1.00140.31           N  
ANISOU 3814  N   TRP C   7    20217  15199  17894   -518    268   2610       N  
ATOM   3815  CA  TRP C   7      53.409  37.836  69.832  1.00135.70           C  
ANISOU 3815  CA  TRP C   7    19167  14680  17712   -604    136   2196       C  
ATOM   3816  C   TRP C   7      52.579  39.073  69.593  1.00126.85           C  
ANISOU 3816  C   TRP C   7    17393  14013  16788  -1088    250   1928       C  
ATOM   3817  O   TRP C   7      52.831  39.817  68.664  1.00121.24           O  
ANISOU 3817  O   TRP C   7    16183  13632  16250  -1028     73   1616       O  
ATOM   3818  CB  TRP C   7      52.857  36.659  69.043  1.00147.60           C  
ANISOU 3818  CB  TRP C   7    21081  15462  19536   -820    249   2147       C  
ATOM   3819  CG  TRP C   7      53.927  35.756  68.516  1.00159.49           C  
ANISOU 3819  CG  TRP C   7    22957  16636  21005   -203      8   2157       C  
ATOM   3820  CD1 TRP C   7      54.067  34.413  68.754  1.00167.00           C  
ANISOU 3820  CD1 TRP C   7    24685  16853  21911      0     81   2419       C  
ATOM   3821  CD2 TRP C   7      55.022  36.129  67.669  1.00160.28           C  
ANISOU 3821  CD2 TRP C   7    22677  17107  21113    311   -309   1889       C  
ATOM   3822  NE1 TRP C   7      55.174  33.927  68.097  1.00165.95           N  
ANISOU 3822  NE1 TRP C   7    24659  16620  21772    660   -194   2307       N  
ATOM   3823  CE2 TRP C   7      55.780  34.958  67.424  1.00162.87           C  
ANISOU 3823  CE2 TRP C   7    23539  16932  21411    848   -424   1974       C  
ATOM   3824  CE3 TRP C   7      55.429  37.337  67.079  1.00154.76           C  
ANISOU 3824  CE3 TRP C   7    21260  17091  20451    360   -471   1584       C  
ATOM   3825  CZ2 TRP C   7      56.929  34.963  66.626  1.00160.85           C  
ANISOU 3825  CZ2 TRP C   7    23053  16902  21160   1440   -686   1737       C  
ATOM   3826  CZ3 TRP C   7      56.575  37.338  66.284  1.00154.02           C  
ANISOU 3826  CZ3 TRP C   7    20968  17201  20349    891   -710   1374       C  
ATOM   3827  CH2 TRP C   7      57.310  36.158  66.068  1.00157.68           C  
ANISOU 3827  CH2 TRP C   7    21909  17218  20784   1428   -811   1438       C  
ATOM   3828  N   LYS C   8      51.611  39.310  70.475  1.00129.01           N  
ANISOU 3828  N   LYS C   8    17696  14307  17011  -1535    566   2065       N  
ATOM   3829  CA  LYS C   8      50.729  40.470  70.361  1.00127.16           C  
ANISOU 3829  CA  LYS C   8    16860  14480  16975  -1956    707   1820       C  
ATOM   3830  C   LYS C   8      51.515  41.754  70.621  1.00119.68           C  
ANISOU 3830  C   LYS C   8    15484  14170  15817  -1660    514   1699       C  
ATOM   3831  O   LYS C   8      51.338  42.742  69.929  1.00114.38           O  
ANISOU 3831  O   LYS C   8    14287  13809  15362  -1754    444   1413       O  
ATOM   3832  CB  LYS C   8      49.528  40.347  71.328  1.00136.15           C  
ANISOU 3832  CB  LYS C   8    18137  15495  18097  -2483   1149   1987       C  
ATOM   3833  CG  LYS C   8      48.317  41.220  70.976  1.00137.48           C  
ANISOU 3833  CG  LYS C   8    17690  15925  18619  -2971   1337   1692       C  
ATOM   3834  CD  LYS C   8      48.399  42.613  71.623  1.00145.79           C  
ANISOU 3834  CD  LYS C   8    18330  17570  19490  -2891   1368   1600       C  
ATOM   3835  CE  LYS C   8      47.389  43.595  71.011  1.00149.71           C  
ANISOU 3835  CE  LYS C   8    18166  18335  20378  -3195   1446   1266       C  
ATOM   3836  NZ  LYS C   8      47.678  45.037  71.311  1.00140.28           N  
ANISOU 3836  NZ  LYS C   8    16580  17649  19071  -3014   1391   1110       N  
ATOM   3837  N   ARG C   9      52.415  41.704  71.597  1.00123.90           N  
ANISOU 3837  N   ARG C   9    16277  14878  15921  -1291    412   1916       N  
ATOM   3838  CA  ARG C   9      53.290  42.837  71.936  1.00124.68           C  
ANISOU 3838  CA  ARG C   9    15999  15580  15791  -1024    209   1774       C  
ATOM   3839  C   ARG C   9      54.270  43.193  70.816  1.00124.12           C  
ANISOU 3839  C   ARG C   9    15567  15711  15882   -704   -107   1514       C  
ATOM   3840  O   ARG C   9      54.336  44.354  70.357  1.00124.19           O  
ANISOU 3840  O   ARG C   9    15074  16080  16030   -805   -143   1242       O  
ATOM   3841  CB  ARG C   9      54.086  42.515  73.190  1.00126.22           C  
ANISOU 3841  CB  ARG C   9    16581  15920  15457   -664    103   2053       C  
ATOM   3842  CG  ARG C   9      53.409  42.910  74.469  1.00124.14           C  
ANISOU 3842  CG  ARG C   9    16459  15819  14888   -947    389   2191       C  
ATOM   3843  CD  ARG C   9      54.349  42.709  75.620  1.00127.59           C  
ANISOU 3843  CD  ARG C   9    17243  16504  14731   -519    187   2425       C  
ATOM   3844  NE  ARG C   9      53.964  43.536  76.733  1.00132.17           N  
ANISOU 3844  NE  ARG C   9    17776  17466  14977   -743    382   2397       N  
ATOM   3845  CZ  ARG C   9      54.700  44.528  77.224  1.00139.36           C  
ANISOU 3845  CZ  ARG C   9    18375  18959  15614   -575    161   2175       C  
ATOM   3846  NH1 ARG C   9      55.903  44.809  76.716  1.00134.28           N  
ANISOU 3846  NH1 ARG C   9    17400  18616  15004   -193   -258   1975       N  
ATOM   3847  NH2 ARG C   9      54.242  45.226  78.249  1.00153.07           N  
ANISOU 3847  NH2 ARG C   9    20132  20991  17037   -809    384   2126       N  
ATOM   3848  N   GLU C  10      55.062  42.206  70.412  1.00122.22           N  
ANISOU 3848  N   GLU C  10    15607  15225  15604   -301   -306   1606       N  
ATOM   3849  CA  GLU C  10      56.039  42.398  69.378  1.00118.11           C  
ANISOU 3849  CA  GLU C  10    14778  14891  15206     24   -554   1368       C  
ATOM   3850  C   GLU C  10      55.443  43.011  68.107  1.00118.87           C  
ANISOU 3850  C   GLU C  10    14495  14991  15677   -293   -486   1077       C  
ATOM   3851  O   GLU C  10      56.016  43.934  67.544  1.00121.30           O  
ANISOU 3851  O   GLU C  10    14376  15677  16034   -223   -583    851       O  
ATOM   3852  CB  GLU C  10      56.717  41.102  69.050  1.00116.46           C  
ANISOU 3852  CB  GLU C  10    14977  14308  14965    476   -706   1492       C  
ATOM   3853  CG  GLU C  10      57.972  41.300  68.260  1.00118.53           C  
ANISOU 3853  CG  GLU C  10    14898  14884  15252    920   -954   1260       C  
ATOM   3854  CD  GLU C  10      59.154  41.691  69.124  1.00127.42           C  
ANISOU 3854  CD  GLU C  10    15824  16541  16046   1340  -1187   1290       C  
ATOM   3855  OE1 GLU C  10      59.016  41.707  70.369  1.00133.10           O  
ANISOU 3855  OE1 GLU C  10    16762  17349  16458   1338  -1190   1521       O  
ATOM   3856  OE2 GLU C  10      60.231  41.962  68.556  1.00129.79           O  
ANISOU 3856  OE2 GLU C  10    15739  17197  16376   1668  -1365   1065       O  
ATOM   3857  N   LEU C  11      54.287  42.506  67.676  1.00117.64           N  
ANISOU 3857  N   LEU C  11    14503  14424  15769   -655   -318   1085       N  
ATOM   3858  CA  LEU C  11      53.709  42.892  66.384  1.00113.42           C  
ANISOU 3858  CA  LEU C  11    13671  13871  15550   -889   -323    818       C  
ATOM   3859  C   LEU C  11      52.974  44.213  66.422  1.00106.30           C  
ANISOU 3859  C   LEU C  11    12328  13299  14763  -1213   -215    689       C  
ATOM   3860  O   LEU C  11      52.907  44.914  65.419  1.00107.30           O  
ANISOU 3860  O   LEU C  11    12142  13581  15043  -1249   -289    481       O  
ATOM   3861  CB  LEU C  11      52.749  41.819  65.870  1.00120.49           C  
ANISOU 3861  CB  LEU C  11    14867  14234  16677  -1164   -232    815       C  
ATOM   3862  CG  LEU C  11      53.250  40.466  65.366  1.00126.88           C  
ANISOU 3862  CG  LEU C  11    16141  14571  17496   -900   -326    840       C  
ATOM   3863  CD1 LEU C  11      52.113  39.824  64.599  1.00130.24           C  
ANISOU 3863  CD1 LEU C  11    16679  14583  18222  -1329   -243    686       C  
ATOM   3864  CD2 LEU C  11      54.488  40.592  64.481  1.00127.70           C  
ANISOU 3864  CD2 LEU C  11    16102  14887  17530   -421   -551    663       C  
ATOM   3865  N   PHE C  12      52.369  44.528  67.551  1.00103.08           N  
ANISOU 3865  N   PHE C  12    11931  12964  14268  -1434    -21    815       N  
ATOM   3866  CA  PHE C  12      51.443  45.648  67.598  1.00108.56           C  
ANISOU 3866  CA  PHE C  12    12243  13879  15126  -1745    126    680       C  
ATOM   3867  C   PHE C  12      51.839  46.700  68.631  1.00112.18           C  
ANISOU 3867  C   PHE C  12    12549  14719  15355  -1692    196    682       C  
ATOM   3868  O   PHE C  12      51.234  47.774  68.696  1.00113.85           O  
ANISOU 3868  O   PHE C  12    12449  15120  15689  -1873    318    543       O  
ATOM   3869  CB  PHE C  12      50.000  45.153  67.825  1.00118.25           C  
ANISOU 3869  CB  PHE C  12    13520  14847  16561  -2168    369    722       C  
ATOM   3870  CG  PHE C  12      49.487  44.236  66.726  1.00122.59           C  
ANISOU 3870  CG  PHE C  12    14154  15046  17377  -2308    285    628       C  
ATOM   3871  CD1 PHE C  12      48.979  44.761  65.539  1.00122.71           C  
ANISOU 3871  CD1 PHE C  12    13809  15165  17647  -2389    147    380       C  
ATOM   3872  CD2 PHE C  12      49.530  42.850  66.876  1.00122.69           C  
ANISOU 3872  CD2 PHE C  12    14648  14606  17360  -2344    331    781       C  
ATOM   3873  CE1 PHE C  12      48.526  43.923  64.529  1.00118.94           C  
ANISOU 3873  CE1 PHE C  12    13413  14409  17369  -2525     33    244       C  
ATOM   3874  CE2 PHE C  12      49.091  42.012  65.864  1.00119.39           C  
ANISOU 3874  CE2 PHE C  12    14330  13844  17185  -2500    251    636       C  
ATOM   3875  CZ  PHE C  12      48.585  42.550  64.694  1.00119.63           C  
ANISOU 3875  CZ  PHE C  12    13961  14043  17449  -2603     91    346       C  
ATOM   3876  N   GLY C  13      52.895  46.410  69.394  1.00114.34           N  
ANISOU 3876  N   GLY C  13    13036  15112  15293  -1410     90    809       N  
ATOM   3877  CA  GLY C  13      53.256  47.215  70.555  1.00107.29           C  
ANISOU 3877  CA  GLY C  13    12077  14578  14111  -1386    140    801       C  
ATOM   3878  C   GLY C  13      54.172  48.368  70.231  1.00104.92           C  
ANISOU 3878  C   GLY C  13    11410  14651  13801  -1257    -10    559       C  
ATOM   3879  O   GLY C  13      55.212  48.192  69.602  1.00103.24           O  
ANISOU 3879  O   GLY C  13    11124  14525  13576   -992   -228    500       O  
ATOM   3880  N   GLY C  14      53.777  49.558  70.661  1.00104.08           N  
ANISOU 3880  N   GLY C  14    11076  14752  13716  -1463    141    400       N  
ATOM   3881  CA  GLY C  14      54.698  50.681  70.759  1.00 99.15           C  
ANISOU 3881  CA  GLY C  14    10186  14478  13007  -1404     48    172       C  
ATOM   3882  C   GLY C  14      55.173  51.239  69.436  1.00 99.55           C  
ANISOU 3882  C   GLY C  14     9970  14534  13318  -1368    -40      9       C  
ATOM   3883  O   GLY C  14      56.300  51.715  69.340  1.00101.00           O  
ANISOU 3883  O   GLY C  14     9976  14981  13416  -1264   -163   -138       O  
ATOM   3884  N   TRP C  15      54.315  51.183  68.408  1.00101.32           N  
ANISOU 3884  N   TRP C  15    10160  14494  13843  -1466     26     27       N  
ATOM   3885  CA  TRP C  15      54.523  51.984  67.182  1.00 95.95           C  
ANISOU 3885  CA  TRP C  15     9267  13813  13374  -1475      3   -113       C  
ATOM   3886  C   TRP C  15      53.987  53.376  67.370  1.00 91.53           C  
ANISOU 3886  C   TRP C  15     8544  13292  12938  -1662    178   -252       C  
ATOM   3887  O   TRP C  15      52.878  53.556  67.909  1.00 91.00           O  
ANISOU 3887  O   TRP C  15     8484  13137  12954  -1795    333   -234       O  
ATOM   3888  CB  TRP C  15      53.826  51.370  65.965  1.00 95.45           C  
ANISOU 3888  CB  TRP C  15     9259  13484  13523  -1464    -48    -50       C  
ATOM   3889  CG  TRP C  15      54.173  49.977  65.687  1.00102.72           C  
ANISOU 3889  CG  TRP C  15    10395  14262  14371  -1297   -186     56       C  
ATOM   3890  CD1 TRP C  15      53.502  48.875  66.108  1.00108.19           C  
ANISOU 3890  CD1 TRP C  15    11329  14715  15064  -1349   -164    200       C  
ATOM   3891  CD2 TRP C  15      55.250  49.510  64.883  1.00105.84           C  
ANISOU 3891  CD2 TRP C  15    10811  14700  14701  -1052   -332     14       C  
ATOM   3892  NE1 TRP C  15      54.102  47.741  65.630  1.00115.44           N  
ANISOU 3892  NE1 TRP C  15    12463  15472  15926  -1131   -305    256       N  
ATOM   3893  CE2 TRP C  15      55.180  48.101  64.872  1.00112.86           C  
ANISOU 3893  CE2 TRP C  15    11987  15338  15556   -918   -415    132       C  
ATOM   3894  CE3 TRP C  15      56.279  50.138  64.189  1.00112.45           C  
ANISOU 3894  CE3 TRP C  15    11461  15756  15510   -944   -361   -119       C  
ATOM   3895  CZ2 TRP C  15      56.101  47.309  64.192  1.00116.74           C  
ANISOU 3895  CZ2 TRP C  15    12576  15791  15987   -622   -546     99       C  
ATOM   3896  CZ3 TRP C  15      57.194  49.354  63.512  1.00122.66           C  
ANISOU 3896  CZ3 TRP C  15    12801  17067  16735   -678   -469   -152       C  
ATOM   3897  CH2 TRP C  15      57.096  47.946  63.519  1.00121.98           C  
ANISOU 3897  CH2 TRP C  15    12999  16729  16617   -490   -571    -51       C  
ATOM   3898  N   THR C  16      54.764  54.365  66.919  1.00 90.87           N  
ANISOU 3898  N   THR C  16     8318  13321  12885  -1676    187   -400       N  
ATOM   3899  CA  THR C  16      54.236  55.699  66.657  1.00 95.76           C  
ANISOU 3899  CA  THR C  16     8849  13841  13691  -1810    352   -509       C  
ATOM   3900  C   THR C  16      53.246  55.652  65.498  1.00102.95           C  
ANISOU 3900  C   THR C  16     9772  14513  14831  -1759    332   -409       C  
ATOM   3901  O   THR C  16      53.237  54.684  64.696  1.00 96.88           O  
ANISOU 3901  O   THR C  16     9064  13682  14063  -1655    182   -307       O  
ATOM   3902  CB  THR C  16      55.333  56.699  66.286  1.00 92.14           C  
ANISOU 3902  CB  THR C  16     8295  13485  13227  -1879    398   -667       C  
ATOM   3903  OG1 THR C  16      55.921  56.320  65.041  1.00 95.45           O  
ANISOU 3903  OG1 THR C  16     8709  13887  13667  -1773    308   -601       O  
ATOM   3904  CG2 THR C  16      56.384  56.741  67.335  1.00 97.66           C  
ANISOU 3904  CG2 THR C  16     8910  14492  13702  -1934    356   -823       C  
ATOM   3905  N   HIS C  17      52.416  56.700  65.412  1.00104.87           N  
ANISOU 3905  N   HIS C  17     9962  14626  15257  -1804    465   -459       N  
ATOM   3906  CA  HIS C  17      51.470  56.876  64.306  1.00 96.08           C  
ANISOU 3906  CA  HIS C  17     8826  13334  14343  -1706    403   -382       C  
ATOM   3907  C   HIS C  17      52.217  56.894  62.976  1.00 94.54           C  
ANISOU 3907  C   HIS C  17     8723  13107  14089  -1614    289   -323       C  
ATOM   3908  O   HIS C  17      51.869  56.159  62.033  1.00 89.06           O  
ANISOU 3908  O   HIS C  17     8066  12371  13401  -1515    118   -243       O  
ATOM   3909  CB  HIS C  17      50.691  58.177  64.490  1.00 92.52           C  
ANISOU 3909  CB  HIS C  17     8320  12755  14078  -1690    565   -454       C  
ATOM   3910  CG  HIS C  17      49.703  58.445  63.406  1.00 95.61           C  
ANISOU 3910  CG  HIS C  17     8668  13003  14654  -1516    454   -371       C  
ATOM   3911  ND1 HIS C  17      50.078  58.854  62.146  1.00 97.21           N  
ANISOU 3911  ND1 HIS C  17     9010  13103  14822  -1394    355   -277       N  
ATOM   3912  CD2 HIS C  17      48.351  58.366  63.389  1.00102.51           C  
ANISOU 3912  CD2 HIS C  17     9358  13860  15728  -1430    416   -376       C  
ATOM   3913  CE1 HIS C  17      49.001  59.013  61.397  1.00101.39           C  
ANISOU 3913  CE1 HIS C  17     9476  13557  15488  -1205    213   -211       C  
ATOM   3914  NE2 HIS C  17      47.940  58.721  62.127  1.00105.12           N  
ANISOU 3914  NE2 HIS C  17     9712  14098  16131  -1222    235   -288       N  
ATOM   3915  N   PHE C  18      53.272  57.709  62.925  1.00 90.41           N  
ANISOU 3915  N   PHE C  18     8237  12619  13492  -1680    406   -391       N  
ATOM   3916  CA  PHE C  18      54.086  57.855  61.744  1.00 81.71           C  
ANISOU 3916  CA  PHE C  18     7224  11510  12310  -1639    393   -345       C  
ATOM   3917  C   PHE C  18      54.707  56.505  61.287  1.00 84.19           C  
ANISOU 3917  C   PHE C  18     7539  11972  12474  -1540    229   -317       C  
ATOM   3918  O   PHE C  18      54.558  56.107  60.127  1.00 80.08           O  
ANISOU 3918  O   PHE C  18     7123  11394  11910  -1422    128   -243       O  
ATOM   3919  CB  PHE C  18      55.136  58.896  62.009  1.00 78.49           C  
ANISOU 3919  CB  PHE C  18     6806  11139  11876  -1818    602   -466       C  
ATOM   3920  CG  PHE C  18      56.094  59.098  60.888  1.00 76.99           C  
ANISOU 3920  CG  PHE C  18     6686  10971  11594  -1842    679   -434       C  
ATOM   3921  CD1 PHE C  18      55.776  59.915  59.830  1.00 80.06           C  
ANISOU 3921  CD1 PHE C  18     7290  11119  12009  -1807    777   -300       C  
ATOM   3922  CD2 PHE C  18      57.339  58.531  60.928  1.00 78.53           C  
ANISOU 3922  CD2 PHE C  18     6734  11443  11660  -1889    678   -538       C  
ATOM   3923  CE1 PHE C  18      56.678  60.145  58.812  1.00 82.21           C  
ANISOU 3923  CE1 PHE C  18     7667  11412  12155  -1867    917   -256       C  
ATOM   3924  CE2 PHE C  18      58.254  58.747  59.909  1.00 81.44           C  
ANISOU 3924  CE2 PHE C  18     7127  11869  11945  -1940    817   -536       C  
ATOM   3925  CZ  PHE C  18      57.917  59.552  58.846  1.00 81.73           C  
ANISOU 3925  CZ  PHE C  18     7417  11652  11984  -1954    960   -389       C  
ATOM   3926  N   GLU C  19      55.344  55.780  62.206  1.00 86.91           N  
ANISOU 3926  N   GLU C  19     7802  12496  12723  -1552    190   -382       N  
ATOM   3927  CA  GLU C  19      55.866  54.455  61.866  1.00 93.55           C  
ANISOU 3927  CA  GLU C  19     8681  13417  13447  -1393     37   -354       C  
ATOM   3928  C   GLU C  19      54.756  53.574  61.295  1.00 96.61           C  
ANISOU 3928  C   GLU C  19     9197  13606  13903  -1316   -107   -260       C  
ATOM   3929  O   GLU C  19      54.966  52.828  60.340  1.00 93.05           O  
ANISOU 3929  O   GLU C  19     8847  13119  13389  -1191   -211   -257       O  
ATOM   3930  CB  GLU C  19      56.476  53.775  63.077  1.00 97.34           C  
ANISOU 3930  CB  GLU C  19     9103  14072  13807  -1350    -22   -388       C  
ATOM   3931  CG  GLU C  19      57.756  54.396  63.585  1.00102.33           C  
ANISOU 3931  CG  GLU C  19     9543  14995  14342  -1405     40   -542       C  
ATOM   3932  CD  GLU C  19      57.925  54.213  65.088  1.00109.13           C  
ANISOU 3932  CD  GLU C  19    10361  16033  15070  -1416    -20   -581       C  
ATOM   3933  OE1 GLU C  19      58.952  54.667  65.643  1.00118.46           O  
ANISOU 3933  OE1 GLU C  19    11348  17512  16149  -1467    -25   -749       O  
ATOM   3934  OE2 GLU C  19      57.027  53.622  65.724  1.00101.07           O  
ANISOU 3934  OE2 GLU C  19     9500  14875  14028  -1393    -56   -455       O  
ATOM   3935  N   ALA C  20      53.568  53.672  61.874  1.00 99.00           N  
ANISOU 3935  N   ALA C  20     9476  13798  14341  -1409    -98   -223       N  
ATOM   3936  CA  ALA C  20      52.459  52.826  61.434  1.00106.12           C  
ANISOU 3936  CA  ALA C  20    10427  14546  15346  -1408   -231   -182       C  
ATOM   3937  C   ALA C  20      52.039  53.156  60.003  1.00105.66           C  
ANISOU 3937  C   ALA C  20    10399  14430  15314  -1327   -346   -186       C  
ATOM   3938  O   ALA C  20      51.949  52.261  59.163  1.00107.03           O  
ANISOU 3938  O   ALA C  20    10680  14550  15437  -1264   -504   -211       O  
ATOM   3939  CB  ALA C  20      51.275  52.930  62.392  1.00109.76           C  
ANISOU 3939  CB  ALA C  20    10779  14959  15966  -1555   -147   -170       C  
ATOM   3940  N   VAL C  21      51.831  54.451  59.733  1.00 97.87           N  
ANISOU 3940  N   VAL C  21     9365  13442  14378  -1311   -267   -164       N  
ATOM   3941  CA  VAL C  21      51.428  54.939  58.413  1.00 95.00           C  
ANISOU 3941  CA  VAL C  21     9084  13030  13982  -1185   -383   -119       C  
ATOM   3942  C   VAL C  21      52.330  54.428  57.291  1.00 97.58           C  
ANISOU 3942  C   VAL C  21     9595  13405  14074  -1091   -443   -124       C  
ATOM   3943  O   VAL C  21      51.844  53.938  56.260  1.00102.33           O  
ANISOU 3943  O   VAL C  21    10293  13993  14593   -997   -645   -138       O  
ATOM   3944  CB  VAL C  21      51.429  56.473  58.384  1.00 95.38           C  
ANISOU 3944  CB  VAL C  21     9156  13007  14075  -1154   -225    -55       C  
ATOM   3945  CG1 VAL C  21      51.201  56.995  56.974  1.00 97.18           C  
ANISOU 3945  CG1 VAL C  21     9567  13172  14182   -977   -335     52       C  
ATOM   3946  CG2 VAL C  21      50.373  57.004  59.319  1.00102.18           C  
ANISOU 3946  CG2 VAL C  21     9837  13813  15173  -1181   -169    -83       C  
ATOM   3947  N   TRP C  22      53.642  54.557  57.484  1.00 93.64           N  
ANISOU 3947  N   TRP C  22     9122  12998  13459  -1118   -267   -146       N  
ATOM   3948  CA  TRP C  22      54.597  54.210  56.443  1.00 89.93           C  
ANISOU 3948  CA  TRP C  22     8788  12613  12768  -1024   -243   -174       C  
ATOM   3949  C   TRP C  22      54.737  52.719  56.242  1.00 90.65           C  
ANISOU 3949  C   TRP C  22     8937  12711  12794   -924   -399   -269       C  
ATOM   3950  O   TRP C  22      54.834  52.252  55.118  1.00 96.66           O  
ANISOU 3950  O   TRP C  22     9861  13476  13387   -812   -480   -316       O  
ATOM   3951  CB  TRP C  22      55.943  54.852  56.709  1.00 82.20           C  
ANISOU 3951  CB  TRP C  22     7733  11773  11726  -1106     17   -208       C  
ATOM   3952  CG  TRP C  22      55.953  56.258  56.315  1.00 84.52           C  
ANISOU 3952  CG  TRP C  22     8116  11983  12014  -1200    204   -116       C  
ATOM   3953  CD1 TRP C  22      55.604  57.336  57.088  1.00 86.86           C  
ANISOU 3953  CD1 TRP C  22     8361  12161  12478  -1330    321    -88       C  
ATOM   3954  CD2 TRP C  22      56.250  56.769  55.030  1.00 86.23           C  
ANISOU 3954  CD2 TRP C  22     8558  12170  12033  -1160    317    -24       C  
ATOM   3955  NE1 TRP C  22      55.685  58.486  56.357  1.00 87.48           N  
ANISOU 3955  NE1 TRP C  22     8640  12091  12505  -1368    498     25       N  
ATOM   3956  CE2 TRP C  22      56.090  58.170  55.089  1.00 88.52           C  
ANISOU 3956  CE2 TRP C  22     8955  12282  12396  -1273    506     89       C  
ATOM   3957  CE3 TRP C  22      56.630  56.183  53.823  1.00 89.27           C  
ANISOU 3957  CE3 TRP C  22     9113  12646  12160  -1034    297    -28       C  
ATOM   3958  CZ2 TRP C  22      56.312  58.991  53.995  1.00 95.08           C  
ANISOU 3958  CZ2 TRP C  22    10083  12999  13041  -1270    683    246       C  
ATOM   3959  CZ3 TRP C  22      56.849  57.000  52.732  1.00 96.17           C  
ANISOU 3959  CZ3 TRP C  22    10256  13467  12815  -1037    475    109       C  
ATOM   3960  CH2 TRP C  22      56.696  58.392  52.826  1.00100.36           C  
ANISOU 3960  CH2 TRP C  22    10917  13796  13417  -1158    669    269       C  
ATOM   3961  N   LEU C  23      54.727  51.964  57.328  1.00 89.40           N  
ANISOU 3961  N   LEU C  23     8695  12525  12746   -956   -432   -297       N  
ATOM   3962  CA  LEU C  23      54.757  50.512  57.216  1.00 95.42           C  
ANISOU 3962  CA  LEU C  23     9585  13189  13480   -859   -567   -368       C  
ATOM   3963  C   LEU C  23      53.526  49.985  56.468  1.00101.86           C  
ANISOU 3963  C   LEU C  23    10510  13842  14347   -907   -771   -414       C  
ATOM   3964  O   LEU C  23      53.652  49.168  55.550  1.00106.03           O  
ANISOU 3964  O   LEU C  23    11217  14311  14757   -809   -879   -527       O  
ATOM   3965  CB  LEU C  23      54.848  49.865  58.587  1.00 93.86           C  
ANISOU 3965  CB  LEU C  23     9350  12940  13370   -886   -554   -329       C  
ATOM   3966  CG  LEU C  23      54.909  48.346  58.539  1.00 93.27           C  
ANISOU 3966  CG  LEU C  23     9490  12668  13280   -769   -664   -370       C  
ATOM   3967  CD1 LEU C  23      56.202  47.881  57.878  1.00 87.56           C  
ANISOU 3967  CD1 LEU C  23     8833  12044  12390   -495   -645   -471       C  
ATOM   3968  CD2 LEU C  23      54.771  47.790  59.944  1.00 96.18           C  
ANISOU 3968  CD2 LEU C  23     9900  12936  13707   -814   -639   -259       C  
ATOM   3969  N   LEU C  24      52.342  50.465  56.862  1.00100.24           N  
ANISOU 3969  N   LEU C  24    10170  13594  14321  -1057   -822   -364       N  
ATOM   3970  CA  LEU C  24      51.100  50.087  56.197  1.00 99.57           C  
ANISOU 3970  CA  LEU C  24    10079  13434  14318  -1127  -1044   -444       C  
ATOM   3971  C   LEU C  24      51.093  50.486  54.726  1.00101.38           C  
ANISOU 3971  C   LEU C  24    10428  13756  14332   -981  -1190   -484       C  
ATOM   3972  O   LEU C  24      50.726  49.688  53.871  1.00106.81           O  
ANISOU 3972  O   LEU C  24    11239  14408  14936   -970  -1396   -632       O  
ATOM   3973  CB  LEU C  24      49.877  50.650  56.936  1.00 98.78           C  
ANISOU 3973  CB  LEU C  24     9720  13341  14469  -1279  -1043   -402       C  
ATOM   3974  CG  LEU C  24      49.676  50.084  58.350  1.00 95.65           C  
ANISOU 3974  CG  LEU C  24     9253  12848  14238  -1463   -888   -370       C  
ATOM   3975  CD1 LEU C  24      48.466  50.686  59.044  1.00 94.31           C  
ANISOU 3975  CD1 LEU C  24     8798  12727  14307  -1609   -826   -361       C  
ATOM   3976  CD2 LEU C  24      49.562  48.572  58.281  1.00100.04           C  
ANISOU 3976  CD2 LEU C  24     9988  13203  14817  -1568   -968   -454       C  
HETATM 3977  N   MSE C  25      51.559  51.688  54.418  1.00 97.38           N  
ANISOU 3977  N   MSE C  25     9938  13355  13706   -879  -1068   -360       N  
HETATM 3978  CA  MSE C  25      51.665  52.082  53.025  1.00100.71           C  
ANISOU 3978  CA  MSE C  25    10560  13857  13846   -726  -1161   -347       C  
HETATM 3979  C   MSE C  25      52.679  51.248  52.268  1.00103.27           C  
ANISOU 3979  C   MSE C  25    11108  14219  13909   -636  -1113   -467       C  
HETATM 3980  O   MSE C  25      52.526  51.023  51.074  1.00109.81           O  
ANISOU 3980  O   MSE C  25    12140  15102  14478   -532  -1265   -544       O  
HETATM 3981  CB  MSE C  25      51.993  53.530  52.859  1.00104.87           C  
ANISOU 3981  CB  MSE C  25    11137  14417  14293   -662   -981   -157       C  
HETATM 3982  CG  MSE C  25      51.957  53.830  51.375  1.00117.20           C  
ANISOU 3982  CG  MSE C  25    12978  16045  15505   -491  -1096   -106       C  
HETATM 3983 SE   MSE C  25      52.886  55.508  51.068  1.00147.15          SE  
ANISOU 3983 SE   MSE C  25    16988  19796  19125   -466   -710    160      SE  
HETATM 3984  CE  MSE C  25      51.408  56.596  51.760  1.00136.45           C  
ANISOU 3984  CE  MSE C  25    15457  18287  18098   -394   -871    302       C  
ATOM   3985  N   PHE C  26      53.723  50.786  52.943  1.00100.52           N  
ANISOU 3985  N   PHE C  26    10721  13865  13605   -641   -911   -502       N  
ATOM   3986  CA  PHE C  26      54.742  49.996  52.266  1.00 99.80           C  
ANISOU 3986  CA  PHE C  26    10800  13823  13294   -497   -835   -642       C  
ATOM   3987  C   PHE C  26      54.202  48.630  51.876  1.00100.07           C  
ANISOU 3987  C   PHE C  26    10997  13699  13327   -472  -1068   -844       C  
ATOM   3988  O   PHE C  26      54.480  48.130  50.786  1.00100.08           O  
ANISOU 3988  O   PHE C  26    11223  13729  13071   -347  -1113  -1003       O  
ATOM   3989  CB  PHE C  26      55.977  49.850  53.135  1.00100.82           C  
ANISOU 3989  CB  PHE C  26    10786  14026  13495   -452   -603   -644       C  
ATOM   3990  CG  PHE C  26      56.956  50.981  52.993  1.00107.41           C  
ANISOU 3990  CG  PHE C  26    11519  15067  14222   -474   -319   -566       C  
ATOM   3991  CD1 PHE C  26      56.977  51.769  51.832  1.00110.43           C  
ANISOU 3991  CD1 PHE C  26    12075  15521  14361   -473   -223   -502       C  
ATOM   3992  CD2 PHE C  26      57.893  51.241  54.000  1.00108.92           C  
ANISOU 3992  CD2 PHE C  26    11461  15390  14533   -512   -142   -565       C  
ATOM   3993  CE1 PHE C  26      57.893  52.803  51.691  1.00107.62           C  
ANISOU 3993  CE1 PHE C  26    11662  15306  13921   -561    100   -426       C  
ATOM   3994  CE2 PHE C  26      58.808  52.268  53.860  1.00111.76           C  
ANISOU 3994  CE2 PHE C  26    11697  15940  14827   -609    139   -543       C  
ATOM   3995  CZ  PHE C  26      58.807  53.050  52.699  1.00111.92           C  
ANISOU 3995  CZ  PHE C  26    11910  15974  14640   -658    291   -468       C  
ATOM   3996  N   LEU C  27      53.415  48.039  52.770  1.00 98.55           N  
ANISOU 3996  N   LEU C  27    10711  13322  13410   -620  -1186   -854       N  
ATOM   3997  CA  LEU C  27      52.770  46.755  52.513  1.00 99.65           C  
ANISOU 3997  CA  LEU C  27    11009  13239  13615   -692  -1385  -1056       C  
ATOM   3998  C   LEU C  27      51.668  46.904  51.478  1.00105.48           C  
ANISOU 3998  C   LEU C  27    11771  14046  14258   -774  -1668  -1180       C  
ATOM   3999  O   LEU C  27      51.457  46.014  50.664  1.00108.67           O  
ANISOU 3999  O   LEU C  27    12383  14362  14544   -776  -1837  -1426       O  
ATOM   4000  CB  LEU C  27      52.206  46.169  53.804  1.00 94.40           C  
ANISOU 4000  CB  LEU C  27    10248  12349  13268   -888  -1370   -998       C  
ATOM   4001  CG  LEU C  27      53.239  46.017  54.914  1.00 93.62           C  
ANISOU 4001  CG  LEU C  27    10140  12215  13214   -769  -1153   -857       C  
ATOM   4002  CD1 LEU C  27      52.597  45.557  56.216  1.00 91.64           C  
ANISOU 4002  CD1 LEU C  27     9851  11759  13208   -972  -1116   -747       C  
ATOM   4003  CD2 LEU C  27      54.357  45.080  54.478  1.00 95.22           C  
ANISOU 4003  CD2 LEU C  27    10585  12328  13264   -495  -1104   -986       C  
ATOM   4004  N   GLY C  28      50.984  48.048  51.501  1.00104.61           N  
ANISOU 4004  N   GLY C  28    11455  14101  14189   -810  -1735  -1027       N  
ATOM   4005  CA  GLY C  28      50.007  48.396  50.468  1.00105.01           C  
ANISOU 4005  CA  GLY C  28    11500  14300  14097   -790  -2047  -1107       C  
ATOM   4006  C   GLY C  28      50.569  48.401  49.051  1.00105.71           C  
ANISOU 4006  C   GLY C  28    11913  14524  13726   -585  -2112  -1196       C  
ATOM   4007  O   GLY C  28      50.046  47.709  48.176  1.00110.41           O  
ANISOU 4007  O   GLY C  28    12645  15144  14160   -601  -2394  -1448       O  
ATOM   4008  N   ILE C  29      51.616  49.202  48.821  1.00100.17           N  
ANISOU 4008  N   ILE C  29    11336  13923  12799   -422  -1836  -1009       N  
ATOM   4009  CA  ILE C  29      52.250  49.301  47.497  1.00106.09           C  
ANISOU 4009  CA  ILE C  29    12420  14824  13065   -237  -1798  -1058       C  
ATOM   4010  C   ILE C  29      52.731  47.926  47.052  1.00109.34           C  
ANISOU 4010  C   ILE C  29    13039  15149  13353   -205  -1807  -1383       C  
ATOM   4011  O   ILE C  29      52.759  47.603  45.853  1.00114.33           O  
ANISOU 4011  O   ILE C  29    13961  15888  13589    -95  -1927  -1566       O  
ATOM   4012  CB  ILE C  29      53.453  50.283  47.511  1.00107.26           C  
ANISOU 4012  CB  ILE C  29    12626  15063  13064   -154  -1381   -823       C  
ATOM   4013  CG1 ILE C  29      53.043  51.649  48.073  1.00109.03           C  
ANISOU 4013  CG1 ILE C  29    12691  15275  13457   -200  -1324   -520       C  
ATOM   4014  CG2 ILE C  29      54.057  50.440  46.121  1.00108.78           C  
ANISOU 4014  CG2 ILE C  29    13184  15426  12722      5  -1278   -849       C  
ATOM   4015  CD1 ILE C  29      51.924  52.328  47.313  1.00114.65           C  
ANISOU 4015  CD1 ILE C  29    13510  16054  13997    -84  -1643   -407       C  
ATOM   4016  N   GLN C  30      53.093  47.114  48.031  1.00108.77           N  
ANISOU 4016  N   GLN C  30    12857  14867  13603   -278  -1683  -1455       N  
ATOM   4017  CA  GLN C  30      53.546  45.769  47.786  1.00111.70           C  
ANISOU 4017  CA  GLN C  30    13445  15060  13934   -214  -1670  -1749       C  
ATOM   4018  C   GLN C  30      52.359  44.871  47.415  1.00112.54           C  
ANISOU 4018  C   GLN C  30    13647  15003  14108   -396  -2038  -2031       C  
ATOM   4019  O   GLN C  30      52.449  44.075  46.476  1.00114.87           O  
ANISOU 4019  O   GLN C  30    14238  15253  14153   -331  -2141  -2344       O  
ATOM   4020  CB  GLN C  30      54.288  45.232  49.023  1.00111.78           C  
ANISOU 4020  CB  GLN C  30    13339  14872  14260   -184  -1443  -1683       C  
ATOM   4021  CG  GLN C  30      55.462  44.317  48.714  1.00114.31           C  
ANISOU 4021  CG  GLN C  30    13867  15114  14448     78  -1253  -1882       C  
ATOM   4022  CD  GLN C  30      56.306  44.809  47.551  1.00116.04           C  
ANISOU 4022  CD  GLN C  30    14207  15636  14243    277  -1066  -1949       C  
ATOM   4023  OE1 GLN C  30      56.361  44.164  46.500  1.00122.86           O  
ANISOU 4023  OE1 GLN C  30    15371  16486  14824    388  -1118  -2230       O  
ATOM   4024  NE2 GLN C  30      56.971  45.956  47.732  1.00109.25           N  
ANISOU 4024  NE2 GLN C  30    13139  15045  13327    293   -816  -1708       N  
ATOM   4025  N   ALA C  31      51.243  45.033  48.137  1.00110.23           N  
ANISOU 4025  N   ALA C  31    13084  14648  14151   -644  -2220  -1953       N  
ATOM   4026  CA  ALA C  31      49.998  44.307  47.836  1.00112.69           C  
ANISOU 4026  CA  ALA C  31    13371  14863  14582   -899  -2572  -2238       C  
ATOM   4027  C   ALA C  31      49.486  44.695  46.477  1.00118.00           C  
ANISOU 4027  C   ALA C  31    14141  15840  14853   -810  -2898  -2392       C  
ATOM   4028  O   ALA C  31      49.131  43.836  45.669  1.00125.14           O  
ANISOU 4028  O   ALA C  31    15247  16701  15597   -891  -3140  -2766       O  
ATOM   4029  CB  ALA C  31      48.939  44.588  48.888  1.00107.11           C  
ANISOU 4029  CB  ALA C  31    12268  14117  14308  -1173  -2639  -2105       C  
ATOM   4030  N   VAL C  32      49.457  45.999  46.218  1.00116.98           N  
ANISOU 4030  N   VAL C  32    13910  16003  14533   -634  -2909  -2105       N  
ATOM   4031  CA  VAL C  32      48.950  46.515  44.957  1.00117.96           C  
ANISOU 4031  CA  VAL C  32    14162  16439  14217   -484  -3240  -2166       C  
ATOM   4032  C   VAL C  32      49.814  46.083  43.752  1.00123.02           C  
ANISOU 4032  C   VAL C  32    15279  17155  14308   -292  -3172  -2362       C  
ATOM   4033  O   VAL C  32      49.273  45.760  42.700  1.00132.21           O  
ANISOU 4033  O   VAL C  32    16626  18488  15119   -268  -3528  -2638       O  
ATOM   4034  CB  VAL C  32      48.729  48.043  45.012  1.00112.67           C  
ANISOU 4034  CB  VAL C  32    13348  15981  13480   -301  -3235  -1761       C  
ATOM   4035  CG1 VAL C  32      48.498  48.612  43.623  1.00115.55           C  
ANISOU 4035  CG1 VAL C  32    13995  16647  13262    -46  -3516  -1741       C  
ATOM   4036  CG2 VAL C  32      47.553  48.363  45.921  1.00108.66           C  
ANISOU 4036  CG2 VAL C  32    12359  15470  13455   -462  -3420  -1697       C  
ATOM   4037  N   VAL C  33      51.143  46.016  43.926  1.00119.43           N  
ANISOU 4037  N   VAL C  33    14997  16601  13779   -160  -2721  -2266       N  
ATOM   4038  CA  VAL C  33      52.027  45.493  42.846  1.00121.95           C  
ANISOU 4038  CA  VAL C  33    15739  16990  13606     26  -2578  -2502       C  
ATOM   4039  C   VAL C  33      51.776  44.011  42.505  1.00125.65           C  
ANISOU 4039  C   VAL C  33    16408  17239  14093    -78  -2767  -3009       C  
ATOM   4040  O   VAL C  33      51.909  43.600  41.349  1.00127.74           O  
ANISOU 4040  O   VAL C  33    17029  17626  13878     32  -2867  -3311       O  
ATOM   4041  CB  VAL C  33      53.530  45.758  43.120  1.00118.62           C  
ANISOU 4041  CB  VAL C  33    15362  16564  13141    197  -2029  -2324       C  
ATOM   4042  CG1 VAL C  33      54.338  44.467  43.066  1.00119.64           C  
ANISOU 4042  CG1 VAL C  33    15675  16488  13293    291  -1842  -2674       C  
ATOM   4043  CG2 VAL C  33      54.078  46.772  42.127  1.00120.09           C  
ANISOU 4043  CG2 VAL C  33    15786  17065  12778    376  -1836  -2125       C  
ATOM   4044  N   PHE C  34      51.373  43.236  43.512  1.00127.92           N  
ANISOU 4044  N   PHE C  34    16503  17185  14916   -309  -2805  -3103       N  
ATOM   4045  CA  PHE C  34      51.103  41.802  43.350  1.00136.50           C  
ANISOU 4045  CA  PHE C  34    17806  17938  16116   -469  -2940  -3568       C  
ATOM   4046  C   PHE C  34      49.688  41.522  42.818  1.00145.78           C  
ANISOU 4046  C   PHE C  34    18907  19202  17278   -763  -3460  -3883       C  
ATOM   4047  O   PHE C  34      49.484  40.581  42.047  1.00155.15           O  
ANISOU 4047  O   PHE C  34    20388  20282  18279   -852  -3650  -4359       O  
ATOM   4048  CB  PHE C  34      51.337  41.071  44.677  1.00133.65           C  
ANISOU 4048  CB  PHE C  34    17345  17122  16311   -594  -2710  -3491       C  
ATOM   4049  CG  PHE C  34      50.576  39.787  44.814  1.00133.64           C  
ANISOU 4049  CG  PHE C  34    17479  16703  16594   -918  -2898  -3872       C  
ATOM   4050  CD1 PHE C  34      49.281  39.780  45.336  1.00131.59           C  
ANISOU 4050  CD1 PHE C  34    16903  16399  16694  -1335  -3153  -3885       C  
ATOM   4051  CD2 PHE C  34      51.164  38.579  44.465  1.00138.48           C  
ANISOU 4051  CD2 PHE C  34    18529  16937  17149   -821  -2780  -4228       C  
ATOM   4052  CE1 PHE C  34      48.584  38.597  45.473  1.00135.04           C  
ANISOU 4052  CE1 PHE C  34    17462  16426  17420  -1716  -3275  -4248       C  
ATOM   4053  CE2 PHE C  34      50.468  37.386  44.602  1.00142.78           C  
ANISOU 4053  CE2 PHE C  34    19260  17009  17981  -1167  -2917  -4586       C  
ATOM   4054  CZ  PHE C  34      49.176  37.396  45.102  1.00140.00           C  
ANISOU 4054  CZ  PHE C  34    18592  16618  17983  -1650  -3157  -4595       C  
ATOM   4055  N   VAL C  35      48.709  42.331  43.229  1.00144.72           N  
ANISOU 4055  N   VAL C  35    18357  19278  17352   -911  -3694  -3660       N  
ATOM   4056  CA  VAL C  35      47.367  42.230  42.634  1.00148.34           C  
ANISOU 4056  CA  VAL C  35    18641  19959  17762  -1136  -4234  -3964       C  
ATOM   4057  C   VAL C  35      47.417  42.682  41.157  1.00149.51           C  
ANISOU 4057  C   VAL C  35    19082  20534  17190   -855  -4515  -4085       C  
ATOM   4058  O   VAL C  35      46.401  42.899  40.530  1.00156.79           O  
ANISOU 4058  O   VAL C  35    19853  21783  17935   -911  -5015  -4261       O  
ATOM   4059  CB  VAL C  35      46.278  42.994  43.458  1.00146.19           C  
ANISOU 4059  CB  VAL C  35    17785  19843  17915  -1310  -4408  -3715       C  
ATOM   4060  CG1 VAL C  35      44.878  42.582  43.018  1.00148.85           C  
ANISOU 4060  CG1 VAL C  35    17840  20371  18345  -1620  -4948  -4134       C  
ATOM   4061  CG2 VAL C  35      46.435  42.702  44.940  1.00143.37           C  
ANISOU 4061  CG2 VAL C  35    17223  19098  18151  -1526  -4031  -3509       C  
ATOM   4062  N   PHE C  36      48.627  42.777  40.619  1.00144.42           N  
ANISOU 4062  N   PHE C  36    18854  19901  16117   -547  -4180  -4005       N  
ATOM   4063  CA  PHE C  36      48.823  42.988  39.205  1.00148.44           C  
ANISOU 4063  CA  PHE C  36    19764  20757  15880   -300  -4349  -4159       C  
ATOM   4064  C   PHE C  36      49.581  41.822  38.623  1.00156.42           C  
ANISOU 4064  C   PHE C  36    21234  21548  16650   -270  -4162  -4619       C  
ATOM   4065  O   PHE C  36      49.401  41.477  37.463  1.00168.66           O  
ANISOU 4065  O   PHE C  36    23124  23305  17652   -214  -4428  -5001       O  
ATOM   4066  CB  PHE C  36      49.613  44.262  38.966  1.00143.38           C  
ANISOU 4066  CB  PHE C  36    19245  20363  14869     42  -4039  -3645       C  
ATOM   4067  CG  PHE C  36      48.763  45.485  38.785  1.00140.59           C  
ANISOU 4067  CG  PHE C  36    18695  20345  14377    155  -4377  -3300       C  
ATOM   4068  CD1 PHE C  36      48.178  46.112  39.881  1.00133.52           C  
ANISOU 4068  CD1 PHE C  36    17308  19370  14053     49  -4403  -2987       C  
ATOM   4069  CD2 PHE C  36      48.578  46.041  37.518  1.00143.18           C  
ANISOU 4069  CD2 PHE C  36    19368  21064  13968    416  -4652  -3269       C  
ATOM   4070  CE1 PHE C  36      47.426  47.270  39.719  1.00131.63           C  
ANISOU 4070  CE1 PHE C  36    16903  19407  13703    230  -4694  -2667       C  
ATOM   4071  CE2 PHE C  36      47.815  47.190  37.352  1.00142.57           C  
ANISOU 4071  CE2 PHE C  36    19155  21261  13754    605  -4976  -2911       C  
ATOM   4072  CZ  PHE C  36      47.241  47.805  38.455  1.00136.73           C  
ANISOU 4072  CZ  PHE C  36    17902  20410  13639    526  -4995  -2617       C  
ATOM   4073  N   ASN C  37      50.440  41.218  39.436  1.00158.18           N  
ANISOU 4073  N   ASN C  37    21479  21357  17264   -271  -3712  -4591       N  
ATOM   4074  CA  ASN C  37      51.326  40.151  38.974  1.00168.24           C  
ANISOU 4074  CA  ASN C  37    23190  22378  18354   -140  -3451  -4990       C  
ATOM   4075  C   ASN C  37      51.295  38.912  39.880  1.00170.79           C  
ANISOU 4075  C   ASN C  37    23509  22095  19287   -359  -3350  -5225       C  
ATOM   4076  O   ASN C  37      52.269  38.638  40.583  1.00173.36           O  
ANISOU 4076  O   ASN C  37    23859  22141  19868   -172  -2926  -5062       O  
ATOM   4077  CB  ASN C  37      52.766  40.676  38.861  1.00167.25           C  
ANISOU 4077  CB  ASN C  37    23197  22385  17962    243  -2901  -4707       C  
ATOM   4078  CG  ASN C  37      53.237  40.808  37.423  1.00173.54           C  
ANISOU 4078  CG  ASN C  37    24439  23536  17961    491  -2845  -4923       C  
ATOM   4079  OD1 ASN C  37      54.423  41.004  37.169  1.00175.27           O  
ANISOU 4079  OD1 ASN C  37    24804  23860  17930    768  -2360  -4830       O  
ATOM   4080  ND2 ASN C  37      52.309  40.698  36.475  1.00177.48           N  
ANISOU 4080  ND2 ASN C  37    25137  24256  18039    387  -3336  -5231       N  
ATOM   4081  N   PRO C  38      50.184  38.142  39.851  1.00174.28           N  
ANISOU 4081  N   PRO C  38    23934  22330  19953   -755  -3741  -5618       N  
ATOM   4082  CA  PRO C  38      50.083  37.019  40.790  1.00174.22           C  
ANISOU 4082  CA  PRO C  38    23966  21678  20550  -1015  -3605  -5770       C  
ATOM   4083  C   PRO C  38      51.172  35.975  40.529  1.00179.59           C  
ANISOU 4083  C   PRO C  38    25165  21936  21136   -738  -3263  -6074       C  
ATOM   4084  O   PRO C  38      51.585  35.255  41.448  1.00172.09           O  
ANISOU 4084  O   PRO C  38    24302  20445  20637   -723  -2988  -5997       O  
ATOM   4085  CB  PRO C  38      48.691  36.429  40.490  1.00177.92           C  
ANISOU 4085  CB  PRO C  38    24357  22081  21162  -1534  -4093  -6235       C  
ATOM   4086  CG  PRO C  38      47.992  37.450  39.642  1.00178.17           C  
ANISOU 4086  CG  PRO C  38    24150  22803  20742  -1498  -4531  -6204       C  
ATOM   4087  CD  PRO C  38      49.072  38.148  38.889  1.00177.52           C  
ANISOU 4087  CD  PRO C  38    24346  23064  20039   -976  -4301  -5997       C  
ATOM   4088  N   ASP C  39      51.645  35.934  39.282  1.00191.06           N  
ANISOU 4088  N   ASP C  39    26970  23652  21971   -476  -3270  -6398       N  
ATOM   4089  CA  ASP C  39      52.635  34.958  38.821  1.00199.40           C  
ANISOU 4089  CA  ASP C  39    28532  24374  22857   -166  -2957  -6786       C  
ATOM   4090  C   ASP C  39      53.939  34.964  39.636  1.00196.71           C  
ANISOU 4090  C   ASP C  39    28137  23841  22763    259  -2429  -6424       C  
ATOM   4091  O   ASP C  39      54.400  33.907  40.069  1.00202.09           O  
ANISOU 4091  O   ASP C  39    29085  23943  23758    386  -2223  -6611       O  
ATOM   4092  CB  ASP C  39      52.926  35.155  37.320  1.00206.55           C  
ANISOU 4092  CB  ASP C  39    29777  25739  22961     63  -3017  -7137       C  
ATOM   4093  CG  ASP C  39      52.950  36.636  36.906  1.00206.03           C  
ANISOU 4093  CG  ASP C  39    29452  26389  22439    203  -3067  -6680       C  
ATOM   4094  OD1 ASP C  39      52.384  37.485  37.638  1.00200.67           O  
ANISOU 4094  OD1 ASP C  39    28318  25864  22063     30  -3214  -6207       O  
ATOM   4095  OD2 ASP C  39      53.528  36.943  35.841  1.00209.69           O  
ANISOU 4095  OD2 ASP C  39    30209  27235  22228    488  -2932  -6798       O  
ATOM   4096  N   SER C  40      54.529  36.147  39.835  1.00189.72           N  
ANISOU 4096  N   SER C  40    26913  23433  21737    484  -2226  -5923       N  
ATOM   4097  CA  SER C  40      55.700  36.285  40.719  1.00182.70           C  
ANISOU 4097  CA  SER C  40    25836  22461  21120    836  -1785  -5566       C  
ATOM   4098  C   SER C  40      55.271  36.523  42.171  1.00176.29           C  
ANISOU 4098  C   SER C  40    24644  21432  20905    609  -1839  -5116       C  
ATOM   4099  O   SER C  40      55.492  37.599  42.744  1.00173.70           O  
ANISOU 4099  O   SER C  40    23915  21438  20644    636  -1737  -4644       O  
ATOM   4100  CB  SER C  40      56.655  37.384  40.226  1.00177.92           C  
ANISOU 4100  CB  SER C  40    25062  22454  20084   1145  -1475  -5309       C  
ATOM   4101  OG  SER C  40      55.952  38.554  39.847  1.00174.94           O  
ANISOU 4101  OG  SER C  40    24504  22534  19431    922  -1705  -5047       O  
ATOM   4102  N   TRP C  41      54.634  35.507  42.746  1.00175.30           N  
ANISOU 4102  N   TRP C  41    24686  20724  21194    355  -1979  -5285       N  
ATOM   4103  CA  TRP C  41      54.191  35.539  44.130  1.00169.45           C  
ANISOU 4103  CA  TRP C  41    23680  19711  20992    119  -1992  -4901       C  
ATOM   4104  C   TRP C  41      55.385  35.461  45.077  1.00162.93           C  
ANISOU 4104  C   TRP C  41    22781  18750  20372    545  -1638  -4579       C  
ATOM   4105  O   TRP C  41      55.310  35.919  46.213  1.00155.10           O  
ANISOU 4105  O   TRP C  41    21479  17770  19679    462  -1594  -4148       O  
ATOM   4106  CB  TRP C  41      53.240  34.372  44.400  1.00174.36           C  
ANISOU 4106  CB  TRP C  41    24581  19699  21965   -295  -2170  -5200       C  
ATOM   4107  CG  TRP C  41      53.932  33.026  44.390  1.00182.07           C  
ANISOU 4107  CG  TRP C  41    26102  20026  23051    -23  -1961  -5503       C  
ATOM   4108  CD1 TRP C  41      54.331  32.312  43.289  1.00191.04           C  
ANISOU 4108  CD1 TRP C  41    27686  21024  23875    193  -1932  -6039       C  
ATOM   4109  CD2 TRP C  41      54.327  32.257  45.530  1.00181.68           C  
ANISOU 4109  CD2 TRP C  41    26241  19364  23422    118  -1744  -5281       C  
ATOM   4110  NE1 TRP C  41      54.945  31.143  43.678  1.00195.52           N  
ANISOU 4110  NE1 TRP C  41    28701  20898  24691    476  -1703  -6176       N  
ATOM   4111  CE2 TRP C  41      54.951  31.080  45.047  1.00189.09           C  
ANISOU 4111  CE2 TRP C  41    27753  19773  24320    447  -1599  -5695       C  
ATOM   4112  CE3 TRP C  41      54.211  32.441  46.911  1.00175.92           C  
ANISOU 4112  CE3 TRP C  41    25294  18476  23067     24  -1659  -4772       C  
ATOM   4113  CZ2 TRP C  41      55.456  30.090  45.902  1.00188.73           C  
ANISOU 4113  CZ2 TRP C  41    28078  19015  24614    720  -1391  -5580       C  
ATOM   4114  CZ3 TRP C  41      54.713  31.451  47.761  1.00179.11           C  
ANISOU 4114  CZ3 TRP C  41    26080  18212  23762    269  -1458  -4649       C  
ATOM   4115  CH2 TRP C  41      55.328  30.293  47.249  1.00182.91           C  
ANISOU 4115  CH2 TRP C  41    27141  18146  24211    631  -1336  -5035       C  
ATOM   4116  N   LEU C  42      56.485  34.880  44.594  1.00155.79           N  
ANISOU 4116  N   LEU C  42    21136  17375  20682  -3237  -3215  -4556       N  
ATOM   4117  CA  LEU C  42      57.665  34.640  45.424  1.00153.32           C  
ANISOU 4117  CA  LEU C  42    21178  16427  20648  -2750  -3005  -4303       C  
ATOM   4118  C   LEU C  42      58.289  35.936  45.857  1.00146.60           C  
ANISOU 4118  C   LEU C  42    19942  15977  19780  -2119  -2964  -3968       C  
ATOM   4119  O   LEU C  42      58.356  36.227  47.051  1.00142.05           O  
ANISOU 4119  O   LEU C  42    19219  15392  19359  -2014  -2879  -3578       O  
ATOM   4120  CB  LEU C  42      58.706  33.793  44.682  1.00153.94           C  
ANISOU 4120  CB  LEU C  42    21896  15827  20766  -2494  -2889  -4611       C  
ATOM   4121  CG  LEU C  42      58.890  32.318  45.057  1.00156.66           C  
ANISOU 4121  CG  LEU C  42    22928  15261  21334  -2770  -2722  -4689       C  
ATOM   4122  CD1 LEU C  42      60.343  31.936  44.863  1.00155.70           C  
ANISOU 4122  CD1 LEU C  42    23297  14554  21306  -2097  -2513  -4697       C  
ATOM   4123  CD2 LEU C  42      58.453  32.019  46.484  1.00154.19           C  
ANISOU 4123  CD2 LEU C  42    22553  14765  21266  -3036  -2645  -4280       C  
ATOM   4124  N   ALA C  43      58.747  36.715  44.877  1.00144.75           N  
ANISOU 4124  N   ALA C  43    19567  16092  19338  -1725  -3018  -4127       N  
ATOM   4125  CA  ALA C  43      59.385  37.999  45.132  1.00141.92           C  
ANISOU 4125  CA  ALA C  43    18896  16101  18923  -1158  -2968  -3854       C  
ATOM   4126  C   ALA C  43      58.475  38.945  45.922  1.00142.16           C  
ANISOU 4126  C   ALA C  43    18418  16689  18904  -1270  -3000  -3538       C  
ATOM   4127  O   ALA C  43      58.954  39.784  46.695  1.00143.44           O  
ANISOU 4127  O   ALA C  43    18433  16961  19107   -918  -2900  -3222       O  
ATOM   4128  CB  ALA C  43      59.829  38.642  43.826  1.00141.76           C  
ANISOU 4128  CB  ALA C  43    18801  16403  18654   -814  -3029  -4098       C  
ATOM   4129  N   SER C  44      57.165  38.796  45.756  1.00141.86           N  
ANISOU 4129  N   SER C  44    18123  17021  18756  -1771  -3126  -3617       N  
ATOM   4130  CA  SER C  44      56.242  39.620  46.517  1.00136.21           C  
ANISOU 4130  CA  SER C  44    16928  16849  17977  -1848  -3129  -3298       C  
ATOM   4131  C   SER C  44      56.120  39.211  47.980  1.00133.88           C  
ANISOU 4131  C   SER C  44    16691  16249  17927  -2026  -3024  -2977       C  
ATOM   4132  O   SER C  44      56.049  40.070  48.844  1.00132.80           O  
ANISOU 4132  O   SER C  44    16306  16364  17788  -1800  -2936  -2651       O  
ATOM   4133  CB  SER C  44      54.897  39.739  45.836  1.00134.79           C  
ANISOU 4133  CB  SER C  44    16348  17325  17539  -2250  -3292  -3427       C  
ATOM   4134  OG  SER C  44      54.907  40.868  44.992  1.00127.91           O  
ANISOU 4134  OG  SER C  44    15182  17014  16401  -1847  -3324  -3451       O  
ATOM   4135  N   VAL C  45      56.154  37.904  48.256  1.00133.26           N  
ANISOU 4135  N   VAL C  45    16991  15592  18050  -2407  -3009  -3068       N  
ATOM   4136  CA  VAL C  45      56.356  37.424  49.636  1.00129.10           C  
ANISOU 4136  CA  VAL C  45    16618  14653  17781  -2471  -2876  -2744       C  
ATOM   4137  C   VAL C  45      57.725  37.897  50.140  1.00127.56           C  
ANISOU 4137  C   VAL C  45    16579  14205  17680  -1854  -2733  -2542       C  
ATOM   4138  O   VAL C  45      57.856  38.347  51.273  1.00128.46           O  
ANISOU 4138  O   VAL C  45    16555  14391  17863  -1713  -2638  -2193       O  
ATOM   4139  CB  VAL C  45      56.267  35.877  49.750  1.00126.63           C  
ANISOU 4139  CB  VAL C  45    16781  13666  17667  -2946  -2847  -2879       C  
ATOM   4140  CG1 VAL C  45      56.760  35.418  51.100  1.00124.55           C  
ANISOU 4140  CG1 VAL C  45    16726  12931  17664  -2854  -2680  -2514       C  
ATOM   4141  CG2 VAL C  45      54.848  35.414  49.559  1.00130.63           C  
ANISOU 4141  CG2 VAL C  45    17091  14466  18077  -3675  -2979  -2999       C  
ATOM   4142  N   ALA C  46      58.733  37.818  49.273  1.00123.29           N  
ANISOU 4142  N   ALA C  46    16306  13429  17107  -1504  -2720  -2763       N  
ATOM   4143  CA  ALA C  46      60.087  38.201  49.641  1.00113.23           C  
ANISOU 4143  CA  ALA C  46    15159  11978  15885   -951  -2596  -2580       C  
ATOM   4144  C   ALA C  46      60.177  39.680  50.008  1.00107.07           C  
ANISOU 4144  C   ALA C  46    13990  11738  14950   -654  -2577  -2360       C  
ATOM   4145  O   ALA C  46      61.019  40.064  50.801  1.00108.41           O  
ANISOU 4145  O   ALA C  46    14177  11852  15161   -364  -2470  -2100       O  
ATOM   4146  CB  ALA C  46      61.077  37.851  48.532  1.00110.33           C  
ANISOU 4146  CB  ALA C  46    15110  11338  15472   -635  -2584  -2864       C  
ATOM   4147  N   ALA C  47      59.295  40.502  49.452  1.00101.98           N  
ANISOU 4147  N   ALA C  47    13012  11627  14108   -736  -2666  -2451       N  
ATOM   4148  CA  ALA C  47      59.263  41.911  49.823  1.00 96.77           C  
ANISOU 4148  CA  ALA C  47    12051  11426  13291   -462  -2604  -2238       C  
ATOM   4149  C   ALA C  47      58.529  42.127  51.131  1.00 95.22           C  
ANISOU 4149  C   ALA C  47    11659  11372  13148   -653  -2536  -1923       C  
ATOM   4150  O   ALA C  47      59.109  42.609  52.087  1.00 95.01           O  
ANISOU 4150  O   ALA C  47    11654  11296  13147   -461  -2417  -1673       O  
ATOM   4151  CB  ALA C  47      58.653  42.740  48.724  1.00101.23           C  
ANISOU 4151  CB  ALA C  47    12357  12501  13604   -380  -2683  -2409       C  
ATOM   4152  N   VAL C  48      57.266  41.716  51.185  1.00 98.65           N  
ANISOU 4152  N   VAL C  48    11900  12002  13578  -1063  -2611  -1936       N  
ATOM   4153  CA  VAL C  48      56.460  41.836  52.415  1.00103.72           C  
ANISOU 4153  CA  VAL C  48    12329  12819  14259  -1267  -2542  -1627       C  
ATOM   4154  C   VAL C  48      57.184  41.352  53.692  1.00108.69           C  
ANISOU 4154  C   VAL C  48    13185  13013  15096  -1250  -2428  -1374       C  
ATOM   4155  O   VAL C  48      57.273  42.094  54.675  1.00109.58           O  
ANISOU 4155  O   VAL C  48    13186  13288  15161  -1089  -2312  -1107       O  
ATOM   4156  CB  VAL C  48      55.089  41.148  52.277  1.00104.05           C  
ANISOU 4156  CB  VAL C  48    12159  13086  14290  -1800  -2652  -1679       C  
ATOM   4157  CG1 VAL C  48      54.396  41.043  53.629  1.00102.45           C  
ANISOU 4157  CG1 VAL C  48    11784  12978  14162  -2029  -2568  -1340       C  
ATOM   4158  CG2 VAL C  48      54.232  41.924  51.309  1.00105.80           C  
ANISOU 4158  CG2 VAL C  48    12010  13958  14231  -1757  -2736  -1795       C  
ATOM   4159  N   THR C  49      57.673  40.109  53.681  1.00113.21           N  
ANISOU 4159  N   THR C  49    14092  13044  15878  -1409  -2445  -1450       N  
ATOM   4160  CA  THR C  49      58.656  39.672  54.677  1.00109.64           C  
ANISOU 4160  CA  THR C  49    13884  12182  15592  -1251  -2328  -1210       C  
ATOM   4161  C   THR C  49      59.971  40.210  54.204  1.00108.27           C  
ANISOU 4161  C   THR C  49    13839  11956  15340   -775  -2295  -1279       C  
ATOM   4162  O   THR C  49      60.512  39.725  53.239  1.00116.71           O  
ANISOU 4162  O   THR C  49    15130  12781  16432   -664  -2337  -1522       O  
ATOM   4163  CB  THR C  49      58.756  38.120  54.789  1.00110.70           C  
ANISOU 4163  CB  THR C  49    14383  11710  15968  -1522  -2315  -1238       C  
ATOM   4164  OG1 THR C  49      59.264  37.568  53.568  1.00110.74           O  
ANISOU 4164  OG1 THR C  49    14682  11408  15983  -1435  -2365  -1579       O  
ATOM   4165  CG2 THR C  49      57.399  37.499  55.091  1.00115.65           C  
ANISOU 4165  CG2 THR C  49    14896  12387  16657  -2098  -2363  -1211       C  
ATOM   4166  N   GLY C  50      60.456  41.255  54.835  1.00104.37           N  
ANISOU 4166  N   GLY C  50    13207  11726  14722   -516  -2214  -1079       N  
ATOM   4167  CA  GLY C  50      61.650  41.900  54.358  1.00101.40           C  
ANISOU 4167  CA  GLY C  50    12905  11394  14226   -123  -2187  -1137       C  
ATOM   4168  C   GLY C  50      61.510  43.360  54.534  1.00 99.09           C  
ANISOU 4168  C   GLY C  50    12401  11539  13710     12  -2132  -1069       C  
ATOM   4169  O   GLY C  50      62.399  44.014  55.061  1.00103.74           O  
ANISOU 4169  O   GLY C  50    13015  12204  14197    206  -2048   -922       O  
ATOM   4170  N   ILE C  51      60.367  43.884  54.120  1.00100.69           N  
ANISOU 4170  N   ILE C  51    12398  12048  13810    -98  -2165  -1163       N  
ATOM   4171  CA  ILE C  51      59.964  45.217  54.542  1.00104.35           C  
ANISOU 4171  CA  ILE C  51    12690  12888  14068     17  -2056  -1035       C  
ATOM   4172  C   ILE C  51      59.694  45.186  56.036  1.00106.69           C  
ANISOU 4172  C   ILE C  51    12943  13187  14405   -131  -1955   -742       C  
ATOM   4173  O   ILE C  51      60.207  46.018  56.778  1.00110.49           O  
ANISOU 4173  O   ILE C  51    13467  13756  14755      0  -1830   -593       O  
ATOM   4174  CB  ILE C  51      58.740  45.733  53.764  1.00102.28           C  
ANISOU 4174  CB  ILE C  51    12190  13007  13666     -6  -2091  -1148       C  
ATOM   4175  CG1 ILE C  51      59.185  46.306  52.422  1.00103.94           C  
ANISOU 4175  CG1 ILE C  51    12434  13325  13733    259  -2131  -1376       C  
ATOM   4176  CG2 ILE C  51      58.030  46.816  54.547  1.00105.11           C  
ANISOU 4176  CG2 ILE C  51    12386  13697  13852     75  -1932   -933       C  
ATOM   4177  CD1 ILE C  51      58.108  46.295  51.358  1.00109.69           C  
ANISOU 4177  CD1 ILE C  51    12937  14384  14357    190  -2236  -1544       C  
ATOM   4178  N   LEU C  52      58.961  44.168  56.486  1.00108.14           N  
ANISOU 4178  N   LEU C  52    13071  13255  14762   -438  -2006   -664       N  
ATOM   4179  CA  LEU C  52      58.806  43.932  57.908  1.00105.92           C  
ANISOU 4179  CA  LEU C  52    12766  12936  14541   -587  -1918   -370       C  
ATOM   4180  C   LEU C  52      60.144  43.674  58.625  1.00109.95           C  
ANISOU 4180  C   LEU C  52    13480  13191  15104   -459  -1867   -217       C  
ATOM   4181  O   LEU C  52      60.366  44.204  59.717  1.00103.92           O  
ANISOU 4181  O   LEU C  52    12689  12562  14234   -433  -1758      2       O  
ATOM   4182  CB  LEU C  52      57.786  42.823  58.193  1.00106.00           C  
ANISOU 4182  CB  LEU C  52    12689  12855  14729   -976  -1979   -305       C  
ATOM   4183  CG  LEU C  52      56.348  43.354  58.196  1.00106.95           C  
ANISOU 4183  CG  LEU C  52    12482  13440  14713  -1118  -1966   -266       C  
ATOM   4184  CD1 LEU C  52      55.618  42.929  56.938  1.00108.22           C  
ANISOU 4184  CD1 LEU C  52    12531  13711  14876  -1304  -2117   -524       C  
ATOM   4185  CD2 LEU C  52      55.579  42.934  59.439  1.00103.97           C  
ANISOU 4185  CD2 LEU C  52    11966  13140  14398  -1395  -1899     24       C  
ATOM   4186  N   CYS C  53      61.048  42.901  58.003  1.00112.16           N  
ANISOU 4186  N   CYS C  53    13954  13151  15508   -357  -1934   -327       N  
ATOM   4187  CA  CYS C  53      62.343  42.645  58.639  1.00105.37           C  
ANISOU 4187  CA  CYS C  53    13233  12141  14662   -186  -1881   -138       C  
ATOM   4188  C   CYS C  53      63.031  43.952  58.997  1.00102.47           C  
ANISOU 4188  C   CYS C  53    12806  12094  14032    -13  -1804    -74       C  
ATOM   4189  O   CYS C  53      63.257  44.233  60.169  1.00110.82           O  
ANISOU 4189  O   CYS C  53    13825  13282  14998    -67  -1721    166       O  
ATOM   4190  CB  CYS C  53      63.253  41.787  57.781  1.00105.10           C  
ANISOU 4190  CB  CYS C  53    13409  11777  14745     -2  -1932   -268       C  
ATOM   4191  SG  CYS C  53      64.867  41.452  58.563  1.00117.95           S  
ANISOU 4191  SG  CYS C  53    15133  13336  16344    273  -1853     35       S  
ATOM   4192  N   VAL C  54      63.319  44.769  57.995  1.00 95.40           N  
ANISOU 4192  N   VAL C  54    11919  11332  12995    158  -1822   -295       N  
ATOM   4193  CA  VAL C  54      64.091  45.994  58.216  1.00 90.25           C  
ANISOU 4193  CA  VAL C  54    11277  10929  12082    283  -1736   -260       C  
ATOM   4194  C   VAL C  54      63.360  47.080  59.023  1.00 88.61           C  
ANISOU 4194  C   VAL C  54    11015  10964  11688    178  -1607   -175       C  
ATOM   4195  O   VAL C  54      63.983  47.816  59.779  1.00 89.29           O  
ANISOU 4195  O   VAL C  54    11157  11196  11572    159  -1509    -63       O  
ATOM   4196  CB  VAL C  54      64.617  46.585  56.910  1.00 86.22           C  
ANISOU 4196  CB  VAL C  54    10816  10478  11465    491  -1769   -498       C  
ATOM   4197  CG1 VAL C  54      65.526  45.571  56.210  1.00 83.72           C  
ANISOU 4197  CG1 VAL C  54    10580   9943  11283    647  -1861   -561       C  
ATOM   4198  CG2 VAL C  54      63.454  47.013  56.022  1.00 81.32           C  
ANISOU 4198  CG2 VAL C  54    10124   9945  10828    497  -1788   -702       C  
ATOM   4199  N   VAL C  55      62.051  47.173  58.884  1.00 85.09           N  
ANISOU 4199  N   VAL C  55    10463  10586  11280    106  -1593   -223       N  
ATOM   4200  CA  VAL C  55      61.310  48.132  59.701  1.00 83.23           C  
ANISOU 4200  CA  VAL C  55    10189  10572  10859     67  -1434   -114       C  
ATOM   4201  C   VAL C  55      61.441  47.755  61.187  1.00 87.10           C  
ANISOU 4201  C   VAL C  55    10673  11061  11359   -109  -1377    147       C  
ATOM   4202  O   VAL C  55      61.651  48.616  62.037  1.00 87.03           O  
ANISOU 4202  O   VAL C  55    10744  11197  11124   -127  -1234    239       O  
ATOM   4203  CB  VAL C  55      59.833  48.277  59.231  1.00 82.05           C  
ANISOU 4203  CB  VAL C  55     9863  10588  10721     69  -1422   -171       C  
ATOM   4204  CG1 VAL C  55      58.923  48.771  60.351  1.00 78.05           C  
ANISOU 4204  CG1 VAL C  55     9275  10286  10092      7  -1258     25       C  
ATOM   4205  CG2 VAL C  55      59.760  49.203  58.025  1.00 77.89           C  
ANISOU 4205  CG2 VAL C  55     9363  10186  10043    311  -1394   -369       C  
ATOM   4206  N   PHE C  56      61.419  46.451  61.467  1.00 91.40           N  
ANISOU 4206  N   PHE C  56    11161  11419  12145   -242  -1481    262       N  
ATOM   4207  CA  PHE C  56      61.607  45.933  62.834  1.00 95.14           C  
ANISOU 4207  CA  PHE C  56    11618  11886  12644   -389  -1437    548       C  
ATOM   4208  C   PHE C  56      63.034  46.135  63.389  1.00 99.55           C  
ANISOU 4208  C   PHE C  56    12271  12500  13051   -326  -1416    664       C  
ATOM   4209  O   PHE C  56      63.198  46.430  64.583  1.00102.55           O  
ANISOU 4209  O   PHE C  56    12639  13054  13269   -431  -1327    863       O  
ATOM   4210  CB  PHE C  56      61.215  44.457  62.911  1.00 93.72           C  
ANISOU 4210  CB  PHE C  56    11399  11444  12766   -537  -1529    656       C  
ATOM   4211  CG  PHE C  56      59.744  44.229  62.988  1.00 98.00           C  
ANISOU 4211  CG  PHE C  56    11784  12057  13392   -738  -1524    672       C  
ATOM   4212  CD1 PHE C  56      58.893  44.789  62.059  1.00101.77           C  
ANISOU 4212  CD1 PHE C  56    12157  12699  13810   -704  -1544    460       C  
ATOM   4213  CD2 PHE C  56      59.205  43.448  63.991  1.00105.71           C  
ANISOU 4213  CD2 PHE C  56    12688  12990  14485   -961  -1495    929       C  
ATOM   4214  CE1 PHE C  56      57.522  44.574  62.126  1.00105.25           C  
ANISOU 4214  CE1 PHE C  56    12388  13312  14290   -898  -1544    507       C  
ATOM   4215  CE2 PHE C  56      57.838  43.231  64.069  1.00106.24           C  
ANISOU 4215  CE2 PHE C  56    12569  13189  14606  -1182  -1491    967       C  
ATOM   4216  CZ  PHE C  56      56.996  43.795  63.132  1.00106.76           C  
ANISOU 4216  CZ  PHE C  56    12496  13472  14595  -1155  -1520    756       C  
ATOM   4217  N   VAL C  57      64.060  45.961  62.537  1.00 93.59           N  
ANISOU 4217  N   VAL C  57    11587  11651  12321   -165  -1497    553       N  
ATOM   4218  CA  VAL C  57      65.445  46.326  62.919  1.00 90.79           C  
ANISOU 4218  CA  VAL C  57    11267  11472  11756   -109  -1481    656       C  
ATOM   4219  C   VAL C  57      65.531  47.822  63.290  1.00 88.41           C  
ANISOU 4219  C   VAL C  57    11035  11442  11111   -200  -1358    582       C  
ATOM   4220  O   VAL C  57      66.093  48.188  64.328  1.00 87.32           O  
ANISOU 4220  O   VAL C  57    10903  11528  10747   -338  -1295    743       O  
ATOM   4221  CB  VAL C  57      66.480  45.980  61.811  1.00 86.11           C  
ANISOU 4221  CB  VAL C  57    10712  10787  11217    111  -1573    543       C  
ATOM   4222  CG1 VAL C  57      67.808  46.669  62.075  1.00 81.11           C  
ANISOU 4222  CG1 VAL C  57    10065  10462  10290    129  -1549    622       C  
ATOM   4223  CG2 VAL C  57      66.683  44.488  61.728  1.00 84.23           C  
ANISOU 4223  CG2 VAL C  57    10485  10263  11255    219  -1639    674       C  
ATOM   4224  N   GLY C  58      64.925  48.668  62.465  1.00 85.06           N  
ANISOU 4224  N   GLY C  58    10686  10997  10634   -131  -1307    346       N  
ATOM   4225  CA  GLY C  58      64.915  50.101  62.717  1.00 88.28           C  
ANISOU 4225  CA  GLY C  58    11249  11566  10725   -187  -1143    260       C  
ATOM   4226  C   GLY C  58      64.311  50.406  64.059  1.00 94.05           C  
ANISOU 4226  C   GLY C  58    12004  12413  11317   -353  -1007    411       C  
ATOM   4227  O   GLY C  58      64.788  51.280  64.777  1.00 97.33           O  
ANISOU 4227  O   GLY C  58    12573  12980  11427   -495   -882    425       O  
ATOM   4228  N   LYS C  59      63.256  49.665  64.400  1.00101.41           N  
ANISOU 4228  N   LYS C  59    12789  13284  12455   -364  -1026    522       N  
ATOM   4229  CA  LYS C  59      62.593  49.774  65.705  1.00102.48           C  
ANISOU 4229  CA  LYS C  59    12902  13549  12484   -504   -901    702       C  
ATOM   4230  C   LYS C  59      63.425  49.140  66.828  1.00102.82           C  
ANISOU 4230  C   LYS C  59    12886  13698  12481   -671   -951    948       C  
ATOM   4231  O   LYS C  59      63.280  49.490  68.008  1.00100.08           O  
ANISOU 4231  O   LYS C  59    12571  13531  11923   -816   -833   1081       O  
ATOM   4232  CB  LYS C  59      61.214  49.116  65.644  1.00100.10           C  
ANISOU 4232  CB  LYS C  59    12417  13201  12416   -487   -919    769       C  
ATOM   4233  CG  LYS C  59      60.072  50.082  65.425  1.00 99.61           C  
ANISOU 4233  CG  LYS C  59    12378  13253  12215   -360   -749    675       C  
ATOM   4234  CD  LYS C  59      59.951  51.016  66.596  1.00 99.50           C  
ANISOU 4234  CD  LYS C  59    12524  13396  11883   -406   -519    756       C  
ATOM   4235  CE  LYS C  59      58.528  51.102  67.089  1.00100.11           C  
ANISOU 4235  CE  LYS C  59    12462  13635  11938   -349   -379    881       C  
ATOM   4236  NZ  LYS C  59      58.413  52.229  68.058  1.00102.80           N  
ANISOU 4236  NZ  LYS C  59    13048  14095  11916   -319   -101    899       N  
ATOM   4237  N   GLY C  60      64.291  48.208  66.449  1.00102.76           N  
ANISOU 4237  N   GLY C  60    12796  13601  12647   -620  -1109   1021       N  
ATOM   4238  CA  GLY C  60      65.104  47.488  67.403  1.00101.70           C  
ANISOU 4238  CA  GLY C  60    12569  13594  12479   -703  -1157   1305       C  
ATOM   4239  C   GLY C  60      64.348  46.335  68.019  1.00101.75           C  
ANISOU 4239  C   GLY C  60    12451  13469  12741   -742  -1178   1545       C  
ATOM   4240  O   GLY C  60      64.710  45.872  69.086  1.00104.14           O  
ANISOU 4240  O   GLY C  60    12676  13916  12973   -824  -1165   1829       O  
ATOM   4241  N   LYS C  61      63.279  45.887  67.344  1.00 99.52           N  
ANISOU 4241  N   LYS C  61    12142  12940  12729   -711  -1206   1439       N  
ATOM   4242  CA  LYS C  61      62.477  44.725  67.792  1.00 99.33           C  
ANISOU 4242  CA  LYS C  61    12020  12750  12971   -811  -1227   1649       C  
ATOM   4243  C   LYS C  61      63.144  43.395  67.447  1.00102.44           C  
ANISOU 4243  C   LYS C  61    12449  12842  13630   -720  -1329   1772       C  
ATOM   4244  O   LYS C  61      63.696  43.228  66.351  1.00105.20           O  
ANISOU 4244  O   LYS C  61    12883  13014  14073   -559  -1408   1583       O  
ATOM   4245  CB  LYS C  61      61.094  44.764  67.167  1.00 96.23           C  
ANISOU 4245  CB  LYS C  61    11566  12275  12721   -870  -1224   1487       C  
ATOM   4246  CG  LYS C  61      60.252  45.926  67.622  1.00 99.67           C  
ANISOU 4246  CG  LYS C  61    11961  12998  12908   -896  -1077   1442       C  
ATOM   4247  CD  LYS C  61      58.787  45.696  67.316  1.00100.58           C  
ANISOU 4247  CD  LYS C  61    11915  13141  13159   -972  -1068   1422       C  
ATOM   4248  CE  LYS C  61      57.927  46.692  68.068  1.00106.06           C  
ANISOU 4248  CE  LYS C  61    12550  14154  13591   -952   -876   1485       C  
ATOM   4249  NZ  LYS C  61      56.862  46.012  68.861  1.00113.15           N  
ANISOU 4249  NZ  LYS C  61    13237  15170  14582  -1139   -841   1738       N  
ATOM   4250  N   ILE C  62      63.045  42.434  68.363  1.00104.06           N  
ANISOU 4250  N   ILE C  62    12615  12969  13952   -802  -1303   2096       N  
ATOM   4251  CA  ILE C  62      63.785  41.163  68.246  1.00104.95           C  
ANISOU 4251  CA  ILE C  62    12815  12779  14279   -661  -1340   2290       C  
ATOM   4252  C   ILE C  62      63.195  40.205  67.222  1.00107.46           C  
ANISOU 4252  C   ILE C  62    13275  12615  14939   -685  -1393   2125       C  
ATOM   4253  O   ILE C  62      63.907  39.346  66.676  1.00110.25           O  
ANISOU 4253  O   ILE C  62    13790  12647  15449   -492  -1412   2147       O  
ATOM   4254  CB  ILE C  62      63.879  40.434  69.591  1.00105.10           C  
ANISOU 4254  CB  ILE C  62    12776  12857  14299   -719  -1266   2732       C  
ATOM   4255  CG1 ILE C  62      64.733  39.180  69.441  1.00104.88           C  
ANISOU 4255  CG1 ILE C  62    12879  12507  14463   -484  -1262   2963       C  
ATOM   4256  CG2 ILE C  62      62.484  40.100  70.122  1.00104.09           C  
ANISOU 4256  CG2 ILE C  62    12593  12646  14309  -1000  -1216   2820       C  
ATOM   4257  CD1 ILE C  62      65.767  39.029  70.517  1.00106.51           C  
ANISOU 4257  CD1 ILE C  62    12974  13036  14456   -331  -1211   3374       C  
ATOM   4258  N   SER C  63      61.892  40.344  66.979  1.00108.14           N  
ANISOU 4258  N   SER C  63    13302  12676  15109   -925  -1405   1969       N  
ATOM   4259  CA  SER C  63      61.169  39.470  66.056  1.00110.75           C  
ANISOU 4259  CA  SER C  63    13746  12617  15718  -1066  -1465   1792       C  
ATOM   4260  C   SER C  63      61.433  39.818  64.624  1.00106.26           C  
ANISOU 4260  C   SER C  63    13257  11965  15150   -919  -1557   1407       C  
ATOM   4261  O   SER C  63      60.765  39.313  63.748  1.00111.52           O  
ANISOU 4261  O   SER C  63    13993  12400  15977  -1068  -1621   1190       O  
ATOM   4262  CB  SER C  63      59.672  39.563  66.292  1.00114.38           C  
ANISOU 4262  CB  SER C  63    14035  13215  16207  -1400  -1457   1781       C  
ATOM   4263  OG  SER C  63      59.183  40.817  65.839  1.00109.47           O  
ANISOU 4263  OG  SER C  63    13251  12960  15380  -1357  -1471   1546       O  
ATOM   4264  N   ASN C  64      62.370  40.726  64.387  1.00104.39           N  
ANISOU 4264  N   ASN C  64    13000  11959  14704   -664  -1562   1318       N  
ATOM   4265  CA  ASN C  64      62.842  40.976  63.040  1.00105.90           C  
ANISOU 4265  CA  ASN C  64    13282  12064  14890   -476  -1639    997       C  
ATOM   4266  C   ASN C  64      63.442  39.711  62.454  1.00106.70           C  
ANISOU 4266  C   ASN C  64    13619  11706  15214   -343  -1659    988       C  
ATOM   4267  O   ASN C  64      63.279  39.438  61.273  1.00113.11           O  
ANISOU 4267  O   ASN C  64    14552  12302  16122   -323  -1725    692       O  
ATOM   4268  CB  ASN C  64      63.866  42.130  63.006  1.00105.81           C  
ANISOU 4268  CB  ASN C  64    13218  12386  14598   -258  -1622    957       C  
ATOM   4269  CG  ASN C  64      65.305  41.643  63.092  1.00107.97           C  
ANISOU 4269  CG  ASN C  64    13567  12607  14847     -2  -1617   1125       C  
ATOM   4270  OD1 ASN C  64      65.924  41.287  62.074  1.00109.86           O  
ANISOU 4270  OD1 ASN C  64    13920  12664  15156    213  -1660    970       O  
ATOM   4271  ND2 ASN C  64      65.854  41.637  64.306  1.00105.21           N  
ANISOU 4271  ND2 ASN C  64    13134  12473  14367     -5  -1556   1458       N  
ATOM   4272  N   TYR C  65      64.078  38.908  63.306  1.00109.58           N  
ANISOU 4272  N   TYR C  65    14066  11919  15647   -246  -1583   1327       N  
ATOM   4273  CA  TYR C  65      64.913  37.798  62.840  1.00116.02           C  
ANISOU 4273  CA  TYR C  65    15146  12313  16622     13  -1545   1379       C  
ATOM   4274  C   TYR C  65      64.138  36.664  62.180  1.00120.17           C  
ANISOU 4274  C   TYR C  65    15952  12278  17426   -179  -1544   1208       C  
ATOM   4275  O   TYR C  65      64.613  36.068  61.204  1.00124.84           O  
ANISOU 4275  O   TYR C  65    16805  12518  18111     13  -1538   1018       O  
ATOM   4276  CB  TYR C  65      65.789  37.264  63.961  1.00117.56           C  
ANISOU 4276  CB  TYR C  65    15341  12540  16784    218  -1438   1840       C  
ATOM   4277  CG  TYR C  65      66.932  38.182  64.313  1.00115.63           C  
ANISOU 4277  CG  TYR C  65    14876  12823  16233    455  -1448   1972       C  
ATOM   4278  CD1 TYR C  65      67.940  38.451  63.396  1.00111.56           C  
ANISOU 4278  CD1 TYR C  65    14380  12394  15612    766  -1479   1821       C  
ATOM   4279  CD2 TYR C  65      67.003  38.779  65.565  1.00114.67           C  
ANISOU 4279  CD2 TYR C  65    14526  13143  15898    333  -1423   2243       C  
ATOM   4280  CE1 TYR C  65      68.985  39.289  63.717  1.00113.92           C  
ANISOU 4280  CE1 TYR C  65    14460  13220  15604    909  -1492   1948       C  
ATOM   4281  CE2 TYR C  65      68.048  39.614  65.898  1.00113.83           C  
ANISOU 4281  CE2 TYR C  65    14230  13545  15472    463  -1436   2345       C  
ATOM   4282  CZ  TYR C  65      69.037  39.867  64.974  1.00115.79           C  
ANISOU 4282  CZ  TYR C  65    14484  13887  15622    731  -1474   2202       C  
ATOM   4283  OH  TYR C  65      70.079  40.713  65.303  1.00120.17           O  
ANISOU 4283  OH  TYR C  65    14832  14995  15830    789  -1493   2308       O  
ATOM   4284  N   LEU C  66      62.955  36.362  62.707  1.00118.18           N  
ANISOU 4284  N   LEU C  66    15659  11958  17286   -582  -1541   1270       N  
ATOM   4285  CA  LEU C  66      62.100  35.372  62.087  1.00123.69           C  
ANISOU 4285  CA  LEU C  66    16604  12183  18207   -895  -1553   1079       C  
ATOM   4286  C   LEU C  66      61.712  35.789  60.664  1.00125.75           C  
ANISOU 4286  C   LEU C  66    16861  12498  18421   -968  -1684    599       C  
ATOM   4287  O   LEU C  66      61.865  35.011  59.715  1.00132.58           O  
ANISOU 4287  O   LEU C  66    18046  12927  19401   -956  -1686    358       O  
ATOM   4288  CB  LEU C  66      60.858  35.127  62.925  1.00126.99           C  
ANISOU 4288  CB  LEU C  66    16892  12655  18701  -1362  -1540   1248       C  
ATOM   4289  CG  LEU C  66      59.797  34.280  62.219  1.00133.42           C  
ANISOU 4289  CG  LEU C  66    17894  13109  19688  -1825  -1583   1003       C  
ATOM   4290  CD1 LEU C  66      60.381  32.959  61.718  1.00131.66           C  
ANISOU 4290  CD1 LEU C  66    18204  12148  19670  -1739  -1486    951       C  
ATOM   4291  CD2 LEU C  66      58.601  34.044  63.131  1.00136.76           C  
ANISOU 4291  CD2 LEU C  66    18138  13660  20162  -2303  -1562   1227       C  
ATOM   4292  N   PHE C  67      61.212  37.017  60.524  1.00121.49           N  
ANISOU 4292  N   PHE C  67    15980  12490  17691  -1027  -1772    470       N  
ATOM   4293  CA  PHE C  67      60.932  37.597  59.206  1.00119.56           C  
ANISOU 4293  CA  PHE C  67    15673  12405  17348  -1020  -1889     64       C  
ATOM   4294  C   PHE C  67      62.146  37.543  58.296  1.00117.15           C  
ANISOU 4294  C   PHE C  67    15576  11921  17013   -616  -1891   -107       C  
ATOM   4295  O   PHE C  67      62.049  37.105  57.155  1.00122.16           O  
ANISOU 4295  O   PHE C  67    16397  12325  17693   -647  -1948   -427       O  
ATOM   4296  CB  PHE C  67      60.445  39.044  59.333  1.00115.28           C  
ANISOU 4296  CB  PHE C  67    14764  12461  16574  -1003  -1924     40       C  
ATOM   4297  CG  PHE C  67      59.091  39.170  59.955  1.00118.79           C  
ANISOU 4297  CG  PHE C  67    14966  13157  17009  -1371  -1925    152       C  
ATOM   4298  CD1 PHE C  67      57.944  38.861  59.232  1.00121.97           C  
ANISOU 4298  CD1 PHE C  67    15282  13617  17444  -1714  -2018    -57       C  
ATOM   4299  CD2 PHE C  67      58.957  39.587  61.273  1.00120.49           C  
ANISOU 4299  CD2 PHE C  67    15019  13606  17152  -1385  -1829    477       C  
ATOM   4300  CE1 PHE C  67      56.691  38.968  59.812  1.00122.57           C  
ANISOU 4300  CE1 PHE C  67    15080  14007  17483  -2047  -2013     83       C  
ATOM   4301  CE2 PHE C  67      57.705  39.695  61.863  1.00121.36           C  
ANISOU 4301  CE2 PHE C  67    14890  13985  17236  -1691  -1811    604       C  
ATOM   4302  CZ  PHE C  67      56.571  39.384  61.132  1.00124.24           C  
ANISOU 4302  CZ  PHE C  67    15135  14432  17636  -2014  -1901    421       C  
ATOM   4303  N   GLY C  68      63.288  37.985  58.809  1.00111.84           N  
ANISOU 4303  N   GLY C  68    14858  11401  16234   -256  -1826    108       N  
ATOM   4304  CA  GLY C  68      64.520  38.007  58.032  1.00110.20           C  
ANISOU 4304  CA  GLY C  68    14784  11128  15960    156  -1816      5       C  
ATOM   4305  C   GLY C  68      64.843  36.652  57.450  1.00115.17           C  
ANISOU 4305  C   GLY C  68    15812  11167  16781    259  -1757    -80       C  
ATOM   4306  O   GLY C  68      65.210  36.539  56.268  1.00116.17           O  
ANISOU 4306  O   GLY C  68    16096  11162  16880    438  -1788   -378       O  
ATOM   4307  N   LEU C  69      64.676  35.615  58.274  1.00116.47           N  
ANISOU 4307  N   LEU C  69    16173  10951  17127    147  -1652    179       N  
ATOM   4308  CA  LEU C  69      64.979  34.240  57.878  1.00121.34           C  
ANISOU 4308  CA  LEU C  69    17265  10903  17932    254  -1535    146       C  
ATOM   4309  C   LEU C  69      64.233  33.837  56.609  1.00123.02           C  
ANISOU 4309  C   LEU C  69    17717  10817  18207    -28  -1613   -335       C  
ATOM   4310  O   LEU C  69      64.844  33.333  55.667  1.00124.97           O  
ANISOU 4310  O   LEU C  69    18284  10736  18460    235  -1562   -553       O  
ATOM   4311  CB  LEU C  69      64.673  33.259  59.029  1.00125.42           C  
ANISOU 4311  CB  LEU C  69    17962  11055  18637     85  -1398    516       C  
ATOM   4312  CG  LEU C  69      65.242  31.828  58.969  1.00127.52           C  
ANISOU 4312  CG  LEU C  69    18774  10594  19084    326  -1192    644       C  
ATOM   4313  CD1 LEU C  69      64.327  30.896  58.181  1.00130.68           C  
ANISOU 4313  CD1 LEU C  69    19611  10387  19654   -107  -1181    281       C  
ATOM   4314  CD2 LEU C  69      66.652  31.821  58.400  1.00127.86           C  
ANISOU 4314  CD2 LEU C  69    18924  10637  19018    982  -1107    666       C  
ATOM   4315  N   ILE C  70      62.914  34.064  56.595  1.00113.42           N  
ANISOU 4315  N   ILE C  70    16846  10634  15612    992   -789    325       N  
ATOM   4316  CA  ILE C  70      62.083  33.830  55.400  1.00110.78           C  
ANISOU 4316  CA  ILE C  70    16692   9945  15453    441   -785    -98       C  
ATOM   4317  C   ILE C  70      62.583  34.681  54.250  1.00105.25           C  
ANISOU 4317  C   ILE C  70    15517   9808  14662    551   -973   -382       C  
ATOM   4318  O   ILE C  70      62.939  34.165  53.174  1.00106.95           O  
ANISOU 4318  O   ILE C  70    15917   9886  14832    718   -951   -684       O  
ATOM   4319  CB  ILE C  70      60.603  34.202  55.654  1.00106.36           C  
ANISOU 4319  CB  ILE C  70    15907   9531  14972   -358   -817   -162       C  
ATOM   4320  CG1 ILE C  70      59.968  33.236  56.653  1.00114.53           C  
ANISOU 4320  CG1 ILE C  70    17463   9991  16062   -709   -557     80       C  
ATOM   4321  CG2 ILE C  70      59.824  34.208  54.350  1.00103.68           C  
ANISOU 4321  CG2 ILE C  70    15403   9410  14579   -850   -865   -653       C  
ATOM   4322  CD1 ILE C  70      58.736  33.793  57.340  1.00116.99           C  
ANISOU 4322  CD1 ILE C  70    17316  10831  16304  -1313   -624    159       C  
ATOM   4323  N   SER C  71      62.632  35.986  54.501  1.00 98.30           N  
ANISOU 4323  N   SER C  71    14123   9507  13719    457  -1085   -285       N  
ATOM   4324  CA  SER C  71      62.852  36.965  53.477  1.00 96.01           C  
ANISOU 4324  CA  SER C  71    13520   9631  13327    427  -1139   -443       C  
ATOM   4325  C   SER C  71      64.128  36.722  52.699  1.00103.70           C  
ANISOU 4325  C   SER C  71    14429  10853  14120    819  -1152   -581       C  
ATOM   4326  O   SER C  71      64.090  36.647  51.464  1.00108.78           O  
ANISOU 4326  O   SER C  71    15036  11595  14700    845  -1183   -807       O  
ATOM   4327  CB  SER C  71      62.865  38.357  54.071  1.00 90.08           C  
ANISOU 4327  CB  SER C  71    12541   9170  12513    268  -1073   -296       C  
ATOM   4328  OG  SER C  71      63.334  39.289  53.111  1.00 90.57           O  
ANISOU 4328  OG  SER C  71    12509   9472  12430    260   -977   -363       O  
ATOM   4329  N   VAL C  72      65.264  36.622  53.409  1.00108.99           N  
ANISOU 4329  N   VAL C  72    14958  11873  14578   1170  -1131   -460       N  
ATOM   4330  CA  VAL C  72      66.579  36.478  52.739  1.00114.93           C  
ANISOU 4330  CA  VAL C  72    15455  13240  14973   1609  -1143   -592       C  
ATOM   4331  C   VAL C  72      66.700  35.183  51.922  1.00121.31           C  
ANISOU 4331  C   VAL C  72    16682  13639  15772   2173  -1132   -757       C  
ATOM   4332  O   VAL C  72      67.425  35.138  50.923  1.00123.98           O  
ANISOU 4332  O   VAL C  72    16819  14433  15854   2463  -1164   -968       O  
ATOM   4333  CB  VAL C  72      67.799  36.620  53.709  1.00116.70           C  
ANISOU 4333  CB  VAL C  72    15218  14393  14728   1925  -1116   -479       C  
ATOM   4334  CG1 VAL C  72      67.960  38.060  54.172  1.00115.33           C  
ANISOU 4334  CG1 VAL C  72    14626  14750  14442   1138  -1030   -574       C  
ATOM   4335  CG2 VAL C  72      67.706  35.652  54.891  1.00117.64           C  
ANISOU 4335  CG2 VAL C  72    15617  14277  14804   2507  -1074   -158       C  
ATOM   4336  N   SER C  73      65.975  34.142  52.346  1.00123.52           N  
ANISOU 4336  N   SER C  73    17618  13019  16295   2254  -1019   -700       N  
ATOM   4337  CA  SER C  73      66.030  32.836  51.684  1.00124.26           C  
ANISOU 4337  CA  SER C  73    18414  12410  16388   2688   -846   -940       C  
ATOM   4338  C   SER C  73      65.380  32.956  50.331  1.00122.42           C  
ANISOU 4338  C   SER C  73    18103  12149  16260   2137   -920  -1442       C  
ATOM   4339  O   SER C  73      66.043  32.840  49.291  1.00118.73           O  
ANISOU 4339  O   SER C  73    17494  12061  15556   2511   -961  -1727       O  
ATOM   4340  CB  SER C  73      65.304  31.782  52.521  1.00123.61           C  
ANISOU 4340  CB  SER C  73    19228  11203  16533   2618   -553   -765       C  
ATOM   4341  OG  SER C  73      65.834  31.724  53.830  1.00120.85           O  
ANISOU 4341  OG  SER C  73    18867  11052  15996   3215   -481   -204       O  
ATOM   4342  N   LEU C  74      64.082  33.232  50.349  1.00120.36           N  
ANISOU 4342  N   LEU C  74    17802  11695  16233   1304   -946  -1545       N  
ATOM   4343  CA  LEU C  74      63.356  33.549  49.146  1.00122.78           C  
ANISOU 4343  CA  LEU C  74    17771  12417  16462    821  -1043  -1959       C  
ATOM   4344  C   LEU C  74      64.169  34.477  48.232  1.00119.68           C  
ANISOU 4344  C   LEU C  74    16774  12889  15806   1181  -1198  -1917       C  
ATOM   4345  O   LEU C  74      64.509  34.103  47.100  1.00116.68           O  
ANISOU 4345  O   LEU C  74    16346  12770  15217   1383  -1211  -2297       O  
ATOM   4346  CB  LEU C  74      61.997  34.164  49.493  1.00122.25           C  
ANISOU 4346  CB  LEU C  74    17386  12602  16459    132  -1098  -1877       C  
ATOM   4347  CG  LEU C  74      61.051  33.264  50.310  1.00126.91           C  
ANISOU 4347  CG  LEU C  74    18472  12530  17217   -482   -907  -1969       C  
ATOM   4348  CD1 LEU C  74      59.712  33.948  50.543  1.00125.27           C  
ANISOU 4348  CD1 LEU C  74    17714  12996  16886  -1073   -997  -1927       C  
ATOM   4349  CD2 LEU C  74      60.853  31.912  49.642  1.00131.06           C  
ANISOU 4349  CD2 LEU C  74    19668  12412  17716   -881   -638  -2603       C  
ATOM   4350  N   TYR C  75      64.507  35.666  48.738  1.00116.57           N  
ANISOU 4350  N   TYR C  75    15995  12910  15386   1192  -1248  -1494       N  
ATOM   4351  CA  TYR C  75      65.250  36.653  47.947  1.00116.92           C  
ANISOU 4351  CA  TYR C  75    15599  13668  15155   1315  -1258  -1399       C  
ATOM   4352  C   TYR C  75      66.482  36.021  47.327  1.00126.15           C  
ANISOU 4352  C   TYR C  75    16686  15202  16043   1835  -1281  -1618       C  
ATOM   4353  O   TYR C  75      66.819  36.304  46.174  1.00127.36           O  
ANISOU 4353  O   TYR C  75    16535  15935  15919   1926  -1299  -1752       O  
ATOM   4354  CB  TYR C  75      65.631  37.872  48.798  1.00114.69           C  
ANISOU 4354  CB  TYR C  75    15164  13548  14866   1087  -1151  -1024       C  
ATOM   4355  CG  TYR C  75      66.539  38.892  48.107  1.00116.53           C  
ANISOU 4355  CG  TYR C  75    15110  14391  14774    979  -1002   -933       C  
ATOM   4356  CD1 TYR C  75      66.007  39.954  47.377  1.00118.36           C  
ANISOU 4356  CD1 TYR C  75    15398  14658  14914    807   -811   -712       C  
ATOM   4357  CD2 TYR C  75      67.922  38.817  48.231  1.00119.71           C  
ANISOU 4357  CD2 TYR C  75    15199  15431  14852   1064   -981  -1022       C  
ATOM   4358  CE1 TYR C  75      66.836  40.891  46.762  1.00118.92           C  
ANISOU 4358  CE1 TYR C  75    15390  15122  14670    589   -539   -566       C  
ATOM   4359  CE2 TYR C  75      68.754  39.742  47.615  1.00120.37           C  
ANISOU 4359  CE2 TYR C  75    15006  16160  14567    721   -773   -983       C  
ATOM   4360  CZ  TYR C  75      68.207  40.774  46.889  1.00118.66           C  
ANISOU 4360  CZ  TYR C  75    15022  15703  14358    412   -521   -745       C  
ATOM   4361  OH  TYR C  75      69.033  41.679  46.286  1.00122.20           O  
ANISOU 4361  OH  TYR C  75    15365  16640  14424    -29   -192   -651       O  
ATOM   4362  N   ALA C  76      67.138  35.137  48.076  1.00133.28           N  
ANISOU 4362  N   ALA C  76    17858  15861  16922   2318  -1251  -1613       N  
ATOM   4363  CA  ALA C  76      68.347  34.483  47.575  1.00144.22           C  
ANISOU 4363  CA  ALA C  76    19162  17737  17898   3094  -1242  -1785       C  
ATOM   4364  C   ALA C  76      68.039  33.697  46.307  1.00145.22           C  
ANISOU 4364  C   ALA C  76    19569  17620  17987   3257  -1229  -2287       C  
ATOM   4365  O   ALA C  76      68.783  33.759  45.325  1.00143.83           O  
ANISOU 4365  O   ALA C  76    19017  18209  17421   3608  -1278  -2486       O  
ATOM   4366  CB  ALA C  76      68.957  33.580  48.640  1.00153.48           C  
ANISOU 4366  CB  ALA C  76    20698  18674  18940   3875  -1134  -1592       C  
ATOM   4367  N   TYR C  77      66.921  32.981  46.328  1.00142.38           N  
ANISOU 4367  N   TYR C  77    19815  16320  17962   2876  -1134  -2560       N  
ATOM   4368  CA  TYR C  77      66.473  32.222  45.173  1.00146.18           C  
ANISOU 4368  CA  TYR C  77    20571  16604  18364   2754  -1064  -3220       C  
ATOM   4369  C   TYR C  77      66.143  33.184  44.025  1.00140.17           C  
ANISOU 4369  C   TYR C  77    18998  16889  17369   2380  -1256  -3321       C  
ATOM   4370  O   TYR C  77      66.746  33.116  42.949  1.00138.93           O  
ANISOU 4370  O   TYR C  77    18542  17399  16844   2746  -1302  -3603       O  
ATOM   4371  CB  TYR C  77      65.255  31.371  45.562  1.00148.92           C  
ANISOU 4371  CB  TYR C  77    21666  15876  19037   2057   -846  -3551       C  
ATOM   4372  CG  TYR C  77      64.617  30.601  44.436  1.00151.90           C  
ANISOU 4372  CG  TYR C  77    22307  16135  19273   1560   -706  -4429       C  
ATOM   4373  CD1 TYR C  77      65.119  29.377  44.038  1.00161.08           C  
ANISOU 4373  CD1 TYR C  77    24379  16487  20334   2002   -380  -4979       C  
ATOM   4374  CD2 TYR C  77      63.475  31.082  43.804  1.00150.30           C  
ANISOU 4374  CD2 TYR C  77    21462  16711  18934    679   -843  -4752       C  
ATOM   4375  CE1 TYR C  77      64.522  28.660  43.017  1.00172.84           C  
ANISOU 4375  CE1 TYR C  77    26161  17861  21649   1364   -185  -5958       C  
ATOM   4376  CE2 TYR C  77      62.869  30.379  42.784  1.00158.95           C  
ANISOU 4376  CE2 TYR C  77    22633  18006  19755     79   -708  -5687       C  
ATOM   4377  CZ  TYR C  77      63.392  29.169  42.391  1.00171.16           C  
ANISOU 4377  CZ  TYR C  77    25120  18649  21263    304   -373  -6354       C  
ATOM   4378  OH  TYR C  77      62.783  28.459  41.375  1.00183.19           O  
ANISOU 4378  OH  TYR C  77    26764  20370  22467   -467   -174  -7458       O  
ATOM   4379  N   VAL C  78      65.245  34.127  44.300  1.00132.83           N  
ANISOU 4379  N   VAL C  78    17724  16174  16570   1812  -1329  -2996       N  
ATOM   4380  CA  VAL C  78      64.767  35.076  43.300  1.00131.19           C  
ANISOU 4380  CA  VAL C  78    16874  16913  16056   1646  -1411  -2920       C  
ATOM   4381  C   VAL C  78      65.898  35.908  42.682  1.00132.65           C  
ANISOU 4381  C   VAL C  78    16633  17847  15918   2046  -1414  -2592       C  
ATOM   4382  O   VAL C  78      65.820  36.277  41.518  1.00138.12           O  
ANISOU 4382  O   VAL C  78    16905  19352  16222   2144  -1426  -2650       O  
ATOM   4383  CB  VAL C  78      63.675  36.015  43.881  1.00129.69           C  
ANISOU 4383  CB  VAL C  78    16522  16775  15976   1271  -1400  -2481       C  
ATOM   4384  CG1 VAL C  78      63.231  37.050  42.850  1.00129.08           C  
ANISOU 4384  CG1 VAL C  78    15899  17698  15446   1432  -1380  -2223       C  
ATOM   4385  CG2 VAL C  78      62.482  35.207  44.385  1.00127.69           C  
ANISOU 4385  CG2 VAL C  78    16508  16115  15891    717  -1386  -2857       C  
ATOM   4386  N   SER C  79      66.947  36.201  43.453  1.00137.59           N  
ANISOU 4386  N   SER C  79    19784  17603  14891    540   -971  -1519       N  
ATOM   4387  CA  SER C  79      68.087  36.954  42.894  1.00138.29           C  
ANISOU 4387  CA  SER C  79    19983  17075  15484    799   -899  -1969       C  
ATOM   4388  C   SER C  79      68.967  36.087  41.976  1.00142.92           C  
ANISOU 4388  C   SER C  79    20480  17073  16749    825   -980  -1954       C  
ATOM   4389  O   SER C  79      69.675  36.610  41.102  1.00143.04           O  
ANISOU 4389  O   SER C  79    20389  16976  16983    913   -735  -2256       O  
ATOM   4390  CB  SER C  79      68.916  37.658  43.985  1.00136.35           C  
ANISOU 4390  CB  SER C  79    19729  17017  15060    753  -1131  -2215       C  
ATOM   4391  OG  SER C  79      69.432  36.750  44.932  1.00136.23           O  
ANISOU 4391  OG  SER C  79    19576  17280  14905    410  -1598  -1687       O  
ATOM   4392  N   TYR C  80      68.890  34.766  42.161  1.00145.25           N  
ANISOU 4392  N   TYR C  80    20705  17063  17419    713  -1389  -1634       N  
ATOM   4393  CA  TYR C  80      69.535  33.820  41.251  1.00147.30           C  
ANISOU 4393  CA  TYR C  80    20777  16655  18534    960  -1521  -2066       C  
ATOM   4394  C   TYR C  80      68.759  33.708  39.948  1.00147.11           C  
ANISOU 4394  C   TYR C  80    20875  16749  18268    952  -1142  -2546       C  
ATOM   4395  O   TYR C  80      69.340  33.797  38.860  1.00151.77           O  
ANISOU 4395  O   TYR C  80    21246  17544  18874   1136   -755  -3284       O  
ATOM   4396  CB  TYR C  80      69.673  32.437  41.906  1.00156.35           C  
ANISOU 4396  CB  TYR C  80    21805  17008  20592    864  -2433  -1564       C  
ATOM   4397  CG  TYR C  80      69.778  31.276  40.919  1.00161.37           C  
ANISOU 4397  CG  TYR C  80    22314  16677  22323   1197  -2749  -2310       C  
ATOM   4398  CD1 TYR C  80      70.778  31.248  39.934  1.00163.84           C  
ANISOU 4398  CD1 TYR C  80    22201  16938  23113   1833  -2331  -3580       C  
ATOM   4399  CD2 TYR C  80      68.892  30.202  40.983  1.00162.02           C  
ANISOU 4399  CD2 TYR C  80    22590  16009  22959    827  -3516  -1864       C  
ATOM   4400  CE1 TYR C  80      70.868  30.200  39.035  1.00166.63           C  
ANISOU 4400  CE1 TYR C  80    22343  16561  24407   2267  -2577  -4756       C  
ATOM   4401  CE2 TYR C  80      68.984  29.147  40.093  1.00168.39           C  
ANISOU 4401  CE2 TYR C  80    23322  15705  24952   1175  -3975  -2865       C  
ATOM   4402  CZ  TYR C  80      69.971  29.154  39.121  1.00171.55           C  
ANISOU 4402  CZ  TYR C  80    23312  16106  25762   1988  -3463  -4497       C  
ATOM   4403  OH  TYR C  80      70.058  28.113  38.235  1.00184.59           O  
ANISOU 4403  OH  TYR C  80    24798  16804  28533   2457  -3875  -5962       O  
ATOM   4404  N   THR C  81      67.447  33.505  40.061  1.00143.80           N  
ANISOU 4404  N   THR C  81    20679  16485  17474    626  -1263  -2088       N  
ATOM   4405  CA  THR C  81      66.587  33.365  38.885  1.00142.42           C  
ANISOU 4405  CA  THR C  81    20605  16504  17004    470  -1078  -2393       C  
ATOM   4406  C   THR C  81      66.648  34.617  38.007  1.00136.71           C  
ANISOU 4406  C   THR C  81    19840  16466  15636    498   -499  -2567       C  
ATOM   4407  O   THR C  81      66.041  34.672  36.938  1.00141.77           O  
ANISOU 4407  O   THR C  81    20498  17525  15841    250   -382  -2683       O  
ATOM   4408  CB  THR C  81      65.108  33.044  39.263  1.00146.09           C  
ANISOU 4408  CB  THR C  81    21132  17202  17172     17  -1359  -1650       C  
ATOM   4409  OG1 THR C  81      64.432  34.236  39.705  1.00138.57           O  
ANISOU 4409  OG1 THR C  81    20052  17050  15546     88   -956  -1288       O  
ATOM   4410  CG2 THR C  81      65.031  31.949  40.354  1.00148.84           C  
ANISOU 4410  CG2 THR C  81    21427  17073  18053   -356  -2119   -906       C  
ATOM   4411  N   PHE C  82      67.402  35.609  38.454  1.00132.94           N  
ANISOU 4411  N   PHE C  82    19284  16078  15146    653   -319  -2449       N  
ATOM   4412  CA  PHE C  82      67.579  36.819  37.688  1.00138.33           C  
ANISOU 4412  CA  PHE C  82    19886  17170  15502    495    -73  -2289       C  
ATOM   4413  C   PHE C  82      69.031  37.048  37.291  1.00142.18           C  
ANISOU 4413  C   PHE C  82    20036  17919  16067    424    139  -2556       C  
ATOM   4414  O   PHE C  82      69.351  38.035  36.622  1.00145.72           O  
ANISOU 4414  O   PHE C  82    20307  18821  16237     27    224  -2150       O  
ATOM   4415  CB  PHE C  82      67.025  38.020  38.451  1.00138.82           C  
ANISOU 4415  CB  PHE C  82    20057  17019  15668    631   -238  -1883       C  
ATOM   4416  CG  PHE C  82      65.550  38.224  38.262  1.00139.23           C  
ANISOU 4416  CG  PHE C  82    20096  17237  15568    670   -324  -1587       C  
ATOM   4417  CD1 PHE C  82      64.628  37.551  39.070  1.00137.53           C  
ANISOU 4417  CD1 PHE C  82    19816  17234  15203    784   -337  -1584       C  
ATOM   4418  CD2 PHE C  82      65.073  39.074  37.261  1.00138.50           C  
ANISOU 4418  CD2 PHE C  82    19902  17234  15486    472   -494  -1104       C  
ATOM   4419  CE1 PHE C  82      63.265  37.734  38.895  1.00138.42           C  
ANISOU 4419  CE1 PHE C  82    19676  17718  15198    825   -382  -1302       C  
ATOM   4420  CE2 PHE C  82      63.712  39.248  37.078  1.00140.19           C  
ANISOU 4420  CE2 PHE C  82    19933  17601  15731    577   -678   -774       C  
ATOM   4421  CZ  PHE C  82      62.806  38.583  37.900  1.00139.16           C  
ANISOU 4421  CZ  PHE C  82    19649  17752  15470    817   -555   -970       C  
ATOM   4422  N   LYS C  83      69.903  36.128  37.692  1.00142.89           N  
ANISOU 4422  N   LYS C  83    19900  17758  16633    738    111  -3090       N  
ATOM   4423  CA  LYS C  83      71.331  36.224  37.380  1.00150.58           C  
ANISOU 4423  CA  LYS C  83    20270  19170  17774    776    355  -3450       C  
ATOM   4424  C   LYS C  83      72.031  37.378  38.143  1.00149.48           C  
ANISOU 4424  C   LYS C  83    20087  18898  17808    560    158  -2828       C  
ATOM   4425  O   LYS C  83      73.025  37.945  37.664  1.00154.82           O  
ANISOU 4425  O   LYS C  83    20218  20210  18393    223    347  -2702       O  
ATOM   4426  CB  LYS C  83      71.551  36.368  35.863  1.00160.13           C  
ANISOU 4426  CB  LYS C  83    21011  21646  18183    391    898  -3812       C  
ATOM   4427  CG  LYS C  83      70.908  35.267  35.017  1.00167.25           C  
ANISOU 4427  CG  LYS C  83    21949  22803  18794    536   1036  -4765       C  
ATOM   4428  CD  LYS C  83      70.771  35.687  33.554  1.00173.36           C  
ANISOU 4428  CD  LYS C  83    22390  25238  18241   -166   1502  -4843       C  
ATOM   4429  CE  LYS C  83      72.129  35.824  32.876  1.00181.14           C  
ANISOU 4429  CE  LYS C  83    22340  27789  18696   -334   2137  -5428       C  
ATOM   4430  NZ  LYS C  83      72.128  36.923  31.873  1.00185.20           N  
ANISOU 4430  NZ  LYS C  83    22515  30024  17827  -1518   2359  -4335       N  
ATOM   4431  N   LEU C  84      71.505  37.720  39.320  1.00141.03           N  
ANISOU 4431  N   LEU C  84    19504  17176  16905    657   -246  -2507       N  
ATOM   4432  CA  LEU C  84      72.243  38.551  40.265  1.00135.90           C  
ANISOU 4432  CA  LEU C  84    18845  16281  16509    524   -599  -2299       C  
ATOM   4433  C   LEU C  84      72.995  37.640  41.222  1.00134.34           C  
ANISOU 4433  C   LEU C  84    18411  15921  16708    759   -916  -2398       C  
ATOM   4434  O   LEU C  84      72.469  37.229  42.257  1.00128.37           O  
ANISOU 4434  O   LEU C  84    17954  14993  15828    821  -1259  -2248       O  
ATOM   4435  CB  LEU C  84      71.302  39.515  41.030  1.00134.83           C  
ANISOU 4435  CB  LEU C  84    19230  15762  16235    539   -883  -2253       C  
ATOM   4436  CG  LEU C  84      71.054  40.928  40.448  1.00135.87           C  
ANISOU 4436  CG  LEU C  84    19472  15537  16613    273  -1097  -1985       C  
ATOM   4437  CD1 LEU C  84      69.902  41.625  41.161  1.00135.33           C  
ANISOU 4437  CD1 LEU C  84    19746  15008  16663    676  -1351  -2388       C  
ATOM   4438  CD2 LEU C  84      72.307  41.800  40.487  1.00140.69           C  
ANISOU 4438  CD2 LEU C  84    19856  15921  17679   -240  -1501  -1705       C  
ATOM   4439  N   TYR C  85      74.223  37.301  40.849  1.00143.43           N  
ANISOU 4439  N   TYR C  85    18868  17308  18320    831   -850  -2552       N  
ATOM   4440  CA  TYR C  85      75.005  36.304  41.583  1.00153.98           C  
ANISOU 4440  CA  TYR C  85    19768  18338  20396   1169  -1324  -2565       C  
ATOM   4441  C   TYR C  85      75.629  36.855  42.870  1.00156.64           C  
ANISOU 4441  C   TYR C  85    20132  18632  20750    832  -1961  -2069       C  
ATOM   4442  O   TYR C  85      75.851  36.111  43.818  1.00158.44           O  
ANISOU 4442  O   TYR C  85    20262  18613  21325    894  -2621  -1692       O  
ATOM   4443  CB  TYR C  85      76.074  35.670  40.676  1.00162.32           C  
ANISOU 4443  CB  TYR C  85    19803  19755  22114   1595  -1005  -3194       C  
ATOM   4444  CG  TYR C  85      75.507  35.084  39.398  1.00166.27           C  
ANISOU 4444  CG  TYR C  85    20230  20552  22390   1881   -396  -4028       C  
ATOM   4445  CD1 TYR C  85      74.604  34.010  39.434  1.00165.66           C  
ANISOU 4445  CD1 TYR C  85    20604  19650  22688   2228   -707  -4320       C  
ATOM   4446  CD2 TYR C  85      75.858  35.608  38.150  1.00171.33           C  
ANISOU 4446  CD2 TYR C  85    20311  22464  22322   1606    388  -4436       C  
ATOM   4447  CE1 TYR C  85      74.069  33.482  38.266  1.00168.47           C  
ANISOU 4447  CE1 TYR C  85    20939  20281  22788   2400   -269  -5249       C  
ATOM   4448  CE2 TYR C  85      75.328  35.085  36.977  1.00175.52           C  
ANISOU 4448  CE2 TYR C  85    20756  23597  22337   1730    920  -5314       C  
ATOM   4449  CZ  TYR C  85      74.438  34.024  37.039  1.00173.78           C  
ANISOU 4449  CZ  TYR C  85    21073  22385  22567   2182    582  -5849       C  
ATOM   4450  OH  TYR C  85      73.918  33.506  35.878  1.00180.58           O  
ANISOU 4450  OH  TYR C  85    21878  23845  22886   2228    996  -6884       O  
ATOM   4451  N   GLY C  86      75.890  38.163  42.896  1.00157.95           N  
ANISOU 4451  N   GLY C  86    20428  19006  20578    359  -1935  -1998       N  
ATOM   4452  CA  GLY C  86      76.355  38.833  44.108  1.00160.17           C  
ANISOU 4452  CA  GLY C  86    20867  19259  20730    -57  -2608  -1811       C  
ATOM   4453  C   GLY C  86      75.361  38.712  45.252  1.00159.03           C  
ANISOU 4453  C   GLY C  86    21380  19186  19858    -88  -2899  -1882       C  
ATOM   4454  O   GLY C  86      75.732  38.372  46.383  1.00163.41           O  
ANISOU 4454  O   GLY C  86    21848  20064  20174   -349  -3528  -1578       O  
ATOM   4455  N   GLU C  87      74.090  38.965  44.954  1.00152.62           N  
ANISOU 4455  N   GLU C  87    21072  18330  18586     99  -2461  -2201       N  
ATOM   4456  CA  GLU C  87      73.052  38.966  45.980  1.00151.10           C  
ANISOU 4456  CA  GLU C  87    21259  18649  17502     53  -2542  -2418       C  
ATOM   4457  C   GLU C  87      72.693  37.563  46.436  1.00151.32           C  
ANISOU 4457  C   GLU C  87    21136  19055  17303    -35  -2737  -1692       C  
ATOM   4458  O   GLU C  87      72.278  37.370  47.566  1.00156.67           O  
ANISOU 4458  O   GLU C  87    21846  20616  17066   -427  -3034  -1463       O  
ATOM   4459  CB  GLU C  87      71.804  39.722  45.505  1.00145.46           C  
ANISOU 4459  CB  GLU C  87    20880  17816  16570    368  -2065  -2998       C  
ATOM   4460  CG  GLU C  87      72.085  41.161  45.074  1.00151.63           C  
ANISOU 4460  CG  GLU C  87    21818  17863  17931    371  -2231  -3490       C  
ATOM   4461  CD  GLU C  87      72.395  42.086  46.246  1.00164.42           C  
ANISOU 4461  CD  GLU C  87    23608  19533  19329    206  -2786  -4346       C  
ATOM   4462  OE1 GLU C  87      71.514  42.251  47.112  1.00172.96           O  
ANISOU 4462  OE1 GLU C  87    24787  21282  19647    457  -2685  -5201       O  
ATOM   4463  OE2 GLU C  87      73.515  42.663  46.293  1.00166.87           O  
ANISOU 4463  OE2 GLU C  87    23863  19370  20168   -221  -3330  -4268       O  
HETATM 4464  N   MSE C  88      72.912  36.576  45.576  1.00166.96           N  
ANISOU 4464  N   MSE C  88    22841  22001  18595   1120   -321  -1818       N  
HETATM 4465  CA  MSE C  88      72.447  35.214  45.855  1.00172.10           C  
ANISOU 4465  CA  MSE C  88    23786  22165  19437   1173   -421  -2395       C  
HETATM 4466  C   MSE C  88      73.334  34.461  46.835  1.00167.37           C  
ANISOU 4466  C   MSE C  88    22867  21317  19409   1428     14  -2320       C  
HETATM 4467  O   MSE C  88      72.827  33.762  47.718  1.00165.74           O  
ANISOU 4467  O   MSE C  88    22594  20669  19707   1274   -226  -2526       O  
HETATM 4468  CB  MSE C  88      72.186  34.446  44.553  1.00185.35           C  
ANISOU 4468  CB  MSE C  88    26301  23774  20349   1366   -416  -2956       C  
HETATM 4469  CG  MSE C  88      73.439  33.822  43.949  1.00194.31           C  
ANISOU 4469  CG  MSE C  88    27742  25016  21070   1999    364  -3028       C  
HETATM 4470 SE   MSE C  88      73.048  31.958  43.451  1.00204.81          SE  
ANISOU 4470 SE   MSE C  88    30165  25606  22045   2282    274  -3979      SE  
HETATM 4471  CE  MSE C  88      72.633  31.233  45.245  1.00188.61           C  
ANISOU 4471  CE  MSE C  88    27577  22908  21176   1912    -44  -3973       C  
HETATM 4472  N   MSE C  89      74.655  34.601  46.691  1.00163.80           N  
ANISOU 4472  N   MSE C  89    22170  21184  18882   1813    649  -1966       N  
HETATM 4473  CA  MSE C  89      75.600  33.936  47.600  1.00159.72           C  
ANISOU 4473  CA  MSE C  89    21273  20512  18900   2120   1063  -1814       C  
HETATM 4474  C   MSE C  89      75.612  34.643  48.930  1.00149.38           C  
ANISOU 4474  C   MSE C  89    19294  19165  18296   1761    780  -1351       C  
HETATM 4475  O   MSE C  89      75.799  34.014  49.978  1.00144.52           O  
ANISOU 4475  O   MSE C  89    18456  18223  18232   1825    796  -1356       O  
HETATM 4476  CB  MSE C  89      77.011  33.852  47.003  1.00169.71           C  
ANISOU 4476  CB  MSE C  89    22377  22242  19859   2688   1841  -1513       C  
HETATM 4477  CG  MSE C  89      77.497  35.183  46.433  1.00180.94           C  
ANISOU 4477  CG  MSE C  89    23444  24324  20980   2506   1976   -897       C  
HETATM 4478 SE   MSE C  89      79.378  35.035  45.844  1.00208.37          SE  
ANISOU 4478 SE   MSE C  89    26434  28553  24184   3212   3056   -321      SE  
HETATM 4479  CE  MSE C  89      79.088  34.957  43.891  1.00210.16           C  
ANISOU 4479  CE  MSE C  89    27603  29117  23129   3597   3394   -712       C  
ATOM   4480  N   LEU C  90      75.378  35.959  48.899  1.00143.98           N  
ANISOU 4480  N   LEU C  90    18385  18767  17553   1401    481   -960       N  
ATOM   4481  CA  LEU C  90      75.365  36.789  50.114  1.00133.44           C  
ANISOU 4481  CA  LEU C  90    16571  17358  16770   1082    148   -532       C  
ATOM   4482  C   LEU C  90      74.234  36.393  51.067  1.00131.69           C  
ANISOU 4482  C   LEU C  90    16406  16690  16938    893   -306   -840       C  
ATOM   4483  O   LEU C  90      74.485  36.103  52.237  1.00132.49           O  
ANISOU 4483  O   LEU C  90    16220  16560  17560    900   -315   -713       O  
ATOM   4484  CB  LEU C  90      75.254  38.275  49.753  1.00126.92           C  
ANISOU 4484  CB  LEU C  90    15700  16824  15696    775   -130   -107       C  
ATOM   4485  CG  LEU C  90      75.752  39.359  50.725  1.00120.26           C  
ANISOU 4485  CG  LEU C  90    14461  15978  15253    494   -372    485       C  
ATOM   4486  CD1 LEU C  90      74.957  40.636  50.511  1.00118.15           C  
ANISOU 4486  CD1 LEU C  90    14447  15703  14740    212   -891    638       C  
ATOM   4487  CD2 LEU C  90      75.687  38.940  52.185  1.00112.88           C  
ANISOU 4487  CD2 LEU C  90    13286  14670  14932    488   -544    447       C  
ATOM   4488  N   ASN C  91      72.995  36.384  50.563  1.00132.85           N  
ANISOU 4488  N   ASN C  91    16888  16769  16816    721   -684  -1193       N  
ATOM   4489  CA  ASN C  91      71.833  36.037  51.382  1.00130.51           C  
ANISOU 4489  CA  ASN C  91    16549  16176  16863    512  -1093  -1401       C  
ATOM   4490  C   ASN C  91      71.865  34.601  51.888  1.00134.80           C  
ANISOU 4490  C   ASN C  91    17180  16306  17729    594   -932  -1714       C  
ATOM   4491  O   ASN C  91      71.632  34.354  53.076  1.00133.95           O  
ANISOU 4491  O   ASN C  91    16818  15967  18108    510  -1030  -1609       O  
ATOM   4492  CB  ASN C  91      70.525  36.311  50.640  1.00132.14           C  
ANISOU 4492  CB  ASN C  91    16994  16499  16714    297  -1553  -1641       C  
ATOM   4493  CG  ASN C  91      70.213  37.794  50.535  1.00133.79           C  
ANISOU 4493  CG  ASN C  91    17093  17002  16739    228  -1844  -1284       C  
ATOM   4494  OD1 ASN C  91      69.319  38.312  51.215  1.00132.51           O  
ANISOU 4494  OD1 ASN C  91    16736  16834  16776    142  -2209  -1176       O  
ATOM   4495  ND2 ASN C  91      70.946  38.487  49.676  1.00138.35           N  
ANISOU 4495  ND2 ASN C  91    17822  17837  16906    302  -1666  -1069       N  
ATOM   4496  N   LEU C  92      72.190  33.657  51.000  1.00139.12           N  
ANISOU 4496  N   LEU C  92    18165  16729  17965    797   -675  -2085       N  
ATOM   4497  CA  LEU C  92      72.177  32.226  51.360  1.00139.99           C  
ANISOU 4497  CA  LEU C  92    18543  16323  18321    888   -576  -2429       C  
ATOM   4498  C   LEU C  92      73.276  31.818  52.378  1.00140.34           C  
ANISOU 4498  C   LEU C  92    18271  16207  18843   1204   -180  -2159       C  
ATOM   4499  O   LEU C  92      72.973  31.219  53.413  1.00139.06           O  
ANISOU 4499  O   LEU C  92    18012  15675  19148   1086   -303  -2152       O  
ATOM   4500  CB  LEU C  92      72.231  31.340  50.109  1.00142.35           C  
ANISOU 4500  CB  LEU C  92    19573  16442  18072   1097   -451  -2946       C  
ATOM   4501  CG  LEU C  92      71.814  29.880  50.312  1.00142.65           C  
ANISOU 4501  CG  LEU C  92    20125  15800  18275   1034   -590  -3396       C  
ATOM   4502  CD1 LEU C  92      70.348  29.792  50.693  1.00138.78           C  
ANISOU 4502  CD1 LEU C  92    19559  15142  18026    372  -1244  -3478       C  
ATOM   4503  CD2 LEU C  92      72.095  29.054  49.068  1.00150.13           C  
ANISOU 4503  CD2 LEU C  92    21949  16508  18586   1380   -424  -3923       C  
ATOM   4504  N   LEU C  93      74.534  32.164  52.089  1.00142.52           N  
ANISOU 4504  N   LEU C  93    18341  16811  18996   1585    277  -1878       N  
ATOM   4505  CA  LEU C  93      75.658  31.768  52.954  1.00142.73           C  
ANISOU 4505  CA  LEU C  93    18006  16771  19452   1925    631  -1578       C  
ATOM   4506  C   LEU C  93      75.811  32.630  54.218  1.00140.85           C  
ANISOU 4506  C   LEU C  93    17178  16642  19694   1665    396  -1066       C  
ATOM   4507  O   LEU C  93      76.165  32.114  55.266  1.00145.84           O  
ANISOU 4507  O   LEU C  93    17620  17020  20771   1772    429   -929       O  
ATOM   4508  CB  LEU C  93      76.985  31.752  52.184  1.00146.72           C  
ANISOU 4508  CB  LEU C  93    18397  17679  19668   2457   1233  -1390       C  
ATOM   4509  CG  LEU C  93      77.022  31.377  50.702  1.00154.30           C  
ANISOU 4509  CG  LEU C  93    19940  18762  19922   2794   1540  -1779       C  
ATOM   4510  CD1 LEU C  93      78.455  31.433  50.201  1.00162.62           C  
ANISOU 4510  CD1 LEU C  93    20671  20342  20772   3392   2237  -1419       C  
ATOM   4511  CD2 LEU C  93      76.418  30.007  50.441  1.00157.66           C  
ANISOU 4511  CD2 LEU C  93    21166  18529  20208   2965   1462  -2454       C  
ATOM   4512  N   VAL C  94      75.580  33.941  54.102  1.00136.21           N  
ANISOU 4512  N   VAL C  94    16391  16395  18968   1360    139   -785       N  
ATOM   4513  CA  VAL C  94      75.855  34.880  55.205  1.00127.96           C  
ANISOU 4513  CA  VAL C  94    14930  15420  18268   1153   -114   -301       C  
ATOM   4514  C   VAL C  94      74.607  35.235  56.023  1.00128.47           C  
ANISOU 4514  C   VAL C  94    15083  15254  18475    865   -591   -390       C  
ATOM   4515  O   VAL C  94      74.578  35.012  57.232  1.00130.42           O  
ANISOU 4515  O   VAL C  94    15195  15263  19092    859   -702   -269       O  
ATOM   4516  CB  VAL C  94      76.544  36.172  54.704  1.00126.65           C  
ANISOU 4516  CB  VAL C  94    14535  15702  17885   1012   -124    159       C  
ATOM   4517  CG1 VAL C  94      76.626  37.208  55.811  1.00121.38           C  
ANISOU 4517  CG1 VAL C  94    13654  14968  17496    726   -549    577       C  
ATOM   4518  CG2 VAL C  94      77.929  35.861  54.184  1.00132.00           C  
ANISOU 4518  CG2 VAL C  94    14905  16724  18523   1315    402    433       C  
ATOM   4519  N   TYR C  95      73.582  35.794  55.371  1.00130.19           N  
ANISOU 4519  N   TYR C  95    15510  15588  18366    677   -855   -563       N  
ATOM   4520  CA  TYR C  95      72.397  36.277  56.100  1.00124.74           C  
ANISOU 4520  CA  TYR C  95    14814  14813  17767    501  -1262   -565       C  
ATOM   4521  C   TYR C  95      71.605  35.149  56.781  1.00125.66           C  
ANISOU 4521  C   TYR C  95    14941  14631  18171    455  -1285   -808       C  
ATOM   4522  O   TYR C  95      71.069  35.344  57.867  1.00126.75           O  
ANISOU 4522  O   TYR C  95    14939  14688  18530    421  -1453   -657       O  
ATOM   4523  CB  TYR C  95      71.465  37.108  55.201  1.00122.94           C  
ANISOU 4523  CB  TYR C  95    14751  14833  17127    377  -1550   -654       C  
ATOM   4524  CG  TYR C  95      72.001  38.463  54.780  1.00123.14           C  
ANISOU 4524  CG  TYR C  95    14813  15085  16887    352  -1656   -312       C  
ATOM   4525  CD1 TYR C  95      73.102  39.048  55.428  1.00124.93           C  
ANISOU 4525  CD1 TYR C  95    14884  15277  17306    340  -1615    101       C  
ATOM   4526  CD2 TYR C  95      71.380  39.187  53.755  1.00125.42           C  
ANISOU 4526  CD2 TYR C  95    15316  15602  16735    290  -1868   -359       C  
ATOM   4527  CE1 TYR C  95      73.589  40.304  55.036  1.00126.31           C  
ANISOU 4527  CE1 TYR C  95    15136  15602  17254    203  -1780    473       C  
ATOM   4528  CE2 TYR C  95      71.856  40.439  53.353  1.00126.82           C  
ANISOU 4528  CE2 TYR C  95    15600  15927  16658    227  -1992      0       C  
ATOM   4529  CZ  TYR C  95      72.958  40.996  53.993  1.00126.54           C  
ANISOU 4529  CZ  TYR C  95    15428  15814  16835    151  -1950    423       C  
ATOM   4530  OH  TYR C  95      73.428  42.232  53.595  1.00120.46           O  
ANISOU 4530  OH  TYR C  95    14801  15133  15833    -19  -2133    833       O  
ATOM   4531  N   VAL C  96      71.544  33.974  56.149  1.00126.97           N  
ANISOU 4531  N   VAL C  96    15328  14612  18300    457  -1119  -1160       N  
ATOM   4532  CA  VAL C  96      70.695  32.887  56.658  1.00130.60           C  
ANISOU 4532  CA  VAL C  96    15862  14744  19016    283  -1216  -1364       C  
ATOM   4533  C   VAL C  96      71.193  32.279  57.989  1.00134.64           C  
ANISOU 4533  C   VAL C  96    16234  14943  19978    400  -1058  -1158       C  
ATOM   4534  O   VAL C  96      70.405  32.106  58.928  1.00142.05           O  
ANISOU 4534  O   VAL C  96    17034  15789  21149    238  -1204  -1042       O  
ATOM   4535  CB  VAL C  96      70.429  31.790  55.599  1.00131.69           C  
ANISOU 4535  CB  VAL C  96    16441  14642  18951    191  -1203  -1826       C  
ATOM   4536  CG1 VAL C  96      69.625  30.649  56.202  1.00129.93           C  
ANISOU 4536  CG1 VAL C  96    16315  14001  19049    -99  -1359  -1954       C  
ATOM   4537  CG2 VAL C  96      69.674  32.377  54.424  1.00135.09           C  
ANISOU 4537  CG2 VAL C  96    17013  15389  18924      8  -1482  -2011       C  
ATOM   4538  N   PRO C  97      72.495  31.973  58.090  1.00132.63           N  
ANISOU 4538  N   PRO C  97    15979  14583  19829    710   -749  -1061       N  
ATOM   4539  CA  PRO C  97      72.945  31.565  59.425  1.00133.37           C  
ANISOU 4539  CA  PRO C  97    15917  14430  20325    828   -682   -800       C  
ATOM   4540  C   PRO C  97      72.870  32.728  60.436  1.00128.55           C  
ANISOU 4540  C   PRO C  97    15033  14033  19777    778   -905   -420       C  
ATOM   4541  O   PRO C  97      72.390  32.544  61.555  1.00129.13           O  
ANISOU 4541  O   PRO C  97    15061  13953  20049    732  -1002   -280       O  
ATOM   4542  CB  PRO C  97      74.397  31.114  59.199  1.00135.73           C  
ANISOU 4542  CB  PRO C  97    16190  14685  20694   1225   -331   -726       C  
ATOM   4543  CG  PRO C  97      74.792  31.696  57.885  1.00139.51           C  
ANISOU 4543  CG  PRO C  97    16692  15535  20781   1306   -194   -813       C  
ATOM   4544  CD  PRO C  97      73.542  31.831  57.070  1.00134.33           C  
ANISOU 4544  CD  PRO C  97    16316  14912  19811   1002   -431  -1157       C  
ATOM   4545  N   VAL C  98      73.274  33.920  60.007  1.00124.62           N  
ANISOU 4545  N   VAL C  98    14435  13857  19055    782  -1002   -259       N  
ATOM   4546  CA  VAL C  98      73.365  35.080  60.898  1.00122.49           C  
ANISOU 4546  CA  VAL C  98    14071  13684  18784    761  -1273     79       C  
ATOM   4547  C   VAL C  98      72.021  35.450  61.560  1.00124.22           C  
ANISOU 4547  C   VAL C  98    14361  13905  18931    701  -1505     53       C  
ATOM   4548  O   VAL C  98      72.003  35.979  62.673  1.00127.87           O  
ANISOU 4548  O   VAL C  98    14856  14301  19427    795  -1669    282       O  
ATOM   4549  CB  VAL C  98      73.992  36.299  60.179  1.00121.31           C  
ANISOU 4549  CB  VAL C  98    13892  13813  18385    695  -1389    272       C  
ATOM   4550  CG1 VAL C  98      73.870  37.555  61.020  1.00122.76           C  
ANISOU 4550  CG1 VAL C  98    14177  13972  18492    639  -1783    551       C  
ATOM   4551  CG2 VAL C  98      75.450  36.027  59.876  1.00127.83           C  
ANISOU 4551  CG2 VAL C  98    14486  14740  19341    788  -1135    485       C  
ATOM   4552  N   GLN C  99      70.907  35.138  60.892  1.00122.28           N  
ANISOU 4552  N   GLN C  99    14134  13759  18565    571  -1521   -205       N  
ATOM   4553  CA  GLN C  99      69.584  35.330  61.490  1.00120.47           C  
ANISOU 4553  CA  GLN C  99    13822  13644  18304    548  -1669   -167       C  
ATOM   4554  C   GLN C  99      69.502  34.715  62.892  1.00123.93           C  
ANISOU 4554  C   GLN C  99    14203  13876  19006    623  -1565     18       C  
ATOM   4555  O   GLN C  99      68.965  35.336  63.819  1.00129.67           O  
ANISOU 4555  O   GLN C  99    14916  14714  19638    798  -1653    218       O  
ATOM   4556  CB  GLN C  99      68.479  34.758  60.591  1.00118.59           C  
ANISOU 4556  CB  GLN C  99    13511  13545  18002    300  -1722   -424       C  
ATOM   4557  CG  GLN C  99      68.186  35.588  59.353  1.00118.26           C  
ANISOU 4557  CG  GLN C  99    13537  13797  17600    269  -1912   -555       C  
ATOM   4558  CD  GLN C  99      67.998  37.067  59.664  1.00118.40           C  
ANISOU 4558  CD  GLN C  99    13574  14029  17383    513  -2115   -324       C  
ATOM   4559  OE1 GLN C  99      67.095  37.450  60.410  1.00121.14           O  
ANISOU 4559  OE1 GLN C  99    13787  14527  17714    672  -2210   -179       O  
ATOM   4560  NE2 GLN C  99      68.857  37.906  59.091  1.00114.11           N  
ANISOU 4560  NE2 GLN C  99    13231  13492  16633    565  -2173   -261       N  
ATOM   4561  N   PHE C 100      70.038  33.497  63.046  1.00122.30           N  
ANISOU 4561  N   PHE C 100    14028  13359  19081    550  -1366    -39       N  
ATOM   4562  CA  PHE C 100      70.011  32.809  64.348  1.00118.28           C  
ANISOU 4562  CA  PHE C 100    13510  12617  18813    605  -1264    170       C  
ATOM   4563  C   PHE C 100      71.037  33.412  65.283  1.00118.92           C  
ANISOU 4563  C   PHE C 100    13671  12619  18894    868  -1329    431       C  
ATOM   4564  O   PHE C 100      70.703  33.826  66.396  1.00120.23           O  
ANISOU 4564  O   PHE C 100    13893  12813  18973   1015  -1405    650       O  
ATOM   4565  CB  PHE C 100      70.254  31.308  64.195  1.00112.88           C  
ANISOU 4565  CB  PHE C 100    12931  11540  18417    464  -1082     38       C  
ATOM   4566  CG  PHE C 100      69.283  30.630  63.288  1.00115.14           C  
ANISOU 4566  CG  PHE C 100    13245  11803  18700    110  -1128   -227       C  
ATOM   4567  CD1 PHE C 100      68.071  30.152  63.778  1.00119.76           C  
ANISOU 4567  CD1 PHE C 100    13675  12427  19400   -194  -1179    -95       C  
ATOM   4568  CD2 PHE C 100      69.576  30.457  61.935  1.00117.17           C  
ANISOU 4568  CD2 PHE C 100    13687  12020  18810     56  -1140   -577       C  
ATOM   4569  CE1 PHE C 100      67.158  29.520  62.932  1.00125.46           C  
ANISOU 4569  CE1 PHE C 100    14400  13126  20143   -636  -1333   -299       C  
ATOM   4570  CE2 PHE C 100      68.674  29.825  61.090  1.00123.09           C  
ANISOU 4570  CE2 PHE C 100    14557  12700  19509   -314  -1288   -846       C  
ATOM   4571  CZ  PHE C 100      67.459  29.359  61.588  1.00125.18           C  
ANISOU 4571  CZ  PHE C 100    14639  12980  19941   -706  -1430   -703       C  
ATOM   4572  N   VAL C 101      72.286  33.468  64.816  1.00117.35           N  
ANISOU 4572  N   VAL C 101    13475  12352  18761    932  -1311    431       N  
ATOM   4573  CA  VAL C 101      73.371  34.169  65.512  1.00114.93           C  
ANISOU 4573  CA  VAL C 101    13181  12025  18461   1072  -1487    720       C  
ATOM   4574  C   VAL C 101      72.894  35.509  66.084  1.00115.03           C  
ANISOU 4574  C   VAL C 101    13376  12159  18169   1122  -1803    851       C  
ATOM   4575  O   VAL C 101      73.069  35.789  67.283  1.00115.10           O  
ANISOU 4575  O   VAL C 101    13563  12036  18132   1261  -1976   1063       O  
ATOM   4576  CB  VAL C 101      74.540  34.442  64.552  1.00112.43           C  
ANISOU 4576  CB  VAL C 101    12711  11843  18165   1053  -1452    751       C  
ATOM   4577  CG1 VAL C 101      75.792  34.777  65.330  1.00110.76           C  
ANISOU 4577  CG1 VAL C 101    12389  11595  18097   1119  -1638   1122       C  
ATOM   4578  CG2 VAL C 101      74.773  33.242  63.656  1.00115.91           C  
ANISOU 4578  CG2 VAL C 101    13090  12203  18747   1116  -1093    507       C  
ATOM   4579  N   GLY C 102      72.312  36.332  65.209  1.00111.33           N  
ANISOU 4579  N   GLY C 102    12942  11909  17449   1056  -1899    715       N  
ATOM   4580  CA  GLY C 102      71.666  37.573  65.595  1.00110.98           C  
ANISOU 4580  CA  GLY C 102    13154  11945  17068   1198  -2178    782       C  
ATOM   4581  C   GLY C 102      70.632  37.424  66.699  1.00117.14           C  
ANISOU 4581  C   GLY C 102    14023  12739  17745   1446  -2111    834       C  
ATOM   4582  O   GLY C 102      70.677  38.151  67.694  1.00120.88           O  
ANISOU 4582  O   GLY C 102    14837  13101  17990   1694  -2319    984       O  
ATOM   4583  N   PHE C 103      69.700  36.481  66.541  1.00116.44           N  
ANISOU 4583  N   PHE C 103    13658  12789  17794   1370  -1833    736       N  
ATOM   4584  CA  PHE C 103      68.669  36.270  67.569  1.00113.93           C  
ANISOU 4584  CA  PHE C 103    13302  12597  17388   1579  -1688    883       C  
ATOM   4585  C   PHE C 103      69.285  35.916  68.917  1.00114.32           C  
ANISOU 4585  C   PHE C 103    13571  12381  17484   1733  -1659   1102       C  
ATOM   4586  O   PHE C 103      68.798  36.349  69.962  1.00108.22           O  
ANISOU 4586  O   PHE C 103    13009  11677  16429   2073  -1652   1267       O  
ATOM   4587  CB  PHE C 103      67.669  35.193  67.156  1.00115.13           C  
ANISOU 4587  CB  PHE C 103    13054  12928  17759   1309  -1443    830       C  
ATOM   4588  CG  PHE C 103      66.626  34.913  68.204  1.00119.12           C  
ANISOU 4588  CG  PHE C 103    13397  13658  18205   1466  -1234   1094       C  
ATOM   4589  CD1 PHE C 103      65.811  35.944  68.688  1.00121.38           C  
ANISOU 4589  CD1 PHE C 103    13713  14298  18104   1918  -1242   1227       C  
ATOM   4590  CD2 PHE C 103      66.476  33.639  68.736  1.00120.68           C  
ANISOU 4590  CD2 PHE C 103    13445  13710  18695   1216  -1007   1251       C  
ATOM   4591  CE1 PHE C 103      64.859  35.701  69.668  1.00123.35           C  
ANISOU 4591  CE1 PHE C 103    13761  14858  18246   2146   -961   1530       C  
ATOM   4592  CE2 PHE C 103      65.525  33.390  69.717  1.00124.50           C  
ANISOU 4592  CE2 PHE C 103    13734  14465  19102   1334   -767   1585       C  
ATOM   4593  CZ  PHE C 103      64.714  34.424  70.182  1.00126.92           C  
ANISOU 4593  CZ  PHE C 103    13987  15229  19005   1818   -710   1737       C  
ATOM   4594  N   ALA C 104      70.359  35.125  68.872  1.00115.98           N  
ANISOU 4594  N   ALA C 104    13749  12306  18011   1543  -1636   1111       N  
ATOM   4595  CA  ALA C 104      71.138  34.771  70.052  1.00115.53           C  
ANISOU 4595  CA  ALA C 104    13891  11982  18021   1673  -1686   1338       C  
ATOM   4596  C   ALA C 104      71.599  36.010  70.806  1.00115.67           C  
ANISOU 4596  C   ALA C 104    14331  11931  17687   1916  -2065   1461       C  
ATOM   4597  O   ALA C 104      71.188  36.233  71.947  1.00119.76           O  
ANISOU 4597  O   ALA C 104    15158  12427  17916   2210  -2085   1606       O  
ATOM   4598  CB  ALA C 104      72.338  33.910  69.658  1.00117.49           C  
ANISOU 4598  CB  ALA C 104    13993  11992  18655   1510  -1648   1332       C  
HETATM 4599  N   MSE C 105      72.430  36.830  70.153  1.00131.50           N  
ANISOU 4599  N   MSE C 105    16511  15740  17713   1385   -671   -587       N  
HETATM 4600  CA  MSE C 105      73.134  37.929  70.831  1.00126.44           C  
ANISOU 4600  CA  MSE C 105    15632  15739  16669   1218   -713      8       C  
HETATM 4601  C   MSE C 105      72.267  39.112  71.109  1.00119.20           C  
ANISOU 4601  C   MSE C 105    14820  14993  15478    644   -797    163       C  
HETATM 4602  O   MSE C 105      72.512  39.840  72.065  1.00118.30           O  
ANISOU 4602  O   MSE C 105    14588  15102  15256    411   -890    527       O  
HETATM 4603  CB  MSE C 105      74.274  38.436  70.002  1.00132.07           C  
ANISOU 4603  CB  MSE C 105    15953  17173  17055   1461   -535    -62       C  
HETATM 4604  CG  MSE C 105      75.248  37.348  69.681  1.00148.18           C  
ANISOU 4604  CG  MSE C 105    17809  19170  19322   2137   -413   -247       C  
HETATM 4605 SE   MSE C 105      76.303  38.100  68.232  1.00181.13          SE  
ANISOU 4605 SE   MSE C 105    21499  24361  22961   2414     21   -393      SE  
HETATM 4606  CE  MSE C 105      74.988  37.918  66.779  1.00170.04           C  
ANISOU 4606  CE  MSE C 105    20586  22984  21035   2556     42  -1149       C  
ATOM   4607  N   TRP C 106      71.281  39.360  70.250  1.00116.06           N  
ANISOU 4607  N   TRP C 106    14585  14588  14924    491   -794   -198       N  
ATOM   4608  CA  TRP C 106      70.276  40.373  70.546  1.00110.16           C  
ANISOU 4608  CA  TRP C 106    13958  13892  14004     54   -855    -30       C  
ATOM   4609  C   TRP C 106      69.466  39.944  71.778  1.00112.22           C  
ANISOU 4609  C   TRP C 106    14391  13612  14635   -203   -943    176       C  
ATOM   4610  O   TRP C 106      69.319  40.719  72.728  1.00111.55           O  
ANISOU 4610  O   TRP C 106    14332  13643  14407   -444   -965    529       O  
ATOM   4611  CB  TRP C 106      69.359  40.607  69.347  1.00108.88           C  
ANISOU 4611  CB  TRP C 106    13852  13993  13521    141   -893   -451       C  
ATOM   4612  CG  TRP C 106      69.763  41.772  68.439  1.00108.27           C  
ANISOU 4612  CG  TRP C 106    13689  14587  12862    336   -645   -179       C  
ATOM   4613  CD1 TRP C 106      71.021  42.070  67.987  1.00110.82           C  
ANISOU 4613  CD1 TRP C 106    13802  15278  13023    569   -314     84       C  
ATOM   4614  CD2 TRP C 106      68.883  42.727  67.822  1.00108.94           C  
ANISOU 4614  CD2 TRP C 106    13851  15028  12511    411   -596    -37       C  
ATOM   4615  NE1 TRP C 106      70.983  43.162  67.150  1.00110.68           N  
ANISOU 4615  NE1 TRP C 106    13764  15725  12563    739     47    486       N  
ATOM   4616  CE2 TRP C 106      69.684  43.584  67.030  1.00111.72           C  
ANISOU 4616  CE2 TRP C 106    14110  15866  12471    715   -137    454       C  
ATOM   4617  CE3 TRP C 106      67.493  42.947  67.867  1.00105.58           C  
ANISOU 4617  CE3 TRP C 106    13505  14580  12027    313   -840   -206       C  
ATOM   4618  CZ2 TRP C 106      69.143  44.651  66.296  1.00112.78           C  
ANISOU 4618  CZ2 TRP C 106    14328  16396  12126   1010    130    917       C  
ATOM   4619  CZ3 TRP C 106      66.957  44.011  67.139  1.00104.79           C  
ANISOU 4619  CZ3 TRP C 106    13437  14986  11392    633   -698    133       C  
ATOM   4620  CH2 TRP C 106      67.780  44.843  66.361  1.00110.76           C  
ANISOU 4620  CH2 TRP C 106    14196  16159  11726   1023   -198    748       C  
ATOM   4621  N   ARG C 107      68.998  38.687  71.776  1.00115.22           N  
ANISOU 4621  N   ARG C 107    14857  13370  15551   -118   -912    -54       N  
ATOM   4622  CA  ARG C 107      68.178  38.133  72.878  1.00116.53           C  
ANISOU 4622  CA  ARG C 107    15153  12916  16205   -320   -777    307       C  
ATOM   4623  C   ARG C 107      68.703  38.488  74.257  1.00114.54           C  
ANISOU 4623  C   ARG C 107    14968  12923  15628   -200   -737   1056       C  
ATOM   4624  O   ARG C 107      67.931  38.723  75.178  1.00121.00           O  
ANISOU 4624  O   ARG C 107    15888  13686  16397   -378   -626   1422       O  
ATOM   4625  CB  ARG C 107      68.056  36.610  72.753  1.00128.75           C  
ANISOU 4625  CB  ARG C 107    16730  13539  18648   -165   -567    106       C  
ATOM   4626  CG  ARG C 107      66.961  35.994  73.631  1.00136.19           C  
ANISOU 4626  CG  ARG C 107    17728  13669  20347   -466   -227    485       C  
ATOM   4627  CD  ARG C 107      66.927  34.478  73.502  1.00147.34           C  
ANISOU 4627  CD  ARG C 107    19140  13879  22959   -349    133    325       C  
ATOM   4628  NE  ARG C 107      68.260  33.900  73.637  1.00154.58           N  
ANISOU 4628  NE  ARG C 107    20197  14708  23826    326    218    694       N  
ATOM   4629  CZ  ARG C 107      68.566  32.640  73.357  1.00164.24           C  
ANISOU 4629  CZ  ARG C 107    21457  14901  26046    633    522    490       C  
ATOM   4630  NH1 ARG C 107      69.814  32.213  73.507  1.00166.08           N  
ANISOU 4630  NH1 ARG C 107    21773  15197  26130   1374    584    894       N  
ATOM   4631  NH2 ARG C 107      67.630  31.805  72.927  1.00174.51           N  
ANISOU 4631  NH2 ARG C 107    22634  15072  28599    208    771   -201       N  
ATOM   4632  N   LYS C 108      70.022  38.519  74.393  1.00112.64           N  
ANISOU 4632  N   LYS C 108    14590  13098  15109    168   -844   1208       N  
ATOM   4633  CA  LYS C 108      70.662  38.811  75.671  1.00111.97           C  
ANISOU 4633  CA  LYS C 108    14429  13521  14592    416   -959   1715       C  
ATOM   4634  C   LYS C 108      70.590  40.282  76.088  1.00107.36           C  
ANISOU 4634  C   LYS C 108    13720  13567  13503     43  -1166   1536       C  
ATOM   4635  O   LYS C 108      70.843  40.599  77.227  1.00106.56           O  
ANISOU 4635  O   LYS C 108    13547  13965  12975    209  -1326   1731       O  
ATOM   4636  CB  LYS C 108      72.125  38.340  75.656  1.00116.98           C  
ANISOU 4636  CB  LYS C 108    14776  14508  15163    977  -1080   1807       C  
ATOM   4637  CG  LYS C 108      72.446  37.224  76.643  1.00124.47           C  
ANISOU 4637  CG  LYS C 108    15828  15291  16172   1688   -964   2525       C  
ATOM   4638  CD  LYS C 108      73.538  36.317  76.115  1.00128.70           C  
ANISOU 4638  CD  LYS C 108    16172  15693  17035   2306   -917   2525       C  
ATOM   4639  CE  LYS C 108      74.527  37.083  75.252  1.00128.57           C  
ANISOU 4639  CE  LYS C 108    15667  16370  16812   2153  -1148   1914       C  
ATOM   4640  NZ  LYS C 108      75.513  36.177  74.588  1.00138.96           N  
ANISOU 4640  NZ  LYS C 108    16769  17562  18467   2788  -1018   1825       N  
ATOM   4641  N   HIS C 109      70.245  41.173  75.162  1.00111.26           N  
ANISOU 4641  N   HIS C 109    14180  14049  14042   -369  -1142   1142       N  
ATOM   4642  CA  HIS C 109      70.426  42.619  75.396  1.00118.39           C  
ANISOU 4642  CA  HIS C 109    14912  15335  14735   -704  -1230    934       C  
ATOM   4643  C   HIS C 109      69.190  43.467  75.104  1.00117.85           C  
ANISOU 4643  C   HIS C 109    15061  15023  14691  -1044  -1089    841       C  
ATOM   4644  O   HIS C 109      69.275  44.497  74.428  1.00116.74           O  
ANISOU 4644  O   HIS C 109    14834  14890  14630  -1247   -963    714       O  
ATOM   4645  CB  HIS C 109      71.650  43.146  74.632  1.00119.32           C  
ANISOU 4645  CB  HIS C 109    14620  15727  14987   -756  -1195    736       C  
ATOM   4646  CG  HIS C 109      72.949  42.634  75.163  1.00128.18           C  
ANISOU 4646  CG  HIS C 109    15330  17304  16068   -427  -1411    739       C  
ATOM   4647  ND1 HIS C 109      73.557  41.497  74.673  1.00132.24           N  
ANISOU 4647  ND1 HIS C 109    15781  17784  16678     47  -1358    882       N  
ATOM   4648  CD2 HIS C 109      73.732  43.071  76.177  1.00134.20           C  
ANISOU 4648  CD2 HIS C 109    15660  18648  16679   -410  -1732    534       C  
ATOM   4649  CE1 HIS C 109      74.669  41.269  75.348  1.00137.77           C  
ANISOU 4649  CE1 HIS C 109    16026  19035  17285    388  -1607    903       C  
ATOM   4650  NE2 HIS C 109      74.798  42.208  76.267  1.00143.32           N  
ANISOU 4650  NE2 HIS C 109    16460  20199  17796    113  -1887    654       N  
HETATM 4651  N   MSE C 110      68.058  43.059  75.668  1.00116.86           N  
ANISOU 4651  N   MSE C 110    15171  14680  14548  -1049  -1031    998       N  
HETATM 4652  CA  MSE C 110      66.785  43.719  75.414  1.00110.47           C  
ANISOU 4652  CA  MSE C 110    14479  13707  13785  -1269   -912    913       C  
HETATM 4653  C   MSE C 110      66.429  44.646  76.559  1.00110.47           C  
ANISOU 4653  C   MSE C 110    14534  13898  13541  -1359   -896    886       C  
HETATM 4654  O   MSE C 110      67.207  44.802  77.494  1.00123.36           O  
ANISOU 4654  O   MSE C 110    16086  15884  14901  -1259  -1046    817       O  
HETATM 4655  CB  MSE C 110      65.782  42.603  75.209  1.00112.06           C  
ANISOU 4655  CB  MSE C 110    14731  13545  14301  -1260   -811    977       C  
HETATM 4656  CG  MSE C 110      66.201  41.792  73.975  1.00119.03           C  
ANISOU 4656  CG  MSE C 110    15529  14277  15417  -1134   -889    696       C  
HETATM 4657 SE   MSE C 110      65.914  42.905  72.367  1.00118.98          SE  
ANISOU 4657 SE   MSE C 110    15435  14693  15077  -1065   -965    364      SE  
HETATM 4658  CE  MSE C 110      66.949  41.922  71.028  1.00119.46           C  
ANISOU 4658  CE  MSE C 110    15397  14913  15078   -682  -1027    -10       C  
ATOM   4659  N   ALA C 111      65.264  45.293  76.475  1.00107.78           N  
ANISOU 4659  N   ALA C 111    14271  13428  13252  -1468   -751    836       N  
ATOM   4660  CA  ALA C 111      64.837  46.321  77.466  1.00106.79           C  
ANISOU 4660  CA  ALA C 111    14207  13443  12924  -1494   -680    665       C  
ATOM   4661  C   ALA C 111      63.482  46.927  77.073  1.00101.37           C  
ANISOU 4661  C   ALA C 111    13552  12566  12398  -1505   -478    670       C  
ATOM   4662  O   ALA C 111      63.025  46.743  75.949  1.00101.27           O  
ANISOU 4662  O   ALA C 111    13464  12433  12581  -1482   -480    747       O  
ATOM   4663  CB  ALA C 111      65.895  47.420  77.605  1.00108.83           C  
ANISOU 4663  CB  ALA C 111    14348  13751  13248  -1635   -788    251       C  
ATOM   4664  N   LEU C 112      62.875  47.691  77.979  1.00 98.69           N  
ANISOU 4664  N   LEU C 112    13273  12317  11905  -1440   -337    510       N  
ATOM   4665  CA  LEU C 112      61.460  48.067  77.835  1.00100.64           C  
ANISOU 4665  CA  LEU C 112    13468  12494  12276  -1335   -113    577       C  
ATOM   4666  C   LEU C 112      61.118  49.180  76.801  1.00105.57           C  
ANISOU 4666  C   LEU C 112    14086  12837  13186  -1218    -37    540       C  
ATOM   4667  O   LEU C 112      60.486  48.901  75.771  1.00104.18           O  
ANISOU 4667  O   LEU C 112    13751  12730  13099  -1084    -92    722       O  
ATOM   4668  CB  LEU C 112      60.817  48.342  79.194  1.00101.87           C  
ANISOU 4668  CB  LEU C 112    13669  12931  12104  -1169    112    479       C  
ATOM   4669  CG  LEU C 112      59.693  47.370  79.597  1.00101.59           C  
ANISOU 4669  CG  LEU C 112    13450  13068  12079  -1117    409    895       C  
ATOM   4670  CD1 LEU C 112      59.825  45.988  78.939  1.00 97.20           C  
ANISOU 4670  CD1 LEU C 112    12745  12285  11902  -1337    342   1219       C  
ATOM   4671  CD2 LEU C 112      59.582  47.264  81.109  1.00102.65           C  
ANISOU 4671  CD2 LEU C 112    13693  13693  11615   -840    690   1014       C  
ATOM   4672  N   GLY C 113      61.527  50.417  77.067  1.00107.06           N  
ANISOU 4672  N   GLY C 113    14409  12723  13546  -1206    102    288       N  
ATOM   4673  CA  GLY C 113      61.191  51.523  76.163  1.00109.49           C  
ANISOU 4673  CA  GLY C 113    14763  12614  14224   -970    353    477       C  
ATOM   4674  C   GLY C 113      59.937  52.216  76.628  1.00113.92           C  
ANISOU 4674  C   GLY C 113    15319  13123  14839   -639    582    394       C  
ATOM   4675  O   GLY C 113      59.055  51.583  77.200  1.00111.68           O  
ANISOU 4675  O   GLY C 113    14882  13270  14278   -575    542    363       O  
ATOM   4676  N   GLU C 114      59.844  53.519  76.360  1.00121.28           N  
ANISOU 4676  N   GLU C 114    16384  13458  16239   -393    925    425       N  
ATOM   4677  CA  GLU C 114      59.086  54.441  77.234  1.00130.88           C  
ANISOU 4677  CA  GLU C 114    17668  14405  17655   -134   1209     31       C  
ATOM   4678  C   GLU C 114      57.612  54.129  77.488  1.00128.27           C  
ANISOU 4678  C   GLU C 114    17113  14623  16999    272   1243    153       C  
ATOM   4679  O   GLU C 114      57.105  54.438  78.551  1.00132.32           O  
ANISOU 4679  O   GLU C 114    17632  15231  17410    402   1421   -286       O  
ATOM   4680  CB  GLU C 114      59.271  55.899  76.807  1.00149.53           C  
ANISOU 4680  CB  GLU C 114    20216  15767  20828     94   1687    103       C  
ATOM   4681  CG  GLU C 114      60.150  56.706  77.761  1.00162.95           C  
ANISOU 4681  CG  GLU C 114    22017  16785  23107   -321   1823   -814       C  
ATOM   4682  CD  GLU C 114      60.613  58.019  77.165  1.00172.51           C  
ANISOU 4682  CD  GLU C 114    23352  16702  25492   -304   2416   -661       C  
ATOM   4683  OE1 GLU C 114      61.600  58.007  76.396  1.00174.15           O  
ANISOU 4683  OE1 GLU C 114    23504  16567  26095   -629   2546   -240       O  
ATOM   4684  OE2 GLU C 114      60.000  59.062  77.477  1.00179.07           O  
ANISOU 4684  OE2 GLU C 114    24314  16790  26932     58   2846   -926       O  
ATOM   4685  N   THR C 115      56.938  53.527  76.508  1.00126.97           N  
ANISOU 4685  N   THR C 115    16667  14900  16675    495   1072    656       N  
ATOM   4686  CA  THR C 115      55.556  53.035  76.682  1.00126.48           C  
ANISOU 4686  CA  THR C 115    16154  15454  16447    744   1053    696       C  
ATOM   4687  C   THR C 115      55.545  51.727  77.472  1.00120.50           C  
ANISOU 4687  C   THR C 115    15211  15128  15444    245    947    552       C  
ATOM   4688  O   THR C 115      54.569  51.401  78.165  1.00122.82           O  
ANISOU 4688  O   THR C 115    15169  15790  15707    308   1171    522       O  
ATOM   4689  CB  THR C 115      54.868  52.780  75.317  1.00130.35           C  
ANISOU 4689  CB  THR C 115    16238  16410  16879   1145    783   1067       C  
ATOM   4690  OG1 THR C 115      55.772  52.083  74.436  1.00128.10           O  
ANISOU 4690  OG1 THR C 115    16041  16216  16412    878    451   1185       O  
ATOM   4691  CG2 THR C 115      54.428  54.105  74.666  1.00137.05           C  
ANISOU 4691  CG2 THR C 115    17173  17009  17890   1974   1037   1456       C  
ATOM   4692  N   ALA C 116      56.635  50.978  77.354  1.00112.84           N  
ANISOU 4692  N   ALA C 116    14431  14084  14359   -189    704    567       N  
ATOM   4693  CA  ALA C 116      56.709  49.622  77.880  1.00107.65           C  
ANISOU 4693  CA  ALA C 116    13626  13690  13586   -567    657    640       C  
ATOM   4694  C   ALA C 116      55.630  48.713  77.282  1.00108.56           C  
ANISOU 4694  C   ALA C 116    13147  14078  14022   -649    595    738       C  
ATOM   4695  O   ALA C 116      55.074  47.903  77.973  1.00108.71           O  
ANISOU 4695  O   ALA C 116    12882  14214  14206   -860    865    857       O  
ATOM   4696  CB  ALA C 116      56.637  49.628  79.412  1.00103.40           C  
ANISOU 4696  CB  ALA C 116    13223  13359  12704   -525    993    564       C  
ATOM   4697  N   GLU C 117      55.340  48.874  75.991  1.00113.49           N  
ANISOU 4697  N   GLU C 117    13524  14846  14749   -443    268    667       N  
ATOM   4698  CA  GLU C 117      54.386  47.992  75.294  1.00123.69           C  
ANISOU 4698  CA  GLU C 117    14098  16515  16382   -546     31    449       C  
ATOM   4699  C   GLU C 117      55.127  46.950  74.456  1.00127.00           C  
ANISOU 4699  C   GLU C 117    14517  16863  16874   -849   -354    223       C  
ATOM   4700  O   GLU C 117      54.502  46.106  73.792  1.00136.68           O  
ANISOU 4700  O   GLU C 117    15122  18337  18470  -1010   -641   -218       O  
ATOM   4701  CB  GLU C 117      53.470  48.792  74.371  1.00129.54           C  
ANISOU 4701  CB  GLU C 117    14427  17776  17016     80   -199    369       C  
ATOM   4702  CG  GLU C 117      52.525  49.758  75.047  1.00139.26           C  
ANISOU 4702  CG  GLU C 117    15500  19110  18300    504    179    515       C  
ATOM   4703  CD  GLU C 117      51.657  50.508  74.040  1.00155.69           C  
ANISOU 4703  CD  GLU C 117    17137  21779  20239   1308    -85    544       C  
ATOM   4704  OE1 GLU C 117      52.031  50.558  72.840  1.00154.55           O  
ANISOU 4704  OE1 GLU C 117    17044  21943  19733   1665   -508    592       O  
ATOM   4705  OE2 GLU C 117      50.603  51.050  74.445  1.00169.47           O  
ANISOU 4705  OE2 GLU C 117    18458  23782  22148   1707    153    566       O  
ATOM   4706  N   THR C 118      56.456  47.053  74.450  1.00123.25           N  
ANISOU 4706  N   THR C 118    14652  16077  16098   -899   -378    399       N  
ATOM   4707  CA  THR C 118      57.319  46.133  73.715  1.00119.01           C  
ANISOU 4707  CA  THR C 118    14187  15458  15573  -1083   -667    203       C  
ATOM   4708  C   THR C 118      58.748  46.167  74.306  1.00113.82           C  
ANISOU 4708  C   THR C 118    14105  14424  14718  -1230   -526    480       C  
ATOM   4709  O   THR C 118      58.996  46.830  75.313  1.00110.22           O  
ANISOU 4709  O   THR C 118    13925  13833  14120  -1234   -275    686       O  
ATOM   4710  CB  THR C 118      57.331  46.454  72.197  1.00121.40           C  
ANISOU 4710  CB  THR C 118    14358  16285  15484   -605  -1068     -4       C  
ATOM   4711  OG1 THR C 118      57.822  45.322  71.466  1.00122.95           O  
ANISOU 4711  OG1 THR C 118    14429  16533  15752   -761  -1375   -462       O  
ATOM   4712  CG2 THR C 118      58.195  47.718  71.884  1.00120.22           C  
ANISOU 4712  CG2 THR C 118    14736  16067  14874   -192   -881    507       C  
ATOM   4713  N   GLU C 119      59.664  45.432  73.698  1.00111.56           N  
ANISOU 4713  N   GLU C 119    13910  14059  14417  -1305   -720    361       N  
ATOM   4714  CA  GLU C 119      61.031  45.426  74.147  1.00109.01           C  
ANISOU 4714  CA  GLU C 119    13960  13522  13935  -1383   -652    565       C  
ATOM   4715  C   GLU C 119      61.935  45.864  73.008  1.00106.43           C  
ANISOU 4715  C   GLU C 119    13743  13358  13337  -1150   -771    559       C  
ATOM   4716  O   GLU C 119      61.793  45.374  71.898  1.00111.31           O  
ANISOU 4716  O   GLU C 119    14192  14246  13852   -954   -977    312       O  
ATOM   4717  CB  GLU C 119      61.409  44.037  74.659  1.00119.79           C  
ANISOU 4717  CB  GLU C 119    15312  14595  15606  -1600   -612    596       C  
ATOM   4718  CG  GLU C 119      60.579  43.574  75.871  1.00141.52           C  
ANISOU 4718  CG  GLU C 119    17971  17171  18627  -1760   -273    873       C  
ATOM   4719  CD  GLU C 119      59.726  42.317  75.596  1.00163.28           C  
ANISOU 4719  CD  GLU C 119    20322  19543  22172  -2031   -150    709       C  
ATOM   4720  OE1 GLU C 119      60.301  41.281  75.174  1.00168.95           O  
ANISOU 4720  OE1 GLU C 119    21043  19869  23279  -2103   -214    562       O  
ATOM   4721  OE2 GLU C 119      58.485  42.354  75.844  1.00164.94           O  
ANISOU 4721  OE2 GLU C 119    20147  19779  22743  -2189     60    678       O  
ATOM   4722  N   GLU C 120      62.787  46.867  73.268  1.00105.59           N  
ANISOU 4722  N   GLU C 120    13852  13128  13138  -1143   -593    781       N  
ATOM   4723  CA  GLU C 120      63.799  47.340  72.285  1.00107.52           C  
ANISOU 4723  CA  GLU C 120    14151  13440  13261   -968   -487    957       C  
ATOM   4724  C   GLU C 120      65.207  46.943  72.704  1.00106.90           C  
ANISOU 4724  C   GLU C 120    14066  13259  13290  -1200   -495    911       C  
ATOM   4725  O   GLU C 120      65.569  47.077  73.874  1.00111.50           O  
ANISOU 4725  O   GLU C 120    14662  13711  13990  -1443   -526    805       O  
ATOM   4726  CB  GLU C 120      63.736  48.877  72.068  1.00110.46           C  
ANISOU 4726  CB  GLU C 120    14632  13590  13747   -804   -121   1298       C  
ATOM   4727  CG  GLU C 120      62.937  49.656  73.114  1.00121.82           C  
ANISOU 4727  CG  GLU C 120    16145  14723  15418   -904    -12   1194       C  
ATOM   4728  CD  GLU C 120      63.510  51.047  73.429  1.00129.89           C  
ANISOU 4728  CD  GLU C 120    17278  15151  16920  -1018    390   1262       C  
ATOM   4729  OE1 GLU C 120      64.626  51.117  73.973  1.00136.47           O  
ANISOU 4729  OE1 GLU C 120    18040  15791  18021  -1413    390    987       O  
ATOM   4730  OE2 GLU C 120      62.811  52.069  73.192  1.00130.28           O  
ANISOU 4730  OE2 GLU C 120    17426  14892  17181   -703    707   1515       O  
ATOM   4731  N   VAL C 121      65.994  46.463  71.734  1.00103.24           N  
ANISOU 4731  N   VAL C 121    12892  12063  14270      7   -580   1373       N  
ATOM   4732  CA  VAL C 121      67.431  46.151  71.916  1.00 99.87           C  
ANISOU 4732  CA  VAL C 121    12685  11628  13633    183   -652   1309       C  
ATOM   4733  C   VAL C 121      68.216  47.373  72.402  1.00103.29           C  
ANISOU 4733  C   VAL C 121    13214  12356  13673    309   -704   1289       C  
ATOM   4734  O   VAL C 121      67.820  48.520  72.144  1.00105.75           O  
ANISOU 4734  O   VAL C 121    13419  12742  14016    264   -639   1226       O  
ATOM   4735  CB  VAL C 121      68.061  45.623  70.594  1.00 96.36           C  
ANISOU 4735  CB  VAL C 121    12184  11168  13259     49   -808    966       C  
ATOM   4736  CG1 VAL C 121      68.472  46.773  69.685  1.00 88.83           C  
ANISOU 4736  CG1 VAL C 121    11133  10611  12006     40  -1069    838       C  
ATOM   4737  CG2 VAL C 121      69.236  44.703  70.874  1.00 97.54           C  
ANISOU 4737  CG2 VAL C 121    12472  11044  13543    246   -667   1038       C  
ATOM   4738  N   LYS C 122      69.309  47.126  73.126  1.00105.35           N  
ANISOU 4738  N   LYS C 122    13585  12807  13633    443   -732   1381       N  
ATOM   4739  CA  LYS C 122      70.126  48.204  73.665  1.00103.89           C  
ANISOU 4739  CA  LYS C 122    13431  13031  13009    403   -745   1197       C  
ATOM   4740  C   LYS C 122      71.176  48.605  72.647  1.00 97.16           C  
ANISOU 4740  C   LYS C 122    12559  12211  12147    444   -966    971       C  
ATOM   4741  O   LYS C 122      72.029  47.829  72.304  1.00 94.61           O  
ANISOU 4741  O   LYS C 122    12231  11885  11830    579  -1124   1082       O  
ATOM   4742  CB  LYS C 122      70.763  47.791  74.999  1.00108.55           C  
ANISOU 4742  CB  LYS C 122    13991  14160  13091    436   -720   1471       C  
ATOM   4743  CG  LYS C 122      69.794  47.836  76.190  1.00115.92           C  
ANISOU 4743  CG  LYS C 122    14934  15281  13827    314   -423   1600       C  
ATOM   4744  CD  LYS C 122      70.484  47.530  77.526  1.00125.11           C  
ANISOU 4744  CD  LYS C 122    15940  17361  14232    281   -432   1945       C  
ATOM   4745  CE  LYS C 122      70.676  46.028  77.746  1.00129.35           C  
ANISOU 4745  CE  LYS C 122    16303  17866  14977    677   -457   2840       C  
ATOM   4746  NZ  LYS C 122      71.644  45.715  78.844  1.00135.03           N  
ANISOU 4746  NZ  LYS C 122    16663  19728  14911    748   -559   3474       N  
ATOM   4747  N   ALA C 123      71.058  49.815  72.125  1.00 97.09           N  
ANISOU 4747  N   ALA C 123    12491  12151  12246    362   -869    727       N  
ATOM   4748  CA  ALA C 123      71.879  50.243  70.998  1.00 97.19           C  
ANISOU 4748  CA  ALA C 123    12440  12167  12320    427  -1026    600       C  
ATOM   4749  C   ALA C 123      73.158  50.904  71.483  1.00 93.65           C  
ANISOU 4749  C   ALA C 123    12003  11985  11595    365  -1005    334       C  
ATOM   4750  O   ALA C 123      73.135  51.640  72.457  1.00 99.30           O  
ANISOU 4750  O   ALA C 123    12707  12869  12153    148   -726     75       O  
ATOM   4751  CB  ALA C 123      71.091  51.191  70.107  1.00 98.55           C  
ANISOU 4751  CB  ALA C 123    12398  12200  12844    438   -857    706       C  
ATOM   4752  N   LYS C 124      74.273  50.616  70.808  1.00 89.05           N  
ANISOU 4752  N   LYS C 124    11404  11485  10942    480  -1248    323       N  
ATOM   4753  CA  LYS C 124      75.586  51.169  71.180  1.00 93.47           C  
ANISOU 4753  CA  LYS C 124    11887  12390  11238    391  -1281     89       C  
ATOM   4754  C   LYS C 124      76.135  52.046  70.059  1.00 92.91           C  
ANISOU 4754  C   LYS C 124    11742  12113  11447    440  -1209    -80       C  
ATOM   4755  O   LYS C 124      75.729  51.911  68.907  1.00 86.22           O  
ANISOU 4755  O   LYS C 124    10881  11039  10837    597  -1263    104       O  
ATOM   4756  CB  LYS C 124      76.593  50.045  71.513  1.00 90.46           C  
ANISOU 4756  CB  LYS C 124    11436  12344  10589    550  -1565    405       C  
ATOM   4757  CG  LYS C 124      76.164  49.136  72.649  1.00 93.47           C  
ANISOU 4757  CG  LYS C 124    11773  13007  10732    589  -1568    816       C  
ATOM   4758  CD  LYS C 124      77.280  48.203  73.103  1.00103.30           C  
ANISOU 4758  CD  LYS C 124    12754  14707  11787    816  -1731   1385       C  
ATOM   4759  CE  LYS C 124      77.601  47.137  72.056  1.00101.83           C  
ANISOU 4759  CE  LYS C 124    12607  13856  12228   1160  -1664   1662       C  
ATOM   4760  NZ  LYS C 124      78.439  46.040  72.620  1.00102.17           N  
ANISOU 4760  NZ  LYS C 124    12304  14139  12376   1503  -1599   2488       N  
ATOM   4761  N   ALA C 125      77.073  52.932  70.407  1.00 97.12           N  
ANISOU 4761  N   ALA C 125    12161  12840  11900    251  -1062   -438       N  
ATOM   4762  CA  ALA C 125      77.677  53.852  69.442  1.00 94.56           C  
ANISOU 4762  CA  ALA C 125    11721  12269  11939    307   -877   -561       C  
ATOM   4763  C   ALA C 125      79.190  53.708  69.414  1.00 95.16           C  
ANISOU 4763  C   ALA C 125    11697  12682  11777    282  -1111   -701       C  
ATOM   4764  O   ALA C 125      79.853  53.981  70.408  1.00100.03           O  
ANISOU 4764  O   ALA C 125    12169  13778  12056    -45  -1093  -1046       O  
ATOM   4765  CB  ALA C 125      77.298  55.287  69.771  1.00 93.92           C  
ANISOU 4765  CB  ALA C 125    11509  11864  12310     63   -209   -919       C  
ATOM   4766  N   LEU C 126      79.725  53.289  68.259  1.00 92.90           N  
ANISOU 4766  N   LEU C 126    11425  12254  11619    572  -1306   -451       N  
ATOM   4767  CA  LEU C 126      81.173  53.320  67.984  1.00 95.04           C  
ANISOU 4767  CA  LEU C 126    11553  12714  11842    607  -1427   -527       C  
ATOM   4768  C   LEU C 126      81.722  54.732  68.058  1.00100.47           C  
ANISOU 4768  C   LEU C 126    12046  13337  12789    348  -1042   -961       C  
ATOM   4769  O   LEU C 126      80.999  55.698  67.763  1.00104.52           O  
ANISOU 4769  O   LEU C 126    12535  13415  13759    316   -575  -1033       O  
ATOM   4770  CB  LEU C 126      81.466  52.774  66.590  1.00 89.22           C  
ANISOU 4770  CB  LEU C 126    10887  11742  11268    920  -1528   -273       C  
ATOM   4771  CG  LEU C 126      81.123  51.330  66.249  1.00 86.93           C  
ANISOU 4771  CG  LEU C 126    10756  11365  10907   1085  -1703    -42       C  
ATOM   4772  CD1 LEU C 126      81.466  51.110  64.799  1.00 88.56           C  
ANISOU 4772  CD1 LEU C 126    10989  11443  11215   1205  -1644    -58       C  
ATOM   4773  CD2 LEU C 126      81.845  50.317  67.133  1.00 84.43           C  
ANISOU 4773  CD2 LEU C 126    10351  11224  10502   1180  -1837    193       C  
ATOM   4774  N   THR C 127      83.010  54.859  68.418  1.00 99.54           N  
ANISOU 4774  N   THR C 127    11703  13625  12489    166  -1149  -1196       N  
ATOM   4775  CA  THR C 127      83.707  56.157  68.317  1.00 99.06           C  
ANISOU 4775  CA  THR C 127    11412  13425  12802   -131   -701  -1705       C  
ATOM   4776  C   THR C 127      84.473  56.248  67.008  1.00 90.18           C  
ANISOU 4776  C   THR C 127    10243  11975  12044    228   -692  -1417       C  
ATOM   4777  O   THR C 127      84.545  55.275  66.258  1.00 83.09           O  
ANISOU 4777  O   THR C 127     9493  11065  11011    621  -1037   -948       O  
ATOM   4778  CB  THR C 127      84.658  56.418  69.489  1.00103.14           C  
ANISOU 4778  CB  THR C 127    11590  14743  12855   -715   -764  -2277       C  
ATOM   4779  OG1 THR C 127      85.881  55.710  69.278  1.00112.58           O  
ANISOU 4779  OG1 THR C 127    12564  16431  13780   -527  -1241  -1924       O  
ATOM   4780  CG2 THR C 127      84.029  55.984  70.791  1.00105.94           C  
ANISOU 4780  CG2 THR C 127    11945  15756  12550  -1037   -930  -2397       C  
ATOM   4781  N   VAL C 128      85.015  57.427  66.724  1.00 87.79           N  
ANISOU 4781  N   VAL C 128     9722  11367  12266     53   -178  -1751       N  
ATOM   4782  CA  VAL C 128      85.591  57.699  65.424  1.00 87.13           C  
ANISOU 4782  CA  VAL C 128     9572  10933  12598    417    -33  -1405       C  
ATOM   4783  C   VAL C 128      86.786  56.771  65.216  1.00 92.95           C  
ANISOU 4783  C   VAL C 128    10262  12094  12959    561   -552  -1259       C  
ATOM   4784  O   VAL C 128      86.986  56.202  64.118  1.00 87.50           O  
ANISOU 4784  O   VAL C 128     9689  11275  12279    970   -687   -828       O  
ATOM   4785  CB  VAL C 128      86.042  59.176  65.315  1.00 90.20           C  
ANISOU 4785  CB  VAL C 128     9655  10838  13777    172    760  -1792       C  
ATOM   4786  CG1 VAL C 128      86.437  59.514  63.890  1.00 88.63           C  
ANISOU 4786  CG1 VAL C 128     9356  10275  14044    643    994  -1219       C  
ATOM   4787  CG2 VAL C 128      84.942  60.120  65.801  1.00 95.93           C  
ANISOU 4787  CG2 VAL C 128    10339  11038  15070    -45   1497  -2021       C  
ATOM   4788  N   ARG C 129      87.569  56.603  66.287  1.00103.98           N  
ANISOU 4788  N   ARG C 129    11413  14095  13997    187   -790  -1598       N  
ATOM   4789  CA  ARG C 129      88.720  55.719  66.272  1.00107.44           C  
ANISOU 4789  CA  ARG C 129    11649  15006  14165    352  -1224  -1289       C  
ATOM   4790  C   ARG C 129      88.243  54.310  65.995  1.00103.40           C  
ANISOU 4790  C   ARG C 129    11412  14424  13448    807  -1550   -692       C  
ATOM   4791  O   ARG C 129      88.602  53.717  64.977  1.00104.71           O  
ANISOU 4791  O   ARG C 129    11693  14264  13827   1190  -1531   -379       O  
ATOM   4792  CB  ARG C 129      89.479  55.783  67.603  1.00116.73           C  
ANISOU 4792  CB  ARG C 129    12344  17166  14841   -176  -1466  -1593       C  
ATOM   4793  CG  ARG C 129      90.987  55.933  67.437  1.00128.91           C  
ANISOU 4793  CG  ARG C 129    13401  19109  16468   -260  -1551  -1589       C  
ATOM   4794  CD  ARG C 129      91.768  55.541  68.697  1.00139.74           C  
ANISOU 4794  CD  ARG C 129    14135  21850  17108   -667  -2007  -1504       C  
ATOM   4795  NE  ARG C 129      91.343  56.266  69.909  1.00147.43           N  
ANISOU 4795  NE  ARG C 129    14907  23577  17530  -1497  -1914  -2311       N  
ATOM   4796  CZ  ARG C 129      92.036  57.246  70.500  1.00156.22           C  
ANISOU 4796  CZ  ARG C 129    15510  25395  18449  -2350  -1712  -3210       C  
ATOM   4797  NH1 ARG C 129      93.194  57.659  69.990  1.00164.28           N  
ANISOU 4797  NH1 ARG C 129    16155  26423  19840  -2436  -1625  -3340       N  
ATOM   4798  NH2 ARG C 129      91.568  57.818  71.604  1.00157.51           N  
ANISOU 4798  NH2 ARG C 129    15517  26271  18057  -3195  -1524  -4076       N  
ATOM   4799  N   GLN C 130      87.371  53.808  66.871  1.00 99.73           N  
ANISOU 4799  N   GLN C 130    11056  14205  12631    713  -1726   -619       N  
ATOM   4800  CA  GLN C 130      86.728  52.505  66.694  1.00 97.90           C  
ANISOU 4800  CA  GLN C 130    11076  13770  12350   1069  -1878   -143       C  
ATOM   4801  C   GLN C 130      86.210  52.291  65.265  1.00 98.98           C  
ANISOU 4801  C   GLN C 130    11555  13262  12789   1338  -1683   -112       C  
ATOM   4802  O   GLN C 130      86.342  51.201  64.711  1.00103.46           O  
ANISOU 4802  O   GLN C 130    12226  13605  13480   1586  -1656    120       O  
ATOM   4803  CB  GLN C 130      85.576  52.353  67.674  1.00 99.29           C  
ANISOU 4803  CB  GLN C 130    11377  14135  12214    885  -1951   -173       C  
ATOM   4804  CG  GLN C 130      85.918  52.657  69.112  1.00102.79           C  
ANISOU 4804  CG  GLN C 130    11453  15465  12136    473  -2110   -310       C  
ATOM   4805  CD  GLN C 130      84.847  52.160  70.056  1.00114.05           C  
ANISOU 4805  CD  GLN C 130    12992  17131  13209    396  -2185   -152       C  
ATOM   4806  OE1 GLN C 130      83.711  52.631  70.028  1.00116.06           O  
ANISOU 4806  OE1 GLN C 130    13553  16968  13576    269  -1963   -476       O  
ATOM   4807  NE2 GLN C 130      85.198  51.187  70.891  1.00121.13           N  
ANISOU 4807  NE2 GLN C 130    13570  18716  13737    524  -2447    483       N  
ATOM   4808  N   TRP C 131      85.599  53.336  64.697  1.00 96.22           N  
ANISOU 4808  N   TRP C 131    11299  12688  12571   1245  -1461   -328       N  
ATOM   4809  CA  TRP C 131      85.102  53.333  63.317  1.00 95.35           C  
ANISOU 4809  CA  TRP C 131    11342  12336  12550   1425  -1310   -204       C  
ATOM   4810  C   TRP C 131      86.246  53.181  62.317  1.00101.08           C  
ANISOU 4810  C   TRP C 131    11994  13009  13402   1606  -1211   -154       C  
ATOM   4811  O   TRP C 131      86.264  52.220  61.527  1.00103.00           O  
ANISOU 4811  O   TRP C 131    12379  13200  13554   1708  -1183   -133       O  
ATOM   4812  CB  TRP C 131      84.330  54.647  63.050  1.00101.55           C  
ANISOU 4812  CB  TRP C 131    12030  13001  13553   1368  -1007   -161       C  
ATOM   4813  CG  TRP C 131      83.567  54.767  61.673  1.00 99.44           C  
ANISOU 4813  CG  TRP C 131    11730  12839  13211   1540   -894    216       C  
ATOM   4814  CD1 TRP C 131      83.643  55.809  60.780  1.00 98.37           C  
ANISOU 4814  CD1 TRP C 131    11324  12707  13342   1702   -543    579       C  
ATOM   4815  CD2 TRP C 131      82.591  53.860  61.135  1.00 92.26           C  
ANISOU 4815  CD2 TRP C 131    10941  12219  11895   1500  -1099    311       C  
ATOM   4816  NE1 TRP C 131      82.805  55.587  59.721  1.00 92.22           N  
ANISOU 4816  NE1 TRP C 131    10438  12399  12201   1783   -603    998       N  
ATOM   4817  CE2 TRP C 131      82.149  54.401  59.913  1.00 90.72           C  
ANISOU 4817  CE2 TRP C 131    10489  12418  11561   1593   -956    734       C  
ATOM   4818  CE3 TRP C 131      82.065  52.633  61.558  1.00 95.54           C  
ANISOU 4818  CE3 TRP C 131    11584  12643  12072   1362  -1330     93       C  
ATOM   4819  CZ2 TRP C 131      81.209  53.766  59.120  1.00 91.58           C  
ANISOU 4819  CZ2 TRP C 131    10533  13123  11140   1442  -1123    837       C  
ATOM   4820  CZ3 TRP C 131      81.112  52.005  60.759  1.00 92.26           C  
ANISOU 4820  CZ3 TRP C 131    11167  12584  11302   1206  -1398     91       C  
ATOM   4821  CH2 TRP C 131      80.699  52.571  59.565  1.00 88.07           C  
ANISOU 4821  CH2 TRP C 131    10351  12629  10480   1195  -1338    405       C  
ATOM   4822  N   LEU C 132      87.211  54.119  62.359  1.00100.19           N  
ANISOU 4822  N   LEU C 132    11639  12883  13543   1579  -1062   -229       N  
ATOM   4823  CA  LEU C 132      88.315  54.141  61.383  1.00 92.76           C  
ANISOU 4823  CA  LEU C 132    10595  11868  12780   1764   -904   -151       C  
ATOM   4824  C   LEU C 132      88.951  52.755  61.213  1.00 92.25           C  
ANISOU 4824  C   LEU C 132    10603  11770  12678   1928   -994    -69       C  
ATOM   4825  O   LEU C 132      89.362  52.389  60.119  1.00 90.63           O  
ANISOU 4825  O   LEU C 132    10466  11449  12519   2066   -775    -65       O  
ATOM   4826  CB  LEU C 132      89.378  55.184  61.757  1.00 91.36           C  
ANISOU 4826  CB  LEU C 132    10081  11681  12948   1638   -740   -306       C  
ATOM   4827  CG  LEU C 132      90.667  55.141  60.908  1.00 89.40           C  
ANISOU 4827  CG  LEU C 132     9676  11357  12935   1837   -587   -197       C  
ATOM   4828  CD1 LEU C 132      90.468  55.799  59.546  1.00 87.97           C  
ANISOU 4828  CD1 LEU C 132     9527  11006  12888   2031   -212     14       C  
ATOM   4829  CD2 LEU C 132      91.850  55.748  61.642  1.00 86.83           C  
ANISOU 4829  CD2 LEU C 132     8932  11190  12869   1613   -574   -409       C  
ATOM   4830  N   LEU C 133      89.009  51.994  62.299  1.00 91.16           N  
ANISOU 4830  N   LEU C 133    10397  11737  12502   1913  -1208     44       N  
ATOM   4831  CA  LEU C 133      89.379  50.598  62.227  1.00 98.60           C  
ANISOU 4831  CA  LEU C 133    11351  12471  13638   2131  -1100    274       C  
ATOM   4832  C   LEU C 133      88.457  49.808  61.312  1.00107.92           C  
ANISOU 4832  C   LEU C 133    12896  13335  14772   2092   -851     34       C  
ATOM   4833  O   LEU C 133      88.918  49.186  60.361  1.00122.45           O  
ANISOU 4833  O   LEU C 133    14806  14903  16816   2159   -477   -112       O  
ATOM   4834  CB  LEU C 133      89.337  49.984  63.596  1.00102.37           C  
ANISOU 4834  CB  LEU C 133    11610  13207  14077   2161  -1324    649       C  
ATOM   4835  CG  LEU C 133      90.670  49.753  64.241  1.00105.64           C  
ANISOU 4835  CG  LEU C 133    11483  13988  14664   2328  -1407   1149       C  
ATOM   4836  CD1 LEU C 133      91.362  51.091  64.432  1.00104.62           C  
ANISOU 4836  CD1 LEU C 133    11080  14338  14332   2047  -1602    858       C  
ATOM   4837  CD2 LEU C 133      90.464  49.018  65.563  1.00108.34           C  
ANISOU 4837  CD2 LEU C 133    11518  14790  14855   2396  -1610   1741       C  
ATOM   4838  N   VAL C 134      87.154  49.813  61.620  1.00107.36           N  
ANISOU 4838  N   VAL C 134    13014  13353  14424   1910  -1006    -77       N  
ATOM   4839  CA  VAL C 134      86.174  48.989  60.884  1.00105.09           C  
ANISOU 4839  CA  VAL C 134    12977  12927  14022   1730   -800   -387       C  
ATOM   4840  C   VAL C 134      86.190  49.277  59.374  1.00104.25           C  
ANISOU 4840  C   VAL C 134    12926  13057  13627   1579   -598   -704       C  
ATOM   4841  O   VAL C 134      86.167  48.354  58.578  1.00104.92           O  
ANISOU 4841  O   VAL C 134    13119  13025  13718   1391   -225  -1111       O  
ATOM   4842  CB  VAL C 134      84.729  49.139  61.444  1.00103.81           C  
ANISOU 4842  CB  VAL C 134    12923  12940  13580   1540  -1045   -399       C  
ATOM   4843  CG1 VAL C 134      83.754  48.313  60.628  1.00109.74           C  
ANISOU 4843  CG1 VAL C 134    13829  13703  14163   1237   -842   -800       C  
ATOM   4844  CG2 VAL C 134      84.663  48.704  62.894  1.00101.81           C  
ANISOU 4844  CG2 VAL C 134    12606  12569  13505   1651  -1183    -87       C  
ATOM   4845  N   VAL C 135      86.240  50.560  58.998  1.00100.45           N  
ANISOU 4845  N   VAL C 135    12310  12935  12919   1629   -746   -512       N  
ATOM   4846  CA  VAL C 135      86.377  50.968  57.585  1.00 99.92           C  
ANISOU 4846  CA  VAL C 135    12165  13289  12507   1560   -557   -569       C  
ATOM   4847  C   VAL C 135      87.586  50.303  56.923  1.00102.26           C  
ANISOU 4847  C   VAL C 135    12501  13335  13015   1616   -176   -829       C  
ATOM   4848  O   VAL C 135      87.487  49.778  55.810  1.00109.22           O  
ANISOU 4848  O   VAL C 135    13442  14517  13539   1352    125  -1229       O  
ATOM   4849  CB  VAL C 135      86.512  52.513  57.454  1.00102.04           C  
ANISOU 4849  CB  VAL C 135    12178  13766  12824   1754   -603    -96       C  
ATOM   4850  CG1 VAL C 135      87.219  52.907  56.153  1.00101.42           C  
ANISOU 4850  CG1 VAL C 135    11944  14017  12573   1836   -328     23       C  
ATOM   4851  CG2 VAL C 135      85.151  53.187  57.568  1.00102.82           C  
ANISOU 4851  CG2 VAL C 135    12147  14211  12709   1687   -745    227       C  
ATOM   4852  N   ALA C 136      88.729  50.353  57.612  1.00 95.96           N  
ANISOU 4852  N   ALA C 136    11605  12088  12767   1906   -154   -617       N  
ATOM   4853  CA  ALA C 136      89.957  49.695  57.178  1.00 92.95           C  
ANISOU 4853  CA  ALA C 136    11183  11339  12794   2051    264   -714       C  
ATOM   4854  C   ALA C 136      89.772  48.191  57.053  1.00 97.48           C  
ANISOU 4854  C   ALA C 136    11923  11463  13649   1911    729  -1099       C  
ATOM   4855  O   ALA C 136      90.040  47.613  56.009  1.00103.20           O  
ANISOU 4855  O   ALA C 136    12744  12099  14368   1719   1279  -1584       O  
ATOM   4856  CB  ALA C 136      91.069  49.998  58.153  1.00 90.78           C  
ANISOU 4856  CB  ALA C 136    10620  10843  13026   2359    110   -275       C  
ATOM   4857  N   ALA C 137      89.331  47.564  58.138  1.00 97.50           N  
ANISOU 4857  N   ALA C 137    11926  11160  13959   1978    619   -901       N  
ATOM   4858  CA  ALA C 137      88.906  46.170  58.127  1.00107.10           C  
ANISOU 4858  CA  ALA C 137    13269  11825  15597   1822   1172  -1236       C  
ATOM   4859  C   ALA C 137      88.257  45.748  56.794  1.00119.95           C  
ANISOU 4859  C   ALA C 137    15124  13656  16793   1249   1613  -2161       C  
ATOM   4860  O   ALA C 137      88.633  44.720  56.217  1.00139.32           O  
ANISOU 4860  O   ALA C 137    17633  15554  19747   1065   2447  -2700       O  
ATOM   4861  CB  ALA C 137      87.961  45.899  59.292  1.00104.31           C  
ANISOU 4861  CB  ALA C 137    12925  11427  15278   1839    850   -946       C  
ATOM   4862  N   SER C 138      87.297  46.545  56.306  1.00130.92           N  
ANISOU 4862  N   SER C 138    11687  18931  19122    380    -98  -3762       N  
ATOM   4863  CA  SER C 138      86.569  46.211  55.068  1.00125.76           C  
ANISOU 4863  CA  SER C 138    11078  18271  18431    689     -4  -3923       C  
ATOM   4864  C   SER C 138      87.450  46.286  53.836  1.00124.66           C  
ANISOU 4864  C   SER C 138    11197  17778  18390   1017     99  -3399       C  
ATOM   4865  O   SER C 138      87.270  45.518  52.903  1.00127.22           O  
ANISOU 4865  O   SER C 138    11843  18006  18487   1116    293  -3346       O  
ATOM   4866  CB  SER C 138      85.371  47.114  54.885  1.00125.48           C  
ANISOU 4866  CB  SER C 138    10716  18302  18656    855   -307  -4665       C  
ATOM   4867  OG  SER C 138      84.733  47.319  56.110  1.00133.37           O  
ANISOU 4867  OG  SER C 138    11308  19687  19678    443   -118  -5397       O  
ATOM   4868  N   VAL C 139      88.397  47.215  53.835  1.00117.90           N  
ANISOU 4868  N   VAL C 139    10257  16729  17811   1050     60  -3084       N  
ATOM   4869  CA  VAL C 139      89.296  47.381  52.713  1.00119.46           C  
ANISOU 4869  CA  VAL C 139    10710  16657  18019   1043    449  -2731       C  
ATOM   4870  C   VAL C 139      90.336  46.240  52.692  1.00126.70           C  
ANISOU 4870  C   VAL C 139    11313  17527  19298   1067    996  -2628       C  
ATOM   4871  O   VAL C 139      90.685  45.715  51.627  1.00136.32           O  
ANISOU 4871  O   VAL C 139    12750  18644  20399   1048   1613  -2689       O  
ATOM   4872  CB  VAL C 139      89.963  48.769  52.764  1.00119.05           C  
ANISOU 4872  CB  VAL C 139    10638  16401  18195    887    253  -2486       C  
ATOM   4873  CG1 VAL C 139      90.946  48.961  51.624  1.00122.00           C  
ANISOU 4873  CG1 VAL C 139    11344  16555  18452    526    931  -2211       C  
ATOM   4874  CG2 VAL C 139      88.899  49.844  52.726  1.00117.97           C  
ANISOU 4874  CG2 VAL C 139    10812  16095  17916    993   -569  -2734       C  
ATOM   4875  N   VAL C 140      90.812  45.859  53.876  1.00128.08           N  
ANISOU 4875  N   VAL C 140    11058  17656  19950   1072    649  -2571       N  
ATOM   4876  CA  VAL C 140      91.607  44.643  54.058  1.00128.97           C  
ANISOU 4876  CA  VAL C 140    10869  17477  20657   1206    633  -2601       C  
ATOM   4877  C   VAL C 140      90.862  43.412  53.504  1.00129.24           C  
ANISOU 4877  C   VAL C 140    11323  17555  20228   1305    771  -2788       C  
ATOM   4878  O   VAL C 140      91.352  42.727  52.589  1.00132.70           O  
ANISOU 4878  O   VAL C 140    11659  17817  20944   1518   1282  -3007       O  
ATOM   4879  CB  VAL C 140      91.917  44.419  55.557  1.00128.86           C  
ANISOU 4879  CB  VAL C 140    10820  17180  20961   1033   -281  -2425       C  
ATOM   4880  CG1 VAL C 140      92.428  43.003  55.804  1.00134.33           C  
ANISOU 4880  CG1 VAL C 140    11506  17322  22208   1160   -822  -2467       C  
ATOM   4881  CG2 VAL C 140      92.909  45.456  56.057  1.00130.03           C  
ANISOU 4881  CG2 VAL C 140    10485  17104  21813    999   -544  -2243       C  
ATOM   4882  N   GLY C 141      89.673  43.154  54.055  1.00121.45           N  
ANISOU 4882  N   GLY C 141    10770  16810  18565   1071    411  -2823       N  
ATOM   4883  CA  GLY C 141      88.896  41.971  53.713  1.00121.63           C  
ANISOU 4883  CA  GLY C 141    11208  16846  18160   1035    391  -2962       C  
ATOM   4884  C   GLY C 141      88.208  42.050  52.357  1.00125.65           C  
ANISOU 4884  C   GLY C 141    12012  17477  18252   1222    824  -3137       C  
ATOM   4885  O   GLY C 141      87.395  41.194  52.019  1.00128.16           O  
ANISOU 4885  O   GLY C 141    12691  17808  18194   1178    735  -3271       O  
ATOM   4886  N   THR C 142      88.514  43.089  51.589  1.00127.06           N  
ANISOU 4886  N   THR C 142    12222  17637  18416   1305   1147  -3094       N  
ATOM   4887  CA  THR C 142      88.089  43.150  50.198  1.00126.81           C  
ANISOU 4887  CA  THR C 142    12872  17462  17847   1312   1393  -3165       C  
ATOM   4888  C   THR C 142      89.041  42.301  49.387  1.00134.93           C  
ANISOU 4888  C   THR C 142    14017  18288  18962   1370   2155  -3295       C  
ATOM   4889  O   THR C 142      88.610  41.476  48.567  1.00135.01           O  
ANISOU 4889  O   THR C 142    14620  18154  18521   1409   2291  -3462       O  
ATOM   4890  CB  THR C 142      88.100  44.596  49.668  1.00124.33           C  
ANISOU 4890  CB  THR C 142    12925  17010  17305   1130   1279  -3021       C  
ATOM   4891  OG1 THR C 142      87.250  45.398  50.474  1.00119.25           O  
ANISOU 4891  OG1 THR C 142    11959  16480  16869   1207    523  -3145       O  
ATOM   4892  CG2 THR C 142      87.606  44.651  48.243  1.00127.67           C  
ANISOU 4892  CG2 THR C 142    14496  17055  16956    929   1221  -3010       C  
ATOM   4893  N   SER C 143      90.347  42.491  49.654  1.00142.96           N  
ANISOU 4893  N   SER C 143    14351  19253  20713   1381   2638  -3358       N  
ATOM   4894  CA  SER C 143      91.428  41.687  49.056  1.00151.14           C  
ANISOU 4894  CA  SER C 143    15011  20081  22332   1490   3479  -3841       C  
ATOM   4895  C   SER C 143      91.261  40.215  49.416  1.00155.08           C  
ANISOU 4895  C   SER C 143    15366  20325  23231   1912   2967  -4061       C  
ATOM   4896  O   SER C 143      91.672  39.326  48.660  1.00162.87           O  
ANISOU 4896  O   SER C 143    16344  21075  24462   2097   3523  -4609       O  
ATOM   4897  CB  SER C 143      92.803  42.182  49.535  1.00151.71           C  
ANISOU 4897  CB  SER C 143    13987  20073  23583   1477   3825  -4018       C  
ATOM   4898  OG  SER C 143      92.855  43.600  49.618  1.00147.47           O  
ANISOU 4898  OG  SER C 143    13591  19720  22718   1062   3871  -3627       O  
ATOM   4899  N   VAL C 144      90.645  39.968  50.576  1.00151.80           N  
ANISOU 4899  N   VAL C 144    14959  19912  22805   1940   1918  -3695       N  
ATOM   4900  CA  VAL C 144      90.354  38.606  51.047  1.00148.87           C  
ANISOU 4900  CA  VAL C 144    14789  19196  22577   2082   1163  -3735       C  
ATOM   4901  C   VAL C 144      89.105  38.018  50.352  1.00146.04           C  
ANISOU 4901  C   VAL C 144    15271  18981  21235   1967   1172  -3732       C  
ATOM   4902  O   VAL C 144      88.988  36.803  50.199  1.00147.41           O  
ANISOU 4902  O   VAL C 144    15738  18798  21473   2113    833  -3892       O  
ATOM   4903  CB  VAL C 144      90.198  38.566  52.596  1.00143.97           C  
ANISOU 4903  CB  VAL C 144    14198  18458  22047   1771     93  -3331       C  
ATOM   4904  CG1 VAL C 144      89.690  37.206  53.065  1.00142.12           C  
ANISOU 4904  CG1 VAL C 144    14612  17821  21567   1570   -786  -3241       C  
ATOM   4905  CG2 VAL C 144      91.518  38.926  53.277  1.00142.65           C  
ANISOU 4905  CG2 VAL C 144    13289  17868  23043   1949   -283  -3342       C  
ATOM   4906  N   TYR C 145      88.197  38.892  49.914  1.00140.58           N  
ANISOU 4906  N   TYR C 145    14953  18670  19788   1737   1370  -3597       N  
ATOM   4907  CA  TYR C 145      87.027  38.463  49.157  1.00141.43           C  
ANISOU 4907  CA  TYR C 145    15779  18782  19176   1653   1210  -3658       C  
ATOM   4908  C   TYR C 145      87.345  38.315  47.652  1.00151.63           C  
ANISOU 4908  C   TYR C 145    17748  19808  20056   1755   1869  -3899       C  
ATOM   4909  O   TYR C 145      86.553  37.751  46.896  1.00158.62           O  
ANISOU 4909  O   TYR C 145    19402  20502  20364   1720   1650  -3971       O  
ATOM   4910  CB  TYR C 145      85.852  39.426  49.391  1.00135.05           C  
ANISOU 4910  CB  TYR C 145    14975  18277  18057   1408    806  -3598       C  
ATOM   4911  CG  TYR C 145      84.588  39.088  48.615  1.00136.19           C  
ANISOU 4911  CG  TYR C 145    15686  18285  17772   1349    380  -3758       C  
ATOM   4912  CD1 TYR C 145      83.837  37.950  48.921  1.00136.34           C  
ANISOU 4912  CD1 TYR C 145    15761  18317  17722   1167     43  -3860       C  
ATOM   4913  CD2 TYR C 145      84.141  39.918  47.573  1.00141.69           C  
ANISOU 4913  CD2 TYR C 145    16988  18696  18151   1379    113  -3784       C  
ATOM   4914  CE1 TYR C 145      82.685  37.641  48.211  1.00144.23           C  
ANISOU 4914  CE1 TYR C 145    17159  19130  18512   1105   -443  -4053       C  
ATOM   4915  CE2 TYR C 145      82.992  39.622  46.856  1.00147.60           C  
ANISOU 4915  CE2 TYR C 145    18282  19112  18685   1354   -597  -3949       C  
ATOM   4916  CZ  TYR C 145      82.265  38.483  47.173  1.00151.63           C  
ANISOU 4916  CZ  TYR C 145    18595  19720  19298   1263   -825  -4118       C  
ATOM   4917  OH  TYR C 145      81.117  38.179  46.463  1.00161.38           O  
ANISOU 4917  OH  TYR C 145    20254  20568  20495   1230  -1624  -4329       O  
ATOM   4918  N   ILE C 146      88.508  38.814  47.237  1.00156.79           N  
ANISOU 4918  N   ILE C 146    18175  20430  20966   1741   2729  -4089       N  
ATOM   4919  CA  ILE C 146      88.988  38.623  45.866  1.00166.94           C  
ANISOU 4919  CA  ILE C 146    20179  21503  21745   1557   3718  -4510       C  
ATOM   4920  C   ILE C 146      89.762  37.291  45.751  1.00181.06           C  
ANISOU 4920  C   ILE C 146    21489  23019  24286   1968   4148  -5184       C  
ATOM   4921  O   ILE C 146      89.587  36.529  44.776  1.00187.06           O  
ANISOU 4921  O   ILE C 146    23041  23526  24507   1950   4536  -5598       O  
ATOM   4922  CB  ILE C 146      89.888  39.806  45.409  1.00171.31           C  
ANISOU 4922  CB  ILE C 146    20742  22176  22169   1058   4699  -4576       C  
ATOM   4923  CG1 ILE C 146      89.101  41.135  45.401  1.00164.08           C  
ANISOU 4923  CG1 ILE C 146    20516  21284  20540    685   3976  -3953       C  
ATOM   4924  CG2 ILE C 146      90.517  39.524  44.044  1.00184.02           C  
ANISOU 4924  CG2 ILE C 146    23154  23620  23144    558   6095  -5217       C  
ATOM   4925  CD1 ILE C 146      88.010  41.225  44.353  1.00164.84           C  
ANISOU 4925  CD1 ILE C 146    22210  20979  19442    360   3380  -3772       C  
ATOM   4926  N   GLU C 147      90.606  37.014  46.757  1.00189.09           N  
ANISOU 4926  N   GLU C 147    21276  23943  26626   2356   3879  -5349       N  
ATOM   4927  CA  GLU C 147      91.355  35.738  46.846  1.00198.65           C  
ANISOU 4927  CA  GLU C 147    21844  24634  29000   2908   3769  -6076       C  
ATOM   4928  C   GLU C 147      90.396  34.546  46.895  1.00195.72           C  
ANISOU 4928  C   GLU C 147    22255  23938  28170   3091   2761  -5885       C  
ATOM   4929  O   GLU C 147      90.408  33.685  46.006  1.00205.47           O  
ANISOU 4929  O   GLU C 147    23937  24862  29267   3282   3134  -6483       O  
ATOM   4930  CB  GLU C 147      92.284  35.712  48.087  1.00198.86           C  
ANISOU 4930  CB  GLU C 147    20603  24341  30612   3266   2988  -6119       C  
ATOM   4931  CG  GLU C 147      93.321  36.828  48.163  1.00199.91           C  
ANISOU 4931  CG  GLU C 147    19748  24712  31493   3099   3834  -6346       C  
ATOM   4932  CD  GLU C 147      94.027  37.069  46.846  1.00215.70           C  
ANISOU 4932  CD  GLU C 147    21572  26911  33471   2809   5712  -7288       C  
ATOM   4933  OE1 GLU C 147      93.947  38.203  46.329  1.00214.58           O  
ANISOU 4933  OE1 GLU C 147    21954  27248  32329   2105   6632  -6988       O  
ATOM   4934  OE2 GLU C 147      94.658  36.125  46.323  1.00232.02           O  
ANISOU 4934  OE2 GLU C 147    23076  28595  36483   3183   6266  -8406       O  
ATOM   4935  N   TRP C 148      89.584  34.493  47.952  1.00182.72           N  
ANISOU 4935  N   TRP C 148    20802  22358  26263   2911   1565  -5132       N  
ATOM   4936  CA  TRP C 148      88.428  33.627  47.980  1.00174.54           C  
ANISOU 4936  CA  TRP C 148    20621  21193  24501   2741    758  -4828       C  
ATOM   4937  C   TRP C 148      87.599  33.973  46.781  1.00174.06           C  
ANISOU 4937  C   TRP C 148    21407  21389  23339   2532   1347  -4836       C  
ATOM   4938  O   TRP C 148      87.662  35.101  46.281  1.00175.77           O  
ANISOU 4938  O   TRP C 148    21715  21929  23137   2322   2035  -4780       O  
ATOM   4939  CB  TRP C 148      87.615  33.865  49.252  1.00166.03           C  
ANISOU 4939  CB  TRP C 148    19604  20382  23097   2209   -123  -4155       C  
ATOM   4940  CG  TRP C 148      86.707  32.721  49.614  1.00167.41           C  
ANISOU 4940  CG  TRP C 148    20482  20286  22840   1842  -1049  -3934       C  
ATOM   4941  CD1 TRP C 148      87.050  31.585  50.297  1.00177.07           C  
ANISOU 4941  CD1 TRP C 148    21995  20794  24486   1790  -2118  -3863       C  
ATOM   4942  CD2 TRP C 148      85.306  32.608  49.328  1.00161.87           C  
ANISOU 4942  CD2 TRP C 148    20316  19906  21281   1370  -1138  -3779       C  
ATOM   4943  NE1 TRP C 148      85.951  30.769  50.446  1.00175.65           N  
ANISOU 4943  NE1 TRP C 148    22631  20548  23558   1176  -2723  -3596       N  
ATOM   4944  CE2 TRP C 148      84.867  31.374  49.865  1.00166.67           C  
ANISOU 4944  CE2 TRP C 148    21510  20096  21718    928  -2051  -3600       C  
ATOM   4945  CE3 TRP C 148      84.381  33.425  48.671  1.00157.75           C  
ANISOU 4945  CE3 TRP C 148    19839  19840  20258   1252   -730  -3822       C  
ATOM   4946  CZ2 TRP C 148      83.541  30.939  49.762  1.00163.91           C  
ANISOU 4946  CZ2 TRP C 148    21623  19930  20723    308  -2299  -3512       C  
ATOM   4947  CZ3 TRP C 148      83.060  32.989  48.567  1.00157.07           C  
ANISOU 4947  CZ3 TRP C 148    20093  19831  19754    799  -1166  -3814       C  
ATOM   4948  CH2 TRP C 148      82.656  31.758  49.111  1.00159.16           C  
ANISOU 4948  CH2 TRP C 148    20772  19831  19869    301  -1809  -3683       C  
ATOM   4949  N   LEU C 149      86.832  33.008  46.297  1.00175.35           N  
ANISOU 4949  N   LEU C 149    22349  21262  23014   2523    890  -4876       N  
ATOM   4950  CA  LEU C 149      85.918  33.252  45.185  1.00174.56           C  
ANISOU 4950  CA  LEU C 149    23256  21187  21880   2283   1035  -4827       C  
ATOM   4951  C   LEU C 149      86.644  33.373  43.844  1.00185.00           C  
ANISOU 4951  C   LEU C 149    25232  22300  22758   2314   2169  -5399       C  
ATOM   4952  O   LEU C 149      86.001  33.459  42.804  1.00192.76           O  
ANISOU 4952  O   LEU C 149    27442  23073  22723   2018   2168  -5376       O  
ATOM   4953  CB  LEU C 149      85.038  34.490  45.458  1.00161.80           C  
ANISOU 4953  CB  LEU C 149    21570  19996  19907   1910    731  -4369       C  
ATOM   4954  CG  LEU C 149      84.362  35.190  44.284  1.00158.82           C  
ANISOU 4954  CG  LEU C 149    22236  19424  18683   1671    654  -4321       C  
ATOM   4955  CD1 LEU C 149      82.984  35.665  44.687  1.00152.38           C  
ANISOU 4955  CD1 LEU C 149    21203  18715  17977   1482   -382  -4105       C  
ATOM   4956  CD2 LEU C 149      85.219  36.342  43.778  1.00160.70           C  
ANISOU 4956  CD2 LEU C 149    22699  19728  18629   1479   1496  -4348       C  
ATOM   4957  N   HIS C 150      87.980  33.380  43.868  1.00182.72           N  
ANISOU 4957  N   HIS C 150    23244  22493  23685   -180   -881  -1905       N  
ATOM   4958  CA  HIS C 150      88.740  33.020  42.672  1.00178.27           C  
ANISOU 4958  CA  HIS C 150    22924  21514  23296    -41   -732  -1680       C  
ATOM   4959  C   HIS C 150      88.429  31.546  42.363  1.00175.63           C  
ANISOU 4959  C   HIS C 150    22691  21374  22665    208  -1248  -1169       C  
ATOM   4960  O   HIS C 150      88.264  31.165  41.208  1.00175.66           O  
ANISOU 4960  O   HIS C 150    23031  21037  22674    423  -1201   -881       O  
ATOM   4961  CB  HIS C 150      90.250  33.240  42.866  1.00175.97           C  
ANISOU 4961  CB  HIS C 150    22206  21335  23318   -330   -492  -2234       C  
ATOM   4962  CG  HIS C 150      90.910  33.982  41.733  1.00173.83           C  
ANISOU 4962  CG  HIS C 150    22238  20286  23521   -409    263  -2360       C  
ATOM   4963  ND1 HIS C 150      90.531  33.826  40.413  1.00169.05           N  
ANISOU 4963  ND1 HIS C 150    22284  19128  22819    -77    449  -1772       N  
ATOM   4964  CD2 HIS C 150      91.935  34.870  41.725  1.00175.26           C  
ANISOU 4964  CD2 HIS C 150    22158  20169  24262   -784    969  -3053       C  
ATOM   4965  CE1 HIS C 150      91.286  34.593  39.646  1.00170.08           C  
ANISOU 4965  CE1 HIS C 150    22660  18606  23356   -198   1270  -1947       C  
ATOM   4966  NE2 HIS C 150      92.148  35.233  40.416  1.00174.18           N  
ANISOU 4966  NE2 HIS C 150    22627  19184  24369   -673   1660  -2749       N  
ATOM   4967  N   HIS C 151      88.286  30.748  43.421  1.00173.34           N  
ANISOU 4967  N   HIS C 151    22124  21631  22106    195  -1652  -1083       N  
ATOM   4968  CA  HIS C 151      87.793  29.371  43.313  1.00168.87           C  
ANISOU 4968  CA  HIS C 151    21665  21104  21391    390  -1934   -617       C  
ATOM   4969  C   HIS C 151      86.407  29.322  42.666  1.00163.53           C  
ANISOU 4969  C   HIS C 151    21273  20159  20701    493  -1905   -503       C  
ATOM   4970  O   HIS C 151      85.520  30.078  43.043  1.00161.89           O  
ANISOU 4970  O   HIS C 151    21085  20002  20423    452  -1855   -662       O  
ATOM   4971  CB  HIS C 151      87.755  28.715  44.701  1.00173.99           C  
ANISOU 4971  CB  HIS C 151    22088  22316  21703    420  -2182   -450       C  
ATOM   4972  CG  HIS C 151      89.098  28.638  45.376  1.00179.52           C  
ANISOU 4972  CG  HIS C 151    22394  23540  22273    496  -2366   -598       C  
ATOM   4973  ND1 HIS C 151      89.969  29.708  45.430  1.00180.05           N  
ANISOU 4973  ND1 HIS C 151    22127  23788  22497    285  -2248  -1242       N  
ATOM   4974  CD2 HIS C 151      89.707  27.625  46.040  1.00179.99           C  
ANISOU 4974  CD2 HIS C 151    22284  24026  22077    820  -2634   -241       C  
ATOM   4975  CE1 HIS C 151      91.060  29.352  46.085  1.00182.92           C  
ANISOU 4975  CE1 HIS C 151    22022  24795  22681    451  -2532  -1410       C  
ATOM   4976  NE2 HIS C 151      90.926  28.094  46.467  1.00183.93           N  
ANISOU 4976  NE2 HIS C 151    22273  25109  22500    854  -2816   -728       N  
ATOM   4977  N   LEU C 152      86.230  28.387  41.728  1.00166.23           N  
ANISOU 4977  N   LEU C 152    21733  20291  21135    632  -1942   -339       N  
ATOM   4978  CA  LEU C 152      85.114  28.403  40.725  1.00173.26           C  
ANISOU 4978  CA  LEU C 152    22781  21066  21981    816  -1956   -438       C  
ATOM   4979  C   LEU C 152      85.259  29.584  39.745  1.00176.76           C  
ANISOU 4979  C   LEU C 152    23521  21312  22325   1054  -1789   -468       C  
ATOM   4980  O   LEU C 152      84.268  30.070  39.176  1.00179.54           O  
ANISOU 4980  O   LEU C 152    24006  21714  22497   1368  -1844   -521       O  
ATOM   4981  CB  LEU C 152      83.696  28.375  41.396  1.00169.12           C  
ANISOU 4981  CB  LEU C 152    22124  20731  21401    775  -2039   -595       C  
ATOM   4982  CG  LEU C 152      82.504  27.636  40.693  1.00163.26           C  
ANISOU 4982  CG  LEU C 152    21244  20061  20724    880  -2112   -884       C  
ATOM   4983  CD1 LEU C 152      81.455  27.169  41.695  1.00160.42           C  
ANISOU 4983  CD1 LEU C 152    20658  19795  20498    642  -2014  -1070       C  
ATOM   4984  CD2 LEU C 152      81.843  28.460  39.590  1.00158.80           C  
ANISOU 4984  CD2 LEU C 152    20762  19642  19930   1306  -2270  -1097       C  
ATOM   4985  N   GLY C 153      86.503  30.014  39.529  1.00176.42           N  
ANISOU 4985  N   GLY C 153    23577  21041  22411    961  -1528   -434       N  
ATOM   4986  CA  GLY C 153      86.759  31.265  38.833  1.00183.17           C  
ANISOU 4986  CA  GLY C 153    24791  21536  23267   1130  -1106   -402       C  
ATOM   4987  C   GLY C 153      86.047  32.364  39.585  1.00192.65           C  
ANISOU 4987  C   GLY C 153    25979  22693  24525   1141   -981   -503       C  
ATOM   4988  O   GLY C 153      85.595  32.160  40.706  1.00197.99           O  
ANISOU 4988  O   GLY C 153    26326  23686  25215    920  -1227   -670       O  
ATOM   4989  N   SER C 154      85.930  33.529  38.986  1.00197.63           N  
ANISOU 4989  N   SER C 154    26997  22893  25199   1426   -517   -378       N  
ATOM   4990  CA  SER C 154      85.115  34.562  39.590  1.00199.19           C  
ANISOU 4990  CA  SER C 154    27181  22961  25540   1517   -344   -470       C  
ATOM   4991  C   SER C 154      84.344  35.315  38.539  1.00202.34           C  
ANISOU 4991  C   SER C 154    28087  23063  25727   2250   -135    -69       C  
ATOM   4992  O   SER C 154      84.911  35.789  37.559  1.00209.10           O  
ANISOU 4992  O   SER C 154    29456  23470  26523   2554    375    268       O  
ATOM   4993  CB  SER C 154      85.968  35.508  40.443  1.00201.41           C  
ANISOU 4993  CB  SER C 154    27270  22926  26329   1025    239   -877       C  
ATOM   4994  OG  SER C 154      86.513  34.823  41.562  1.00201.12           O  
ANISOU 4994  OG  SER C 154    26680  23442  26295    515   -119  -1268       O  
ATOM   4995  N   ALA C 155      83.034  35.384  38.721  1.00202.24           N  
ANISOU 4995  N   ALA C 155    27934  23351  25556   2604   -521    -95       N  
ATOM   4996  CA  ALA C 155      82.182  36.160  37.840  1.00209.58           C  
ANISOU 4996  CA  ALA C 155    29257  24143  26229   3488   -426    284       C  
ATOM   4997  C   ALA C 155      81.354  37.148  38.653  1.00212.73           C  
ANISOU 4997  C   ALA C 155    29489  24313  27026   3579   -230    121       C  
ATOM   4998  O   ALA C 155      80.138  36.995  38.795  1.00220.70           O  
ANISOU 4998  O   ALA C 155    30192  25768  27893   3916   -731    -52       O  
ATOM   4999  CB  ALA C 155      81.288  35.244  37.018  1.00207.17           C  
ANISOU 4999  CB  ALA C 155    28819  24588  25308   4020  -1167    272       C  
ATOM   5000  N   LEU C 156      82.033  38.137  39.224  1.00207.13           N  
ANISOU 5000  N   LEU C 156    28881  22914  26902   3202    552     27       N  
ATOM   5001  CA  LEU C 156      81.369  39.206  39.937  1.00201.38           C  
ANISOU 5001  CA  LEU C 156    28017  21815  26683   3255    943   -177       C  
ATOM   5002  C   LEU C 156      81.767  40.521  39.315  1.00205.75           C  
ANISOU 5002  C   LEU C 156    29195  21337  27642   3715   2005    269       C  
ATOM   5003  O   LEU C 156      82.944  40.883  39.338  1.00202.69           O  
ANISOU 5003  O   LEU C 156    28970  20376  27664   3212   2777    148       O  
ATOM   5004  CB  LEU C 156      81.771  39.190  41.412  1.00195.54           C  
ANISOU 5004  CB  LEU C 156    26684  21233  26379   2249   1040   -930       C  
ATOM   5005  CG  LEU C 156      80.636  39.323  42.418  1.00193.04           C  
ANISOU 5005  CG  LEU C 156    25883  21254  26209   2111    764  -1378       C  
ATOM   5006  CD1 LEU C 156      79.482  38.443  41.969  1.00190.34           C  
ANISOU 5006  CD1 LEU C 156    25435  21528  25355   2622    -66  -1210       C  
ATOM   5007  CD2 LEU C 156      81.112  38.918  43.803  1.00188.02           C  
ANISOU 5007  CD2 LEU C 156    24698  21116  25623   1165    659  -2045       C  
ATOM   5008  N   PRO C 157      80.796  41.250  38.727  1.00164.22           N  
ANISOU 5008  N   PRO C 157    25311  20642  16444   5797   2345  -3176       N  
ATOM   5009  CA  PRO C 157      81.196  42.563  38.290  1.00160.64           C  
ANISOU 5009  CA  PRO C 157    24038  21037  15958   5840   2255  -2721       C  
ATOM   5010  C   PRO C 157      81.534  43.389  39.514  1.00150.42           C  
ANISOU 5010  C   PRO C 157    21847  20000  15305   5729   2105  -2139       C  
ATOM   5011  O   PRO C 157      81.064  43.088  40.609  1.00141.90           O  
ANISOU 5011  O   PRO C 157    20761  18500  14653   5413   1922  -2184       O  
ATOM   5012  CB  PRO C 157      79.936  43.105  37.588  1.00163.67           C  
ANISOU 5012  CB  PRO C 157    24461  21607  16119   5093   1743  -3048       C  
ATOM   5013  CG  PRO C 157      79.078  41.901  37.334  1.00168.01           C  
ANISOU 5013  CG  PRO C 157    25991  21458  16387   4775   1660  -3737       C  
ATOM   5014  CD  PRO C 157      79.361  41.013  38.495  1.00166.08           C  
ANISOU 5014  CD  PRO C 157    25988  20547  16567   4969   1867  -3716       C  
ATOM   5015  N   THR C 158      82.390  44.377  39.332  1.00148.55           N  
ANISOU 5015  N   THR C 158    20895  20444  15102   5990   2197  -1588       N  
ATOM   5016  CA  THR C 158      82.966  45.106  40.436  1.00138.97           C  
ANISOU 5016  CA  THR C 158    18893  19492  14414   5958   2115  -1013       C  
ATOM   5017  C   THR C 158      81.874  45.637  41.356  1.00128.38           C  
ANISOU 5017  C   THR C 158    17313  17944  13522   5209   1594  -1113       C  
ATOM   5018  O   THR C 158      81.907  45.425  42.561  1.00121.30           O  
ANISOU 5018  O   THR C 158    16270  16787  13029   5121   1542   -994       O  
ATOM   5019  CB  THR C 158      83.840  46.258  39.921  1.00142.48           C  
ANISOU 5019  CB  THR C 158    18622  20725  14785   6141   2176   -435       C  
ATOM   5020  OG1 THR C 158      83.032  47.416  39.710  1.00139.60           O  
ANISOU 5020  OG1 THR C 158    17909  20603  14528   5521   1712   -416       O  
ATOM   5021  CG2 THR C 158      84.521  45.860  38.569  1.00151.24           C  
ANISOU 5021  CG2 THR C 158    20051  22141  15271   6777   2631   -462       C  
ATOM   5022  N   LEU C 159      80.882  46.296  40.779  1.00127.81           N  
ANISOU 5022  N   LEU C 159    17207  18011  13343   4704   1229  -1318       N  
ATOM   5023  CA  LEU C 159      79.836  46.888  41.588  1.00118.27           C  
ANISOU 5023  CA  LEU C 159    15724  16683  12528   4072    777  -1362       C  
ATOM   5024  C   LEU C 159      79.032  45.832  42.321  1.00118.23           C  
ANISOU 5024  C   LEU C 159    16200  16049  12670   3816    695  -1761       C  
ATOM   5025  O   LEU C 159      78.787  45.978  43.499  1.00116.16           O  
ANISOU 5025  O   LEU C 159    15675  15630  12829   3591    545  -1635       O  
ATOM   5026  CB  LEU C 159      78.928  47.799  40.768  1.00115.50           C  
ANISOU 5026  CB  LEU C 159    15210  16656  12016   3654    432  -1434       C  
ATOM   5027  CG  LEU C 159      77.693  48.298  41.524  1.00112.21           C  
ANISOU 5027  CG  LEU C 159    14576  16105  11953   3063      3  -1513       C  
ATOM   5028  CD1 LEU C 159      77.172  49.589  40.925  1.00108.09           C  
ANISOU 5028  CD1 LEU C 159    13634  16031  11403   2812   -276  -1310       C  
ATOM   5029  CD2 LEU C 159      76.598  47.235  41.532  1.00118.15           C  
ANISOU 5029  CD2 LEU C 159    15885  16423  12581   2721   -134  -2024       C  
ATOM   5030  N   ASP C 160      78.628  44.765  41.624  1.00124.73           N  
ANISOU 5030  N   ASP C 160    17760  16507  13122   3828    793  -2237       N  
ATOM   5031  CA  ASP C 160      77.938  43.651  42.286  1.00128.23           C  
ANISOU 5031  CA  ASP C 160    18732  16291  13697   3567    740  -2590       C  
ATOM   5032  C   ASP C 160      78.819  43.198  43.420  1.00126.93           C  
ANISOU 5032  C   ASP C 160    18459  15885  13883   3972   1025  -2293       C  
ATOM   5033  O   ASP C 160      78.345  42.644  44.420  1.00125.63           O  
ANISOU 5033  O   ASP C 160    18414  15296  14021   3728    935  -2357       O  
ATOM   5034  CB  ASP C 160      77.712  42.466  41.330  1.00149.10           C  
ANISOU 5034  CB  ASP C 160    22309  18498  15844   3629    897  -3127       C  
ATOM   5035  CG  ASP C 160      76.989  42.863  40.030  1.00167.72           C  
ANISOU 5035  CG  ASP C 160    24809  21195  17719   3282    638  -3411       C  
ATOM   5036  OD1 ASP C 160      77.312  43.927  39.450  1.00176.63           O  
ANISOU 5036  OD1 ASP C 160    25417  22957  18736   3412    603  -3120       O  
ATOM   5037  OD2 ASP C 160      76.136  42.073  39.560  1.00179.34           O  
ANISOU 5037  OD2 ASP C 160    26942  22302  18895   2870    472  -3908       O  
ATOM   5038  N   GLY C 161      80.119  43.446  43.262  1.00127.20           N  
ANISOU 5038  N   GLY C 161    18216  16255  13858   4591   1369  -1912       N  
ATOM   5039  CA  GLY C 161      81.110  43.057  44.258  1.00130.46           C  
ANISOU 5039  CA  GLY C 161    18438  16580  14551   5045   1660  -1531       C  
ATOM   5040  C   GLY C 161      81.131  43.985  45.459  1.00126.29           C  
ANISOU 5040  C   GLY C 161    17160  16337  14485   4739   1385  -1129       C  
ATOM   5041  O   GLY C 161      81.061  43.523  46.599  1.00127.86           O  
ANISOU 5041  O   GLY C 161    17351  16242  14986   4676   1371  -1048       O  
ATOM   5042  N   VAL C 162      81.223  45.298  45.192  1.00124.15           N  
ANISOU 5042  N   VAL C 162    16305  16620  14245   4543   1169   -879       N  
ATOM   5043  CA  VAL C 162      81.257  46.347  46.240  1.00119.66           C  
ANISOU 5043  CA  VAL C 162    15082  16317  14064   4221    890   -532       C  
ATOM   5044  C   VAL C 162      80.082  46.236  47.203  1.00120.63           C  
ANISOU 5044  C   VAL C 162    15292  16076  14463   3710    587   -779       C  
ATOM   5045  O   VAL C 162      80.270  46.227  48.420  1.00128.60           O  
ANISOU 5045  O   VAL C 162    16073  17028  15759   3654    546   -579       O  
ATOM   5046  CB  VAL C 162      81.296  47.787  45.635  1.00114.22           C  
ANISOU 5046  CB  VAL C 162    13912  16143  13342   4009    673   -314       C  
ATOM   5047  CG1 VAL C 162      80.954  48.828  46.683  1.00105.01           C  
ANISOU 5047  CG1 VAL C 162    12290  15059  12548   3568    332   -135       C  
ATOM   5048  CG2 VAL C 162      82.662  48.084  45.041  1.00122.22           C  
ANISOU 5048  CG2 VAL C 162    14614  17644  14179   4474    955    131       C  
ATOM   5049  N   THR C 163      78.876  46.138  46.665  1.00116.02           N  
ANISOU 5049  N   THR C 163    15012  15307  13763   3335    378  -1181       N  
ATOM   5050  CA  THR C 163      77.711  46.003  47.511  1.00120.53           C  
ANISOU 5050  CA  THR C 163    15623  15604  14566   2859    112  -1372       C  
ATOM   5051  C   THR C 163      77.788  44.762  48.437  1.00119.30           C  
ANISOU 5051  C   THR C 163    15804  14968  14556   2956    282  -1425       C  
ATOM   5052  O   THR C 163      77.069  44.681  49.436  1.00127.34           O  
ANISOU 5052  O   THR C 163    16737  15826  15818   2625    110  -1442       O  
ATOM   5053  CB  THR C 163      76.377  46.086  46.703  1.00124.55           C  
ANISOU 5053  CB  THR C 163    16336  16091  14894   2413   -159  -1730       C  
ATOM   5054  OG1 THR C 163      75.352  45.307  47.340  1.00127.45           O  
ANISOU 5054  OG1 THR C 163    16962  16077  15384   2034   -294  -1964       O  
ATOM   5055  CG2 THR C 163      76.575  45.595  45.292  1.00135.58           C  
ANISOU 5055  CG2 THR C 163    18179  17486  15847   2599    -15  -1972       C  
ATOM   5056  N   VAL C 164      78.717  43.852  48.169  1.00113.71           N  
ANISOU 5056  N   VAL C 164    15438  14059  13704   3461    648  -1386       N  
ATOM   5057  CA  VAL C 164      78.795  42.647  48.998  1.00118.05           C  
ANISOU 5057  CA  VAL C 164    16355  14101  14397   3595    833  -1398       C  
ATOM   5058  C   VAL C 164      79.662  42.741  50.271  1.00118.68           C  
ANISOU 5058  C   VAL C 164    15996  14340  14756   3851    941   -923       C  
ATOM   5059  O   VAL C 164      79.244  42.277  51.334  1.00116.09           O  
ANISOU 5059  O   VAL C 164    15705  13748  14653   3658    876   -887       O  
ATOM   5060  CB  VAL C 164      79.123  41.392  48.192  1.00125.38           C  
ANISOU 5060  CB  VAL C 164    18042  14551  15043   3991   1183  -1655       C  
ATOM   5061  CG1 VAL C 164      79.242  40.186  49.125  1.00124.43           C  
ANISOU 5061  CG1 VAL C 164    18301  13856  15118   4158   1389  -1595       C  
ATOM   5062  CG2 VAL C 164      78.039  41.154  47.155  1.00130.24           C  
ANISOU 5062  CG2 VAL C 164    19168  14941  15374   3556    985  -2182       C  
ATOM   5063  N   VAL C 165      80.854  43.339  50.164  1.00119.05           N  
ANISOU 5063  N   VAL C 165    15604  14863  14764   4246   1089   -528       N  
ATOM   5064  CA  VAL C 165      81.662  43.676  51.359  1.00113.60           C  
ANISOU 5064  CA  VAL C 165    14377  14484  14301   4362   1088    -37       C  
ATOM   5065  C   VAL C 165      80.826  44.544  52.307  1.00107.84           C  
ANISOU 5065  C   VAL C 165    13308  13867  13799   3765    686    -72       C  
ATOM   5066  O   VAL C 165      80.604  44.186  53.473  1.00104.63           O  
ANISOU 5066  O   VAL C 165    12863  13315  13574   3641    633     17       O  
ATOM   5067  CB  VAL C 165      82.975  44.432  50.980  1.00114.18           C  
ANISOU 5067  CB  VAL C 165    13930  15177  14274   4713   1211    419       C  
ATOM   5068  CG1 VAL C 165      83.540  45.194  52.178  1.00109.49           C  
ANISOU 5068  CG1 VAL C 165    12703  15004  13891   4536   1016    865       C  
ATOM   5069  CG2 VAL C 165      84.012  43.471  50.421  1.00118.66           C  
ANISOU 5069  CG2 VAL C 165    14727  15712  14646   5457   1696    614       C  
ATOM   5070  N   VAL C 166      80.330  45.661  51.773  1.00103.88           N  
ANISOU 5070  N   VAL C 166    12595  13611  13261   3435    430   -201       N  
ATOM   5071  CA  VAL C 166      79.585  46.643  52.546  1.00 99.90           C  
ANISOU 5071  CA  VAL C 166    11785  13232  12937   2960     92   -229       C  
ATOM   5072  C   VAL C 166      78.430  45.977  53.273  1.00 98.48           C  
ANISOU 5072  C   VAL C 166    11862  12677  12877   2669      0   -478       C  
ATOM   5073  O   VAL C 166      78.244  46.193  54.466  1.00100.49           O  
ANISOU 5073  O   VAL C 166    11909  12979  13292   2496   -113   -361       O  
ATOM   5074  CB  VAL C 166      79.091  47.819  51.650  1.00105.76           C  
ANISOU 5074  CB  VAL C 166    12377  14200  13607   2720   -120   -351       C  
ATOM   5075  CG1 VAL C 166      78.116  48.710  52.389  1.00101.45           C  
ANISOU 5075  CG1 VAL C 166    11637  13675  13232   2299   -417   -440       C  
ATOM   5076  CG2 VAL C 166      80.270  48.643  51.146  1.00107.17           C  
ANISOU 5076  CG2 VAL C 166    12206  14800  13710   2923    -67     -4       C  
ATOM   5077  N   SER C 167      77.707  45.103  52.578  1.00104.18           N  
ANISOU 5077  N   SER C 167    13052  13037  13493   2606     56   -801       N  
ATOM   5078  CA  SER C 167      76.588  44.375  53.198  1.00112.41           C  
ANISOU 5078  CA  SER C 167    14339  13727  14643   2269    -36   -996       C  
ATOM   5079  C   SER C 167      76.975  43.454  54.366  1.00114.10           C  
ANISOU 5079  C   SER C 167    14642  13700  15009   2423    130   -784       C  
ATOM   5080  O   SER C 167      76.203  43.314  55.321  1.00107.21           O  
ANISOU 5080  O   SER C 167    13703  12748  14281   2120      7   -776       O  
ATOM   5081  CB  SER C 167      75.783  43.604  52.160  1.00118.99           C  
ANISOU 5081  CB  SER C 167    15688  14221  15301   2084    -48  -1375       C  
ATOM   5082  OG  SER C 167      74.577  44.288  51.856  1.00126.93           O  
ANISOU 5082  OG  SER C 167    16526  15412  16287   1626   -351  -1552       O  
ATOM   5083  N   ILE C 168      78.155  42.817  54.282  1.00116.69           N  
ANISOU 5083  N   ILE C 168    15099  13946  15289   2927    429   -569       N  
ATOM   5084  CA  ILE C 168      78.636  41.948  55.375  1.00109.43           C  
ANISOU 5084  CA  ILE C 168    14231  12839  14507   3152    610   -279       C  
ATOM   5085  C   ILE C 168      78.983  42.777  56.596  1.00105.71           C  
ANISOU 5085  C   ILE C 168    13179  12828  14155   3059    454     55       C  
ATOM   5086  O   ILE C 168      78.469  42.519  57.673  1.00107.64           O  
ANISOU 5086  O   ILE C 168    13380  12996  14522   2843    376    125       O  
ATOM   5087  CB  ILE C 168      79.846  41.074  54.967  1.00111.63           C  
ANISOU 5087  CB  ILE C 168    14764  12956  14693   3809   1008    -68       C  
ATOM   5088  CG1 ILE C 168      79.538  40.298  53.687  1.00115.22           C  
ANISOU 5088  CG1 ILE C 168    15897  12925  14956   3919   1177   -470       C  
ATOM   5089  CG2 ILE C 168      80.219  40.107  56.097  1.00108.67           C  
ANISOU 5089  CG2 ILE C 168    14469  12347  14473   4048   1196    264       C  
ATOM   5090  CD1 ILE C 168      80.770  39.875  52.916  1.00120.79           C  
ANISOU 5090  CD1 ILE C 168    16781  13641  15472   4637   1579   -313       C  
ATOM   5091  N   VAL C 169      79.830  43.795  56.406  1.00102.30           N  
ANISOU 5091  N   VAL C 169    12324  12884  13662   3179    396    256       N  
ATOM   5092  CA  VAL C 169      80.188  44.752  57.472  1.00103.23           C  
ANISOU 5092  CA  VAL C 169    11933  13450  13837   3003    192    522       C  
ATOM   5093  C   VAL C 169      78.957  45.347  58.184  1.00108.63           C  
ANISOU 5093  C   VAL C 169    12561  14112  14600   2512    -78    286       C  
ATOM   5094  O   VAL C 169      78.872  45.325  59.432  1.00113.03           O  
ANISOU 5094  O   VAL C 169    12970  14770  15205   2393   -147    438       O  
ATOM   5095  CB  VAL C 169      81.111  45.871  56.931  1.00 98.74           C  
ANISOU 5095  CB  VAL C 169    10982  13350  13183   3066    113    712       C  
ATOM   5096  CG1 VAL C 169      80.983  47.162  57.747  1.00 90.50           C  
ANISOU 5096  CG1 VAL C 169     9580  12627  12177   2662   -206    757       C  
ATOM   5097  CG2 VAL C 169      82.545  45.381  56.905  1.00 98.83           C  
ANISOU 5097  CG2 VAL C 169    10805  13615  13129   3555    363   1174       C  
ATOM   5098  N   ALA C 170      78.010  45.865  57.395  1.00105.61           N  
ANISOU 5098  N   ALA C 170    12282  13643  14201   2264   -213    -51       N  
ATOM   5099  CA  ALA C 170      76.719  46.318  57.917  1.00 99.33           C  
ANISOU 5099  CA  ALA C 170    11447  12825  13467   1879   -410   -260       C  
ATOM   5100  C   ALA C 170      76.040  45.254  58.788  1.00 98.23           C  
ANISOU 5100  C   ALA C 170    11487  12430  13406   1768   -343   -252       C  
ATOM   5101  O   ALA C 170      75.628  45.539  59.920  1.00 95.23           O  
ANISOU 5101  O   ALA C 170    10926  12194  13060   1604   -430   -177       O  
ATOM   5102  CB  ALA C 170      75.811  46.723  56.780  1.00101.97           C  
ANISOU 5102  CB  ALA C 170    11885  13099  13757   1700   -518   -559       C  
ATOM   5103  N   GLN C 171      75.939  44.029  58.268  1.00 96.48           N  
ANISOU 5103  N   GLN C 171    11653  11812  13190   1857   -179   -324       N  
ATOM   5104  CA  GLN C 171      75.261  42.941  58.988  1.00 97.81           C  
ANISOU 5104  CA  GLN C 171    12048  11664  13452   1699   -117   -293       C  
ATOM   5105  C   GLN C 171      75.939  42.658  60.316  1.00102.41           C  
ANISOU 5105  C   GLN C 171    12451  12370  14086   1877    -23     76       C  
ATOM   5106  O   GLN C 171      75.291  42.230  61.287  1.00105.36           O  
ANISOU 5106  O   GLN C 171    12814  12691  14526   1679    -39    173       O  
ATOM   5107  CB  GLN C 171      75.229  41.669  58.142  1.00 98.76           C  
ANISOU 5107  CB  GLN C 171    12723  11245  13557   1781     55   -435       C  
ATOM   5108  CG  GLN C 171      74.332  40.580  58.702  1.00101.53           C  
ANISOU 5108  CG  GLN C 171    13368  11194  14015   1482     71   -436       C  
ATOM   5109  CD  GLN C 171      72.905  41.058  58.928  1.00105.71           C  
ANISOU 5109  CD  GLN C 171    13679  11916  14569    946   -184   -576       C  
ATOM   5110  OE1 GLN C 171      72.344  41.784  58.118  1.00106.42           O  
ANISOU 5110  OE1 GLN C 171    13660  12199  14575    758   -354   -809       O  
ATOM   5111  NE2 GLN C 171      72.316  40.643  60.026  1.00114.38           N  
ANISOU 5111  NE2 GLN C 171    14683  13003  15771    731   -193   -384       N  
ATOM   5112  N   VAL C 172      77.248  42.916  60.355  1.00 97.88           N  
ANISOU 5112  N   VAL C 172    11696  12031  13460   2238     65    327       N  
ATOM   5113  CA  VAL C 172      78.077  42.588  61.500  1.00 94.58           C  
ANISOU 5113  CA  VAL C 172    11084  11802  13049   2450    152    743       C  
ATOM   5114  C   VAL C 172      77.923  43.611  62.624  1.00 91.10           C  
ANISOU 5114  C   VAL C 172    10246  11821  12544   2193    -75    819       C  
ATOM   5115  O   VAL C 172      77.694  43.232  63.782  1.00 93.05           O  
ANISOU 5115  O   VAL C 172    10431  12134  12789   2117    -71   1006       O  
ATOM   5116  CB  VAL C 172      79.555  42.387  61.084  1.00 96.70           C  
ANISOU 5116  CB  VAL C 172    11266  12212  13263   2946    342   1053       C  
ATOM   5117  CG1 VAL C 172      80.514  42.855  62.179  1.00 95.81           C  
ANISOU 5117  CG1 VAL C 172    10680  12640  13081   3027    262   1489       C  
ATOM   5118  CG2 VAL C 172      79.795  40.925  60.715  1.00 94.12           C  
ANISOU 5118  CG2 VAL C 172    11398  11365  12997   3328    671   1145       C  
ATOM   5119  N   LEU C 173      78.004  44.900  62.283  1.00 81.44           N  
ANISOU 5119  N   LEU C 173     8806  10886  11251   2053   -264    665       N  
ATOM   5120  CA  LEU C 173      77.590  45.957  63.211  1.00 85.27           C  
ANISOU 5120  CA  LEU C 173     9065  11678  11654   1769   -479    598       C  
ATOM   5121  C   LEU C 173      76.151  45.762  63.752  1.00 92.14           C  
ANISOU 5121  C   LEU C 173    10039  12411  12557   1522   -498    405       C  
ATOM   5122  O   LEU C 173      75.884  45.991  64.946  1.00 90.20           O  
ANISOU 5122  O   LEU C 173     9669  12384  12217   1407   -553    485       O  
ATOM   5123  CB  LEU C 173      77.726  47.326  62.567  1.00 83.03           C  
ANISOU 5123  CB  LEU C 173     8656  11564  11325   1652   -655    416       C  
ATOM   5124  CG  LEU C 173      79.154  47.710  62.171  1.00 87.67           C  
ANISOU 5124  CG  LEU C 173     9042  12408  11858   1812   -675    675       C  
ATOM   5125  CD1 LEU C 173      79.165  48.515  60.885  1.00 92.35           C  
ANISOU 5125  CD1 LEU C 173     9645  12970  12474   1788   -734    499       C  
ATOM   5126  CD2 LEU C 173      79.874  48.465  63.275  1.00 87.25           C  
ANISOU 5126  CD2 LEU C 173     8728  12756  11666   1648   -864    886       C  
HETATM 5127  N   MSE C 174      75.237  45.316  62.886  1.00 97.62           N  
ANISOU 5127  N   MSE C 174    10945  12793  13351   1428   -455    180       N  
HETATM 5128  CA  MSE C 174      73.821  45.157  63.279  1.00 99.82           C  
ANISOU 5128  CA  MSE C 174    11245  13020  13662   1156   -486     54       C  
HETATM 5129  C   MSE C 174      73.611  44.095  64.346  1.00100.88           C  
ANISOU 5129  C   MSE C 174    11428  13077  13822   1120   -370    304       C  
HETATM 5130  O   MSE C 174      72.998  44.370  65.372  1.00101.02           O  
ANISOU 5130  O   MSE C 174    11280  13337  13766    990   -400    365       O  
HETATM 5131  CB  MSE C 174      72.942  44.935  62.065  1.00106.33           C  
ANISOU 5131  CB  MSE C 174    12243  13602  14556    994   -517   -198       C  
HETATM 5132  CG  MSE C 174      71.470  44.921  62.430  1.00102.99           C  
ANISOU 5132  CG  MSE C 174    11724  13254  14151    688   -577   -264       C  
HETATM 5133 SE   MSE C 174      70.803  43.181  61.828  1.00128.34          SE  
ANISOU 5133 SE   MSE C 174    15330  15955  17477    415   -510   -270      SE  
HETATM 5134  CE  MSE C 174      69.577  42.740  63.303  1.00120.70           C  
ANISOU 5134  CE  MSE C 174    14135  15182  16541    104   -489    -11       C  
ATOM   5135  N   ILE C 175      74.130  42.887  64.137  1.00101.15           N  
ANISOU 5135  N   ILE C 175    11712  12773  13946   1269   -213    474       N  
ATOM   5136  CA  ILE C 175      74.045  41.865  65.193  1.00103.34           C  
ANISOU 5136  CA  ILE C 175    12046  12954  14262   1265    -90    789       C  
ATOM   5137  C   ILE C 175      74.766  42.313  66.462  1.00103.14           C  
ANISOU 5137  C   ILE C 175    11718  13382  14085   1402   -113   1075       C  
ATOM   5138  O   ILE C 175      74.284  42.079  67.564  1.00104.25           O  
ANISOU 5138  O   ILE C 175    11756  13688  14165   1283    -96   1257       O  
ATOM   5139  CB  ILE C 175      74.561  40.471  64.753  1.00109.86           C  
ANISOU 5139  CB  ILE C 175    13268  13253  15221   1471    118    949       C  
ATOM   5140  CG1 ILE C 175      75.947  40.561  64.120  1.00109.66           C  
ANISOU 5140  CG1 ILE C 175    13269  13236  15161   1911    219   1028       C  
ATOM   5141  CG2 ILE C 175      73.573  39.806  63.812  1.00114.26           C  
ANISOU 5141  CG2 ILE C 175    14206  13323  15885   1180    114    676       C  
ATOM   5142  CD1 ILE C 175      76.601  39.217  63.921  1.00111.83           C  
ANISOU 5142  CD1 ILE C 175    13923  13033  15534   2263    493   1264       C  
ATOM   5143  N   LEU C 176      75.902  42.998  66.293  1.00101.84           N  
ANISOU 5143  N   LEU C 176    11398  13467  13829   1613   -172   1123       N  
ATOM   5144  CA  LEU C 176      76.647  43.592  67.427  1.00 96.43           C  
ANISOU 5144  CA  LEU C 176    10417  13278  12942   1654   -270   1361       C  
ATOM   5145  C   LEU C 176      75.983  44.833  68.095  1.00 94.45           C  
ANISOU 5145  C   LEU C 176    10013  13368  12505   1390   -454   1119       C  
ATOM   5146  O   LEU C 176      76.562  45.409  69.011  1.00 98.85           O  
ANISOU 5146  O   LEU C 176    10397  14319  12840   1362   -569   1243       O  
ATOM   5147  CB  LEU C 176      78.074  43.946  67.009  1.00 89.79           C  
ANISOU 5147  CB  LEU C 176     9424  12640  12051   1888   -305   1534       C  
ATOM   5148  CG  LEU C 176      79.162  42.864  66.984  1.00 95.05           C  
ANISOU 5148  CG  LEU C 176    10092  13245  12776   2283   -103   1984       C  
ATOM   5149  CD1 LEU C 176      80.504  43.509  67.295  1.00 91.10           C  
ANISOU 5149  CD1 LEU C 176     9217  13290  12106   2390   -228   2294       C  
ATOM   5150  CD2 LEU C 176      78.882  41.712  67.947  1.00 91.47           C  
ANISOU 5150  CD2 LEU C 176     9732  12663  12357   2357     49   2304       C  
ATOM   5151  N   ARG C 177      74.807  45.254  67.594  1.00 86.56           N  
ANISOU 5151  N   ARG C 177     9093  12223  11572   1217   -480    781       N  
ATOM   5152  CA  ARG C 177      73.997  46.343  68.207  1.00 83.39           C  
ANISOU 5152  CA  ARG C 177     8597  12082  11003   1061   -576    556       C  
ATOM   5153  C   ARG C 177      74.559  47.783  68.065  1.00 84.81           C  
ANISOU 5153  C   ARG C 177     8736  12439  11047   1043   -755    349       C  
ATOM   5154  O   ARG C 177      74.320  48.626  68.921  1.00 85.36           O  
ANISOU 5154  O   ARG C 177     8791  12742  10897    970   -825    233       O  
ATOM   5155  CB  ARG C 177      73.707  46.035  69.676  1.00 83.46           C  
ANISOU 5155  CB  ARG C 177     8520  12374  10815   1021   -520    765       C  
ATOM   5156  CG  ARG C 177      72.729  44.904  69.882  1.00 89.49           C  
ANISOU 5156  CG  ARG C 177     9314  12983  11706    940   -360    928       C  
ATOM   5157  CD  ARG C 177      73.126  44.010  71.045  1.00 96.86           C  
ANISOU 5157  CD  ARG C 177    10194  14073  12535    993   -267   1345       C  
ATOM   5158  NE  ARG C 177      73.519  44.779  72.217  1.00100.93           N  
ANISOU 5158  NE  ARG C 177    10575  15073  12700   1011   -352   1383       N  
ATOM   5159  CZ  ARG C 177      74.662  44.613  72.871  1.00107.84           C  
ANISOU 5159  CZ  ARG C 177    11370  16193  13412   1106   -411   1671       C  
ATOM   5160  NH1 ARG C 177      75.527  43.667  72.486  1.00111.15           N  
ANISOU 5160  NH1 ARG C 177    11802  16412  14017   1276   -344   1994       N  
ATOM   5161  NH2 ARG C 177      74.936  45.382  73.921  1.00109.52           N  
ANISOU 5161  NH2 ARG C 177    11500  16866  13247   1045   -529   1651       N  
ATOM   5162  N   TYR C 178      75.283  48.063  66.986  1.00 85.39           N  
ANISOU 5162  N   TYR C 178     8826  12382  11233   1102   -817    302       N  
ATOM   5163  CA  TYR C 178      75.877  49.395  66.807  1.00 84.85           C  
ANISOU 5163  CA  TYR C 178     8729  12445  11064   1029  -1000    163       C  
ATOM   5164  C   TYR C 178      75.061  50.264  65.878  1.00 84.14           C  
ANISOU 5164  C   TYR C 178     8725  12169  11073    994  -1034   -153       C  
ATOM   5165  O   TYR C 178      74.585  49.809  64.842  1.00 91.00           O  
ANISOU 5165  O   TYR C 178     9630  12830  12116   1047   -959   -216       O  
ATOM   5166  CB  TYR C 178      77.329  49.295  66.317  1.00 87.63           C  
ANISOU 5166  CB  TYR C 178     8965  12889  11438   1105  -1059    412       C  
ATOM   5167  CG  TYR C 178      78.287  48.846  67.403  1.00 96.89           C  
ANISOU 5167  CG  TYR C 178     9978  14391  12441   1119  -1094    772       C  
ATOM   5168  CD1 TYR C 178      78.671  49.718  68.434  1.00103.25           C  
ANISOU 5168  CD1 TYR C 178    10730  15524  12974    895  -1301    769       C  
ATOM   5169  CD2 TYR C 178      78.773  47.549  67.430  1.00 99.19           C  
ANISOU 5169  CD2 TYR C 178    10206  14662  12818   1356   -922   1121       C  
ATOM   5170  CE1 TYR C 178      79.530  49.308  69.438  1.00107.06           C  
ANISOU 5170  CE1 TYR C 178    11031  16391  13254    873  -1368   1131       C  
ATOM   5171  CE2 TYR C 178      79.629  47.124  68.434  1.00109.87           C  
ANISOU 5171  CE2 TYR C 178    11368  16369  14007   1406   -949   1522       C  
ATOM   5172  CZ  TYR C 178      80.008  48.007  69.435  1.00110.69           C  
ANISOU 5172  CZ  TYR C 178    11353  16884  13821   1146  -1189   1539       C  
ATOM   5173  OH  TYR C 178      80.855  47.579  70.435  1.00112.63           O  
ANISOU 5173  OH  TYR C 178    11372  17560  13860   1165  -1249   1971       O  
ATOM   5174  N   ARG C 179      74.902  51.525  66.247  1.00 82.93           N  
ANISOU 5174  N   ARG C 179     8636  12084  10788    905  -1149   -348       N  
ATOM   5175  CA  ARG C 179      74.114  52.451  65.448  1.00 80.07           C  
ANISOU 5175  CA  ARG C 179     8355  11553  10515    926  -1166   -600       C  
ATOM   5176  C   ARG C 179      74.771  52.821  64.109  1.00 84.12           C  
ANISOU 5176  C   ARG C 179     8848  11937  11173    929  -1249   -582       C  
ATOM   5177  O   ARG C 179      74.110  53.294  63.222  1.00 89.68           O  
ANISOU 5177  O   ARG C 179     9581  12509  11982    976  -1242   -718       O  
ATOM   5178  CB  ARG C 179      73.809  53.709  66.233  1.00 78.27           C  
ANISOU 5178  CB  ARG C 179     8287  11352  10099    887  -1230   -810       C  
ATOM   5179  CG  ARG C 179      73.833  54.948  65.375  1.00 81.41           C  
ANISOU 5179  CG  ARG C 179     8807  11546  10578    881  -1328   -970       C  
ATOM   5180  CD  ARG C 179      73.251  56.123  66.101  1.00 93.96           C  
ANISOU 5180  CD  ARG C 179    10651  13050  11998    922  -1322  -1218       C  
ATOM   5181  NE  ARG C 179      74.181  56.671  67.073  1.00102.19           N  
ANISOU 5181  NE  ARG C 179    11886  14148  12792    707  -1485  -1264       N  
ATOM   5182  CZ  ARG C 179      75.266  57.366  66.757  1.00113.41           C  
ANISOU 5182  CZ  ARG C 179    13391  15485  14212    464  -1706  -1226       C  
ATOM   5183  NH1 ARG C 179      75.580  57.587  65.477  1.00115.58           N  
ANISOU 5183  NH1 ARG C 179    13563  15621  14729    458  -1757  -1124       N  
ATOM   5184  NH2 ARG C 179      76.049  57.833  67.720  1.00125.32           N  
ANISOU 5184  NH2 ARG C 179    15074  17089  15451    190  -1892  -1264       N  
ATOM   5185  N   GLU C 180      76.073  52.624  63.972  1.00 96.00           N  
ANISOU 5185  N   GLU C 180    10269  13542  12665    896  -1320   -368       N  
ATOM   5186  CA  GLU C 180      76.754  53.055  62.738  1.00100.66           C  
ANISOU 5186  CA  GLU C 180    10808  14081  13355    907  -1382   -307       C  
ATOM   5187  C   GLU C 180      76.425  52.159  61.538  1.00 98.11           C  
ANISOU 5187  C   GLU C 180    10482  13624  13172   1079  -1235   -305       C  
ATOM   5188  O   GLU C 180      76.778  52.475  60.400  1.00 97.68           O  
ANISOU 5188  O   GLU C 180    10402  13540  13172   1125  -1252   -282       O  
ATOM   5189  CB  GLU C 180      78.268  53.179  62.951  1.00103.90           C  
ANISOU 5189  CB  GLU C 180    11063  14729  13684    817  -1498    -16       C  
ATOM   5190  CG  GLU C 180      78.679  54.430  63.741  1.00116.05           C  
ANISOU 5190  CG  GLU C 180    12669  16353  15069    522  -1732    -67       C  
ATOM   5191  CD  GLU C 180      78.142  54.437  65.173  1.00116.29           C  
ANISOU 5191  CD  GLU C 180    12838  16440  14907    443  -1748   -214       C  
ATOM   5192  OE1 GLU C 180      77.933  53.337  65.729  1.00107.62           O  
ANISOU 5192  OE1 GLU C 180    11658  15451  13780    578  -1612   -104       O  
ATOM   5193  OE2 GLU C 180      77.933  55.541  65.741  1.00118.28           O  
ANISOU 5193  OE2 GLU C 180    13312  16607  15018    256  -1883   -433       O  
ATOM   5194  N   GLN C 181      75.728  51.053  61.804  1.00 90.97           N  
ANISOU 5194  N   GLN C 181     9630  12634  12298   1142  -1099   -330       N  
ATOM   5195  CA  GLN C 181      75.297  50.141  60.763  1.00 90.73           C  
ANISOU 5195  CA  GLN C 181     9691  12421  12358   1229   -984   -384       C  
ATOM   5196  C   GLN C 181      74.467  50.891  59.708  1.00 93.93           C  
ANISOU 5196  C   GLN C 181    10115  12769  12802   1178  -1055   -587       C  
ATOM   5197  O   GLN C 181      74.675  50.718  58.514  1.00 98.34           O  
ANISOU 5197  O   GLN C 181    10722  13269  13370   1244  -1034   -607       O  
ATOM   5198  CB  GLN C 181      74.479  49.005  61.371  1.00 93.88           C  
ANISOU 5198  CB  GLN C 181    10175  12708  12787   1188   -875   -388       C  
ATOM   5199  CG  GLN C 181      73.260  49.491  62.160  1.00 96.43           C  
ANISOU 5199  CG  GLN C 181    10434  13121  13081   1051   -913   -508       C  
ATOM   5200  CD  GLN C 181      72.211  48.419  62.345  1.00 90.77           C  
ANISOU 5200  CD  GLN C 181     9762  12309  12419    940   -824   -501       C  
ATOM   5201  OE1 GLN C 181      71.742  47.821  61.377  1.00 83.23           O  
ANISOU 5201  OE1 GLN C 181     8908  11182  11532    860   -816   -580       O  
ATOM   5202  NE2 GLN C 181      71.837  48.165  63.595  1.00 85.46           N  
ANISOU 5202  NE2 GLN C 181     9022  11761  11688    894   -769   -395       N  
ATOM   5203  N   TRP C 182      73.561  51.757  60.169  1.00 90.94           N  
ANISOU 5203  N   TRP C 182     9697  12437  12417   1100  -1121   -711       N  
ATOM   5204  CA  TRP C 182      72.709  52.551  59.275  1.00 88.68           C  
ANISOU 5204  CA  TRP C 182     9386  12140  12167   1099  -1180   -836       C  
ATOM   5205  C   TRP C 182      73.429  53.448  58.262  1.00 85.28           C  
ANISOU 5205  C   TRP C 182     8948  11703  11749   1142  -1264   -796       C  
ATOM   5206  O   TRP C 182      72.936  53.646  57.158  1.00 90.52           O  
ANISOU 5206  O   TRP C 182     9592  12372  12428   1165  -1291   -837       O  
ATOM   5207  CB  TRP C 182      71.672  53.344  60.066  1.00 85.64           C  
ANISOU 5207  CB  TRP C 182     8961  11814  11762   1110  -1181   -926       C  
ATOM   5208  CG  TRP C 182      70.799  52.458  60.874  1.00 86.61           C  
ANISOU 5208  CG  TRP C 182     9029  12014  11864   1059  -1085   -916       C  
ATOM   5209  CD1 TRP C 182      70.878  52.248  62.206  1.00 90.16           C  
ANISOU 5209  CD1 TRP C 182     9490  12535  12229   1055  -1022   -877       C  
ATOM   5210  CD2 TRP C 182      69.747  51.600  60.394  1.00 83.68           C  
ANISOU 5210  CD2 TRP C 182     8573  11683  11536    954  -1056   -909       C  
ATOM   5211  NE1 TRP C 182      69.928  51.345  62.605  1.00 94.37           N  
ANISOU 5211  NE1 TRP C 182     9934  13152  12770    982   -932   -818       N  
ATOM   5212  CE2 TRP C 182      69.219  50.930  61.509  1.00 86.61           C  
ANISOU 5212  CE2 TRP C 182     8890  12141  11875    888   -963   -835       C  
ATOM   5213  CE3 TRP C 182      69.189  51.355  59.136  1.00 78.21           C  
ANISOU 5213  CE3 TRP C 182     7845  10994  10877    867  -1121   -943       C  
ATOM   5214  CZ2 TRP C 182      68.167  50.015  61.408  1.00 78.18           C  
ANISOU 5214  CZ2 TRP C 182     7723  11139  10842    704   -938   -769       C  
ATOM   5215  CZ3 TRP C 182      68.147  50.446  59.039  1.00 73.98           C  
ANISOU 5215  CZ3 TRP C 182     7232  10529  10348    660  -1121   -913       C  
ATOM   5216  CH2 TRP C 182      67.659  49.779  60.167  1.00 72.59           C  
ANISOU 5216  CH2 TRP C 182     6994  10412  10174    564  -1033   -816       C  
ATOM   5217  N   ALA C 183      74.581  53.995  58.619  1.00 81.39           N  
ANISOU 5217  N   ALA C 183     8449  11241  11233   1120  -1323   -679       N  
ATOM   5218  CA  ALA C 183      75.348  54.714  57.622  1.00 79.31           C  
ANISOU 5218  CA  ALA C 183     8144  11003  10984   1125  -1394   -567       C  
ATOM   5219  C   ALA C 183      75.689  53.760  56.483  1.00 86.14           C  
ANISOU 5219  C   ALA C 183     8991  11915  11822   1246  -1294   -504       C  
ATOM   5220  O   ALA C 183      75.495  54.097  55.318  1.00 92.71           O  
ANISOU 5220  O   ALA C 183     9814  12769  12640   1287  -1311   -513       O  
ATOM   5221  CB  ALA C 183      76.586  55.325  58.221  1.00 76.39           C  
ANISOU 5221  CB  ALA C 183     7730  10711  10581   1003  -1497   -395       C  
ATOM   5222  N   LEU C 184      76.119  52.538  56.835  1.00 91.95           N  
ANISOU 5222  N   LEU C 184     9760  12649  12528   1326  -1172   -449       N  
ATOM   5223  CA  LEU C 184      76.427  51.493  55.844  1.00 86.63           C  
ANISOU 5223  CA  LEU C 184     9182  11937  11794   1493  -1026   -437       C  
ATOM   5224  C   LEU C 184      75.197  51.051  55.085  1.00 85.86           C  
ANISOU 5224  C   LEU C 184     9237  11713  11671   1429  -1027   -677       C  
ATOM   5225  O   LEU C 184      75.191  51.088  53.868  1.00 93.78           O  
ANISOU 5225  O   LEU C 184    10297  12752  12583   1484  -1020   -723       O  
ATOM   5226  CB  LEU C 184      77.092  50.281  56.491  1.00 89.42           C  
ANISOU 5226  CB  LEU C 184     9597  12240  12137   1638   -868   -309       C  
ATOM   5227  CG  LEU C 184      78.613  50.211  56.594  1.00 91.84           C  
ANISOU 5227  CG  LEU C 184     9737  12755  12400   1829   -788     21       C  
ATOM   5228  CD1 LEU C 184      79.295  50.634  55.305  1.00 91.60           C  
ANISOU 5228  CD1 LEU C 184     9631  12880  12293   1969   -746    130       C  
ATOM   5229  CD2 LEU C 184      79.088  51.058  57.742  1.00 93.26           C  
ANISOU 5229  CD2 LEU C 184     9700  13135  12598   1642   -955    186       C  
ATOM   5230  N   TRP C 185      74.145  50.647  55.797  1.00 88.61           N  
ANISOU 5230  N   TRP C 185     9628  11968  12070   1286  -1048   -801       N  
ATOM   5231  CA  TRP C 185      72.851  50.319  55.140  1.00 88.56           C  
ANISOU 5231  CA  TRP C 185     9690  11925  12031   1130  -1106   -981       C  
ATOM   5232  C   TRP C 185      72.422  51.332  54.070  1.00 86.83           C  
ANISOU 5232  C   TRP C 185     9361  11867  11761   1119  -1226  -1008       C  
ATOM   5233  O   TRP C 185      71.888  50.938  53.041  1.00 91.29           O  
ANISOU 5233  O   TRP C 185    10013  12459  12214   1037  -1269  -1114       O  
ATOM   5234  CB  TRP C 185      71.720  50.175  56.149  1.00 89.33           C  
ANISOU 5234  CB  TRP C 185     9704  12034  12200    962  -1138  -1016       C  
ATOM   5235  CG  TRP C 185      71.852  49.045  57.078  1.00 91.41           C  
ANISOU 5235  CG  TRP C 185    10085  12144  12501    923  -1030   -970       C  
ATOM   5236  CD1 TRP C 185      71.711  49.087  58.437  1.00 93.30           C  
ANISOU 5236  CD1 TRP C 185    10221  12439  12787    906   -997   -878       C  
ATOM   5237  CD2 TRP C 185      72.148  47.687  56.745  1.00 90.53           C  
ANISOU 5237  CD2 TRP C 185    10255  11775  12366    915   -925   -998       C  
ATOM   5238  NE1 TRP C 185      71.907  47.836  58.970  1.00 93.24           N  
ANISOU 5238  NE1 TRP C 185    10365  12255  12804    878   -887   -800       N  
ATOM   5239  CE2 TRP C 185      72.172  46.958  57.951  1.00 91.53           C  
ANISOU 5239  CE2 TRP C 185    10409  11802  12564    890   -834   -876       C  
ATOM   5240  CE3 TRP C 185      72.409  47.016  55.550  1.00 88.81           C  
ANISOU 5240  CE3 TRP C 185    10315  11378  12049    948   -881  -1121       C  
ATOM   5241  CZ2 TRP C 185      72.424  45.591  57.989  1.00 88.81           C  
ANISOU 5241  CZ2 TRP C 185    10365  11138  12239    900   -701   -845       C  
ATOM   5242  CZ3 TRP C 185      72.666  45.650  55.597  1.00 86.53           C  
ANISOU 5242  CZ3 TRP C 185    10377  10744  11755    970   -736  -1143       C  
ATOM   5243  CH2 TRP C 185      72.669  44.960  56.803  1.00 86.45           C  
ANISOU 5243  CH2 TRP C 185    10391  10595  11861    948   -648   -993       C  
ATOM   5244  N   ILE C 186      72.623  52.633  54.317  1.00 79.71           N  
ANISOU 5244  N   ILE C 186     8300  11059  10927   1181  -1290   -907       N  
ATOM   5245  CA  ILE C 186      72.255  53.629  53.295  1.00 84.61           C  
ANISOU 5245  CA  ILE C 186     8824  11807  11517   1207  -1388   -871       C  
ATOM   5246  C   ILE C 186      73.058  53.443  51.997  1.00 86.35           C  
ANISOU 5246  C   ILE C 186     9110  12098  11600   1289  -1361   -820       C  
ATOM   5247  O   ILE C 186      72.519  53.560  50.902  1.00 92.64           O  
ANISOU 5247  O   ILE C 186     9894  13026  12278   1266  -1426   -849       O  
ATOM   5248  CB  ILE C 186      72.282  55.095  53.815  1.00 82.82           C  
ANISOU 5248  CB  ILE C 186     8501  11564  11402   1263  -1448   -771       C  
ATOM   5249  CG1 ILE C 186      71.026  55.371  54.621  1.00 80.55           C  
ANISOU 5249  CG1 ILE C 186     8145  11285  11173   1261  -1450   -842       C  
ATOM   5250  CG2 ILE C 186      72.261  56.077  52.652  1.00 84.59           C  
ANISOU 5250  CG2 ILE C 186     8656  11875  11606   1327  -1522   -651       C  
ATOM   5251  CD1 ILE C 186      71.253  56.173  55.863  1.00 76.91           C  
ANISOU 5251  CD1 ILE C 186     7747  10695  10779   1309  -1428   -849       C  
ATOM   5252  N   VAL C 187      74.315  53.069  52.125  1.00 86.68           N  
ANISOU 5252  N   VAL C 187     9206  12106  11622   1401  -1252   -725       N  
ATOM   5253  CA  VAL C 187      75.120  52.750  50.960  1.00 86.59           C  
ANISOU 5253  CA  VAL C 187     9260  12195  11442   1550  -1160   -661       C  
ATOM   5254  C   VAL C 187      74.735  51.402  50.303  1.00 88.31           C  
ANISOU 5254  C   VAL C 187     9763  12312  11479   1563  -1070   -888       C  
ATOM   5255  O   VAL C 187      74.644  51.325  49.087  1.00 89.52           O  
ANISOU 5255  O   VAL C 187    10012  12576  11424   1599  -1069   -952       O  
ATOM   5256  CB  VAL C 187      76.608  52.810  51.295  1.00 88.99           C  
ANISOU 5256  CB  VAL C 187     9469  12572  11769   1703  -1051   -412       C  
ATOM   5257  CG1 VAL C 187      77.439  53.113  50.058  1.00 89.23           C  
ANISOU 5257  CG1 VAL C 187     9431  12830  11642   1867   -978   -228       C  
ATOM   5258  CG2 VAL C 187      76.828  53.887  52.331  1.00 94.33           C  
ANISOU 5258  CG2 VAL C 187     9968  13251  12619   1560  -1183   -271       C  
ATOM   5259  N   VAL C 188      74.466  50.357  51.091  1.00 87.44           N  
ANISOU 5259  N   VAL C 188     9824  11973  11426   1504  -1004  -1013       N  
ATOM   5260  CA  VAL C 188      74.013  49.096  50.468  1.00 92.04           C  
ANISOU 5260  CA  VAL C 188    10768  12363  11839   1440   -945  -1256       C  
ATOM   5261  C   VAL C 188      72.673  49.227  49.796  1.00 91.93           C  
ANISOU 5261  C   VAL C 188    10757  12452  11721   1138  -1151  -1427       C  
ATOM   5262  O   VAL C 188      72.384  48.489  48.878  1.00100.54           O  
ANISOU 5262  O   VAL C 188    12145  13474  12580   1041  -1161  -1630       O  
ATOM   5263  CB  VAL C 188      74.002  47.851  51.404  1.00 93.19           C  
ANISOU 5263  CB  VAL C 188    11154  12176  12078   1415   -825  -1322       C  
ATOM   5264  CG1 VAL C 188      74.933  48.032  52.585  1.00 92.34           C  
ANISOU 5264  CG1 VAL C 188    10854  12086  12145   1606   -720  -1069       C  
ATOM   5265  CG2 VAL C 188      72.582  47.506  51.838  1.00 89.36           C  
ANISOU 5265  CG2 VAL C 188    10687  11607  11659   1030   -986  -1464       C  
ATOM   5266  N   ASN C 189      71.855  50.176  50.225  1.00 93.25           N  
ANISOU 5266  N   ASN C 189    10602  12801  12027    999  -1313  -1335       N  
ATOM   5267  CA  ASN C 189      70.535  50.331  49.587  1.00100.18           C  
ANISOU 5267  CA  ASN C 189    11386  13878  12798    734  -1514  -1411       C  
ATOM   5268  C   ASN C 189      70.554  51.133  48.264  1.00100.50           C  
ANISOU 5268  C   ASN C 189    11329  14209  12645    805  -1606  -1345       C  
ATOM   5269  O   ASN C 189      69.974  50.701  47.270  1.00103.61           O  
ANISOU 5269  O   ASN C 189    11847  14736  12784    617  -1723  -1478       O  
ATOM   5270  CB  ASN C 189      69.454  50.821  50.582  1.00 99.62           C  
ANISOU 5270  CB  ASN C 189    11011  13915  12923    597  -1610  -1313       C  
ATOM   5271  CG  ASN C 189      69.123  49.769  51.662  1.00 98.03           C  
ANISOU 5271  CG  ASN C 189    10923  13496  12828    422  -1552  -1382       C  
ATOM   5272  OD1 ASN C 189      68.596  50.103  52.737  1.00 89.19           O  
ANISOU 5272  OD1 ASN C 189     9581  12437  11867    409  -1544  -1278       O  
ATOM   5273  ND2 ASN C 189      69.470  48.498  51.390  1.00 91.99           N  
ANISOU 5273  ND2 ASN C 189    10539  12452  11961    321  -1485  -1546       N  
ATOM   5274  N   ILE C 190      71.282  52.247  48.233  1.00 93.82           N  
ANISOU 5274  N   ILE C 190    10294  13459  11893   1044  -1561  -1132       N  
ATOM   5275  CA  ILE C 190      71.524  52.938  46.970  1.00 91.25           C  
ANISOU 5275  CA  ILE C 190     9899  13391  11379   1144  -1607  -1014       C  
ATOM   5276  C   ILE C 190      72.265  52.044  45.966  1.00 97.20           C  
ANISOU 5276  C   ILE C 190    10969  14142  11818   1232  -1487  -1159       C  
ATOM   5277  O   ILE C 190      72.115  52.204  44.773  1.00102.75           O  
ANISOU 5277  O   ILE C 190    11701  15096  12242   1226  -1552  -1161       O  
ATOM   5278  CB  ILE C 190      72.321  54.219  47.169  1.00 89.05           C  
ANISOU 5278  CB  ILE C 190     9409  13147  11276   1343  -1568   -729       C  
ATOM   5279  CG1 ILE C 190      71.506  55.236  47.959  1.00 84.50           C  
ANISOU 5279  CG1 ILE C 190     8610  12547  10947   1310  -1670   -615       C  
ATOM   5280  CG2 ILE C 190      72.739  54.794  45.831  1.00 87.04           C  
ANISOU 5280  CG2 ILE C 190     9101  13159  10811   1453  -1580   -560       C  
ATOM   5281  CD1 ILE C 190      72.277  56.494  48.318  1.00 86.38           C  
ANISOU 5281  CD1 ILE C 190     8752  12693  11375   1437  -1648   -377       C  
ATOM   5282  N   LEU C 191      73.044  51.089  46.451  1.00 99.89           N  
ANISOU 5282  N   LEU C 191    11565  14210  12176   1349  -1294  -1271       N  
ATOM   5283  CA  LEU C 191      73.755  50.185  45.535  1.00102.03           C  
ANISOU 5283  CA  LEU C 191    12206  14431  12129   1525  -1115  -1423       C  
ATOM   5284  C   LEU C 191      72.873  49.095  44.945  1.00103.52           C  
ANISOU 5284  C   LEU C 191    12803  14485  12045   1257  -1204  -1786       C  
ATOM   5285  O   LEU C 191      72.795  48.959  43.731  1.00104.90           O  
ANISOU 5285  O   LEU C 191    13174  14833  11847   1245  -1233  -1915       O  
ATOM   5286  CB  LEU C 191      75.014  49.612  46.175  1.00100.81           C  
ANISOU 5286  CB  LEU C 191    12164  14063  12076   1844   -835  -1338       C  
ATOM   5287  CG  LEU C 191      76.068  50.703  46.360  1.00 96.73           C  
ANISOU 5287  CG  LEU C 191    11259  13793  11701   2063   -772   -951       C  
ATOM   5288  CD1 LEU C 191      77.379  50.135  46.861  1.00 91.16           C  
ANISOU 5288  CD1 LEU C 191    10583  13013  11039   2393   -502   -786       C  
ATOM   5289  CD2 LEU C 191      76.261  51.483  45.063  1.00 97.92           C  
ANISOU 5289  CD2 LEU C 191    11287  14302  11613   2144   -800   -811       C  
ATOM   5290  N   THR C 192      72.171  48.355  45.802  1.00101.83           N  
ANISOU 5290  N   THR C 192    12714  13985  11991    992  -1270  -1935       N  
ATOM   5291  CA  THR C 192      71.252  47.304  45.337  1.00108.93           C  
ANISOU 5291  CA  THR C 192    14011  14720  12654    606  -1407  -2263       C  
ATOM   5292  C   THR C 192      70.088  47.810  44.438  1.00116.21           C  
ANISOU 5292  C   THR C 192    14743  16063  13347    239  -1733  -2286       C  
ATOM   5293  O   THR C 192      69.580  47.051  43.606  1.00124.10           O  
ANISOU 5293  O   THR C 192    16119  17036  13994    -67  -1863  -2566       O  
ATOM   5294  CB  THR C 192      70.673  46.495  46.498  1.00102.79           C  
ANISOU 5294  CB  THR C 192    13330  13594  12130    337  -1435  -2329       C  
ATOM   5295  OG1 THR C 192      71.719  46.153  47.394  1.00103.61           O  
ANISOU 5295  OG1 THR C 192    13518  13395  12453    694  -1156  -2226       O  
ATOM   5296  CG2 THR C 192      70.040  45.228  45.991  1.00107.93           C  
ANISOU 5296  CG2 THR C 192    14534  13946  12526    -58  -1530  -2674       C  
ATOM   5297  N   ILE C 193      69.665  49.070  44.610  1.00105.81           N  
ANISOU 5297  N   ILE C 193    12871  15123  12208    268  -1866  -1984       N  
ATOM   5298  CA  ILE C 193      68.679  49.645  43.696  1.00102.25           C  
ANISOU 5298  CA  ILE C 193    12176  15143  11531     25  -2144  -1909       C  
ATOM   5299  C   ILE C 193      69.253  49.664  42.283  1.00102.72           C  
ANISOU 5299  C   ILE C 193    12475  15399  11152    163  -2112  -1998       C  
ATOM   5300  O   ILE C 193      68.586  49.234  41.340  1.00106.90           O  
ANISOU 5300  O   ILE C 193    13190  16137  11287   -159  -2318  -2180       O  
ATOM   5301  CB  ILE C 193      68.217  51.059  44.120  1.00101.94           C  
ANISOU 5301  CB  ILE C 193    11539  15418  11773    155  -2228  -1527       C  
ATOM   5302  CG1 ILE C 193      67.258  50.982  45.296  1.00101.96           C  
ANISOU 5302  CG1 ILE C 193    11294  15373  12070    -47  -2306  -1458       C  
ATOM   5303  CG2 ILE C 193      67.485  51.739  42.983  1.00106.11           C  
ANISOU 5303  CG2 ILE C 193    11813  16469  12033     50  -2458  -1366       C  
ATOM   5304  CD1 ILE C 193      67.008  52.320  45.947  1.00100.51           C  
ANISOU 5304  CD1 ILE C 193    10651  15348  12190    209  -2283  -1130       C  
ATOM   5305  N   SER C 194      70.512  50.116  42.156  1.00100.31           N  
ANISOU 5305  N   SER C 194    12171  15055  10886    618  -1854  -1862       N  
ATOM   5306  CA  SER C 194      71.257  50.087  40.871  1.00102.80           C  
ANISOU 5306  CA  SER C 194    12720  15570  10769    844  -1737  -1912       C  
ATOM   5307  C   SER C 194      71.408  48.690  40.327  1.00107.11           C  
ANISOU 5307  C   SER C 194    13939  15836  10919    764  -1641  -2359       C  
ATOM   5308  O   SER C 194      71.330  48.492  39.134  1.00117.01           O  
ANISOU 5308  O   SER C 194    15455  17322  11680    712  -1695  -2525       O  
ATOM   5309  CB  SER C 194      72.653  50.675  41.029  1.00104.04           C  
ANISOU 5309  CB  SER C 194    12728  15721  11081   1331  -1443  -1638       C  
ATOM   5310  OG  SER C 194      72.613  51.998  41.497  1.00109.48           O  
ANISOU 5310  OG  SER C 194    12896  16584  12115   1384  -1528  -1248       O  
ATOM   5311  N   LEU C 195      71.686  47.727  41.210  1.00107.90           N  
ANISOU 5311  N   LEU C 195    14363  15412  11219    787  -1478  -2548       N  
ATOM   5312  CA  LEU C 195      71.795  46.311  40.818  1.00109.66           C  
ANISOU 5312  CA  LEU C 195    15341  15210  11113    715  -1362  -2996       C  
ATOM   5313  C   LEU C 195      70.552  45.794  40.125  1.00112.22           C  
ANISOU 5313  C   LEU C 195    15946  15612  11077     98  -1718  -3310       C  
ATOM   5314  O   LEU C 195      70.642  45.199  39.055  1.00126.02           O  
ANISOU 5314  O   LEU C 195    18244  17339  12299     51  -1703  -3641       O  
ATOM   5315  CB  LEU C 195      72.118  45.430  42.014  1.00108.79           C  
ANISOU 5315  CB  LEU C 195    15473  14512  11350    793  -1167  -3066       C  
ATOM   5316  CG  LEU C 195      73.569  45.463  42.429  1.00112.31           C  
ANISOU 5316  CG  LEU C 195    15887  14826  11959   1438   -757  -2856       C  
ATOM   5317  CD1 LEU C 195      73.870  44.274  43.322  1.00120.20           C  
ANISOU 5317  CD1 LEU C 195    17316  15204  13149   1533   -542  -2992       C  
ATOM   5318  CD2 LEU C 195      74.466  45.468  41.197  1.00112.92           C  
ANISOU 5318  CD2 LEU C 195    16215  15108  11581   1872   -510  -2908       C  
ATOM   5319  N   TRP C 196      69.393  46.016  40.725  1.00150.21           N  
ANISOU 5319  N   TRP C 196    25151  16043  15879  -2698  -1611  -3325       N  
ATOM   5320  CA  TRP C 196      68.161  45.597  40.100  1.00144.17           C  
ANISOU 5320  CA  TRP C 196    24492  15560  14727  -2931  -1532  -3661       C  
ATOM   5321  C   TRP C 196      67.743  46.502  38.927  1.00143.74           C  
ANISOU 5321  C   TRP C 196    23928  15934  14752  -2783  -1635  -3383       C  
ATOM   5322  O   TRP C 196      66.928  46.101  38.108  1.00146.39           O  
ANISOU 5322  O   TRP C 196    24320  16616  14685  -2822  -1591  -3639       O  
ATOM   5323  CB  TRP C 196      67.044  45.498  41.119  1.00140.05           C  
ANISOU 5323  CB  TRP C 196    24093  14887  14231  -3306  -1561  -4146       C  
ATOM   5324  CG  TRP C 196      67.196  44.390  42.092  1.00137.41           C  
ANISOU 5324  CG  TRP C 196    24294  14231  13681  -3404  -1339  -4389       C  
ATOM   5325  CD1 TRP C 196      67.667  44.485  43.360  1.00135.91           C  
ANISOU 5325  CD1 TRP C 196    24222  13790  13628  -3296  -1366  -4384       C  
ATOM   5326  CD2 TRP C 196      66.808  43.028  41.908  1.00138.33           C  
ANISOU 5326  CD2 TRP C 196    24862  14245  13449  -3581  -1050  -4681       C  
ATOM   5327  NE1 TRP C 196      67.614  43.263  43.982  1.00135.92           N  
ANISOU 5327  NE1 TRP C 196    24745  13574  13323  -3364  -1048  -4553       N  
ATOM   5328  CE2 TRP C 196      67.086  42.351  43.115  1.00137.74           C  
ANISOU 5328  CE2 TRP C 196    25174  13829  13331  -3581   -840  -4725       C  
ATOM   5329  CE3 TRP C 196      66.255  42.311  40.840  1.00140.86           C  
ANISOU 5329  CE3 TRP C 196    25262  14724  13534  -3690   -970  -4945       C  
ATOM   5330  CZ2 TRP C 196      66.841  40.988  43.285  1.00140.26           C  
ANISOU 5330  CZ2 TRP C 196    25940  13883  13468  -3733   -491  -4923       C  
ATOM   5331  CZ3 TRP C 196      66.000  40.951  41.010  1.00143.06           C  
ANISOU 5331  CZ3 TRP C 196    25961  14704  13688  -3870   -701  -5266       C  
ATOM   5332  CH2 TRP C 196      66.301  40.303  42.223  1.00142.91           C  
ANISOU 5332  CH2 TRP C 196    26310  14270  13720  -3914   -432  -5202       C  
ATOM   5333  N   ALA C 197      68.288  47.715  38.855  1.00140.92           N  
ANISOU 5333  N   ALA C 197    23037  15542  14961  -2576  -1775  -2873       N  
ATOM   5334  CA  ALA C 197      67.989  48.592  37.732  1.00141.40           C  
ANISOU 5334  CA  ALA C 197    22588  16009  15129  -2344  -1794  -2452       C  
ATOM   5335  C   ALA C 197      68.808  48.225  36.519  1.00144.77           C  
ANISOU 5335  C   ALA C 197    23013  16790  15201  -1863  -1567  -1952       C  
ATOM   5336  O   ALA C 197      68.318  48.300  35.395  1.00149.32           O  
ANISOU 5336  O   ALA C 197    23438  17916  15381  -1595  -1499  -1828       O  
ATOM   5337  CB  ALA C 197      68.195  50.046  38.093  1.00140.29           C  
ANISOU 5337  CB  ALA C 197    21802  15629  15871  -2299  -1996  -2051       C  
ATOM   5338  N   VAL C 198      70.063  47.834  36.721  1.00145.00           N  
ANISOU 5338  N   VAL C 198    23195  16571  15325  -1677  -1452  -1663       N  
ATOM   5339  CA  VAL C 198      70.872  47.420  35.578  1.00147.73           C  
ANISOU 5339  CA  VAL C 198    23559  17301  15269  -1161  -1210  -1176       C  
ATOM   5340  C   VAL C 198      70.484  46.024  35.133  1.00150.35           C  
ANISOU 5340  C   VAL C 198    24496  17915  14714  -1150  -1127  -1764       C  
ATOM   5341  O   VAL C 198      70.467  45.736  33.940  1.00155.02           O  
ANISOU 5341  O   VAL C 198    25065  19082  14753   -699  -1023  -1631       O  
ATOM   5342  CB  VAL C 198      72.420  47.602  35.767  1.00146.10           C  
ANISOU 5342  CB  VAL C 198    23185  16781  15544   -885  -1095   -547       C  
ATOM   5343  CG1 VAL C 198      72.763  49.055  36.035  1.00145.92           C  
ANISOU 5343  CG1 VAL C 198    22411  16449  16584   -854  -1205     27       C  
ATOM   5344  CG2 VAL C 198      72.973  46.703  36.856  1.00142.76           C  
ANISOU 5344  CG2 VAL C 198    23300  15890  15051  -1127  -1137   -999       C  
ATOM   5345  N   ALA C 199      70.072  45.191  36.088  1.00149.72           N  
ANISOU 5345  N   ALA C 199    24906  17446  14535  -1608  -1183  -2441       N  
ATOM   5346  CA  ALA C 199      69.599  43.850  35.777  1.00154.22           C  
ANISOU 5346  CA  ALA C 199    25988  18122  14486  -1683  -1122  -3073       C  
ATOM   5347  C   ALA C 199      68.478  43.903  34.760  1.00160.95           C  
ANISOU 5347  C   ALA C 199    26659  19530  14964  -1581  -1228  -3401       C  
ATOM   5348  O   ALA C 199      68.289  42.963  33.993  1.00166.28           O  
ANISOU 5348  O   ALA C 199    27576  20494  15109  -1372  -1226  -3820       O  
ATOM   5349  CB  ALA C 199      69.136  43.143  37.034  1.00151.84           C  
ANISOU 5349  CB  ALA C 199    26105  17273  14314  -2214  -1112  -3633       C  
ATOM   5350  N   TRP C 200      67.738  45.015  34.754  1.00164.37           N  
ANISOU 5350  N   TRP C 200    26638  20119  15694  -1684  -1356  -3260       N  
ATOM   5351  CA  TRP C 200      66.632  45.222  33.810  1.00170.78           C  
ANISOU 5351  CA  TRP C 200    27210  21514  16163  -1540  -1484  -3550       C  
ATOM   5352  C   TRP C 200      67.129  45.498  32.371  1.00175.76           C  
ANISOU 5352  C   TRP C 200    27566  22888  16323   -742  -1401  -3022       C  
ATOM   5353  O   TRP C 200      66.326  45.657  31.448  1.00181.39           O  
ANISOU 5353  O   TRP C 200    28067  24228  16624   -433  -1510  -3229       O  
ATOM   5354  CB  TRP C 200      65.654  46.307  34.352  1.00170.40           C  
ANISOU 5354  CB  TRP C 200    26785  21376  16581  -1907  -1639  -3575       C  
ATOM   5355  CG  TRP C 200      64.891  47.132  33.329  1.00177.78           C  
ANISOU 5355  CG  TRP C 200    27249  22967  17329  -1571  -1737  -3426       C  
ATOM   5356  CD1 TRP C 200      65.244  48.355  32.854  1.00179.73           C  
ANISOU 5356  CD1 TRP C 200    26972  23466  17851  -1180  -1677  -2609       C  
ATOM   5357  CD2 TRP C 200      63.606  46.828  32.735  1.00183.74           C  
ANISOU 5357  CD2 TRP C 200    27973  24169  17669  -1596  -1909  -4111       C  
ATOM   5358  NE1 TRP C 200      64.295  48.822  31.966  1.00184.31           N  
ANISOU 5358  NE1 TRP C 200    27236  24685  18107   -896  -1768  -2679       N  
ATOM   5359  CE2 TRP C 200      63.280  47.907  31.875  1.00186.91           C  
ANISOU 5359  CE2 TRP C 200    27861  25172  17984  -1138  -1944  -3643       C  
ATOM   5360  CE3 TRP C 200      62.717  45.740  32.826  1.00187.19           C  
ANISOU 5360  CE3 TRP C 200    28715  24532  17874  -1933  -2033  -5068       C  
ATOM   5361  CZ2 TRP C 200      62.097  47.933  31.106  1.00191.55           C  
ANISOU 5361  CZ2 TRP C 200    28267  26367  18143   -966  -2134  -4151       C  
ATOM   5362  CZ3 TRP C 200      61.538  45.764  32.053  1.00191.91           C  
ANISOU 5362  CZ3 TRP C 200    29085  25675  18157  -1809  -2250  -5622       C  
ATOM   5363  CH2 TRP C 200      61.244  46.856  31.209  1.00193.63           C  
ANISOU 5363  CH2 TRP C 200    28826  26563  18179  -1310  -2315  -5185       C  
ATOM   5364  N   PHE C 201      68.460  45.494  32.186  1.00174.78           N  
ANISOU 5364  N   PHE C 201    27448  22734  16224   -352  -1197  -2352       N  
ATOM   5365  CA  PHE C 201      69.072  45.621  30.846  1.00178.33           C  
ANISOU 5365  CA  PHE C 201    27670  23922  16166    508  -1032  -1756       C  
ATOM   5366  C   PHE C 201      69.909  44.404  30.439  1.00180.62           C  
ANISOU 5366  C   PHE C 201    28406  24335  15884    870   -935  -1933       C  
ATOM   5367  O   PHE C 201      70.265  44.265  29.275  1.00185.38           O  
ANISOU 5367  O   PHE C 201    28903  25665  15866   1657   -834  -1645       O  
ATOM   5368  CB  PHE C 201      69.936  46.891  30.735  1.00178.07           C  
ANISOU 5368  CB  PHE C 201    27061  23864  16731    824   -808   -583       C  
ATOM   5369  CG  PHE C 201      69.288  48.131  31.299  1.00177.34           C  
ANISOU 5369  CG  PHE C 201    26508  23478  17395    436   -921   -383       C  
ATOM   5370  CD1 PHE C 201      67.914  48.201  31.491  1.00177.05           C  
ANISOU 5370  CD1 PHE C 201    26509  23523  17238     51  -1167  -1089       C  
ATOM   5371  CD2 PHE C 201      70.057  49.246  31.612  1.00177.88           C  
ANISOU 5371  CD2 PHE C 201    26048  23169  18368    480   -796    497       C  
ATOM   5372  CE1 PHE C 201      67.325  49.347  32.010  1.00176.16           C  
ANISOU 5372  CE1 PHE C 201    25974  23157  17801   -269  -1284   -921       C  
ATOM   5373  CE2 PHE C 201      69.468  50.397  32.125  1.00177.00           C  
ANISOU 5373  CE2 PHE C 201    25480  22750  19020    155   -943    624       C  
ATOM   5374  CZ  PHE C 201      68.101  50.448  32.320  1.00175.41           C  
ANISOU 5374  CZ  PHE C 201    25375  22680  18592   -204  -1185    -80       C  
ATOM   5375  N   LYS C 202      70.239  43.541  31.397  1.00180.02           N  
ANISOU 5375  N   LYS C 202    28815  23586  15996    366   -949  -2371       N  
ATOM   5376  CA  LYS C 202      71.081  42.363  31.109  1.00184.75           C  
ANISOU 5376  CA  LYS C 202    29858  24207  16129    674   -856  -2545       C  
ATOM   5377  C   LYS C 202      70.570  41.077  31.787  1.00182.36           C  
ANISOU 5377  C   LYS C 202    30121  23377  15790    128   -978  -3534       C  
ATOM   5378  O   LYS C 202      71.038  40.711  32.871  1.00178.28           O  
ANISOU 5378  O   LYS C 202    29912  22179  15647   -305   -881  -3542       O  
ATOM   5379  CB  LYS C 202      72.559  42.627  31.480  1.00187.62           C  
ANISOU 5379  CB  LYS C 202    30181  24272  16832    839   -612  -1711       C  
ATOM   5380  CG  LYS C 202      73.269  43.621  30.558  1.00194.39           C  
ANISOU 5380  CG  LYS C 202    30466  25684  17709   1550   -394   -647       C  
ATOM   5381  CD  LYS C 202      74.787  43.439  30.555  1.00197.50           C  
ANISOU 5381  CD  LYS C 202    30884  25949  18207   1904   -139     32       C  
ATOM   5382  CE  LYS C 202      75.443  44.295  29.468  1.00202.79           C  
ANISOU 5382  CE  LYS C 202    30949  27254  18845   2724    161   1152       C  
ATOM   5383  NZ  LYS C 202      76.894  43.992  29.283  1.00202.75           N  
ANISOU 5383  NZ  LYS C 202    30954  27243  18838   3171    440   1805       N  
ATOM   5384  N   ASN C 203      69.634  40.378  31.139  1.00183.99           N  
ANISOU 5384  N   ASN C 203    30423  23894  15587    207  -1182  -4356       N  
ATOM   5385  CA  ASN C 203      69.124  40.750  29.815  1.00187.61           C  
ANISOU 5385  CA  ASN C 203    30527  25273  15482    869  -1332  -4413       C  
ATOM   5386  C   ASN C 203      67.744  41.395  29.951  1.00187.10           C  
ANISOU 5386  C   ASN C 203    30157  25273  15660    479  -1530  -4780       C  
ATOM   5387  O   ASN C 203      66.786  40.737  30.356  1.00185.88           O  
ANISOU 5387  O   ASN C 203    30171  24762  15692    -45  -1711  -5660       O  
ATOM   5388  CB  ASN C 203      69.032  39.489  28.921  1.00191.40           C  
ANISOU 5388  CB  ASN C 203    31276  26127  15317   1348  -1526  -5246       C  
ATOM   5389  CG  ASN C 203      69.354  39.768  27.455  1.00195.24           C  
ANISOU 5389  CG  ASN C 203    31482  27725  14974   2459  -1555  -4934       C  
ATOM   5390  OD1 ASN C 203      68.525  40.282  26.713  1.00198.41           O  
ANISOU 5390  OD1 ASN C 203    31530  28806  15051   2829  -1733  -5104       O  
ATOM   5391  ND2 ASN C 203      70.541  39.366  27.025  1.00195.93           N  
ANISOU 5391  ND2 ASN C 203    31733  28049  14662   3061  -1376  -4506       N  
ATOM   5392  N   GLY C 204      67.667  42.697  29.666  1.00187.90           N  
ANISOU 5392  N   GLY C 204    29775  25765  15853    717  -1464  -4051       N  
ATOM   5393  CA  GLY C 204      66.393  43.433  29.605  1.00191.25           C  
ANISOU 5393  CA  GLY C 204    29850  26406  16410    502  -1651  -4309       C  
ATOM   5394  C   GLY C 204      65.301  42.993  30.570  1.00191.24           C  
ANISOU 5394  C   GLY C 204    30034  25779  16849   -372  -1826  -5166       C  
ATOM   5395  O   GLY C 204      64.133  42.913  30.188  1.00193.37           O  
ANISOU 5395  O   GLY C 204    30149  26341  16980   -430  -2069  -5845       O  
ATOM   5396  N   GLU C 205      65.671  42.717  31.824  1.00190.01           N  
ANISOU 5396  N   GLU C 205    30175  24794  17223   -998  -1688  -5114       N  
ATOM   5397  CA  GLU C 205      64.697  42.206  32.812  1.00191.33           C  
ANISOU 5397  CA  GLU C 205    30528  24356  17812  -1769  -1754  -5815       C  
ATOM   5398  C   GLU C 205      65.041  42.382  34.305  1.00187.83           C  
ANISOU 5398  C   GLU C 205    30270  23155  17940  -2332  -1574  -5513       C  
ATOM   5399  O   GLU C 205      66.206  42.363  34.703  1.00191.03           O  
ANISOU 5399  O   GLU C 205    30853  23309  18419  -2205  -1412  -5004       O  
ATOM   5400  CB  GLU C 205      64.339  40.738  32.533  1.00194.87           C  
ANISOU 5400  CB  GLU C 205    31300  24646  18095  -1843  -1842  -6722       C  
ATOM   5401  CG  GLU C 205      62.913  40.536  32.046  1.00198.44           C  
ANISOU 5401  CG  GLU C 205    31507  25344  18544  -1978  -2126  -7589       C  
ATOM   5402  CD  GLU C 205      61.861  41.075  33.018  1.00196.97           C  
ANISOU 5402  CD  GLU C 205    31145  24777  18915  -2673  -2110  -7687       C  
ATOM   5403  OE1 GLU C 205      62.220  41.792  33.978  1.00189.25           O  
ANISOU 5403  OE1 GLU C 205    30185  23476  18244  -2943  -1925  -7058       O  
ATOM   5404  OE2 GLU C 205      60.666  40.786  32.812  1.00201.32           O  
ANISOU 5404  OE2 GLU C 205    31505  25375  19612  -2906  -2308  -8436       O  
ATOM   5405  N   THR C 206      63.987  42.522  35.116  1.00140.00           N  
ANISOU 5405  N   THR C 206    18591  20815  13787   1453  -3027  -4177       N  
ATOM   5406  CA  THR C 206      64.096  42.624  36.585  1.00130.25           C  
ANISOU 5406  CA  THR C 206    17249  19082  13157   1396  -2860  -3867       C  
ATOM   5407  C   THR C 206      62.742  42.335  37.266  1.00130.28           C  
ANISOU 5407  C   THR C 206    17200  18689  13610    916  -3104  -3884       C  
ATOM   5408  O   THR C 206      61.718  42.138  36.583  1.00143.45           O  
ANISOU 5408  O   THR C 206    18834  20528  15142    632  -3419  -4134       O  
ATOM   5409  CB  THR C 206      64.623  44.001  37.041  1.00119.00           C  
ANISOU 5409  CB  THR C 206    15467  17956  11788   1486  -2632  -3258       C  
ATOM   5410  OG1 THR C 206      64.448  44.122  38.443  1.00115.16           O  
ANISOU 5410  OG1 THR C 206    14865  17014  11877   1364  -2543  -2993       O  
ATOM   5411  CG2 THR C 206      63.877  45.121  36.372  1.00117.17           C  
ANISOU 5411  CG2 THR C 206    15026  18169  11324   1326  -2852  -2945       C  
ATOM   5412  N   SER C 207      62.740  42.269  38.593  1.00123.06           N  
ANISOU 5412  N   SER C 207    16259  17310  13186    793  -2957  -3663       N  
ATOM   5413  CA  SER C 207      61.497  42.049  39.317  1.00125.85           C  
ANISOU 5413  CA  SER C 207    16496  17397  13922    261  -3104  -3675       C  
ATOM   5414  C   SER C 207      61.077  43.274  40.102  1.00119.24           C  
ANISOU 5414  C   SER C 207    15147  16781  13376    182  -3034  -3197       C  
ATOM   5415  O   SER C 207      61.816  43.775  40.940  1.00111.71           O  
ANISOU 5415  O   SER C 207    14139  15697  12608    386  -2780  -2848       O  
ATOM   5416  CB  SER C 207      61.570  40.799  40.215  1.00129.78           C  
ANISOU 5416  CB  SER C 207    17490  17125  14692     34  -3037  -3881       C  
ATOM   5417  OG  SER C 207      62.091  41.097  41.496  1.00128.97           O  
ANISOU 5417  OG  SER C 207    17362  16729  14912    126  -2787  -3499       O  
ATOM   5418  N   LEU C 208      59.872  43.752  39.827  1.00124.35           N  
ANISOU 5418  N   LEU C 208    15405  17788  14054    -79  -3293  -3235       N  
ATOM   5419  CA  LEU C 208      59.383  44.966  40.458  1.00122.20           C  
ANISOU 5419  CA  LEU C 208    14640  17763  14027    -51  -3298  -2867       C  
ATOM   5420  C   LEU C 208      59.196  44.872  41.975  1.00121.40           C  
ANISOU 5420  C   LEU C 208    14423  17310  14392   -318  -3056  -2725       C  
ATOM   5421  O   LEU C 208      59.531  45.814  42.679  1.00122.59           O  
ANISOU 5421  O   LEU C 208    14375  17485  14717   -110  -2902  -2351       O  
ATOM   5422  CB  LEU C 208      58.115  45.473  39.795  1.00124.04           C  
ANISOU 5422  CB  LEU C 208    14445  18514  14168   -152  -3699  -3021       C  
ATOM   5423  CG  LEU C 208      58.116  46.990  39.668  1.00123.49           C  
ANISOU 5423  CG  LEU C 208    14102  18774  14042    254  -3826  -2605       C  
ATOM   5424  CD1 LEU C 208      58.951  47.421  38.461  1.00124.68           C  
ANISOU 5424  CD1 LEU C 208    14588  19125  13659    608  -3898  -2426       C  
ATOM   5425  CD2 LEU C 208      56.699  47.532  39.575  1.00126.71           C  
ANISOU 5425  CD2 LEU C 208    13967  19620  14555    209  -4227  -2769       C  
ATOM   5426  N   PRO C 209      58.683  43.725  42.490  1.00121.23           N  
ANISOU 5426  N   PRO C 209    14594  16936  14531   -828  -3017  -3020       N  
ATOM   5427  CA  PRO C 209      58.492  43.694  43.938  1.00118.27           C  
ANISOU 5427  CA  PRO C 209    14141  16281  14512  -1131  -2769  -2845       C  
ATOM   5428  C   PRO C 209      59.793  43.945  44.717  1.00116.99           C  
ANISOU 5428  C   PRO C 209    14256  15759  14434   -737  -2485  -2467       C  
ATOM   5429  O   PRO C 209      59.765  44.581  45.775  1.00120.19           O  
ANISOU 5429  O   PRO C 209    14424  16162  15079   -759  -2308  -2193       O  
ATOM   5430  CB  PRO C 209      57.973  42.277  44.200  1.00121.92           C  
ANISOU 5430  CB  PRO C 209    15007  16311  15006  -1781  -2770  -3192       C  
ATOM   5431  CG  PRO C 209      57.390  41.835  42.907  1.00128.68           C  
ANISOU 5431  CG  PRO C 209    15851  17433  15605  -1918  -3090  -3616       C  
ATOM   5432  CD  PRO C 209      58.231  42.474  41.847  1.00127.39           C  
ANISOU 5432  CD  PRO C 209    15710  17541  15152  -1213  -3194  -3502       C  
ATOM   5433  N   LEU C 210      60.922  43.480  44.188  1.00115.50           N  
ANISOU 5433  N   LEU C 210    14511  15345  14029   -353  -2453  -2503       N  
ATOM   5434  CA  LEU C 210      62.183  43.587  44.923  1.00111.99           C  
ANISOU 5434  CA  LEU C 210    14279  14623  13647     24  -2218  -2234       C  
ATOM   5435  C   LEU C 210      62.968  44.873  44.631  1.00110.12           C  
ANISOU 5435  C   LEU C 210    13712  14819  13307    468  -2125  -1917       C  
ATOM   5436  O   LEU C 210      63.609  45.425  45.530  1.00109.56           O  
ANISOU 5436  O   LEU C 210    13554  14676  13395    619  -1934  -1619       O  
ATOM   5437  CB  LEU C 210      63.051  42.339  44.731  1.00112.79           C  
ANISOU 5437  CB  LEU C 210    15014  14242  13597    248  -2228  -2494       C  
ATOM   5438  CG  LEU C 210      62.455  41.017  45.237  1.00117.27           C  
ANISOU 5438  CG  LEU C 210    16136  14155  14263   -226  -2317  -2733       C  
ATOM   5439  CD1 LEU C 210      63.500  39.914  45.245  1.00118.88           C  
ANISOU 5439  CD1 LEU C 210    17058  13764  14344    183  -2368  -2936       C  
ATOM   5440  CD2 LEU C 210      61.836  41.177  46.619  1.00116.87           C  
ANISOU 5440  CD2 LEU C 210    15996  13906  14501   -712  -2169  -2463       C  
ATOM   5441  N   LEU C 211      62.908  45.354  43.388  1.00108.83           N  
ANISOU 5441  N   LEU C 211    13411  15096  12841    619  -2269  -1972       N  
ATOM   5442  CA  LEU C 211      63.420  46.681  43.075  1.00105.14           C  
ANISOU 5442  CA  LEU C 211    12695  15019  12234    873  -2214  -1622       C  
ATOM   5443  C   LEU C 211      62.660  47.719  43.880  1.00108.68           C  
ANISOU 5443  C   LEU C 211    12792  15510  12989    744  -2254  -1342       C  
ATOM   5444  O   LEU C 211      63.260  48.638  44.436  1.00113.31           O  
ANISOU 5444  O   LEU C 211    13280  16108  13665    887  -2107  -1009       O  
ATOM   5445  CB  LEU C 211      63.310  46.983  41.579  1.00104.99           C  
ANISOU 5445  CB  LEU C 211    12689  15438  11764    975  -2409  -1708       C  
ATOM   5446  CG  LEU C 211      63.638  48.417  41.124  1.00103.84           C  
ANISOU 5446  CG  LEU C 211    12414  15648  11390   1122  -2422  -1299       C  
ATOM   5447  CD1 LEU C 211      64.938  48.944  41.738  1.00102.44           C  
ANISOU 5447  CD1 LEU C 211    12233  15445  11241   1252  -2084  -1006       C  
ATOM   5448  CD2 LEU C 211      63.694  48.484  39.611  1.00105.32           C  
ANISOU 5448  CD2 LEU C 211    12758  16246  11013   1196  -2585  -1397       C  
ATOM   5449  N   LEU C 212      61.336  47.567  43.959  1.00112.45           N  
ANISOU 5449  N   LEU C 212    13053  16047  13623    471  -2457  -1531       N  
ATOM   5450  CA  LEU C 212      60.538  48.461  44.790  1.00111.69           C  
ANISOU 5450  CA  LEU C 212    12560  16048  13826    403  -2495  -1381       C  
ATOM   5451  C   LEU C 212      60.879  48.290  46.253  1.00110.79           C  
ANISOU 5451  C   LEU C 212    12474  15599  14021    268  -2193  -1253       C  
ATOM   5452  O   LEU C 212      60.975  49.270  46.992  1.00109.56           O  
ANISOU 5452  O   LEU C 212    12121  15466  14038    395  -2112  -1003       O  
ATOM   5453  CB  LEU C 212      59.038  48.271  44.563  1.00111.17           C  
ANISOU 5453  CB  LEU C 212    12136  16266  13837    138  -2765  -1711       C  
ATOM   5454  CG  LEU C 212      58.324  49.439  43.867  1.00114.70           C  
ANISOU 5454  CG  LEU C 212    12252  17143  14184    438  -3133  -1658       C  
ATOM   5455  CD1 LEU C 212      56.835  49.346  44.107  1.00128.87           C  
ANISOU 5455  CD1 LEU C 212    13500  19293  16169    207  -3345  -2026       C  
ATOM   5456  CD2 LEU C 212      58.833  50.794  44.331  1.00108.89           C  
ANISOU 5456  CD2 LEU C 212    11504  16333  13534    799  -3087  -1239       C  
HETATM 5457  N   MSE C 213      61.093  47.043  46.665  1.00111.23           N  
ANISOU 5457  N   MSE C 213    12852  15299  14109     27  -2058  -1421       N  
HETATM 5458  CA  MSE C 213      61.489  46.762  48.029  1.00110.04           C  
ANISOU 5458  CA  MSE C 213    12853  14789  14167    -92  -1808  -1277       C  
HETATM 5459  C   MSE C 213      62.718  47.559  48.426  1.00106.53           C  
ANISOU 5459  C   MSE C 213    12429  14320  13726    306  -1655   -948       C  
HETATM 5460  O   MSE C 213      62.732  48.179  49.488  1.00108.13           O  
ANISOU 5460  O   MSE C 213    12472  14486  14125    280  -1522   -753       O  
HETATM 5461  CB  MSE C 213      61.749  45.291  48.222  1.00112.06           C  
ANISOU 5461  CB  MSE C 213    13650  14561  14366   -301  -1766  -1466       C  
HETATM 5462  CG  MSE C 213      62.199  45.088  49.648  1.00115.16           C  
ANISOU 5462  CG  MSE C 213    14264  14578  14912   -376  -1556  -1257       C  
HETATM 5463 SE   MSE C 213      62.708  43.228  49.881  1.00131.38          SE  
ANISOU 5463 SE   MSE C 213    17238  15840  16839   -498  -1604  -1441      SE  
HETATM 5464  CE  MSE C 213      64.397  43.299  48.881  1.00129.36           C  
ANISOU 5464  CE  MSE C 213    17104  15684  16360    379  -1671  -1493       C  
ATOM   5465  N   TYR C 214      63.752  47.561  47.580  1.00102.36           N  
ANISOU 5465  N   TYR C 214    12064  13873  12953    638  -1659   -925       N  
ATOM   5466  CA  TYR C 214      64.981  48.298  47.897  1.00 96.87           C  
ANISOU 5466  CA  TYR C 214    11328  13253  12222    930  -1496   -659       C  
ATOM   5467  C   TYR C 214      64.838  49.803  47.940  1.00 98.55           C  
ANISOU 5467  C   TYR C 214    11248  13709  12487    964  -1515   -371       C  
ATOM   5468  O   TYR C 214      65.633  50.470  48.594  1.00104.33           O  
ANISOU 5468  O   TYR C 214    11928  14430  13283   1056  -1368   -147       O  
ATOM   5469  CB  TYR C 214      66.151  47.880  47.008  1.00 97.78           C  
ANISOU 5469  CB  TYR C 214    11614  13514  12022   1229  -1447   -775       C  
ATOM   5470  CG  TYR C 214      66.873  46.733  47.589  1.00 99.97           C  
ANISOU 5470  CG  TYR C 214    12198  13452  12331   1404  -1382   -951       C  
ATOM   5471  CD1 TYR C 214      67.874  46.928  48.523  1.00 99.69           C  
ANISOU 5471  CD1 TYR C 214    12127  13366  12381   1612  -1241   -803       C  
ATOM   5472  CD2 TYR C 214      66.475  45.435  47.311  1.00106.61           C  
ANISOU 5472  CD2 TYR C 214    13420  13957  13126   1352  -1513  -1271       C  
ATOM   5473  CE1 TYR C 214      68.498  45.859  49.133  1.00104.80           C  
ANISOU 5473  CE1 TYR C 214    13115  13655  13049   1859  -1266   -961       C  
ATOM   5474  CE2 TYR C 214      67.097  44.352  47.905  1.00110.77           C  
ANISOU 5474  CE2 TYR C 214    14374  14036  13677   1564  -1529  -1420       C  
ATOM   5475  CZ  TYR C 214      68.104  44.568  48.823  1.00110.27           C  
ANISOU 5475  CZ  TYR C 214    14272  13937  13685   1858  -1423  -1257       C  
ATOM   5476  OH  TYR C 214      68.726  43.498  49.427  1.00116.04           O  
ANISOU 5476  OH  TYR C 214    15477  14199  14412   2165  -1519  -1402       O  
ATOM   5477  N   VAL C 215      63.822  50.350  47.273  1.00 95.92           N  
ANISOU 5477  N   VAL C 215    10753  13571  12119    908  -1737   -395       N  
ATOM   5478  CA  VAL C 215      63.515  51.764  47.457  1.00 96.27           C  
ANISOU 5478  CA  VAL C 215    10611  13713  12251    994  -1834   -147       C  
ATOM   5479  C   VAL C 215      62.928  51.994  48.846  1.00100.20           C  
ANISOU 5479  C   VAL C 215    10896  14064  13112    891  -1751   -156       C  
ATOM   5480  O   VAL C 215      63.343  52.906  49.547  1.00101.37           O  
ANISOU 5480  O   VAL C 215    11009  14132  13374    977  -1669     58       O  
ATOM   5481  CB  VAL C 215      62.606  52.332  46.352  1.00102.01           C  
ANISOU 5481  CB  VAL C 215    11266  14682  12808   1086  -2181   -179       C  
ATOM   5482  CG1 VAL C 215      62.247  53.794  46.630  1.00 98.76           C  
ANISOU 5482  CG1 VAL C 215    10767  14252  12505   1266  -2356     57       C  
ATOM   5483  CG2 VAL C 215      63.303  52.220  45.018  1.00109.87           C  
ANISOU 5483  CG2 VAL C 215    12522  15862  13360   1156  -2223   -125       C  
HETATM 5484  N   MSE C 216      62.017  51.118  49.270  1.00105.36           N  
ANISOU 5484  N   MSE C 216    11431  14694  13907    644  -1741   -423       N  
HETATM 5485  CA  MSE C 216      61.416  51.232  50.609  1.00105.20           C  
ANISOU 5485  CA  MSE C 216    11190  14623  14155    462  -1604   -472       C  
HETATM 5486  C   MSE C 216      62.464  50.990  51.667  1.00 99.37           C  
ANISOU 5486  C   MSE C 216    10692  13595  13468    442  -1339   -290       C  
HETATM 5487  O   MSE C 216      62.440  51.613  52.724  1.00 98.13           O  
ANISOU 5487  O   MSE C 216    10405  13412  13466    440  -1224   -199       O  
HETATM 5488  CB  MSE C 216      60.245  50.279  50.757  1.00108.57           C  
ANISOU 5488  CB  MSE C 216    11455  15154  14642     59  -1611   -803       C  
HETATM 5489  CG  MSE C 216      59.308  50.426  49.563  1.00117.74           C  
ANISOU 5489  CG  MSE C 216    12356  16670  15709    116  -1932  -1031       C  
HETATM 5490 SE   MSE C 216      57.868  49.075  49.659  1.00140.59          SE  
ANISOU 5490 SE   MSE C 216    15008  19771  18636   -567  -1928  -1525      SE  
HETATM 5491  CE  MSE C 216      56.704  49.815  48.256  1.00145.62           C  
ANISOU 5491  CE  MSE C 216    15117  21033  19178   -271  -2439  -1810       C  
ATOM   5492  N   TYR C 217      63.405  50.097  51.376  1.00 93.92           N  
ANISOU 5492  N   TYR C 217    10349  12710  12624    486  -1274   -276       N  
ATOM   5493  CA  TYR C 217      64.568  49.890  52.234  1.00 89.56           C  
ANISOU 5493  CA  TYR C 217    10016  11937  12073    600  -1103   -122       C  
ATOM   5494  C   TYR C 217      65.353  51.173  52.474  1.00 89.80           C  
ANISOU 5494  C   TYR C 217     9890  12101  12128    809  -1054    117       C  
ATOM   5495  O   TYR C 217      65.767  51.437  53.596  1.00 98.53           O  
ANISOU 5495  O   TYR C 217    10994  13104  13336    805   -933    226       O  
ATOM   5496  CB  TYR C 217      65.501  48.837  51.639  1.00 88.76           C  
ANISOU 5496  CB  TYR C 217    10254  11694  11774    778  -1117   -222       C  
ATOM   5497  CG  TYR C 217      65.166  47.437  52.040  1.00 91.88           C  
ANISOU 5497  CG  TYR C 217    11039  11703  12166    577  -1131   -392       C  
ATOM   5498  CD1 TYR C 217      63.904  47.125  52.557  1.00 94.23           C  
ANISOU 5498  CD1 TYR C 217    11312  11912  12577    109  -1112   -475       C  
ATOM   5499  CD2 TYR C 217      66.097  46.395  51.876  1.00 92.72           C  
ANISOU 5499  CD2 TYR C 217    11568  11534  12125    842  -1177   -503       C  
ATOM   5500  CE1 TYR C 217      63.579  45.826  52.916  1.00100.07           C  
ANISOU 5500  CE1 TYR C 217    12519  12238  13265   -213  -1119   -599       C  
ATOM   5501  CE2 TYR C 217      65.780  45.085  52.229  1.00 99.89           C  
ANISOU 5501  CE2 TYR C 217    13005  11944  13005    649  -1248   -640       C  
ATOM   5502  CZ  TYR C 217      64.517  44.807  52.753  1.00104.68           C  
ANISOU 5502  CZ  TYR C 217    13661  12405  13705     58  -1209   -656       C  
ATOM   5503  OH  TYR C 217      64.186  43.520  53.115  1.00112.88           O  
ANISOU 5503  OH  TYR C 217    15318  12899  14671   -272  -1268   -755       O  
ATOM   5504  N   LEU C 218      65.580  51.944  51.408  1.00 83.53           N  
ANISOU 5504  N   LEU C 218     9023  11518  11194    942  -1156    203       N  
ATOM   5505  CA  LEU C 218      66.386  53.156  51.474  1.00 83.59           C  
ANISOU 5505  CA  LEU C 218     8982  11614  11164   1030  -1117    446       C  
ATOM   5506  C   LEU C 218      65.743  54.186  52.398  1.00 84.99           C  
ANISOU 5506  C   LEU C 218     9019  11691  11579    996  -1153    526       C  
ATOM   5507  O   LEU C 218      66.414  54.769  53.271  1.00 88.25           O  
ANISOU 5507  O   LEU C 218     9430  12032  12068    990  -1044    651       O  
ATOM   5508  CB  LEU C 218      66.571  53.751  50.067  1.00 84.81           C  
ANISOU 5508  CB  LEU C 218     9198  11979  11046   1075  -1237    550       C  
ATOM   5509  CG  LEU C 218      67.701  54.747  49.684  1.00 87.56           C  
ANISOU 5509  CG  LEU C 218     9615  12476  11177   1028  -1156    804       C  
ATOM   5510  CD1 LEU C 218      67.132  55.822  48.765  1.00 82.76           C  
ANISOU 5510  CD1 LEU C 218     9162  11871  10411   1004  -1390    999       C  
ATOM   5511  CD2 LEU C 218      68.472  55.386  50.856  1.00 80.75           C  
ANISOU 5511  CD2 LEU C 218     8685  11523  10471    956  -1008    933       C  
ATOM   5512  N   CYS C 219      64.449  54.412  52.216  1.00 84.92           N  
ANISOU 5512  N   CYS C 219     8863  11724  11677   1003  -1322    401       N  
ATOM   5513  CA  CYS C 219      63.722  55.299  53.099  1.00 85.26           C  
ANISOU 5513  CA  CYS C 219     8722  11730  11942   1055  -1368    363       C  
ATOM   5514  C   CYS C 219      63.909  54.863  54.548  1.00 88.90           C  
ANISOU 5514  C   CYS C 219     9140  12100  12535    901  -1119    310       C  
ATOM   5515  O   CYS C 219      64.449  55.619  55.375  1.00 94.63           O  
ANISOU 5515  O   CYS C 219     9894  12728  13330    945  -1046    420       O  
ATOM   5516  CB  CYS C 219      62.250  55.308  52.744  1.00 89.92           C  
ANISOU 5516  CB  CYS C 219     9038  12510  12616   1111  -1576    110       C  
ATOM   5517  SG  CYS C 219      61.922  55.862  51.066  1.00101.06           S  
ANISOU 5517  SG  CYS C 219    10551  14030  13815   1353  -1962    178       S  
ATOM   5518  N   ASN C 220      63.499  53.628  54.838  1.00 85.23           N  
ANISOU 5518  N   ASN C 220     8679  11642  12063    681  -1005    152       N  
ATOM   5519  CA  ASN C 220      63.563  53.072  56.181  1.00 79.81           C  
ANISOU 5519  CA  ASN C 220     8057  10849  11417    475   -789    127       C  
ATOM   5520  C   ASN C 220      64.964  53.132  56.786  1.00 83.64           C  
ANISOU 5520  C   ASN C 220     8773  11167  11836    587   -696    333       C  
ATOM   5521  O   ASN C 220      65.116  53.350  57.985  1.00 86.76           O  
ANISOU 5521  O   ASN C 220     9179  11516  12268    526   -578    364       O  
ATOM   5522  CB  ASN C 220      63.031  51.640  56.169  1.00 79.38           C  
ANISOU 5522  CB  ASN C 220     8151  10722  11286    154   -722    -17       C  
ATOM   5523  CG  ASN C 220      63.416  50.852  57.413  1.00 86.91           C  
ANISOU 5523  CG  ASN C 220     9415  11438  12167    -63   -536     58       C  
ATOM   5524  OD1 ASN C 220      62.775  50.983  58.477  1.00 85.67           O  
ANISOU 5524  OD1 ASN C 220     9139  11376  12035   -320   -377     -2       O  
ATOM   5525  ND2 ASN C 220      64.466  49.994  57.285  1.00 88.03           N  
ANISOU 5525  ND2 ASN C 220     9981  11288  12175     66   -573    168       N  
ATOM   5526  N   SER C 221      65.987  52.940  55.959  1.00 91.44           N  
ANISOU 5526  N   SER C 221     9904  12142  12695    753   -751    431       N  
ATOM   5527  CA  SER C 221      67.353  52.988  56.459  1.00 91.13           C  
ANISOU 5527  CA  SER C 221     9967  12078  12578    882   -686    554       C  
ATOM   5528  C   SER C 221      67.749  54.402  56.913  1.00 88.17           C  
ANISOU 5528  C   SER C 221     9446  11775  12279    898   -678    676       C  
ATOM   5529  O   SER C 221      68.633  54.549  57.754  1.00 93.47           O  
ANISOU 5529  O   SER C 221    10135  12451  12925    924   -617    731       O  
ATOM   5530  CB  SER C 221      68.356  52.403  55.445  1.00 91.00           C  
ANISOU 5530  CB  SER C 221    10040  12162  12374   1066   -720    537       C  
ATOM   5531  OG  SER C 221      68.657  53.326  54.414  1.00 97.10           O  
ANISOU 5531  OG  SER C 221    10678  13156  13059   1083   -755    623       O  
ATOM   5532  N   VAL C 222      67.063  55.437  56.401  1.00 78.89           N  
ANISOU 5532  N   VAL C 222     8168  10621  11184    897   -781    698       N  
ATOM   5533  CA  VAL C 222      67.225  56.768  56.989  1.00 71.15           C  
ANISOU 5533  CA  VAL C 222     7162   9574  10297    900   -812    774       C  
ATOM   5534  C   VAL C 222      66.473  56.851  58.295  1.00 73.02           C  
ANISOU 5534  C   VAL C 222     7301   9761  10680    873   -739    624       C  
ATOM   5535  O   VAL C 222      67.001  57.360  59.280  1.00 73.54           O  
ANISOU 5535  O   VAL C 222     7392   9779  10767    844   -679    643       O  
ATOM   5536  CB  VAL C 222      66.811  57.923  56.061  1.00 71.57           C  
ANISOU 5536  CB  VAL C 222     7276   9560  10356    973  -1015    861       C  
ATOM   5537  CG1 VAL C 222      66.484  59.157  56.886  1.00 68.72           C  
ANISOU 5537  CG1 VAL C 222     6944   9012  10154   1038  -1099    828       C  
ATOM   5538  CG2 VAL C 222      67.931  58.254  55.102  1.00 68.82           C  
ANISOU 5538  CG2 VAL C 222     7082   9280   9784    866  -1018   1076       C  
ATOM   5539  N   TYR C 223      65.260  56.304  58.333  1.00 74.73           N  
ANISOU 5539  N   TYR C 223     7381  10051  10959    834   -725    442       N  
ATOM   5540  CA  TYR C 223      64.547  56.179  59.619  1.00 78.67           C  
ANISOU 5540  CA  TYR C 223     7753  10620  11515    713   -574    265       C  
ATOM   5541  C   TYR C 223      65.377  55.448  60.680  1.00 80.43           C  
ANISOU 5541  C   TYR C 223     8188  10764  11606    566   -408    362       C  
ATOM   5542  O   TYR C 223      65.489  55.915  61.812  1.00 84.71           O  
ANISOU 5542  O   TYR C 223     8723  11323  12139    536   -322    323       O  
ATOM   5543  CB  TYR C 223      63.222  55.465  59.462  1.00 79.12           C  
ANISOU 5543  CB  TYR C 223     7598  10870  11593    551   -528     38       C  
ATOM   5544  CG  TYR C 223      62.388  55.568  60.695  1.00 84.05           C  
ANISOU 5544  CG  TYR C 223     8003  11695  12233    389   -340   -190       C  
ATOM   5545  CD1 TYR C 223      61.933  56.818  61.133  1.00 88.29           C  
ANISOU 5545  CD1 TYR C 223     8298  12349  12898    640   -401   -380       C  
ATOM   5546  CD2 TYR C 223      62.083  54.433  61.469  1.00 89.97           C  
ANISOU 5546  CD2 TYR C 223     8848  12507  12827    -27   -100   -227       C  
ATOM   5547  CE1 TYR C 223      61.177  56.951  62.274  1.00 93.55           C  
ANISOU 5547  CE1 TYR C 223     8709  13295  13540    520   -199   -660       C  
ATOM   5548  CE2 TYR C 223      61.310  54.552  62.630  1.00 97.36           C  
ANISOU 5548  CE2 TYR C 223     9569  13723  13700   -256    128   -448       C  
ATOM   5549  CZ  TYR C 223      60.859  55.826  63.018  1.00101.61           C  
ANISOU 5549  CZ  TYR C 223     9755  14481  14371     41     93   -693       C  
ATOM   5550  OH  TYR C 223      60.105  56.000  64.140  1.00102.77           O  
ANISOU 5550  OH  TYR C 223     9628  14992  14425   -137    338   -984       O  
ATOM   5551  N   GLY C 224      65.927  54.286  60.305  1.00 80.82           N  
ANISOU 5551  N   GLY C 224     8461  10719  11528    519   -402    461       N  
ATOM   5552  CA  GLY C 224      66.795  53.488  61.186  1.00 77.60           C  
ANISOU 5552  CA  GLY C 224     8340  10183  10959    496   -346    563       C  
ATOM   5553  C   GLY C 224      67.884  54.312  61.848  1.00 75.04           C  
ANISOU 5553  C   GLY C 224     7987   9908  10617    640   -375    644       C  
ATOM   5554  O   GLY C 224      67.985  54.368  63.077  1.00 73.19           O  
ANISOU 5554  O   GLY C 224     7838   9669  10301    568   -310    642       O  
ATOM   5555  N   TYR C 225      68.672  54.991  61.039  1.00 72.65           N  
ANISOU 5555  N   TYR C 225     7565   9686  10353    780   -467    704       N  
ATOM   5556  CA  TYR C 225      69.684  55.875  61.565  1.00 75.93           C  
ANISOU 5556  CA  TYR C 225     7909  10188  10751    810   -495    748       C  
ATOM   5557  C   TYR C 225      69.102  56.855  62.592  1.00 76.10           C  
ANISOU 5557  C   TYR C 225     7886  10164  10864    714   -455    663       C  
ATOM   5558  O   TYR C 225      69.574  56.912  63.740  1.00 76.84           O  
ANISOU 5558  O   TYR C 225     8036  10293  10867    687   -432    640       O  
ATOM   5559  CB  TYR C 225      70.374  56.610  60.446  1.00 75.75           C  
ANISOU 5559  CB  TYR C 225     7771  10277  10731    812   -555    823       C  
ATOM   5560  CG  TYR C 225      71.774  57.024  60.759  1.00 79.78           C  
ANISOU 5560  CG  TYR C 225     8179  10991  11140    779   -569    846       C  
ATOM   5561  CD1 TYR C 225      72.086  57.585  61.967  1.00 82.58           C  
ANISOU 5561  CD1 TYR C 225     8527  11343  11506    708   -580    802       C  
ATOM   5562  CD2 TYR C 225      72.780  56.914  59.812  1.00 89.13           C  
ANISOU 5562  CD2 TYR C 225     9223  12450  12192    784   -562    868       C  
ATOM   5563  CE1 TYR C 225      73.368  58.018  62.250  1.00 92.74           C  
ANISOU 5563  CE1 TYR C 225     9659  12881  12694    624   -613    780       C  
ATOM   5564  CE2 TYR C 225      74.071  57.363  60.076  1.00 95.50           C  
ANISOU 5564  CE2 TYR C 225     9823  13573  12890    682   -556    833       C  
ATOM   5565  CZ  TYR C 225      74.356  57.912  61.304  1.00 95.88           C  
ANISOU 5565  CZ  TYR C 225     9856  13599  12973    593   -598    789       C  
ATOM   5566  OH  TYR C 225      75.634  58.349  61.609  1.00107.78           O  
ANISOU 5566  OH  TYR C 225    11106  15479  14366    449   -615    709       O  
ATOM   5567  N   ILE C 226      68.046  57.574  62.213  1.00 75.51           N  
ANISOU 5567  N   ILE C 226     7715  10033  10941    714   -475    575       N  
ATOM   5568  CA  ILE C 226      67.355  58.478  63.171  1.00 75.80           C  
ANISOU 5568  CA  ILE C 226     7687  10050  11063    717   -447    395       C  
ATOM   5569  C   ILE C 226      66.904  57.783  64.481  1.00 76.90           C  
ANISOU 5569  C   ILE C 226     7839  10308  11070    590   -264    278       C  
ATOM   5570  O   ILE C 226      67.272  58.227  65.574  1.00 80.97           O  
ANISOU 5570  O   ILE C 226     8407  10852  11505    561   -229    213       O  
ATOM   5571  CB  ILE C 226      66.169  59.204  62.540  1.00 73.97           C  
ANISOU 5571  CB  ILE C 226     7320   9781  11004    863   -548    244       C  
ATOM   5572  CG1 ILE C 226      66.651  60.352  61.688  1.00 76.62           C  
ANISOU 5572  CG1 ILE C 226     7802   9897  11412    961   -764    370       C  
ATOM   5573  CG2 ILE C 226      65.283  59.774  63.610  1.00 79.30           C  
ANISOU 5573  CG2 ILE C 226     7851  10544  11734    932   -479    -53       C  
ATOM   5574  CD1 ILE C 226      65.906  60.469  60.381  1.00 81.87           C  
ANISOU 5574  CD1 ILE C 226     8448  10520  12135   1116   -938    397       C  
ATOM   5575  N   ASN C 227      66.144  56.688  64.359  1.00 72.90           N  
ANISOU 5575  N   ASN C 227     7331   9868  10497    455   -151    257       N  
ATOM   5576  CA  ASN C 227      65.565  56.002  65.520  1.00 75.47           C  
ANISOU 5576  CA  ASN C 227     7730  10313  10630    203     56    173       C  
ATOM   5577  C   ASN C 227      66.575  55.335  66.389  1.00 78.77           C  
ANISOU 5577  C   ASN C 227     8500  10629  10798    149     53    360       C  
ATOM   5578  O   ASN C 227      66.473  55.391  67.620  1.00 85.95           O  
ANISOU 5578  O   ASN C 227     9507  11638  11511     10    171    304       O  
ATOM   5579  CB  ASN C 227      64.561  54.955  65.090  1.00 81.21           C  
ANISOU 5579  CB  ASN C 227     8435  11106  11315    -51    170    126       C  
ATOM   5580  CG  ASN C 227      63.666  54.509  66.236  1.00 91.20           C  
ANISOU 5580  CG  ASN C 227     9694  12594  12361   -440    444    -18       C  
ATOM   5581  OD1 ASN C 227      62.857  55.301  66.758  1.00 97.24           O  
ANISOU 5581  OD1 ASN C 227    10103  13676  13165   -446    574   -311       O  
ATOM   5582  ND2 ASN C 227      63.795  53.239  66.636  1.00 87.96           N  
ANISOU 5582  ND2 ASN C 227     9712  12024  11685   -773    531    167       N  
ATOM   5583  N   TRP C 228      67.510  54.624  65.760  1.00 78.90           N  
ANISOU 5583  N   TRP C 228     8717  10480  10779    286    -95    553       N  
ATOM   5584  CA  TRP C 228      68.656  54.060  66.476  1.00 78.65           C  
ANISOU 5584  CA  TRP C 228     8990  10369  10522    398   -208    699       C  
ATOM   5585  C   TRP C 228      69.497  55.104  67.220  1.00 79.26           C  
ANISOU 5585  C   TRP C 228     8938  10593  10583    508   -283    649       C  
ATOM   5586  O   TRP C 228      70.035  54.812  68.283  1.00 82.76           O  
ANISOU 5586  O   TRP C 228     9602  11061  10781    525   -339    697       O  
ATOM   5587  CB  TRP C 228      69.519  53.199  65.557  1.00 75.71           C  
ANISOU 5587  CB  TRP C 228     8760   9867  10137    645   -385    811       C  
ATOM   5588  CG  TRP C 228      69.090  51.824  65.577  1.00 75.86           C  
ANISOU 5588  CG  TRP C 228     9206   9623   9994    539   -384    893       C  
ATOM   5589  CD1 TRP C 228      67.868  51.356  65.233  1.00 78.50           C  
ANISOU 5589  CD1 TRP C 228     9593   9872  10361    211   -233    848       C  
ATOM   5590  CD2 TRP C 228      69.846  50.696  66.019  1.00 79.59           C  
ANISOU 5590  CD2 TRP C 228    10182   9843  10214    734   -573   1020       C  
ATOM   5591  NE1 TRP C 228      67.804  49.994  65.420  1.00 81.84           N  
ANISOU 5591  NE1 TRP C 228    10577   9953  10562     90   -288    963       N  
ATOM   5592  CE2 TRP C 228      69.009  49.562  65.901  1.00 83.04           C  
ANISOU 5592  CE2 TRP C 228    11068   9947  10535    456   -520   1083       C  
ATOM   5593  CE3 TRP C 228      71.153  50.524  66.482  1.00 80.12           C  
ANISOU 5593  CE3 TRP C 228    10371   9939  10130   1140   -822   1062       C  
ATOM   5594  CZ2 TRP C 228      69.438  48.274  66.235  1.00 84.86           C  
ANISOU 5594  CZ2 TRP C 228    11994   9750  10499    582   -729   1224       C  
ATOM   5595  CZ3 TRP C 228      71.577  49.236  66.826  1.00 83.62           C  
ANISOU 5595  CZ3 TRP C 228    11432  10026  10312   1368  -1056   1173       C  
ATOM   5596  CH2 TRP C 228      70.721  48.135  66.700  1.00 86.13           C  
ANISOU 5596  CH2 TRP C 228    12314   9894  10514   1095  -1017   1273       C  
ATOM   5597  N   THR C 229      69.579  56.326  66.703  1.00 76.38           N  
ANISOU 5597  N   THR C 229     8278  10299  10444    553   -311    553       N  
ATOM   5598  CA  THR C 229      70.141  57.393  67.513  1.00 80.50           C  
ANISOU 5598  CA  THR C 229     8726  10910  10947    545   -363    454       C  
ATOM   5599  C   THR C 229      69.341  57.616  68.801  1.00 88.53           C  
ANISOU 5599  C   THR C 229     9815  11994  11825    412   -217    294       C  
ATOM   5600  O   THR C 229      69.908  57.589  69.899  1.00 95.69           O  
ANISOU 5600  O   THR C 229    10864  12993  12497    390   -256    281       O  
ATOM   5601  CB  THR C 229      70.319  58.697  66.742  1.00 73.76           C  
ANISOU 5601  CB  THR C 229     7688  10006  10331    547   -440    396       C  
ATOM   5602  OG1 THR C 229      71.322  58.505  65.758  1.00 80.45           O  
ANISOU 5602  OG1 THR C 229     8460  10915  11191    588   -538    536       O  
ATOM   5603  CG2 THR C 229      70.785  59.789  67.668  1.00 70.66           C  
ANISOU 5603  CG2 THR C 229     7300   9635   9913    473   -500    252       C  
ATOM   5604  N   LYS C 230      68.029  57.816  68.669  1.00 93.91           N  
ANISOU 5604  N   LYS C 230    10366  12703  12613    336    -53    136       N  
ATOM   5605  CA  LYS C 230      67.158  57.971  69.844  1.00 96.96           C  
ANISOU 5605  CA  LYS C 230    10736  13281  12823    187    150    -86       C  
ATOM   5606  C   LYS C 230      67.381  56.809  70.831  1.00 94.31           C  
ANISOU 5606  C   LYS C 230    10750  13001  12083    -26    242     82       C  
ATOM   5607  O   LYS C 230      67.342  56.995  72.052  1.00102.21           O  
ANISOU 5607  O   LYS C 230    11863  14166  12805   -142    336    -23       O  
ATOM   5608  CB  LYS C 230      65.672  58.086  69.430  1.00 93.23           C  
ANISOU 5608  CB  LYS C 230     9967  12959  12495    141    322   -322       C  
ATOM   5609  CG  LYS C 230      65.306  59.440  68.797  1.00 97.93           C  
ANISOU 5609  CG  LYS C 230    10306  13483  13418    443    175   -556       C  
ATOM   5610  CD  LYS C 230      64.236  59.313  67.687  1.00103.62           C  
ANISOU 5610  CD  LYS C 230    10752  14268  14348    533    162   -651       C  
ATOM   5611  CE  LYS C 230      62.808  59.539  68.196  1.00110.80           C  
ANISOU 5611  CE  LYS C 230    11277  15579  15241    542    354  -1090       C  
ATOM   5612  NZ  LYS C 230      62.257  60.886  67.848  1.00110.80           N  
ANISOU 5612  NZ  LYS C 230    11060  15534  15503   1007    142  -1424       N  
ATOM   5613  N   LEU C 231      67.688  55.644  70.281  1.00 84.25           N  
ANISOU 5613  N   LEU C 231     9716  11548  10747    -48    170    343       N  
ATOM   5614  CA  LEU C 231      67.828  54.417  71.034  1.00 82.86           C  
ANISOU 5614  CA  LEU C 231    10026  11275  10179   -230    189    555       C  
ATOM   5615  C   LEU C 231      69.152  54.419  71.792  1.00 84.73           C  
ANISOU 5615  C   LEU C 231    10510  11488  10194      2    -66    672       C  
ATOM   5616  O   LEU C 231      69.211  54.075  72.972  1.00 90.57           O  
ANISOU 5616  O   LEU C 231    11602  12276  10534   -134    -47    739       O  
ATOM   5617  CB  LEU C 231      67.817  53.261  70.048  1.00 84.78           C  
ANISOU 5617  CB  LEU C 231    10492  11241  10479   -227    109    748       C  
ATOM   5618  CG  LEU C 231      67.016  51.967  70.140  1.00 84.49           C  
ANISOU 5618  CG  LEU C 231    10879  11020  10202   -624    249    881       C  
ATOM   5619  CD1 LEU C 231      65.669  52.116  70.823  1.00 87.23           C  
ANISOU 5619  CD1 LEU C 231    11081  11673  10389  -1149    625    706       C  
ATOM   5620  CD2 LEU C 231      66.846  51.475  68.714  1.00 81.56           C  
ANISOU 5620  CD2 LEU C 231    10421  10462  10106   -538    169    891       C  
ATOM   5621  N   VAL C 232      70.222  54.792  71.100  1.00 85.07           N  
ANISOU 5621  N   VAL C 232    10351  11513  10456    333   -309    683       N  
ATOM   5622  CA  VAL C 232      71.546  54.871  71.716  1.00 87.66           C  
ANISOU 5622  CA  VAL C 232    10757  11941  10605    578   -586    716       C  
ATOM   5623  C   VAL C 232      71.551  55.814  72.919  1.00 88.64           C  
ANISOU 5623  C   VAL C 232    10829  12284  10566    450   -542    539       C  
ATOM   5624  O   VAL C 232      72.243  55.565  73.883  1.00 96.37           O  
ANISOU 5624  O   VAL C 232    12047  13358  11212    538   -725    584       O  
ATOM   5625  CB  VAL C 232      72.641  55.294  70.690  1.00 89.06           C  
ANISOU 5625  CB  VAL C 232    10566  12219  11052    845   -783    673       C  
ATOM   5626  CG1 VAL C 232      73.777  56.036  71.373  1.00 81.29           C  
ANISOU 5626  CG1 VAL C 232     9400  11513   9973    937   -985    547       C  
ATOM   5627  CG2 VAL C 232      73.173  54.078  69.945  1.00 90.19           C  
ANISOU 5627  CG2 VAL C 232    10876  12231  11159   1138   -954    816       C  
ATOM   5628  N   LYS C 233      70.773  56.894  72.855  1.00 84.82           N  
ANISOU 5628  N   LYS C 233    10056  11873  10296    292   -339    307       N  
ATOM   5629  CA  LYS C 233      70.641  57.779  73.998  1.00 86.33           C  
ANISOU 5629  CA  LYS C 233    10229  12249  10321    187   -279     66       C  
ATOM   5630  C   LYS C 233      69.873  57.139  75.131  1.00 92.13           C  
ANISOU 5630  C   LYS C 233    11285  13108  10612    -48    -67     81       C  
ATOM   5631  O   LYS C 233      70.257  57.271  76.269  1.00102.71           O  
ANISOU 5631  O   LYS C 233    12822  14609  11593    -85   -130     26       O  
ATOM   5632  CB  LYS C 233      69.995  59.103  73.612  1.00 87.62           C  
ANISOU 5632  CB  LYS C 233    10066  12398  10827    176   -169   -233       C  
ATOM   5633  CG  LYS C 233      70.986  60.232  73.373  1.00100.07           C  
ANISOU 5633  CG  LYS C 233    11496  13916  12609    253   -402   -345       C  
ATOM   5634  CD  LYS C 233      70.304  61.469  72.783  1.00110.49           C  
ANISOU 5634  CD  LYS C 233    12655  15046  14279    286   -364   -580       C  
ATOM   5635  CE  LYS C 233      71.120  62.082  71.641  1.00110.71           C  
ANISOU 5635  CE  LYS C 233    12598  14871  14593    277   -560   -461       C  
ATOM   5636  NZ  LYS C 233      70.339  62.157  70.364  1.00101.56           N  
ANISOU 5636  NZ  LYS C 233    11360  13507  13722    371   -515   -380       N  
ATOM   5637  N   ARG C 234      68.792  56.431  74.827  1.00 97.89           N  
ANISOU 5637  N   ARG C 234    12076  13799  11319   -270    190    151       N  
ATOM   5638  CA  ARG C 234      67.979  55.832  75.891  1.00108.67           C  
ANISOU 5638  CA  ARG C 234    13743  15343  12201   -649    466    162       C  
ATOM   5639  C   ARG C 234      68.842  54.963  76.810  1.00114.19           C  
ANISOU 5639  C   ARG C 234    15059  15941  12386   -652    245    469       C  
ATOM   5640  O   ARG C 234      68.429  54.630  77.921  1.00128.42           O  
ANISOU 5640  O   ARG C 234    17216  17909  13666   -975    419    503       O  
ATOM   5641  CB  ARG C 234      66.777  55.026  75.328  1.00117.35           C  
ANISOU 5641  CB  ARG C 234    14831  16426  13328   -996    760    218       C  
ATOM   5642  CG  ARG C 234      65.671  55.868  74.662  1.00119.84           C  
ANISOU 5642  CG  ARG C 234    14516  16978  14037   -994    987   -162       C  
ATOM   5643  CD  ARG C 234      64.295  55.199  74.768  1.00124.28           C  
ANISOU 5643  CD  ARG C 234    14992  17823  14404  -1504   1383   -261       C  
ATOM   5644  NE  ARG C 234      63.747  55.357  76.123  1.00139.52           N  
ANISOU 5644  NE  ARG C 234    16960  20203  15847  -1849   1705   -473       N  
ATOM   5645  CZ  ARG C 234      63.702  54.387  77.036  1.00141.46           C  
ANISOU 5645  CZ  ARG C 234    17767  20483  15498  -2349   1868   -214       C  
ATOM   5646  NH1 ARG C 234      64.119  53.161  76.723  1.00143.52           N  
ANISOU 5646  NH1 ARG C 234    18635  20279  15618  -2525   1705    255       N  
ATOM   5647  NH2 ARG C 234      63.226  54.639  78.261  1.00134.73           N  
ANISOU 5647  NH2 ARG C 234    16924  20113  14154  -2673   2185   -436       N  
ATOM   5648  N   HIS C 235      70.062  54.651  76.369  1.00110.83           N  
ANISOU 5648  N   HIS C 235    14745  15294  12069   -267   -155    662       N  
ATOM   5649  CA  HIS C 235      70.924  53.723  77.108  1.00120.60           C  
ANISOU 5649  CA  HIS C 235    16588  16396  12836   -118   -475    949       C  
ATOM   5650  C   HIS C 235      72.398  54.145  77.171  1.00128.72           C  
ANISOU 5650  C   HIS C 235    17437  17539  13932    360   -920    885       C  
ATOM   5651  O   HIS C 235      73.268  53.513  76.561  1.00126.06           O  
ANISOU 5651  O   HIS C 235    17160  17046  13690    746  -1247   1024       O  
ATOM   5652  CB  HIS C 235      70.750  52.340  76.535  1.00115.50           C  
ANISOU 5652  CB  HIS C 235    16436  15330  12119   -141   -542   1278       C  
ATOM   5653  CG  HIS C 235      69.325  52.015  76.240  1.00121.92           C  
ANISOU 5653  CG  HIS C 235    17264  16101  12959   -680   -101   1276       C  
ATOM   5654  ND1 HIS C 235      68.943  50.990  75.405  1.00126.44           N  
ANISOU 5654  ND1 HIS C 235    18114  16301  13625   -798    -90   1468       N  
ATOM   5655  CD2 HIS C 235      68.180  52.606  76.657  1.00126.07           C  
ANISOU 5655  CD2 HIS C 235    17495  16978  13428  -1130    339   1036       C  
ATOM   5656  CE1 HIS C 235      67.623  50.953  75.337  1.00126.29           C  
ANISOU 5656  CE1 HIS C 235    17955  16431  13598  -1362    341   1366       C  
ATOM   5657  NE2 HIS C 235      67.138  51.928  76.084  1.00122.00           N  
ANISOU 5657  NE2 HIS C 235    17025  16363  12967  -1543    612   1089       N  
ATOM   5658  N   SER C 236      72.663  55.213  77.934  1.00136.77           N  
ANISOU 5658  N   SER C 236    18209  18880  14875    323   -929    619       N  
ATOM   5659  CA  SER C 236      73.927  55.943  77.847  1.00142.93           C  
ANISOU 5659  CA  SER C 236    18612  19869  15824    624  -1270    440       C  
ATOM   5660  C   SER C 236      74.096  56.972  78.962  1.00160.91           C  
ANISOU 5660  C   SER C 236    20803  22457  17879    488  -1287    147       C  
ATOM   5661  O   SER C 236      73.288  57.052  79.903  1.00164.84           O  
ANISOU 5661  O   SER C 236    21568  23042  18021    222  -1047     83       O  
ATOM   5662  CB  SER C 236      74.042  56.659  76.493  1.00135.26           C  
ANISOU 5662  CB  SER C 236    17070  18857  15465    665  -1198    304       C  
ATOM   5663  OG  SER C 236      73.812  55.777  75.416  1.00138.83           O  
ANISOU 5663  OG  SER C 236    17575  19055  16117    777  -1158    519       O  
ATOM   5664  N   GLY C 237      75.109  57.819  78.783  1.00135.30           N  
ATOM   5665  CA  GLY C 237      75.647  58.672  79.834  1.00162.57           C  
ATOM   5666  C   GLY C 237      74.691  59.511  80.657  1.00187.90           C  
ATOM   5667  O   GLY C 237      74.832  59.591  81.877  1.00198.96           O  
ATOM   5668  N   GLN C 238      73.749  60.176  79.998  1.00197.89           N  
ATOM   5669  CA  GLN C 238      72.789  61.013  80.714  1.00195.60           C  
ATOM   5670  C   GLN C 238      73.477  62.260  81.276  1.00184.52           C  
ATOM   5671  O   GLN C 238      73.433  62.523  82.484  1.00172.13           O  
ATOM   5672  CB  GLN C 238      72.122  60.210  81.854  1.00188.80           C  
ATOM   5673  CG  GLN C 238      70.644  59.898  81.650  1.00174.43           C  
ATOM   5674  CD  GLN C 238      70.375  58.993  80.451  1.00172.92           C  
ATOM   5675  OE1 GLN C 238      70.868  57.855  80.374  1.00154.68           O  
ATOM   5676  NE2 GLN C 238      69.569  59.488  79.518  1.00168.39           N  
TER    5677      GLN C 238                                                      
HETATM 5678  O2R NNR A 301      46.454  68.717  42.649  1.00103.42           O  
HETATM 5679  C2R NNR A 301      47.694  68.037  42.039  1.00116.32           C  
HETATM 5680  C3R NNR A 301      47.498  67.906  40.532  1.00109.58           C  
HETATM 5681  O3R NNR A 301      46.234  67.496  40.265  1.00129.51           O  
HETATM 5682  C4R NNR A 301      48.458  66.806  40.157  1.00107.10           C  
HETATM 5683  C5R NNR A 301      49.904  67.425  39.933  1.00 98.85           C  
HETATM 5684  O5R NNR A 301      50.575  66.723  38.834  1.00111.41           O  
HETATM 5685  O4R NNR A 301      48.415  65.963  41.165  1.00104.97           O  
HETATM 5686  C1R NNR A 301      47.923  66.801  42.459  1.00114.65           C  
HETATM 5687  N1  NNR A 301      48.970  66.761  43.502  1.00113.97           N  
HETATM 5688  C2  NNR A 301      50.203  66.195  43.253  1.00103.92           C  
HETATM 5689  C6  NNR A 301      48.742  67.319  44.736  1.00122.70           C  
HETATM 5690  C5  NNR A 301      49.737  67.321  45.733  1.00100.86           C  
HETATM 5691  C4  NNR A 301      50.944  66.761  45.471  1.00 97.59           C  
HETATM 5692  C3  NNR A 301      51.194  66.206  44.250  1.00101.51           C  
HETATM 5693  C7  NNR A 301      52.560  65.584  43.986  1.00105.46           C  
HETATM 5694  O7  NNR A 301      52.635  64.546  43.414  1.00 97.77           O  
HETATM 5695  N7  NNR A 301      53.754  66.248  44.433  1.00121.57           N  
HETATM 5696  C1  BOG A 302      57.449  87.085  50.122  1.00101.48           C  
HETATM 5697  O1  BOG A 302      57.702  85.946  49.379  1.00 90.66           O  
HETATM 5698  C2  BOG A 302      56.898  86.758  51.502  1.00109.72           C  
HETATM 5699  O2  BOG A 302      55.672  85.919  51.444  1.00 91.78           O  
HETATM 5700  C3  BOG A 302      56.621  88.057  52.192  1.00119.31           C  
HETATM 5701  O3  BOG A 302      55.893  87.835  53.448  1.00121.90           O  
HETATM 5702  C4  BOG A 302      57.897  88.803  52.425  1.00118.50           C  
HETATM 5703  O4  BOG A 302      57.640  90.091  52.994  1.00117.59           O  
HETATM 5704  C5  BOG A 302      58.705  89.011  51.147  1.00115.18           C  
HETATM 5705  O5  BOG A 302      58.718  87.847  50.233  1.00110.81           O  
HETATM 5706  C6  BOG A 302      60.107  89.261  51.543  1.00127.26           C  
HETATM 5707  O6  BOG A 302      60.464  90.599  51.219  1.00142.53           O  
HETATM 5708  C1' BOG A 302      57.783  86.190  47.944  1.00 78.40           C  
HETATM 5709  C2' BOG A 302      58.187  84.852  47.254  1.00 77.13           C  
HETATM 5710  C3' BOG A 302      57.678  84.814  45.845  1.00 72.00           C  
HETATM 5711  C4' BOG A 302      56.852  83.515  45.709  1.00 83.08           C  
HETATM 5712  C5' BOG A 302      56.644  83.133  44.195  1.00 94.67           C  
HETATM 5713  C6' BOG A 302      55.915  84.254  43.394  1.00100.38           C  
HETATM 5714  C7' BOG A 302      54.600  83.761  42.736  1.00102.02           C  
HETATM 5715  C8' BOG A 302      54.512  82.191  42.720  1.00102.55           C  
HETATM 5716  O2R NNR B 301      84.137  74.730  44.988  1.00104.89           O  
HETATM 5717  C2R NNR B 301      83.815  73.329  44.455  1.00109.82           C  
HETATM 5718  C3R NNR B 301      84.850  72.947  43.412  1.00 95.97           C  
HETATM 5719  O3R NNR B 301      85.112  74.055  42.680  1.00 91.03           O  
HETATM 5720  C4R NNR B 301      84.133  71.884  42.592  1.00 89.89           C  
HETATM 5721  C5R NNR B 301      84.172  70.511  43.370  1.00 80.60           C  
HETATM 5722  O5R NNR B 301      83.934  69.440  42.429  1.00 83.03           O  
HETATM 5723  O4R NNR B 301      82.895  72.294  42.532  1.00104.68           O  
HETATM 5724  C1R NNR B 301      82.653  73.237  43.834  1.00111.25           C  
HETATM 5725  N1  NNR B 301      81.646  72.682  44.753  1.00101.37           N  
HETATM 5726  C2  NNR B 301      80.805  71.619  44.422  1.00 86.80           C  
HETATM 5727  C6  NNR B 301      81.574  73.243  46.009  1.00106.24           C  
HETATM 5728  C5  NNR B 301      80.680  72.754  46.968  1.00103.94           C  
HETATM 5729  C4  NNR B 301      79.867  71.702  46.651  1.00 89.25           C  
HETATM 5730  C3  NNR B 301      79.897  71.140  45.409  1.00 88.81           C  
HETATM 5731  C7  NNR B 301      78.942  69.972  45.170  1.00 95.26           C  
HETATM 5732  O7  NNR B 301      78.598  69.674  44.064  1.00 84.28           O  
HETATM 5733  N7  NNR B 301      78.452  69.230  46.320  1.00100.95           N  
HETATM 5734  C1  BOG B 302      66.684  77.617  56.904  1.00121.82           C  
HETATM 5735  O1  BOG B 302      66.360  76.364  56.354  1.00135.45           O  
HETATM 5736  C2  BOG B 302      66.331  78.816  55.966  1.00122.70           C  
HETATM 5737  O2  BOG B 302      67.075  78.798  54.646  1.00 94.16           O  
HETATM 5738  C3  BOG B 302      66.513  80.163  56.652  1.00114.90           C  
HETATM 5739  O3  BOG B 302      65.868  81.210  55.846  1.00 99.54           O  
HETATM 5740  C4  BOG B 302      65.999  80.221  58.077  1.00111.91           C  
HETATM 5741  O4  BOG B 302      66.462  81.416  58.736  1.00100.19           O  
HETATM 5742  C5  BOG B 302      66.385  78.998  58.932  1.00106.09           C  
HETATM 5743  O5  BOG B 302      66.034  77.722  58.261  1.00105.94           O  
HETATM 5744  C6  BOG B 302      65.706  79.061  60.249  1.00109.66           C  
HETATM 5745  O6  BOG B 302      65.867  77.808  60.910  1.00115.21           O  
HETATM 5746  C1' BOG B 302      67.510  75.529  55.980  1.00121.36           C  
HETATM 5747  C2' BOG B 302      67.606  74.221  56.856  1.00 93.42           C  
HETATM 5748  C3' BOG B 302      68.371  73.208  56.049  1.00 88.18           C  
HETATM 5749  C4' BOG B 302      67.393  72.306  55.254  1.00 76.05           C  
HETATM 5750  C5' BOG B 302      67.844  72.207  53.767  1.00 77.02           C  
HETATM 5751  C6' BOG B 302      67.617  70.757  53.256  1.00 78.51           C  
HETATM 5752  C7' BOG B 302      67.832  70.713  51.723  1.00 90.67           C  
HETATM 5753  C8' BOG B 302      67.016  69.543  51.061  1.00 86.93           C  
HETATM 5754  C1  BOG B 303      88.578  64.503  65.195  1.00101.00           C  
HETATM 5755  O1  BOG B 303      88.294  64.218  63.847  1.00 92.27           O  
HETATM 5756  C2  BOG B 303      87.873  65.791  65.603  1.00101.96           C  
HETATM 5757  O2  BOG B 303      88.186  66.876  64.663  1.00116.16           O  
HETATM 5758  C3  BOG B 303      88.251  66.185  66.985  1.00 98.01           C  
HETATM 5759  O3  BOG B 303      87.643  67.479  67.309  1.00100.79           O  
HETATM 5760  C4  BOG B 303      87.828  65.131  67.944  1.00 99.79           C  
HETATM 5761  O4  BOG B 303      88.158  65.520  69.296  1.00 92.82           O  
HETATM 5762  C5  BOG B 303      88.462  63.767  67.575  1.00102.25           C  
HETATM 5763  O5  BOG B 303      88.226  63.374  66.144  1.00 94.07           O  
HETATM 5764  C6  BOG B 303      87.929  62.710  68.464  1.00115.46           C  
HETATM 5765  O6  BOG B 303      88.477  62.863  69.778  1.00126.93           O  
HETATM 5766  C1' BOG B 303      88.332  62.816  63.476  1.00 92.63           C  
HETATM 5767  C2' BOG B 303      88.983  62.690  62.063  1.00 96.27           C  
HETATM 5768  C3' BOG B 303      87.909  62.695  61.025  1.00 95.50           C  
HETATM 5769  C4' BOG B 303      88.398  63.494  59.798  1.00 95.97           C  
HETATM 5770  C5' BOG B 303      89.506  62.659  59.082  1.00100.42           C  
HETATM 5771  C6' BOG B 303      89.723  63.176  57.637  1.00110.39           C  
HETATM 5772  C7' BOG B 303      90.732  64.345  57.616  1.00 99.73           C  
HETATM 5773  C8' BOG B 303      90.982  64.792  56.139  1.00 95.32           C  
HETATM 5774  O2R NNR C 301      68.463  41.514  59.085  1.00105.58           O  
HETATM 5775  C2R NNR C 301      68.453  42.155  57.693  1.00103.59           C  
HETATM 5776  C3R NNR C 301      68.404  41.065  56.616  1.00104.16           C  
HETATM 5777  O3R NNR C 301      68.987  39.936  57.093  1.00125.38           O  
HETATM 5778  C4R NNR C 301      69.233  41.603  55.469  1.00105.77           C  
HETATM 5779  C5R NNR C 301      68.350  42.346  54.382  1.00111.39           C  
HETATM 5780  O5R NNR C 301      69.235  43.146  53.528  1.00117.91           O  
HETATM 5781  O4R NNR C 301      70.083  42.428  56.013  1.00103.24           O  
HETATM 5782  C1R NNR C 301      69.534  42.839  57.467  1.00 99.60           C  
HETATM 5783  N1  NNR C 301      69.287  44.293  57.515  1.00 99.32           N  
HETATM 5784  C2  NNR C 301      69.207  45.052  56.338  1.00 83.42           C  
HETATM 5785  C6  NNR C 301      69.125  44.919  58.729  1.00 95.62           C  
HETATM 5786  C5  NNR C 301      68.873  46.312  58.773  1.00 95.41           C  
HETATM 5787  C4  NNR C 301      68.813  47.052  57.612  1.00 77.23           C  
HETATM 5788  C3  NNR C 301      68.960  46.442  56.403  1.00 77.25           C  
HETATM 5789  C7  NNR C 301      68.844  47.285  55.145  1.00 88.53           C  
HETATM 5790  O7  NNR C 301      69.362  46.936  54.126  1.00 99.16           O  
HETATM 5791  N7  NNR C 301      68.090  48.509  55.180  1.00102.10           N  
HETATM 5792  C1  BOG C 302      49.028  50.885  67.509  1.00124.67           C  
HETATM 5793  O1  BOG C 302      49.372  50.887  66.168  1.00107.69           O  
HETATM 5794  C2  BOG C 302      50.250  51.233  68.348  1.00141.13           C  
HETATM 5795  O2  BOG C 302      51.321  50.229  68.180  1.00129.00           O  
HETATM 5796  C3  BOG C 302      49.897  51.299  69.791  1.00153.92           C  
HETATM 5797  O3  BOG C 302      51.112  51.615  70.543  1.00158.22           O  
HETATM 5798  C4  BOG C 302      48.836  52.312  70.079  1.00151.21           C  
HETATM 5799  O4  BOG C 302      48.387  52.165  71.439  1.00136.47           O  
HETATM 5800  C5  BOG C 302      47.619  52.260  69.126  1.00141.55           C  
HETATM 5801  O5  BOG C 302      47.914  51.871  67.707  1.00128.76           O  
HETATM 5802  C6  BOG C 302      47.012  53.618  69.109  1.00142.32           C  
HETATM 5803  O6  BOG C 302      45.627  53.541  68.786  1.00145.08           O  
HETATM 5804  C1' BOG C 302      49.546  49.572  65.578  1.00100.23           C  
HETATM 5805  C2' BOG C 302      50.440  49.732  64.306  1.00 94.48           C  
HETATM 5806  C3' BOG C 302      50.572  48.411  63.589  1.00 89.41           C  
HETATM 5807  C4' BOG C 302      51.317  48.661  62.241  1.00 87.12           C  
HETATM 5808  C5' BOG C 302      51.543  47.317  61.484  1.00 81.58           C  
HETATM 5809  C6' BOG C 302      52.463  46.390  62.318  1.00101.14           C  
HETATM 5810  C7' BOG C 302      51.878  44.957  62.377  1.00113.08           C  
HETATM 5811  C8' BOG C 302      52.547  44.035  61.298  1.00103.31           C  
CONECT  195  201                                                                
CONECT  201  195  202                                                           
CONECT  202  201  203  205                                                      
CONECT  203  202  204  209                                                      
CONECT  204  203                                                                
CONECT  205  202  206                                                           
CONECT  206  205  207                                                           
CONECT  207  206  208                                                           
CONECT  208  207                                                                
CONECT  209  203                                                                
CONECT  681  688                                                                
CONECT  688  681  689                                                           
CONECT  689  688  690  692                                                      
CONECT  690  689  691  696                                                      
CONECT  691  690                                                                
CONECT  692  689  693                                                           
CONECT  693  692  694                                                           
CONECT  694  693  695                                                           
CONECT  695  694                                                                
CONECT  696  690  697                                                           
CONECT  697  696  698  700                                                      
CONECT  698  697  699  704                                                      
CONECT  699  698                                                                
CONECT  700  697  701                                                           
CONECT  701  700  702                                                           
CONECT  702  701  703                                                           
CONECT  703  702                                                                
CONECT  704  698                                                                
CONECT  820  823                                                                
CONECT  823  820  824                                                           
CONECT  824  823  825  827                                                      
CONECT  825  824  826  831                                                      
CONECT  826  825                                                                
CONECT  827  824  828                                                           
CONECT  828  827  829                                                           
CONECT  829  828  830                                                           
CONECT  830  829                                                                
CONECT  831  825                                                                
CONECT  867  875                                                                
CONECT  875  867  876                                                           
CONECT  876  875  877  879                                                      
CONECT  877  876  878  883                                                      
CONECT  878  877                                                                
CONECT  879  876  880                                                           
CONECT  880  879  881                                                           
CONECT  881  880  882                                                           
CONECT  882  881                                                                
CONECT  883  877                                                                
CONECT 1345 1351                                                                
CONECT 1351 1345 1352                                                           
CONECT 1352 1351 1353 1355                                                      
CONECT 1353 1352 1354 1359                                                      
CONECT 1354 1353                                                                
CONECT 1355 1352 1356                                                           
CONECT 1356 1355 1357                                                           
CONECT 1357 1356 1358                                                           
CONECT 1358 1357                                                                
CONECT 1359 1353                                                                
CONECT 1675 1681                                                                
CONECT 1681 1675 1682                                                           
CONECT 1682 1681 1683 1685                                                      
CONECT 1683 1682 1684 1689                                                      
CONECT 1684 1683                                                                
CONECT 1685 1682 1686                                                           
CONECT 1686 1685 1687                                                           
CONECT 1687 1686 1688                                                           
CONECT 1688 1687                                                                
CONECT 1689 1683                                                                
CONECT 1703 1708                                                                
CONECT 1708 1703 1709                                                           
CONECT 1709 1708 1710 1712                                                      
CONECT 1710 1709 1711 1716                                                      
CONECT 1711 1710                                                                
CONECT 1712 1709 1713                                                           
CONECT 1713 1712 1714                                                           
CONECT 1714 1713 1715                                                           
CONECT 1715 1714                                                                
CONECT 1716 1710                                                                
CONECT 2083 2089                                                                
CONECT 2089 2083 2090                                                           
CONECT 2090 2089 2091 2093                                                      
CONECT 2091 2090 2092 2097                                                      
CONECT 2092 2091                                                                
CONECT 2093 2090 2094                                                           
CONECT 2094 2093 2095                                                           
CONECT 2095 2094 2096                                                           
CONECT 2096 2095                                                                
CONECT 2097 2091                                                                
CONECT 2569 2576                                                                
CONECT 2576 2569 2577                                                           
CONECT 2577 2576 2578 2580                                                      
CONECT 2578 2577 2579 2584                                                      
CONECT 2579 2578                                                                
CONECT 2580 2577 2581                                                           
CONECT 2581 2580 2582                                                           
CONECT 2582 2581 2583                                                           
CONECT 2583 2582                                                                
CONECT 2584 2578 2585                                                           
CONECT 2585 2584 2586 2588                                                      
CONECT 2586 2585 2587 2592                                                      
CONECT 2587 2586                                                                
CONECT 2588 2585 2589                                                           
CONECT 2589 2588 2590                                                           
CONECT 2590 2589 2591                                                           
CONECT 2591 2590                                                                
CONECT 2592 2586                                                                
CONECT 2708 2711                                                                
CONECT 2711 2708 2712                                                           
CONECT 2712 2711 2713 2715                                                      
CONECT 2713 2712 2714 2719                                                      
CONECT 2714 2713                                                                
CONECT 2715 2712 2716                                                           
CONECT 2716 2715 2717                                                           
CONECT 2717 2716 2718                                                           
CONECT 2718 2717                                                                
CONECT 2719 2713                                                                
CONECT 2755 2763                                                                
CONECT 2763 2755 2764                                                           
CONECT 2764 2763 2765 2767                                                      
CONECT 2765 2764 2766 2771                                                      
CONECT 2766 2765                                                                
CONECT 2767 2764 2768                                                           
CONECT 2768 2767 2769                                                           
CONECT 2769 2768 2770                                                           
CONECT 2770 2769                                                                
CONECT 2771 2765                                                                
CONECT 3233 3239                                                                
CONECT 3239 3233 3240                                                           
CONECT 3240 3239 3241 3243                                                      
CONECT 3241 3240 3242 3247                                                      
CONECT 3242 3241                                                                
CONECT 3243 3240 3244                                                           
CONECT 3244 3243 3245                                                           
CONECT 3245 3244 3246                                                           
CONECT 3246 3245                                                                
CONECT 3247 3241                                                                
CONECT 3563 3569                                                                
CONECT 3569 3563 3570                                                           
CONECT 3570 3569 3571 3573                                                      
CONECT 3571 3570 3572 3577                                                      
CONECT 3572 3571                                                                
CONECT 3573 3570 3574                                                           
CONECT 3574 3573 3575                                                           
CONECT 3575 3574 3576                                                           
CONECT 3576 3575                                                                
CONECT 3577 3571                                                                
CONECT 3591 3596                                                                
CONECT 3596 3591 3597                                                           
CONECT 3597 3596 3598 3600                                                      
CONECT 3598 3597 3599 3604                                                      
CONECT 3599 3598                                                                
CONECT 3600 3597 3601                                                           
CONECT 3601 3600 3602                                                           
CONECT 3602 3601 3603                                                           
CONECT 3603 3602                                                                
CONECT 3604 3598                                                                
CONECT 3971 3977                                                                
CONECT 3977 3971 3978                                                           
CONECT 3978 3977 3979 3981                                                      
CONECT 3979 3978 3980 3985                                                      
CONECT 3980 3979                                                                
CONECT 3981 3978 3982                                                           
CONECT 3982 3981 3983                                                           
CONECT 3983 3982 3984                                                           
CONECT 3984 3983                                                                
CONECT 3985 3979                                                                
CONECT 4457 4464                                                                
CONECT 4464 4457 4465                                                           
CONECT 4465 4464 4466 4468                                                      
CONECT 4466 4465 4467 4472                                                      
CONECT 4467 4466                                                                
CONECT 4468 4465 4469                                                           
CONECT 4469 4468 4470                                                           
CONECT 4470 4469 4471                                                           
CONECT 4471 4470                                                                
CONECT 4472 4466 4473                                                           
CONECT 4473 4472 4474 4476                                                      
CONECT 4474 4473 4475 4480                                                      
CONECT 4475 4474                                                                
CONECT 4476 4473 4477                                                           
CONECT 4477 4476 4478                                                           
CONECT 4478 4477 4479                                                           
CONECT 4479 4478                                                                
CONECT 4480 4474                                                                
CONECT 4596 4599                                                                
CONECT 4599 4596 4600                                                           
CONECT 4600 4599 4601 4603                                                      
CONECT 4601 4600 4602 4607                                                      
CONECT 4602 4601                                                                
CONECT 4603 4600 4604                                                           
CONECT 4604 4603 4605                                                           
CONECT 4605 4604 4606