CNRS Nantes University UFIP UFIP
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***  CHAPERONE 10-AUG-17 5OPW  ***

elNémo ID: 19090211062436515

Job options:

ID        	=	 19090211062436515
JOBID     	=	 CHAPERONE 10-AUG-17 5OPW
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 1
DQMIN     	=	 0
DQMAX     	=	 1000
DQSTEP    	=	 200
DOGRAPHS  	=	 0

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    CHAPERONE                               10-AUG-17   5OPW              
TITLE     CRYSTAL STRUCTURE OF THE GROEL MUTANT A109C                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 60 KDA CHAPERONIN;                                         
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N;                     
COMPND   4 FRAGMENT: GROEL;                                                     
COMPND   5 SYNONYM: GROEL PROTEIN,PROTEIN CPN60;                                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI (STRAIN K12);                  
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 GENE: GROL, GROEL, MOPA, B4143, JW4103;                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    CHAPERONIN, CHAPERONE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.YAN,Q.SHI,A.BRACHER,G.MILICIC,A.K.SINGH,F.U.HARTL,M.HAYER-HARTL     
REVDAT   3   07-FEB-18 5OPW    1       JRNL                                     
REVDAT   2   24-JAN-18 5OPW    1       JRNL                                     
REVDAT   1   10-JAN-18 5OPW    0                                                
JRNL        AUTH   X.YAN,Q.SHI,A.BRACHER,G.MILICIC,A.K.SINGH,F.U.HARTL,         
JRNL        AUTH 2 M.HAYER-HARTL                                                
JRNL        TITL   GROEL RING SEPARATION AND EXCHANGE IN THE CHAPERONIN         
JRNL        TITL 2 REACTION.                                                    
JRNL        REF    CELL                          V. 172   605 2018              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   29336887                                                     
JRNL        DOI    10.1016/J.CELL.2017.12.010                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0071                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 160056                         
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) : 0.245                           
REMARK   3   R VALUE            (WORKING SET) : 0.245                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8289                            
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) : 3.19                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 11339                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 614                          
REMARK   3   BIN FREE R VALUE                    : 0.3400                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 53984                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
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) : 83.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.69000                                             
REMARK   3    B22 (A**2) : -0.46000                                             
REMARK   3    B33 (A**2) : 1.77000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.68000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.477         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.444         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 62.815        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.899                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 54383 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A): 54866 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 73430 ; 0.822 ; 1.988       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):126420 ; 0.939 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  7322 ; 3.733 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  2100 ;31.713 ;26.067       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES): 10094 ;12.621 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   308 ;15.961 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  8932 ; 0.045 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 61824 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A): 10248 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 91                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A     2    525       B     2    525   32397 0.040 0.050     
REMARK   3    2     A     2    525       C     2    525   32404 0.030 0.050     
REMARK   3    3     A     2    525       D     2    525   32422 0.030 0.050     
REMARK   3    4     A     2    525       E     2    525   32335 0.030 0.050     
REMARK   3    5     A     2    525       F     2    525   32277 0.040 0.050     
REMARK   3    6     A     2    525       G     2    525   32404 0.030 0.050     
REMARK   3    7     A     2    525       H     2    525   32319 0.040 0.050     
REMARK   3    8     A     2    525       I     2    525   32353 0.040 0.050     
REMARK   3    9     A     2    525       J     2    525   32359 0.040 0.050     
REMARK   3   10     A     2    525       K     2    525   32345 0.040 0.050     
REMARK   3   11     A     2    525       L     2    525   32197 0.050 0.050     
REMARK   3   12     A     2    525       M     2    525   32272 0.040 0.050     
REMARK   3   13     A     2    525       N     2    525   32301 0.040 0.050     
REMARK   3   14     B     2    525       C     2    525   32525 0.030 0.050     
REMARK   3   15     B     2    525       D     2    525   32506 0.030 0.050     
REMARK   3   16     B     2    525       E     2    525   32458 0.030 0.050     
REMARK   3   17     B     2    525       F     2    525   32395 0.040 0.050     
REMARK   3   18     B     2    525       G     2    525   32466 0.030 0.050     
REMARK   3   19     B     2    525       H     2    525   32469 0.030 0.050     
REMARK   3   20     B     2    525       I     2    525   32487 0.030 0.050     
REMARK   3   21     B     2    525       J     2    525   32463 0.040 0.050     
REMARK   3   22     B     2    525       K     2    525   32485 0.030 0.050     
REMARK   3   23     B     2    525       L     2    525   32315 0.040 0.050     
REMARK   3   24     B     2    525       M     2    525   32358 0.040 0.050     
REMARK   3   25     B     2    525       N     2    525   32430 0.040 0.050     
REMARK   3   26     C     2    525       D     2    525   32488 0.030 0.050     
REMARK   3   27     C     2    525       E     2    525   32427 0.030 0.050     
REMARK   3   28     C     2    525       F     2    525   32434 0.030 0.050     
REMARK   3   29     C     2    525       G     2    525   32524 0.020 0.050     
REMARK   3   30     C     2    525       H     2    525   32443 0.030 0.050     
REMARK   3   31     C     2    525       I     2    525   32474 0.030 0.050     
REMARK   3   32     C     2    525       J     2    525   32438 0.040 0.050     
REMARK   3   33     C     2    525       K     2    525   32399 0.030 0.050     
REMARK   3   34     C     2    525       L     2    525   32316 0.040 0.050     
REMARK   3   35     C     2    525       M     2    525   32356 0.040 0.050     
REMARK   3   36     C     2    525       N     2    525   32423 0.040 0.050     
REMARK   3   37     D     2    525       E     2    525   32360 0.040 0.050     
REMARK   3   38     D     2    525       F     2    525   32397 0.040 0.050     
REMARK   3   39     D     2    525       G     2    525   32484 0.030 0.050     
REMARK   3   40     D     2    525       H     2    525   32372 0.040 0.050     
REMARK   3   41     D     2    525       I     2    525   32452 0.030 0.050     
REMARK   3   42     D     2    525       J     2    525   32426 0.040 0.050     
REMARK   3   43     D     2    525       K     2    525   32396 0.040 0.050     
REMARK   3   44     D     2    525       L     2    525   32301 0.040 0.050     
REMARK   3   45     D     2    525       M     2    525   32309 0.040 0.050     
REMARK   3   46     D     2    525       N     2    525   32353 0.040 0.050     
REMARK   3   47     E     2    525       F     2    525   32377 0.040 0.050     
REMARK   3   48     E     2    525       G     2    525   32382 0.030 0.050     
REMARK   3   49     E     2    525       H     2    525   32496 0.030 0.050     
REMARK   3   50     E     2    525       I     2    525   32490 0.030 0.050     
REMARK   3   51     E     2    525       J     2    525   32397 0.040 0.050     
REMARK   3   52     E     2    525       K     2    525   32373 0.030 0.050     
REMARK   3   53     E     2    525       L     2    525   32313 0.040 0.050     
REMARK   3   54     E     2    525       M     2    525   32441 0.030 0.050     
REMARK   3   55     E     2    525       N     2    525   32418 0.040 0.050     
REMARK   3   56     F     2    525       G     2    525   32364 0.030 0.050     
REMARK   3   57     F     2    525       H     2    525   32444 0.040 0.050     
REMARK   3   58     F     2    525       I     2    525   32518 0.030 0.050     
REMARK   3   59     F     2    525       J     2    525   32323 0.040 0.050     
REMARK   3   60     F     2    525       K     2    525   32272 0.040 0.050     
REMARK   3   61     F     2    525       L     2    525   32369 0.040 0.050     
REMARK   3   62     F     2    525       M     2    525   32296 0.040 0.050     
REMARK   3   63     F     2    525       N     2    525   32421 0.040 0.050     
REMARK   3   64     G     2    525       H     2    525   32377 0.030 0.050     
REMARK   3   65     G     2    525       I     2    525   32417 0.030 0.050     
REMARK   3   66     G     2    525       J     2    525   32461 0.030 0.050     
REMARK   3   67     G     2    525       K     2    525   32464 0.030 0.050     
REMARK   3   68     G     2    525       L     2    525   32284 0.040 0.050     
REMARK   3   69     G     2    525       M     2    525   32346 0.040 0.050     
REMARK   3   70     G     2    525       N     2    525   32389 0.040 0.050     
REMARK   3   71     H     2    525       I     2    525   32554 0.030 0.050     
REMARK   3   72     H     2    525       J     2    525   32425 0.040 0.050     
REMARK   3   73     H     2    525       K     2    525   32376 0.040 0.050     
REMARK   3   74     H     2    525       L     2    525   32403 0.040 0.050     
REMARK   3   75     H     2    525       M     2    525   32384 0.040 0.050     
REMARK   3   76     H     2    525       N     2    525   32473 0.040 0.050     
REMARK   3   77     I     2    525       J     2    525   32450 0.040 0.050     
REMARK   3   78     I     2    525       K     2    525   32422 0.030 0.050     
REMARK   3   79     I     2    525       L     2    525   32449 0.040 0.050     
REMARK   3   80     I     2    525       M     2    525   32442 0.030 0.050     
REMARK   3   81     I     2    525       N     2    525   32544 0.030 0.050     
REMARK   3   82     J     2    525       K     2    525   32479 0.030 0.050     
REMARK   3   83     J     2    525       L     2    525   32286 0.040 0.050     
REMARK   3   84     J     2    525       M     2    525   32350 0.040 0.050     
REMARK   3   85     J     2    525       N     2    525   32375 0.040 0.050     
REMARK   3   86     K     2    525       L     2    525   32286 0.040 0.050     
REMARK   3   87     K     2    525       M     2    525   32326 0.040 0.050     
REMARK   3   88     K     2    525       N     2    525   32354 0.040 0.050     
REMARK   3   89     L     2    525       M     2    525   32241 0.050 0.050     
REMARK   3   90     L     2    525       N     2    525   32338 0.040 0.050     
REMARK   3   91     M     2    525       N     2    525   32388 0.040 0.050     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 42                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   135                          
REMARK   3    RESIDUE RANGE :   A   410        A   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  60.2456  -9.6097   8.7460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0376 T22:   0.0467                                     
REMARK   3      T33:   0.3375 T12:   0.0020                                     
REMARK   3      T13:  -0.0374 T23:   0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0049 L22:   2.7402                                     
REMARK   3      L33:   0.3684 L12:  -0.6259                                     
REMARK   3      L13:   0.1202 L23:   0.2733                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0288 S12:   0.0793 S13:  -0.0332                       
REMARK   3      S21:   0.1900 S22:   0.0554 S23:   0.0232                       
REMARK   3      S31:  -0.0157 S32:  -0.0211 S33:  -0.0843                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   136        A   190                          
REMARK   3    RESIDUE RANGE :   A   375        A   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.1217 -26.5463 -15.8812              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4172 T22:   0.4210                                     
REMARK   3      T33:   0.6440 T12:   0.0461                                     
REMARK   3      T13:  -0.0675 T23:  -0.1267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8002 L22:   2.2468                                     
REMARK   3      L33:   6.4789 L12:   1.6193                                     
REMARK   3      L13:   2.8261 L23:   1.6890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1984 S12:  -0.0480 S13:  -0.3422                       
REMARK   3      S21:  -0.2105 S22:  -0.0201 S23:  -0.1002                       
REMARK   3      S31:   0.5038 S32:  -0.4164 S33:  -0.1783                       
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   191        A   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  56.2228  -5.6896 -29.8703              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7710 T22:   0.7741                                     
REMARK   3      T33:   1.1658 T12:  -0.0121                                     
REMARK   3      T13:  -0.1925 T23:   0.0701                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0007 L22:   5.9534                                     
REMARK   3      L33:   3.0628 L12:   0.6368                                     
REMARK   3      L13:   0.6975 L23:  -0.2311                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1015 S12:   0.3312 S13:   0.9183                       
REMARK   3      S21:  -0.7394 S22:   0.0938 S23:   1.0854                       
REMARK   3      S31:  -0.0937 S32:  -0.2562 S33:  -0.1953                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   135                          
REMARK   3    RESIDUE RANGE :   B   410        B   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.5946 -41.1017   9.2913              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0367 T22:   0.1446                                     
REMARK   3      T33:   0.4407 T12:  -0.0164                                     
REMARK   3      T13:  -0.0125 T23:  -0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2131 L22:   3.3067                                     
REMARK   3      L33:   0.9764 L12:   0.3446                                     
REMARK   3      L13:   0.2011 L23:  -0.0457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1419 S12:   0.0382 S13:  -0.1349                       
REMARK   3      S21:   0.0434 S22:  -0.0763 S23:  -0.0492                       
REMARK   3      S31:   0.1433 S32:   0.0572 S33:  -0.0656                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   136        B   190                          
REMARK   3    RESIDUE RANGE :   B   375        B   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.7192 -56.7281 -14.9408              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5140 T22:   0.3156                                     
REMARK   3      T33:   0.8685 T12:  -0.0510                                     
REMARK   3      T13:  -0.0760 T23:  -0.1593                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5687 L22:   0.5617                                     
REMARK   3      L33:   4.8813 L12:  -0.4396                                     
REMARK   3      L13:   2.1311 L23:  -1.0288                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1524 S12:   0.0293 S13:  -0.2710                       
REMARK   3      S21:  -0.0783 S22:   0.1878 S23:   0.3635                       
REMARK   3      S31:   0.2336 S32:  -0.2200 S33:  -0.3402                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   191        B   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.2442 -36.4352 -29.1619              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6890 T22:   0.9010                                     
REMARK   3      T33:   0.9904 T12:  -0.1827                                     
REMARK   3      T13:  -0.0918 T23:   0.0710                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5482 L22:   5.4733                                     
REMARK   3      L33:   2.0751 L12:   1.7046                                     
REMARK   3      L13:   0.2073 L23:  -0.6699                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3051 S12:   0.7703 S13:   0.8537                       
REMARK   3      S21:  -0.6136 S22:   0.5096 S23:   0.4513                       
REMARK   3      S31:  -0.0521 S32:   0.0296 S33:  -0.2044                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C   135                          
REMARK   3    RESIDUE RANGE :   C   410        C   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3588 -41.1852   9.7848              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0478 T22:   0.0227                                     
REMARK   3      T33:   0.3300 T12:   0.0204                                     
REMARK   3      T13:  -0.0356 T23:  -0.0403                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2428 L22:   2.5899                                     
REMARK   3      L33:   0.8276 L12:   0.2912                                     
REMARK   3      L13:   0.1743 L23:   0.2028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0372 S12:  -0.1608 S13:  -0.0271                       
REMARK   3      S21:  -0.0528 S22:   0.0051 S23:  -0.0339                       
REMARK   3      S31:   0.1655 S32:   0.0286 S33:   0.0321                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   136        C   190                          
REMARK   3    RESIDUE RANGE :   C   375        C   409                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.8903 -43.3780 -14.3212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3453 T22:   0.2479                                     
REMARK   3      T33:   0.7102 T12:  -0.0430                                     
REMARK   3      T13:  -0.0536 T23:  -0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5448 L22:   2.6059                                     
REMARK   3      L33:   6.0500 L12:  -1.4194                                     
REMARK   3      L13:   1.3243 L23:  -3.7002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0849 S12:   0.1840 S13:  -0.1048                       
REMARK   3      S21:   0.1432 S22:   0.1779 S23:   0.3644                       
REMARK   3      S31:  -0.3952 S32:  -0.5204 S33:  -0.2627                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   191        C   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6121 -39.1668 -28.8786              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4571 T22:   0.2994                                     
REMARK   3      T33:   0.9640 T12:  -0.0082                                     
REMARK   3      T13:   0.0486 T23:   0.0938                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1117 L22:   4.8619                                     
REMARK   3      L33:   2.7479 L12:  -0.0966                                     
REMARK   3      L13:   0.0616 L23:   0.1545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1019 S12:   0.3989 S13:   1.0162                       
REMARK   3      S21:  -0.3201 S22:   0.1604 S23:  -0.6766                       
REMARK   3      S31:  -0.5245 S32:   0.2477 S33:  -0.2623                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     2        D   135                          
REMARK   3    RESIDUE RANGE :   D   410        D   525                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.3526 -10.3443  10.6928              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0167 T22:   0.0123                                     
REMARK   3      T33:   0.3477 T12:   0.0127                                     
REMARK   3      T13:  -0.0611 T23:  -0.0392                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8728 L22:   2.5213                                     
REMARK   3      L33:   0.9995 L12:  -0.3060                                     
REMARK   3      L13:  -0.1988 L23:   0.3522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0482 S12:   0.0196 S13:  -0.0624                       
REMARK   3      S21:   0.0391 S22:   0.0428 S23:   0.0277                       
REMARK   3      S31:  -0.0545 S32:  -0.0757 S33:   0.0054                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   136        D   190                          
REMARK   3    RESIDUE RANGE :   D   375        D   409                          
REMARK   3    ORIGIN FOR THE GROUP (A): -43.0851   2.4735 -13.2668              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6092 T22:   0.4386                                     
REMARK   3      T33:   0.6987 T12:   0.0395                                     
REMARK   3      T13:   0.0773 T23:   0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8476 L22:   6.4379                                     
REMARK   3      L33:   3.8247 L12:   1.0348                                     
REMARK   3      L13:  -0.3097 L23:  -4.5695                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4550 S12:   0.2140 S13:   0.4144                       
REMARK   3      S21:   0.5289 S22:  -0.1604 S23:   0.2138                       
REMARK   3      S31:  -0.6762 S32:   0.0516 S33:  -0.2946                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   191        D   374                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.8948 -12.1349 -27.9590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7927 T22:   0.5194                                     
REMARK   3      T33:   1.0313 T12:   0.1694                                     
REMARK   3      T13:   0.1724 T23:   0.0920                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9104 L22:   5.6339                                     
REMARK   3      L33:   4.7524 L12:  -1.2441                                     
REMARK   3      L13:   0.4988 L23:  -0.1291                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3397 S12:   0.6776 S13:   0.0908                       
REMARK   3      S21:  -0.9023 S22:  -0.2685 S23:  -1.2446                       
REMARK   3      S31:  -0.0117 S32:   0.2594 S33:  -0.0712                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E     2        E   135                          
REMARK   3    RESIDUE RANGE :   E   410        E   525                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0177  28.6976  10.8966              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1166 T22:   0.0379                                     
REMARK   3      T33:   0.3916 T12:  -0.0140                                     
REMARK   3      T13:  -0.0671 T23:   0.0259                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2762 L22:   3.5833                                     
REMARK   3      L33:   0.9881 L12:  -0.0382                                     
REMARK   3      L13:  -0.3308 L23:   0.1577                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1152 S12:   0.0489 S13:   0.1677                       
REMARK   3      S21:   0.1313 S22:  -0.0689 S23:   0.1190                       
REMARK   3      S31:  -0.1283 S32:  -0.1584 S33:  -0.0463                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   136        E   190                          
REMARK   3    RESIDUE RANGE :   E   375        E   409                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.1817  47.1596 -13.3455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7205 T22:   0.3994                                     
REMARK   3      T33:   0.8533 T12:  -0.0305                                     
REMARK   3      T13:  -0.1251 T23:   0.1907                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0943 L22:   1.1718                                     
REMARK   3      L33:   6.0268 L12:   1.5333                                     
REMARK   3      L13:  -1.8174 L23:  -1.3768                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1200 S12:   0.2175 S13:   0.4772                       
REMARK   3      S21:  -0.3092 S22:   0.1694 S23:   0.1780                       
REMARK   3      S31:  -0.1868 S32:   0.4105 S33:  -0.0494                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   191        E   374                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.7455  24.4271 -27.7046              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1887 T22:   0.6872                                     
REMARK   3      T33:   1.2471 T12:  -0.2062                                     
REMARK   3      T13:  -0.0021 T23:  -0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2451 L22:   5.5668                                     
REMARK   3      L33:   3.9209 L12:   0.0853                                     
REMARK   3      L13:  -0.0426 L23:   0.0500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2963 S12:   0.5017 S13:  -0.9791                       
REMARK   3      S21:  -0.7243 S22:   0.4085 S23:  -0.9892                       
REMARK   3      S31:   0.2158 S32:   0.1719 S33:  -0.1122                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F     2        F   135                          
REMARK   3    RESIDUE RANGE :   F   410        F   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8690  46.0800   9.9271              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0534 T22:   0.0249                                     
REMARK   3      T33:   0.4290 T12:   0.0045                                     
REMARK   3      T13:  -0.1046 T23:   0.0220                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3732 L22:   2.8954                                     
REMARK   3      L33:   0.9819 L12:   1.1137                                     
REMARK   3      L13:  -0.2671 L23:  -0.0746                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0791 S12:  -0.1632 S13:   0.0667                       
REMARK   3      S21:   0.0343 S22:  -0.0619 S23:  -0.0138                       
REMARK   3      S31:  -0.0918 S32:  -0.0543 S33:  -0.0172                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   136        F   190                          
REMARK   3    RESIDUE RANGE :   F   375        F   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.5612  56.1608 -14.8209              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4219 T22:   0.2678                                     
REMARK   3      T33:   0.7222 T12:   0.0855                                     
REMARK   3      T13:  -0.0155 T23:  -0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9968 L22:   1.1668                                     
REMARK   3      L33:   6.2504 L12:  -0.8798                                     
REMARK   3      L13:  -1.6509 L23:   2.5545                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0246 S12:   0.0375 S13:   0.2892                       
REMARK   3      S21:   0.0200 S22:   0.2492 S23:  -0.3544                       
REMARK   3      S31:   0.1686 S32:   0.7489 S33:  -0.2738                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   F   191        F   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9306  42.4475 -28.6423              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5697 T22:   0.3349                                     
REMARK   3      T33:   1.0545 T12:   0.0624                                     
REMARK   3      T13:  -0.0735 T23:  -0.0983                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2994 L22:   3.8605                                     
REMARK   3      L33:   2.7716 L12:  -0.3284                                     
REMARK   3      L13:  -0.2247 L23:   0.5096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0100 S12:   0.3037 S13:  -1.5188                       
REMARK   3      S21:  -0.2108 S22:   0.1024 S23:   0.2651                       
REMARK   3      S31:   0.6692 S32:   0.0460 S33:  -0.1123                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G     2        G   135                          
REMARK   3    RESIDUE RANGE :   G   410        G   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.9326  29.0659   9.0607              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1233 T22:   0.1099                                     
REMARK   3      T33:   0.3318 T12:   0.0286                                     
REMARK   3      T13:  -0.0533 T23:   0.0562                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6221 L22:   2.3863                                     
REMARK   3      L33:   1.1448 L12:  -0.1999                                     
REMARK   3      L13:   0.1588 L23:   0.1343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1410 S12:   0.0149 S13:   0.0448                       
REMARK   3      S21:   0.0298 S22:   0.1528 S23:  -0.1105                       
REMARK   3      S31:  -0.1463 S32:   0.2258 S33:  -0.0117                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   136        G   190                          
REMARK   3    RESIDUE RANGE :   G   375        G   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  68.0500  23.8326 -15.7332              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4550 T22:   0.7004                                     
REMARK   3      T33:   0.8553 T12:   0.0843                                     
REMARK   3      T13:  -0.0361 T23:   0.0864                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6457 L22:   1.1748                                     
REMARK   3      L33:   6.0107 L12:  -0.4145                                     
REMARK   3      L13:  -0.1023 L23:   2.1643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2752 S12:   0.2083 S13:  -0.1892                       
REMARK   3      S21:  -0.0512 S22:   0.0274 S23:  -0.3454                       
REMARK   3      S31:   0.4385 S32:   0.3489 S33:  -0.3025                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   191        G   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.9627  30.1345 -29.7837              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6696 T22:   0.7528                                     
REMARK   3      T33:   0.9736 T12:   0.2941                                     
REMARK   3      T13:  -0.1763 T23:  -0.1092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6938 L22:   4.7481                                     
REMARK   3      L33:   4.2477 L12:  -0.4617                                     
REMARK   3      L13:  -0.2804 L23:  -0.0348                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2052 S12:   0.6244 S13:  -0.6053                       
REMARK   3      S21:  -0.5105 S22:  -0.2455 S23:   0.9375                       
REMARK   3      S31:   0.0742 S32:  -0.2011 S33:   0.0404                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     2        H   135                          
REMARK   3    RESIDUE RANGE :   H   410        H   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.0147  39.9167  44.0013              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1568 T22:   0.1282                                     
REMARK   3      T33:   0.4098 T12:  -0.0036                                     
REMARK   3      T13:  -0.0422 T23:   0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2804 L22:   2.6072                                     
REMARK   3      L33:   0.7432 L12:  -0.0039                                     
REMARK   3      L13:  -0.0614 L23:  -0.2720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1140 S12:   0.1582 S13:   0.0981                       
REMARK   3      S21:   0.0516 S22:   0.1484 S23:   0.0812                       
REMARK   3      S31:  -0.1018 S32:  -0.1268 S33:  -0.0344                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   136        H   190                          
REMARK   3    RESIDUE RANGE :   H   375        H   409                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.5778  40.3599  68.8946              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4375 T22:   0.5717                                     
REMARK   3      T33:   0.7235 T12:   0.1230                                     
REMARK   3      T13:   0.0446 T23:  -0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4118 L22:   4.9717                                     
REMARK   3      L33:   4.9154 L12:   2.3340                                     
REMARK   3      L13:  -0.0734 L23:  -3.0726                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0767 S12:  -0.1040 S13:  -0.0718                       
REMARK   3      S21:  -0.0988 S22:   0.3238 S23:   0.3667                       
REMARK   3      S31:   0.1755 S32:  -0.7583 S33:  -0.4005                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   191        H   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3960  37.6559  82.3146              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5980 T22:   0.6176                                     
REMARK   3      T33:   0.7974 T12:   0.0460                                     
REMARK   3      T13:  -0.0537 T23:  -0.0529                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9374 L22:   5.4153                                     
REMARK   3      L33:   3.6776 L12:  -0.3329                                     
REMARK   3      L13:  -0.5974 L23:  -0.0380                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2172 S12:  -0.2145 S13:  -0.3202                       
REMARK   3      S21:   0.3141 S22:  -0.0179 S23:  -0.7021                       
REMARK   3      S31:   0.0142 S32:   0.3329 S33:  -0.1993                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I     2        I   135                          
REMARK   3    RESIDUE RANGE :   I   410        I   525                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.3976   6.9257  44.1654              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0656 T22:   0.1516                                     
REMARK   3      T33:   0.3778 T12:  -0.0086                                     
REMARK   3      T13:  -0.0413 T23:   0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6932 L22:   2.2068                                     
REMARK   3      L33:   1.0642 L12:   0.1296                                     
REMARK   3      L13:   0.1118 L23:   0.1980                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0019 S12:  -0.0717 S13:   0.0041                       
REMARK   3      S21:  -0.1381 S22:  -0.0231 S23:   0.0291                       
REMARK   3      S31:   0.0438 S32:  -0.1845 S33:   0.0212                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   136        I   190                          
REMARK   3    RESIDUE RANGE :   I   375        I   409                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.9505  -7.1213  68.6091              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4254 T22:   0.5790                                     
REMARK   3      T33:   0.6622 T12:  -0.0396                                     
REMARK   3      T13:   0.0097 T23:   0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1178 L22:   4.9360                                     
REMARK   3      L33:   5.2241 L12:   0.7246                                     
REMARK   3      L13:   1.2825 L23:  -2.2801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0578 S12:  -0.0757 S13:  -0.4173                       
REMARK   3      S21:   0.1831 S22:   0.1195 S23:   0.1750                       
REMARK   3      S31:   0.5380 S32:  -0.1424 S33:  -0.1773                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   I   191        I   374                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.5327   8.9761  82.6079              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8013 T22:   0.6287                                     
REMARK   3      T33:   0.9070 T12:  -0.0578                                     
REMARK   3      T13:  -0.1181 T23:  -0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5371 L22:   4.4794                                     
REMARK   3      L33:   3.2966 L12:   1.9794                                     
REMARK   3      L13:  -0.4443 L23:  -0.1643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2737 S12:  -0.4404 S13:  -0.1125                       
REMARK   3      S21:   0.6092 S22:  -0.1302 S23:  -0.8758                       
REMARK   3      S31:   0.0937 S32:   0.1453 S33:  -0.1435                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J     2        J   135                          
REMARK   3    RESIDUE RANGE :   J   410        J   525                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.7805 -31.1875  43.6356              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1802 T22:   0.1655                                     
REMARK   3      T33:   0.3669 T12:  -0.0178                                     
REMARK   3      T13:  -0.0041 T23:  -0.0245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2201 L22:   3.1226                                     
REMARK   3      L33:   0.8167 L12:  -0.5262                                     
REMARK   3      L13:  -0.0003 L23:  -0.0424                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0796 S12:  -0.0085 S13:  -0.1333                       
REMARK   3      S21:  -0.0261 S22:  -0.0929 S23:   0.1195                       
REMARK   3      S31:   0.1890 S32:  -0.1023 S33:   0.0132                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J   136        J   190                          
REMARK   3    RESIDUE RANGE :   J   375        J   409                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.4273 -49.6488  67.7303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8215 T22:   0.4655                                     
REMARK   3      T33:   0.9289 T12:  -0.0650                                     
REMARK   3      T13:  -0.0378 T23:   0.0502                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2543 L22:   0.4483                                     
REMARK   3      L33:   5.7802 L12:  -0.5595                                     
REMARK   3      L13:   2.4429 L23:  -1.1569                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2074 S12:   0.1078 S13:  -0.3377                       
REMARK   3      S21:   0.2511 S22:  -0.0764 S23:  -0.2345                       
REMARK   3      S31:   0.2896 S32:   0.3614 S33:  -0.1309                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   J   191        J   374                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.8658 -27.1557  82.3135              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9617 T22:   0.6989                                     
REMARK   3      T33:   1.0264 T12:   0.0467                                     
REMARK   3      T13:  -0.0206 T23:   0.0374                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5441 L22:   3.9324                                     
REMARK   3      L33:   3.7499 L12:   0.1260                                     
REMARK   3      L13:  -0.4239 L23:   0.4662                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1005 S12:  -0.3087 S13:   0.8013                       
REMARK   3      S21:   0.4523 S22:   0.0963 S23:  -0.4112                       
REMARK   3      S31:  -0.1829 S32:  -0.0301 S33:  -0.1968                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K     2        K   135                          
REMARK   3    RESIDUE RANGE :   K   410        K   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3085 -45.8359  42.9683              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1826 T22:   0.1941                                     
REMARK   3      T33:   0.4370 T12:  -0.0030                                     
REMARK   3      T13:  -0.0565 T23:   0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8005 L22:   2.4182                                     
REMARK   3      L33:   0.8515 L12:  -1.1215                                     
REMARK   3      L13:   0.0219 L23:   0.5270                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0376 S12:  -0.0018 S13:  -0.1688                       
REMARK   3      S21:   0.1796 S22:  -0.0068 S23:  -0.1409                       
REMARK   3      S31:   0.1538 S32:   0.1155 S33:  -0.0308                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   136        K   190                          
REMARK   3    RESIDUE RANGE :   K   375        K   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.5012 -55.3936  67.0693              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8282 T22:   0.8227                                     
REMARK   3      T33:   1.0284 T12:   0.1576                                     
REMARK   3      T13:  -0.1016 T23:   0.0934                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9214 L22:   0.1849                                     
REMARK   3      L33:   3.6539 L12:   0.6988                                     
REMARK   3      L13:   1.1045 L23:   0.0942                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3402 S12:  -0.0667 S13:  -0.2143                       
REMARK   3      S21:   0.1955 S22:   0.1266 S23:  -0.1427                       
REMARK   3      S31:  -0.1452 S32:   0.4817 S33:  -0.4669                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   K   191        K   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.9839 -44.1457  81.7781              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2005 T22:   1.2037                                     
REMARK   3      T33:   1.1877 T12:   0.0786                                     
REMARK   3      T13:   0.0709 T23:   0.1085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2969 L22:   1.7179                                     
REMARK   3      L33:   1.5947 L12:  -1.2206                                     
REMARK   3      L13:  -0.5094 L23:  -0.5574                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1714 S12:  -0.2520 S13:   0.4872                       
REMARK   3      S21:   0.2387 S22:   0.1681 S23:   0.3544                       
REMARK   3      S31:  -0.4518 S32:  -0.2266 S33:  -0.3395                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     2        L   135                          
REMARK   3    RESIDUE RANGE :   L   410        L   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.8079 -25.9456  42.4951              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1709 T22:   0.2496                                     
REMARK   3      T33:   0.3897 T12:   0.0093                                     
REMARK   3      T13:  -0.0674 T23:   0.0334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2659 L22:   2.0357                                     
REMARK   3      L33:   0.9967 L12:   0.4834                                     
REMARK   3      L13:  -0.2202 L23:   0.1036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0463 S12:  -0.0108 S13:  -0.0818                       
REMARK   3      S21:  -0.0759 S22:   0.0582 S23:  -0.1263                       
REMARK   3      S31:   0.0923 S32:   0.2223 S33:  -0.0119                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   136        L   190                          
REMARK   3    RESIDUE RANGE :   L   375        L   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.9645 -19.3399  66.9030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5524 T22:   0.8736                                     
REMARK   3      T33:   0.8527 T12:  -0.0247                                     
REMARK   3      T13:  -0.0039 T23:   0.0390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5653 L22:   3.8231                                     
REMARK   3      L33:   6.2668 L12:   1.0294                                     
REMARK   3      L13:   1.3388 L23:   3.1575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1698 S12:  -0.1327 S13:   0.1126                       
REMARK   3      S21:   0.0508 S22:   0.1221 S23:  -0.3456                       
REMARK   3      S31:  -0.5430 S32:   0.3327 S33:  -0.2920                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   191        L   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.9241 -27.5156  81.7111              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1304 T22:   1.3041                                     
REMARK   3      T33:   1.4077 T12:  -0.3041                                     
REMARK   3      T13:   0.1704 T23:  -0.0647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5769 L22:   2.7503                                     
REMARK   3      L33:   2.4865 L12:   1.3272                                     
REMARK   3      L13:   0.7373 L23:   0.2610                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6598 S12:  -0.8664 S13:   0.1114                       
REMARK   3      S21:   0.6310 S22:  -0.7301 S23:   1.1887                       
REMARK   3      S31:   0.0453 S32:  -0.2936 S33:   0.0703                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M     2        M   135                          
REMARK   3    RESIDUE RANGE :   M   410        M   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  59.9231  13.4410  42.3687              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0764 T22:   0.2129                                     
REMARK   3      T33:   0.3667 T12:  -0.0043                                     
REMARK   3      T13:  -0.0880 T23:   0.0257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9360 L22:   3.0010                                     
REMARK   3      L33:   0.8507 L12:   0.2869                                     
REMARK   3      L13:  -0.3391 L23:   0.0844                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0192 S12:  -0.0103 S13:   0.0408                       
REMARK   3      S21:  -0.1214 S22:   0.0718 S23:   0.0476                       
REMARK   3      S31:  -0.0804 S32:   0.1458 S33:  -0.0526                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   136        M   190                          
REMARK   3    RESIDUE RANGE :   M   375        M   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  65.1680  30.8751  66.7892              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5071 T22:   0.6469                                     
REMARK   3      T33:   0.7247 T12:  -0.0362                                     
REMARK   3      T13:   0.0272 T23:  -0.0394                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3738 L22:   4.1380                                     
REMARK   3      L33:   6.3314 L12:  -2.1909                                     
REMARK   3      L13:  -2.0936 L23:   0.3831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2116 S12:  -0.2886 S13:   0.3432                       
REMARK   3      S21:   0.2009 S22:   0.2497 S23:   0.2194                       
REMARK   3      S31:  -0.7925 S32:  -0.1816 S33:  -0.4613                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   M   191        M   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.5774   9.2223  80.9408              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6343 T22:   0.9389                                     
REMARK   3      T33:   1.4094 T12:   0.0670                                     
REMARK   3      T13:   0.2426 T23:   0.0856                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6106 L22:   5.8230                                     
REMARK   3      L33:   3.3211 L12:  -0.2225                                     
REMARK   3      L13:  -0.4213 L23:  -1.0716                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1363 S12:  -0.2406 S13:  -0.7785                       
REMARK   3      S21:   0.5301 S22:   0.3163 S23:   1.4720                       
REMARK   3      S31:   0.1140 S32:  -0.5399 S33:  -0.1800                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 40                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N     2        N   135                          
REMARK   3    RESIDUE RANGE :   N   410        N   525                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8417  42.8573  42.9014              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1505 T22:   0.1761                                     
REMARK   3      T33:   0.4549 T12:  -0.0211                                     
REMARK   3      T13:  -0.0628 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6558 L22:   3.2492                                     
REMARK   3      L33:   1.0886 L12:  -0.3279                                     
REMARK   3      L13:  -0.2096 L23:  -0.0429                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1117 S12:   0.0679 S13:   0.1947                       
REMARK   3      S21:   0.0508 S22:  -0.0329 S23:  -0.1104                       
REMARK   3      S31:  -0.2750 S32:   0.1733 S33:  -0.0788                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 41                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N   136        N   190                          
REMARK   3    RESIDUE RANGE :   N   375        N   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.9274  57.7078  67.6153              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7420 T22:   0.6746                                     
REMARK   3      T33:   0.8989 T12:   0.0855                                     
REMARK   3      T13:  -0.1261 T23:  -0.0351                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5482 L22:   1.5189                                     
REMARK   3      L33:   3.9619 L12:  -1.1513                                     
REMARK   3      L13:  -3.6582 L23:   1.2031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1069 S12:  -0.1013 S13:   0.1766                       
REMARK   3      S21:   0.1865 S22:   0.2838 S23:   0.2466                       
REMARK   3      S31:   0.0349 S32:  -0.2265 S33:  -0.1770                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 42                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   N   191        N   374                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.8077  38.4297  81.2544              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9287 T22:   1.3584                                     
REMARK   3      T33:   1.6867 T12:   0.1949                                     
REMARK   3      T13:   0.0192 T23:   0.3553                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5250 L22:   4.8915                                     
REMARK   3      L33:   2.5690 L12:  -2.9293                                     
REMARK   3      L13:  -0.0132 L23:  -0.2129                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4545 S12:  -1.0414 S13:  -1.3752                       
REMARK   3      S21:   0.5003 S22:   0.7804 S23:   0.7326                       
REMARK   3      S31:   0.2233 S32:  -0.1394 S33:  -0.3259                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 5OPW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200006178.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-AUG-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96600                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.3.11                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 168385                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.17500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 6.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.86100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP 11.2.08                                        
REMARK 200 STARTING MODEL: PDBID 4WSC                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CITRATE, PH 5.5, AND 15 %   
REMARK 280  PEG 6000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      131.02350            
REMARK 290   SMTRY3   2  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRADECAMERIC             
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 48690 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 293870 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -223.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N                            
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     LYS A   526                                                      
REMARK 465     ASN A   527                                                      
REMARK 465     ASP A   528                                                      
REMARK 465     ALA A   529                                                      
REMARK 465     ALA A   530                                                      
REMARK 465     ASP A   531                                                      
REMARK 465     LEU A   532                                                      
REMARK 465     GLY A   533                                                      
REMARK 465     ALA A   534                                                      
REMARK 465     ALA A   535                                                      
REMARK 465     GLY A   536                                                      
REMARK 465     GLY A   537                                                      
REMARK 465     MET A   538                                                      
REMARK 465     GLY A   539                                                      
REMARK 465     GLY A   540                                                      
REMARK 465     MET A   541                                                      
REMARK 465     GLY A   542                                                      
REMARK 465     GLY A   543                                                      
REMARK 465     MET A   544                                                      
REMARK 465     GLY A   545                                                      
REMARK 465     GLY A   546                                                      
REMARK 465     MET A   547                                                      
REMARK 465     MET A   548                                                      
REMARK 465     LYS B   526                                                      
REMARK 465     ASN B   527                                                      
REMARK 465     ASP B   528                                                      
REMARK 465     ALA B   529                                                      
REMARK 465     ALA B   530                                                      
REMARK 465     ASP B   531                                                      
REMARK 465     LEU B   532                                                      
REMARK 465     GLY B   533                                                      
REMARK 465     ALA B   534                                                      
REMARK 465     ALA B   535                                                      
REMARK 465     GLY B   536                                                      
REMARK 465     GLY B   537                                                      
REMARK 465     MET B   538                                                      
REMARK 465     GLY B   539                                                      
REMARK 465     GLY B   540                                                      
REMARK 465     MET B   541                                                      
REMARK 465     GLY B   542                                                      
REMARK 465     GLY B   543                                                      
REMARK 465     MET B   544                                                      
REMARK 465     GLY B   545                                                      
REMARK 465     GLY B   546                                                      
REMARK 465     MET B   547                                                      
REMARK 465     MET B   548                                                      
REMARK 465     LYS C   526                                                      
REMARK 465     ASN C   527                                                      
REMARK 465     ASP C   528                                                      
REMARK 465     ALA C   529                                                      
REMARK 465     ALA C   530                                                      
REMARK 465     ASP C   531                                                      
REMARK 465     LEU C   532                                                      
REMARK 465     GLY C   533                                                      
REMARK 465     ALA C   534                                                      
REMARK 465     ALA C   535                                                      
REMARK 465     GLY C   536                                                      
REMARK 465     GLY C   537                                                      
REMARK 465     MET C   538                                                      
REMARK 465     GLY C   539                                                      
REMARK 465     GLY C   540                                                      
REMARK 465     MET C   541                                                      
REMARK 465     GLY C   542                                                      
REMARK 465     GLY C   543                                                      
REMARK 465     MET C   544                                                      
REMARK 465     GLY C   545                                                      
REMARK 465     GLY C   546                                                      
REMARK 465     MET C   547                                                      
REMARK 465     MET C   548                                                      
REMARK 465     LYS D   526                                                      
REMARK 465     ASN D   527                                                      
REMARK 465     ASP D   528                                                      
REMARK 465     ALA D   529                                                      
REMARK 465     ALA D   530                                                      
REMARK 465     ASP D   531                                                      
REMARK 465     LEU D   532                                                      
REMARK 465     GLY D   533                                                      
REMARK 465     ALA D   534                                                      
REMARK 465     ALA D   535                                                      
REMARK 465     GLY D   536                                                      
REMARK 465     GLY D   537                                                      
REMARK 465     MET D   538                                                      
REMARK 465     GLY D   539                                                      
REMARK 465     GLY D   540                                                      
REMARK 465     MET D   541                                                      
REMARK 465     GLY D   542                                                      
REMARK 465     GLY D   543                                                      
REMARK 465     MET D   544                                                      
REMARK 465     GLY D   545                                                      
REMARK 465     GLY D   546                                                      
REMARK 465     MET D   547                                                      
REMARK 465     MET D   548                                                      
REMARK 465     LYS E   526                                                      
REMARK 465     ASN E   527                                                      
REMARK 465     ASP E   528                                                      
REMARK 465     ALA E   529                                                      
REMARK 465     ALA E   530                                                      
REMARK 465     ASP E   531                                                      
REMARK 465     LEU E   532                                                      
REMARK 465     GLY E   533                                                      
REMARK 465     ALA E   534                                                      
REMARK 465     ALA E   535                                                      
REMARK 465     GLY E   536                                                      
REMARK 465     GLY E   537                                                      
REMARK 465     MET E   538                                                      
REMARK 465     GLY E   539                                                      
REMARK 465     GLY E   540                                                      
REMARK 465     MET E   541                                                      
REMARK 465     GLY E   542                                                      
REMARK 465     GLY E   543                                                      
REMARK 465     MET E   544                                                      
REMARK 465     GLY E   545                                                      
REMARK 465     GLY E   546                                                      
REMARK 465     MET E   547                                                      
REMARK 465     MET E   548                                                      
REMARK 465     LYS F   526                                                      
REMARK 465     ASN F   527                                                      
REMARK 465     ASP F   528                                                      
REMARK 465     ALA F   529                                                      
REMARK 465     ALA F   530                                                      
REMARK 465     ASP F   531                                                      
REMARK 465     LEU F   532                                                      
REMARK 465     GLY F   533                                                      
REMARK 465     ALA F   534                                                      
REMARK 465     ALA F   535                                                      
REMARK 465     GLY F   536                                                      
REMARK 465     GLY F   537                                                      
REMARK 465     MET F   538                                                      
REMARK 465     GLY F   539                                                      
REMARK 465     GLY F   540                                                      
REMARK 465     MET F   541                                                      
REMARK 465     GLY F   542                                                      
REMARK 465     GLY F   543                                                      
REMARK 465     MET F   544                                                      
REMARK 465     GLY F   545                                                      
REMARK 465     GLY F   546                                                      
REMARK 465     MET F   547                                                      
REMARK 465     MET F   548                                                      
REMARK 465     LYS G   526                                                      
REMARK 465     ASN G   527                                                      
REMARK 465     ASP G   528                                                      
REMARK 465     ALA G   529                                                      
REMARK 465     ALA G   530                                                      
REMARK 465     ASP G   531                                                      
REMARK 465     LEU G   532                                                      
REMARK 465     GLY G   533                                                      
REMARK 465     ALA G   534                                                      
REMARK 465     ALA G   535                                                      
REMARK 465     GLY G   536                                                      
REMARK 465     GLY G   537                                                      
REMARK 465     MET G   538                                                      
REMARK 465     GLY G   539                                                      
REMARK 465     GLY G   540                                                      
REMARK 465     MET G   541                                                      
REMARK 465     GLY G   542                                                      
REMARK 465     GLY G   543                                                      
REMARK 465     MET G   544                                                      
REMARK 465     GLY G   545                                                      
REMARK 465     GLY G   546                                                      
REMARK 465     MET G   547                                                      
REMARK 465     MET G   548                                                      
REMARK 465     LYS H   526                                                      
REMARK 465     ASN H   527                                                      
REMARK 465     ASP H   528                                                      
REMARK 465     ALA H   529                                                      
REMARK 465     ALA H   530                                                      
REMARK 465     ASP H   531                                                      
REMARK 465     LEU H   532                                                      
REMARK 465     GLY H   533                                                      
REMARK 465     ALA H   534                                                      
REMARK 465     ALA H   535                                                      
REMARK 465     GLY H   536                                                      
REMARK 465     GLY H   537                                                      
REMARK 465     MET H   538                                                      
REMARK 465     GLY H   539                                                      
REMARK 465     GLY H   540                                                      
REMARK 465     MET H   541                                                      
REMARK 465     GLY H   542                                                      
REMARK 465     GLY H   543                                                      
REMARK 465     MET H   544                                                      
REMARK 465     GLY H   545                                                      
REMARK 465     GLY H   546                                                      
REMARK 465     MET H   547                                                      
REMARK 465     MET H   548                                                      
REMARK 465     LYS I   526                                                      
REMARK 465     ASN I   527                                                      
REMARK 465     ASP I   528                                                      
REMARK 465     ALA I   529                                                      
REMARK 465     ALA I   530                                                      
REMARK 465     ASP I   531                                                      
REMARK 465     LEU I   532                                                      
REMARK 465     GLY I   533                                                      
REMARK 465     ALA I   534                                                      
REMARK 465     ALA I   535                                                      
REMARK 465     GLY I   536                                                      
REMARK 465     GLY I   537                                                      
REMARK 465     MET I   538                                                      
REMARK 465     GLY I   539                                                      
REMARK 465     GLY I   540                                                      
REMARK 465     MET I   541                                                      
REMARK 465     GLY I   542                                                      
REMARK 465     GLY I   543                                                      
REMARK 465     MET I   544                                                      
REMARK 465     GLY I   545                                                      
REMARK 465     GLY I   546                                                      
REMARK 465     MET I   547                                                      
REMARK 465     MET I   548                                                      
REMARK 465     LYS J   526                                                      
REMARK 465     ASN J   527                                                      
REMARK 465     ASP J   528                                                      
REMARK 465     ALA J   529                                                      
REMARK 465     ALA J   530                                                      
REMARK 465     ASP J   531                                                      
REMARK 465     LEU J   532                                                      
REMARK 465     GLY J   533                                                      
REMARK 465     ALA J   534                                                      
REMARK 465     ALA J   535                                                      
REMARK 465     GLY J   536                                                      
REMARK 465     GLY J   537                                                      
REMARK 465     MET J   538                                                      
REMARK 465     GLY J   539                                                      
REMARK 465     GLY J   540                                                      
REMARK 465     MET J   541                                                      
REMARK 465     GLY J   542                                                      
REMARK 465     GLY J   543                                                      
REMARK 465     MET J   544                                                      
REMARK 465     GLY J   545                                                      
REMARK 465     GLY J   546                                                      
REMARK 465     MET J   547                                                      
REMARK 465     MET J   548                                                      
REMARK 465     LYS K   526                                                      
REMARK 465     ASN K   527                                                      
REMARK 465     ASP K   528                                                      
REMARK 465     ALA K   529                                                      
REMARK 465     ALA K   530                                                      
REMARK 465     ASP K   531                                                      
REMARK 465     LEU K   532                                                      
REMARK 465     GLY K   533                                                      
REMARK 465     ALA K   534                                                      
REMARK 465     ALA K   535                                                      
REMARK 465     GLY K   536                                                      
REMARK 465     GLY K   537                                                      
REMARK 465     MET K   538                                                      
REMARK 465     GLY K   539                                                      
REMARK 465     GLY K   540                                                      
REMARK 465     MET K   541                                                      
REMARK 465     GLY K   542                                                      
REMARK 465     GLY K   543                                                      
REMARK 465     MET K   544                                                      
REMARK 465     GLY K   545                                                      
REMARK 465     GLY K   546                                                      
REMARK 465     MET K   547                                                      
REMARK 465     MET K   548                                                      
REMARK 465     LYS L   526                                                      
REMARK 465     ASN L   527                                                      
REMARK 465     ASP L   528                                                      
REMARK 465     ALA L   529                                                      
REMARK 465     ALA L   530                                                      
REMARK 465     ASP L   531                                                      
REMARK 465     LEU L   532                                                      
REMARK 465     GLY L   533                                                      
REMARK 465     ALA L   534                                                      
REMARK 465     ALA L   535                                                      
REMARK 465     GLY L   536                                                      
REMARK 465     GLY L   537                                                      
REMARK 465     MET L   538                                                      
REMARK 465     GLY L   539                                                      
REMARK 465     GLY L   540                                                      
REMARK 465     MET L   541                                                      
REMARK 465     GLY L   542                                                      
REMARK 465     GLY L   543                                                      
REMARK 465     MET L   544                                                      
REMARK 465     GLY L   545                                                      
REMARK 465     GLY L   546                                                      
REMARK 465     MET L   547                                                      
REMARK 465     MET L   548                                                      
REMARK 465     LYS M   526                                                      
REMARK 465     ASN M   527                                                      
REMARK 465     ASP M   528                                                      
REMARK 465     ALA M   529                                                      
REMARK 465     ALA M   530                                                      
REMARK 465     ASP M   531                                                      
REMARK 465     LEU M   532                                                      
REMARK 465     GLY M   533                                                      
REMARK 465     ALA M   534                                                      
REMARK 465     ALA M   535                                                      
REMARK 465     GLY M   536                                                      
REMARK 465     GLY M   537                                                      
REMARK 465     MET M   538                                                      
REMARK 465     GLY M   539                                                      
REMARK 465     GLY M   540                                                      
REMARK 465     MET M   541                                                      
REMARK 465     GLY M   542                                                      
REMARK 465     GLY M   543                                                      
REMARK 465     MET M   544                                                      
REMARK 465     GLY M   545                                                      
REMARK 465     GLY M   546                                                      
REMARK 465     MET M   547                                                      
REMARK 465     MET M   548                                                      
REMARK 465     LYS N   526                                                      
REMARK 465     ASN N   527                                                      
REMARK 465     ASP N   528                                                      
REMARK 465     ALA N   529                                                      
REMARK 465     ALA N   530                                                      
REMARK 465     ASP N   531                                                      
REMARK 465     LEU N   532                                                      
REMARK 465     GLY N   533                                                      
REMARK 465     ALA N   534                                                      
REMARK 465     ALA N   535                                                      
REMARK 465     GLY N   536                                                      
REMARK 465     GLY N   537                                                      
REMARK 465     MET N   538                                                      
REMARK 465     GLY N   539                                                      
REMARK 465     GLY N   540                                                      
REMARK 465     MET N   541                                                      
REMARK 465     GLY N   542                                                      
REMARK 465     GLY N   543                                                      
REMARK 465     MET N   544                                                      
REMARK 465     GLY N   545                                                      
REMARK 465     GLY N   546                                                      
REMARK 465     MET N   547                                                      
REMARK 465     MET N   548                                                      
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   OD1  ASN A   229     O    GLY G   269              1.83            
REMARK 500   O    LYS L   171     NH1  ARG L   404              2.02            
REMARK 500   O    LYS M   171     NH2  ARG M   404              2.07            
REMARK 500   O    GLY L   269     OD1  ASN M   229              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    MET I   166     OD2  ASP M   359     1455     2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU F 232   CD    GLU F 232   OE2    -0.086                       
REMARK 500    ARG N 368   CD    ARG N 368   NE     -0.113                       
REMARK 500    ARG N 368   CZ    ARG N 368   NH1    -0.102                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  13   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    VAL A 499   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    VAL A 499   CA  -  CB  -  CG2 ANGL. DEV. =  11.2 DEGREES          
REMARK 500    MET C 193   CG  -  SD  -  CE  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    ARG E  13   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG E  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    CYS F 109   CA  -  CB  -  SG  ANGL. DEV. =   8.1 DEGREES          
REMARK 500    GLU F 232   CG  -  CD  -  OE1 ANGL. DEV. =  14.0 DEGREES          
REMARK 500    GLU F 232   CG  -  CD  -  OE2 ANGL. DEV. = -15.2 DEGREES          
REMARK 500    ARG F 350   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG F 350   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG G 284   CD  -  NE  -  CZ  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG G 284   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG G 284   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG H  13   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG H  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    CYS J 109   CA  -  CB  -  SG  ANGL. DEV. =   7.6 DEGREES          
REMARK 500    TYR K 203   CB  -  CG  -  CD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    TYR K 203   CB  -  CG  -  CD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG L  13   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG L  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    CYS L 109   CA  -  CB  -  SG  ANGL. DEV. =   7.1 DEGREES          
REMARK 500    MET L 193   N   -  CA  -  CB  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    ARG L 404   CG  -  CD  -  NE  ANGL. DEV. = -14.2 DEGREES          
REMARK 500    ARG M 284   NE  -  CZ  -  NH2 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    ARG M 404   CG  -  CD  -  NE  ANGL. DEV. = -17.1 DEGREES          
REMARK 500    ARG N 284   CD  -  NE  -  CZ  ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG N 284   NE  -  CZ  -  NH1 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ARG N 284   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG N 368   NE  -  CZ  -  NH1 ANGL. DEV. = -18.5 DEGREES          
REMARK 500    ARG N 368   NE  -  CZ  -  NH2 ANGL. DEV. =  17.2 DEGREES          
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    LYS A  34       32.03    -99.21                                   
REMARK 500    SER A 139      -68.08    -96.09                                   
REMARK 500    ALA A 152       30.40    -99.61                                   
REMARK 500    ASP A 328       38.79   -147.30                                   
REMARK 500    ASP A 334       77.93     58.93                                   
REMARK 500    LYS B  34       32.05    -99.30                                   
REMARK 500    SER B 139      -68.31    -95.99                                   
REMARK 500    ALA B 152       30.44    -99.61                                   
REMARK 500    ASP B 328       39.30   -147.32                                   
REMARK 500    ASP B 334       77.83     59.04                                   
REMARK 500    LYS C  34       32.13    -99.44                                   
REMARK 500    SER C 139      -68.32    -95.95                                   
REMARK 500    ALA C 152       30.28    -99.52                                   
REMARK 500    ASP C 328       39.01   -147.38                                   
REMARK 500    ASP C 334       77.85     59.12                                   
REMARK 500    LYS D  34       32.13    -99.38                                   
REMARK 500    SER D 139      -68.23    -95.99                                   
REMARK 500    ALA D 152       30.36    -99.53                                   
REMARK 500    ASP D 328       39.12   -147.38                                   
REMARK 500    ASP D 334       77.89     59.18                                   
REMARK 500    LYS E  34       32.07    -99.35                                   
REMARK 500    SER E 139      -68.46    -96.04                                   
REMARK 500    ALA E 152       30.30    -99.39                                   
REMARK 500    ASP E 328       39.15   -147.38                                   
REMARK 500    ASP E 334       77.91     59.18                                   
REMARK 500    LYS F  34       32.09    -99.48                                   
REMARK 500    SER F 139      -68.23    -96.09                                   
REMARK 500    ALA F 152       30.37    -99.58                                   
REMARK 500    ASP F 328       39.03   -147.46                                   
REMARK 500    ASP F 334       77.84     59.15                                   
REMARK 500    LYS G  34       32.04    -99.24                                   
REMARK 500    SER G 139      -68.60    -95.99                                   
REMARK 500    ALA G 152       30.36    -99.33                                   
REMARK 500    ASP G 328       38.84   -147.63                                   
REMARK 500    ASP G 334       78.00     59.19                                   
REMARK 500    LYS H  34       32.10    -99.33                                   
REMARK 500    SER H 139      -68.22    -96.08                                   
REMARK 500    ALA H 152       30.39    -99.68                                   
REMARK 500    ASP H 328       39.05   -147.36                                   
REMARK 500    ASP H 334       78.04     58.89                                   
REMARK 500    LYS I  34       32.02    -99.33                                   
REMARK 500    SER I 139      -68.29    -96.08                                   
REMARK 500    ALA I 152       30.39    -99.51                                   
REMARK 500    ASP I 328       39.25   -147.45                                   
REMARK 500    ASP I 334       77.89     59.17                                   
REMARK 500    LYS J  34       32.06    -99.39                                   
REMARK 500    SER J 139      -68.44    -96.03                                   
REMARK 500    ALA J 152       30.30    -99.43                                   
REMARK 500    ASP J 328       39.13   -147.35                                   
REMARK 500    ASP J 334       77.91     59.22                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      70 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5OPX   RELATED DB: PDB                                   
DBREF  5OPW A    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW B    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW C    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW D    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW E    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW F    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW G    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW H    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW I    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW J    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW K    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW L    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW M    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
DBREF  5OPW N    2   548  UNP    P0A6F5   CH60_ECOLI       2    548             
SEQADV 5OPW CYS A  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS B  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS C  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS D  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS E  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS F  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS G  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS H  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS I  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS J  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS K  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS L  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS M  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQADV 5OPW CYS N  109  UNP  P0A6F5    ALA   109 ENGINEERED MUTATION            
SEQRES   1 A  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 A  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 A  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 A  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 A  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 A  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 A  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 A  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 A  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 A  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 A  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 A  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 A  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 A  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 A  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 A  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 A  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 A  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 A  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 A  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 A  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 A  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 A  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 A  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 A  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 A  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 A  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 A  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 A  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 A  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 A  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 A  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 A  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 A  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 A  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 A  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 A  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 A  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 A  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 A  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 A  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 A  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 A  547  MET                                                          
SEQRES   1 B  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 B  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 B  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 B  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 B  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 B  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 B  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 B  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 B  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 B  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 B  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 B  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 B  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 B  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 B  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 B  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 B  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 B  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 B  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 B  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 B  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 B  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 B  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 B  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 B  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 B  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 B  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 B  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 B  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 B  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 B  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 B  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 B  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 B  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 B  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 B  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 B  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 B  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 B  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 B  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 B  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 B  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 B  547  MET                                                          
SEQRES   1 C  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 C  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 C  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 C  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 C  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 C  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 C  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 C  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 C  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 C  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 C  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 C  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 C  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 C  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 C  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 C  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 C  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 C  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 C  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 C  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 C  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 C  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 C  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 C  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 C  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 C  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 C  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 C  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 C  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 C  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 C  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 C  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 C  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 C  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 C  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 C  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 C  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 C  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 C  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 C  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 C  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 C  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 C  547  MET                                                          
SEQRES   1 D  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 D  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 D  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 D  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 D  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 D  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 D  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 D  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 D  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 D  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 D  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 D  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 D  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 D  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 D  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 D  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 D  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 D  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 D  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 D  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 D  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 D  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 D  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 D  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 D  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 D  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 D  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 D  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 D  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 D  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 D  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 D  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 D  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 D  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 D  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 D  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 D  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 D  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 D  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 D  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 D  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 D  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 D  547  MET                                                          
SEQRES   1 E  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 E  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 E  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 E  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 E  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 E  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 E  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 E  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 E  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 E  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 E  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 E  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 E  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 E  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 E  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 E  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 E  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 E  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 E  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 E  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 E  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 E  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 E  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 E  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 E  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 E  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 E  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 E  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 E  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 E  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 E  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 E  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 E  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 E  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 E  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 E  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 E  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 E  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 E  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 E  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 E  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 E  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 E  547  MET                                                          
SEQRES   1 F  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 F  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 F  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 F  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 F  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 F  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 F  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 F  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 F  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 F  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 F  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 F  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 F  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 F  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 F  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 F  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 F  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 F  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 F  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 F  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 F  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 F  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 F  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 F  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 F  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 F  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 F  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 F  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 F  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 F  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 F  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 F  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 F  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 F  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 F  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 F  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 F  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 F  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 F  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 F  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 F  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 F  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 F  547  MET                                                          
SEQRES   1 G  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 G  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 G  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 G  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 G  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 G  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 G  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 G  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 G  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 G  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 G  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 G  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 G  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 G  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 G  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 G  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 G  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 G  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 G  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 G  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 G  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 G  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 G  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 G  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 G  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 G  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 G  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 G  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 G  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 G  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 G  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 G  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 G  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 G  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 G  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 G  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 G  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 G  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 G  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 G  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 G  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 G  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 G  547  MET                                                          
SEQRES   1 H  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 H  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 H  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 H  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 H  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 H  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 H  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 H  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 H  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 H  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 H  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 H  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 H  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 H  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 H  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 H  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 H  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 H  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 H  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 H  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 H  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 H  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 H  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 H  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 H  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 H  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 H  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 H  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 H  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 H  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 H  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 H  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 H  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 H  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 H  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 H  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 H  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 H  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 H  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 H  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 H  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 H  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 H  547  MET                                                          
SEQRES   1 I  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 I  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 I  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 I  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 I  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 I  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 I  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 I  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 I  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 I  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 I  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 I  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 I  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 I  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 I  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 I  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 I  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 I  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 I  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 I  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 I  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 I  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 I  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 I  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 I  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 I  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 I  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 I  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 I  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 I  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 I  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 I  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 I  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 I  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 I  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 I  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 I  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 I  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 I  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 I  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 I  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 I  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 I  547  MET                                                          
SEQRES   1 J  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 J  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 J  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 J  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 J  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 J  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 J  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 J  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 J  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 J  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 J  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 J  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 J  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 J  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 J  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 J  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 J  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 J  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 J  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 J  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 J  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 J  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 J  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 J  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 J  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 J  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 J  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 J  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 J  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 J  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 J  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 J  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 J  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 J  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 J  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 J  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 J  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 J  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 J  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 J  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 J  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 J  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 J  547  MET                                                          
SEQRES   1 K  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 K  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 K  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 K  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 K  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 K  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 K  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 K  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 K  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 K  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 K  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 K  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 K  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 K  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 K  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 K  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 K  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 K  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 K  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 K  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 K  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 K  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 K  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 K  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 K  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 K  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 K  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 K  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 K  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 K  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 K  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 K  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 K  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 K  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 K  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 K  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 K  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 K  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 K  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 K  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 K  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 K  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 K  547  MET                                                          
SEQRES   1 L  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 L  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 L  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 L  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 L  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 L  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 L  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 L  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 L  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 L  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 L  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 L  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 L  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 L  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 L  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 L  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 L  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 L  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 L  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 L  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 L  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 L  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 L  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 L  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 L  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 L  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 L  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 L  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 L  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 L  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 L  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 L  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 L  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 L  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 L  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 L  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 L  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 L  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 L  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 L  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 L  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 L  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 L  547  MET                                                          
SEQRES   1 M  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 M  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 M  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 M  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 M  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 M  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 M  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 M  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 M  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 M  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 M  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 M  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 M  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 M  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 M  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 M  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 M  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 M  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 M  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 M  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 M  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 M  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 M  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 M  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 M  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 M  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 M  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 M  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 M  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 M  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 M  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 M  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 M  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 M  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 M  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 M  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 M  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 M  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 M  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 M  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 M  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 M  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 M  547  MET                                                          
SEQRES   1 N  547  ALA ALA LYS ASP VAL LYS PHE GLY ASN ASP ALA ARG VAL          
SEQRES   2 N  547  LYS MET LEU ARG GLY VAL ASN VAL LEU ALA ASP ALA VAL          
SEQRES   3 N  547  LYS VAL THR LEU GLY PRO LYS GLY ARG ASN VAL VAL LEU          
SEQRES   4 N  547  ASP LYS SER PHE GLY ALA PRO THR ILE THR LYS ASP GLY          
SEQRES   5 N  547  VAL SER VAL ALA ARG GLU ILE GLU LEU GLU ASP LYS PHE          
SEQRES   6 N  547  GLU ASN MET GLY ALA GLN MET VAL LYS GLU VAL ALA SER          
SEQRES   7 N  547  LYS ALA ASN ASP ALA ALA GLY ASP GLY THR THR THR ALA          
SEQRES   8 N  547  THR VAL LEU ALA GLN ALA ILE ILE THR GLU GLY LEU LYS          
SEQRES   9 N  547  ALA VAL ALA CYS GLY MET ASN PRO MET ASP LEU LYS ARG          
SEQRES  10 N  547  GLY ILE ASP LYS ALA VAL THR ALA ALA VAL GLU GLU LEU          
SEQRES  11 N  547  LYS ALA LEU SER VAL PRO CYS SER ASP SER LYS ALA ILE          
SEQRES  12 N  547  ALA GLN VAL GLY THR ILE SER ALA ASN SER ASP GLU THR          
SEQRES  13 N  547  VAL GLY LYS LEU ILE ALA GLU ALA MET ASP LYS VAL GLY          
SEQRES  14 N  547  LYS GLU GLY VAL ILE THR VAL GLU ASP GLY THR GLY LEU          
SEQRES  15 N  547  GLN ASP GLU LEU ASP VAL VAL GLU GLY MET GLN PHE ASP          
SEQRES  16 N  547  ARG GLY TYR LEU SER PRO TYR PHE ILE ASN LYS PRO GLU          
SEQRES  17 N  547  THR GLY ALA VAL GLU LEU GLU SER PRO PHE ILE LEU LEU          
SEQRES  18 N  547  ALA ASP LYS LYS ILE SER ASN ILE ARG GLU MET LEU PRO          
SEQRES  19 N  547  VAL LEU GLU ALA VAL ALA LYS ALA GLY LYS PRO LEU LEU          
SEQRES  20 N  547  ILE ILE ALA GLU ASP VAL GLU GLY GLU ALA LEU ALA THR          
SEQRES  21 N  547  LEU VAL VAL ASN THR MET ARG GLY ILE VAL LYS VAL ALA          
SEQRES  22 N  547  ALA VAL LYS ALA PRO GLY PHE GLY ASP ARG ARG LYS ALA          
SEQRES  23 N  547  MET LEU GLN ASP ILE ALA THR LEU THR GLY GLY THR VAL          
SEQRES  24 N  547  ILE SER GLU GLU ILE GLY MET GLU LEU GLU LYS ALA THR          
SEQRES  25 N  547  LEU GLU ASP LEU GLY GLN ALA LYS ARG VAL VAL ILE ASN          
SEQRES  26 N  547  LYS ASP THR THR THR ILE ILE ASP GLY VAL GLY GLU GLU          
SEQRES  27 N  547  ALA ALA ILE GLN GLY ARG VAL ALA GLN ILE ARG GLN GLN          
SEQRES  28 N  547  ILE GLU GLU ALA THR SER ASP TYR ASP ARG GLU LYS LEU          
SEQRES  29 N  547  GLN GLU ARG VAL ALA LYS LEU ALA GLY GLY VAL ALA VAL          
SEQRES  30 N  547  ILE LYS VAL GLY ALA ALA THR GLU VAL GLU MET LYS GLU          
SEQRES  31 N  547  LYS LYS ALA ARG VAL GLU ASP ALA LEU HIS ALA THR ARG          
SEQRES  32 N  547  ALA ALA VAL GLU GLU GLY VAL VAL ALA GLY GLY GLY VAL          
SEQRES  33 N  547  ALA LEU ILE ARG VAL ALA SER LYS LEU ALA ASP LEU ARG          
SEQRES  34 N  547  GLY GLN ASN GLU ASP GLN ASN VAL GLY ILE LYS VAL ALA          
SEQRES  35 N  547  LEU ARG ALA MET GLU ALA PRO LEU ARG GLN ILE VAL LEU          
SEQRES  36 N  547  ASN CYS GLY GLU GLU PRO SER VAL VAL ALA ASN THR VAL          
SEQRES  37 N  547  LYS GLY GLY ASP GLY ASN TYR GLY TYR ASN ALA ALA THR          
SEQRES  38 N  547  GLU GLU TYR GLY ASN MET ILE ASP MET GLY ILE LEU ASP          
SEQRES  39 N  547  PRO THR LYS VAL THR ARG SER ALA LEU GLN TYR ALA ALA          
SEQRES  40 N  547  SER VAL ALA GLY LEU MET ILE THR THR GLU CYS MET VAL          
SEQRES  41 N  547  THR ASP LEU PRO LYS ASN ASP ALA ALA ASP LEU GLY ALA          
SEQRES  42 N  547  ALA GLY GLY MET GLY GLY MET GLY GLY MET GLY GLY MET          
SEQRES  43 N  547  MET                                                          
HELIX    1 AA1 GLY A    9  VAL A   29  1                                  21    
HELIX    2 AA2 ASP A   52  ILE A   60  1                                   9    
HELIX    3 AA3 ASP A   64  GLY A   86  1                                  23    
HELIX    4 AA4 GLY A   88  GLY A  110  1                                  23    
HELIX    5 AA5 ASN A  112  SER A  135  1                                  24    
HELIX    6 AA6 ASP A  140  ALA A  152  1                                  13    
HELIX    7 AA7 ASP A  155  GLY A  170  1                                  16    
HELIX    8 AA8 SER A  201  ILE A  205  5                                   5    
HELIX    9 AA9 MET A  233  GLY A  244  1                                  12    
HELIX   10 AB1 GLU A  255  GLY A  269  1                                  15    
HELIX   11 AB2 PHE A  281  GLY A  297  1                                  17    
HELIX   12 AB3 GLU A  338  ALA A  356  1                                  19    
HELIX   13 AB4 SER A  358  GLY A  375  1                                  18    
HELIX   14 AB5 THR A  385  GLY A  410  1                                  26    
HELIX   15 AB6 GLY A  416  LEU A  426  1                                  11    
HELIX   16 AB7 ASN A  433  MET A  447  1                                  15    
HELIX   17 AB8 GLU A  448  GLY A  459  1                                  12    
HELIX   18 AB9 GLU A  461  GLY A  472  1                                  12    
HELIX   19 AC1 THR A  497  THR A  516  1                                  20    
HELIX   20 AC2 GLY B    9  VAL B   29  1                                  21    
HELIX   21 AC3 ASP B   52  ILE B   60  1                                   9    
HELIX   22 AC4 ASP B   64  GLY B   86  1                                  23    
HELIX   23 AC5 GLY B   88  GLY B  110  1                                  23    
HELIX   24 AC6 ASN B  112  SER B  135  1                                  24    
HELIX   25 AC7 ASP B  140  ALA B  152  1                                  13    
HELIX   26 AC8 ASP B  155  GLY B  170  1                                  16    
HELIX   27 AC9 SER B  201  ILE B  205  5                                   5    
HELIX   28 AD1 MET B  233  GLY B  244  1                                  12    
HELIX   29 AD2 GLU B  255  GLY B  269  1                                  15    
HELIX   30 AD3 PHE B  281  GLY B  297  1                                  17    
HELIX   31 AD4 GLU B  338  ALA B  356  1                                  19    
HELIX   32 AD5 SER B  358  GLY B  375  1                                  18    
HELIX   33 AD6 THR B  385  GLY B  410  1                                  26    
HELIX   34 AD7 GLY B  416  LEU B  426  1                                  11    
HELIX   35 AD8 ASN B  433  MET B  447  1                                  15    
HELIX   36 AD9 GLU B  448  GLY B  459  1                                  12    
HELIX   37 AE1 GLU B  461  GLY B  472  1                                  12    
HELIX   38 AE2 THR B  497  THR B  516  1                                  20    
HELIX   39 AE3 GLY C    9  VAL C   29  1                                  21    
HELIX   40 AE4 ASP C   52  ILE C   60  1                                   9    
HELIX   41 AE5 ASP C   64  GLY C   86  1                                  23    
HELIX   42 AE6 GLY C   88  GLY C  110  1                                  23    
HELIX   43 AE7 ASN C  112  SER C  135  1                                  24    
HELIX   44 AE8 ASP C  140  ALA C  152  1                                  13    
HELIX   45 AE9 ASP C  155  GLY C  170  1                                  16    
HELIX   46 AF1 SER C  201  ILE C  205  5                                   5    
HELIX   47 AF2 MET C  233  GLY C  244  1                                  12    
HELIX   48 AF3 GLU C  255  GLY C  269  1                                  15    
HELIX   49 AF4 PHE C  281  GLY C  297  1                                  17    
HELIX   50 AF5 GLU C  338  ALA C  356  1                                  19    
HELIX   51 AF6 SER C  358  GLY C  375  1                                  18    
HELIX   52 AF7 THR C  385  GLY C  410  1                                  26    
HELIX   53 AF8 GLY C  416  LEU C  426  1                                  11    
HELIX   54 AF9 ASN C  433  MET C  447  1                                  15    
HELIX   55 AG1 GLU C  448  GLY C  459  1                                  12    
HELIX   56 AG2 GLU C  461  GLY C  472  1                                  12    
HELIX   57 AG3 THR C  497  THR C  516  1                                  20    
HELIX   58 AG4 GLY D    9  VAL D   29  1                                  21    
HELIX   59 AG5 ASP D   52  ILE D   60  1                                   9    
HELIX   60 AG6 ASP D   64  GLY D   86  1                                  23    
HELIX   61 AG7 GLY D   88  GLY D  110  1                                  23    
HELIX   62 AG8 ASN D  112  SER D  135  1                                  24    
HELIX   63 AG9 ASP D  140  ALA D  152  1                                  13    
HELIX   64 AH1 ASP D  155  GLY D  170  1                                  16    
HELIX   65 AH2 SER D  201  ILE D  205  5                                   5    
HELIX   66 AH3 MET D  233  GLY D  244  1                                  12    
HELIX   67 AH4 GLU D  255  GLY D  269  1                                  15    
HELIX   68 AH5 PHE D  281  GLY D  297  1                                  17    
HELIX   69 AH6 GLU D  338  ALA D  356  1                                  19    
HELIX   70 AH7 SER D  358  GLY D  375  1                                  18    
HELIX   71 AH8 THR D  385  GLY D  410  1                                  26    
HELIX   72 AH9 GLY D  416  LEU D  426  1                                  11    
HELIX   73 AI1 ASN D  433  MET D  447  1                                  15    
HELIX   74 AI2 GLU D  448  GLY D  459  1                                  12    
HELIX   75 AI3 GLU D  461  GLY D  472  1                                  12    
HELIX   76 AI4 THR D  497  THR D  516  1                                  20    
HELIX   77 AI5 GLY E    9  VAL E   29  1                                  21    
HELIX   78 AI6 ASP E   52  ILE E   60  1                                   9    
HELIX   79 AI7 ASP E   64  GLY E   86  1                                  23    
HELIX   80 AI8 GLY E   88  GLY E  110  1                                  23    
HELIX   81 AI9 ASN E  112  SER E  135  1                                  24    
HELIX   82 AJ1 ASP E  140  ALA E  152  1                                  13    
HELIX   83 AJ2 ASP E  155  GLY E  170  1                                  16    
HELIX   84 AJ3 SER E  201  ILE E  205  5                                   5    
HELIX   85 AJ4 MET E  233  GLY E  244  1                                  12    
HELIX   86 AJ5 GLU E  255  GLY E  269  1                                  15    
HELIX   87 AJ6 PHE E  281  GLY E  297  1                                  17    
HELIX   88 AJ7 GLU E  338  ALA E  356  1                                  19    
HELIX   89 AJ8 SER E  358  GLY E  375  1                                  18    
HELIX   90 AJ9 THR E  385  GLY E  410  1                                  26    
HELIX   91 AK1 GLY E  416  LEU E  426  1                                  11    
HELIX   92 AK2 ASN E  433  MET E  447  1                                  15    
HELIX   93 AK3 GLU E  448  GLY E  459  1                                  12    
HELIX   94 AK4 GLU E  461  GLY E  472  1                                  12    
HELIX   95 AK5 THR E  497  THR E  516  1                                  20    
HELIX   96 AK6 GLY F    9  VAL F   29  1                                  21    
HELIX   97 AK7 ASP F   52  ILE F   60  1                                   9    
HELIX   98 AK8 ASP F   64  GLY F   86  1                                  23    
HELIX   99 AK9 GLY F   88  CYS F  109  1                                  22    
HELIX  100 AL1 ASN F  112  SER F  135  1                                  24    
HELIX  101 AL2 ASP F  140  ALA F  152  1                                  13    
HELIX  102 AL3 ASP F  155  GLY F  170  1                                  16    
HELIX  103 AL4 SER F  201  ILE F  205  5                                   5    
HELIX  104 AL5 MET F  233  GLY F  244  1                                  12    
HELIX  105 AL6 GLU F  255  GLY F  269  1                                  15    
HELIX  106 AL7 PHE F  281  GLY F  297  1                                  17    
HELIX  107 AL8 GLU F  338  ALA F  356  1                                  19    
HELIX  108 AL9 SER F  358  GLY F  375  1                                  18    
HELIX  109 AM1 THR F  385  GLY F  410  1                                  26    
HELIX  110 AM2 GLY F  416  LEU F  426  1                                  11    
HELIX  111 AM3 ASN F  433  MET F  447  1                                  15    
HELIX  112 AM4 GLU F  448  GLY F  459  1                                  12    
HELIX  113 AM5 GLU F  461  GLY F  472  1                                  12    
HELIX  114 AM6 THR F  497  THR F  516  1                                  20    
HELIX  115 AM7 GLY G    9  VAL G   29  1                                  21    
HELIX  116 AM8 ASP G   52  ILE G   60  1                                   9    
HELIX  117 AM9 ASP G   64  GLY G   86  1                                  23    
HELIX  118 AN1 GLY G   88  GLY G  110  1                                  23    
HELIX  119 AN2 ASN G  112  SER G  135  1                                  24    
HELIX  120 AN3 ASP G  140  ALA G  152  1                                  13    
HELIX  121 AN4 ASP G  155  GLY G  170  1                                  16    
HELIX  122 AN5 SER G  201  ILE G  205  5                                   5    
HELIX  123 AN6 MET G  233  GLY G  244  1                                  12    
HELIX  124 AN7 GLU G  255  GLY G  269  1                                  15    
HELIX  125 AN8 PHE G  281  GLY G  297  1                                  17    
HELIX  126 AN9 GLU G  338  ALA G  356  1                                  19    
HELIX  127 AO1 SER G  358  GLY G  375  1                                  18    
HELIX  128 AO2 THR G  385  GLY G  410  1                                  26    
HELIX  129 AO3 GLY G  416  LEU G  426  1                                  11    
HELIX  130 AO4 ASN G  433  MET G  447  1                                  15    
HELIX  131 AO5 GLU G  448  GLY G  459  1                                  12    
HELIX  132 AO6 GLU G  461  GLY G  472  1                                  12    
HELIX  133 AO7 THR G  497  THR G  516  1                                  20    
HELIX  134 AO8 GLY H    9  VAL H   29  1                                  21    
HELIX  135 AO9 ASP H   52  ILE H   60  1                                   9    
HELIX  136 AP1 ASP H   64  GLY H   86  1                                  23    
HELIX  137 AP2 GLY H   88  GLY H  110  1                                  23    
HELIX  138 AP3 ASN H  112  SER H  135  1                                  24    
HELIX  139 AP4 ASP H  140  ALA H  152  1                                  13    
HELIX  140 AP5 ASP H  155  GLY H  170  1                                  16    
HELIX  141 AP6 SER H  201  ILE H  205  5                                   5    
HELIX  142 AP7 MET H  233  GLY H  244  1                                  12    
HELIX  143 AP8 GLU H  255  GLY H  269  1                                  15    
HELIX  144 AP9 PHE H  281  GLY H  297  1                                  17    
HELIX  145 AQ1 GLU H  338  ALA H  356  1                                  19    
HELIX  146 AQ2 SER H  358  GLY H  375  1                                  18    
HELIX  147 AQ3 THR H  385  GLY H  410  1                                  26    
HELIX  148 AQ4 GLY H  416  LEU H  426  1                                  11    
HELIX  149 AQ5 ASN H  433  MET H  447  1                                  15    
HELIX  150 AQ6 GLU H  448  GLY H  459  1                                  12    
HELIX  151 AQ7 GLU H  461  GLY H  472  1                                  12    
HELIX  152 AQ8 THR H  497  THR H  516  1                                  20    
HELIX  153 AQ9 GLY I    9  VAL I   29  1                                  21    
HELIX  154 AR1 ASP I   52  ILE I   60  1                                   9    
HELIX  155 AR2 ASP I   64  GLY I   86  1                                  23    
HELIX  156 AR3 GLY I   88  GLY I  110  1                                  23    
HELIX  157 AR4 ASN I  112  SER I  135  1                                  24    
HELIX  158 AR5 ASP I  140  ALA I  152  1                                  13    
HELIX  159 AR6 ASP I  155  GLY I  170  1                                  16    
HELIX  160 AR7 SER I  201  ILE I  205  5                                   5    
HELIX  161 AR8 MET I  233  GLY I  244  1                                  12    
HELIX  162 AR9 GLU I  255  GLY I  269  1                                  15    
HELIX  163 AS1 PHE I  281  GLY I  297  1                                  17    
HELIX  164 AS2 GLU I  338  ALA I  356  1                                  19    
HELIX  165 AS3 SER I  358  GLY I  375  1                                  18    
HELIX  166 AS4 THR I  385  GLY I  410  1                                  26    
HELIX  167 AS5 GLY I  416  LEU I  426  1                                  11    
HELIX  168 AS6 ASN I  433  MET I  447  1                                  15    
HELIX  169 AS7 GLU I  448  GLY I  459  1                                  12    
HELIX  170 AS8 GLU I  461  GLY I  472  1                                  12    
HELIX  171 AS9 THR I  497  THR I  516  1                                  20    
HELIX  172 AT1 GLY J    9  VAL J   29  1                                  21    
HELIX  173 AT2 ASP J   52  ILE J   60  1                                   9    
HELIX  174 AT3 ASP J   64  GLY J   86  1                                  23    
HELIX  175 AT4 GLY J   88  GLY J  110  1                                  23    
HELIX  176 AT5 ASN J  112  SER J  135  1                                  24    
HELIX  177 AT6 ASP J  140  ALA J  152  1                                  13    
HELIX  178 AT7 ASP J  155  GLY J  170  1                                  16    
HELIX  179 AT8 SER J  201  ILE J  205  5                                   5    
HELIX  180 AT9 MET J  233  GLY J  244  1                                  12    
HELIX  181 AU1 GLU J  255  GLY J  269  1                                  15    
HELIX  182 AU2 PHE J  281  GLY J  297  1                                  17    
HELIX  183 AU3 GLU J  338  ALA J  356  1                                  19    
HELIX  184 AU4 SER J  358  GLY J  375  1                                  18    
HELIX  185 AU5 THR J  385  GLY J  410  1                                  26    
HELIX  186 AU6 GLY J  416  LEU J  426  1                                  11    
HELIX  187 AU7 ASN J  433  MET J  447  1                                  15    
HELIX  188 AU8 GLU J  448  GLY J  459  1                                  12    
HELIX  189 AU9 GLU J  461  GLY J  472  1                                  12    
HELIX  190 AV1 THR J  497  THR J  516  1                                  20    
HELIX  191 AV2 GLY K    9  VAL K   29  1                                  21    
HELIX  192 AV3 ASP K   52  ILE K   60  1                                   9    
HELIX  193 AV4 ASP K   64  GLY K   86  1                                  23    
HELIX  194 AV5 GLY K   88  GLY K  110  1                                  23    
HELIX  195 AV6 ASN K  112  SER K  135  1                                  24    
HELIX  196 AV7 ASP K  140  ALA K  152  1                                  13    
HELIX  197 AV8 ASP K  155  GLY K  170  1                                  16    
HELIX  198 AV9 SER K  201  ILE K  205  5                                   5    
HELIX  199 AW1 MET K  233  GLY K  244  1                                  12    
HELIX  200 AW2 GLU K  255  GLY K  269  1                                  15    
HELIX  201 AW3 PHE K  281  GLY K  297  1                                  17    
HELIX  202 AW4 GLU K  338  ALA K  356  1                                  19    
HELIX  203 AW5 SER K  358  GLY K  375  1                                  18    
HELIX  204 AW6 THR K  385  GLY K  410  1                                  26    
HELIX  205 AW7 GLY K  416  LEU K  426  1                                  11    
HELIX  206 AW8 ASN K  433  MET K  447  1                                  15    
HELIX  207 AW9 GLU K  448  GLY K  459  1                                  12    
HELIX  208 AX1 GLU K  461  GLY K  472  1                                  12    
HELIX  209 AX2 THR K  497  THR K  516  1                                  20    
HELIX  210 AX3 GLY L    9  VAL L   29  1                                  21    
HELIX  211 AX4 ASP L   52  ILE L   60  1                                   9    
HELIX  212 AX5 ASP L   64  GLY L   86  1                                  23    
HELIX  213 AX6 GLY L   88  GLY L  110  1                                  23    
HELIX  214 AX7 ASN L  112  SER L  135  1                                  24    
HELIX  215 AX8 ASP L  140  ALA L  152  1                                  13    
HELIX  216 AX9 ASP L  155  GLY L  170  1                                  16    
HELIX  217 AY1 SER L  201  ILE L  205  5                                   5    
HELIX  218 AY2 MET L  233  GLY L  244  1                                  12    
HELIX  219 AY3 GLU L  255  GLY L  269  1                                  15    
HELIX  220 AY4 PHE L  281  GLY L  297  1                                  17    
HELIX  221 AY5 GLU L  338  ALA L  356  1                                  19    
HELIX  222 AY6 SER L  358  GLY L  375  1                                  18    
HELIX  223 AY7 THR L  385  GLY L  410  1                                  26    
HELIX  224 AY8 GLY L  416  LEU L  426  1                                  11    
HELIX  225 AY9 ASN L  433  MET L  447  1                                  15    
HELIX  226 AZ1 GLU L  448  GLY L  459  1                                  12    
HELIX  227 AZ2 GLU L  461  GLY L  472  1                                  12    
HELIX  228 AZ3 THR L  497  THR L  516  1                                  20    
HELIX  229 AZ4 GLY M    9  VAL M   29  1                                  21    
HELIX  230 AZ5 ASP M   52  ILE M   60  1                                   9    
HELIX  231 AZ6 ASP M   64  GLY M   86  1                                  23    
HELIX  232 AZ7 GLY M   88  GLY M  110  1                                  23    
HELIX  233 AZ8 ASN M  112  SER M  135  1                                  24    
HELIX  234 AZ9 ASP M  140  ALA M  152  1                                  13    
HELIX  235 BA1 ASP M  155  GLY M  170  1                                  16    
HELIX  236 BA2 SER M  201  ILE M  205  5                                   5    
HELIX  237 BA3 MET M  233  GLY M  244  1                                  12    
HELIX  238 BA4 GLU M  255  GLY M  269  1                                  15    
HELIX  239 BA5 GLY M  282  GLY M  297  1                                  16    
HELIX  240 BA6 GLU M  338  ALA M  356  1                                  19    
HELIX  241 BA7 SER M  358  GLY M  375  1                                  18    
HELIX  242 BA8 THR M  385  GLY M  410  1                                  26    
HELIX  243 BA9 GLY M  416  LEU M  426  1                                  11    
HELIX  244 BB1 ASN M  433  MET M  447  1                                  15    
HELIX  245 BB2 GLU M  448  GLY M  459  1                                  12    
HELIX  246 BB3 GLU M  461  GLY M  472  1                                  12    
HELIX  247 BB4 THR M  497  THR M  516  1                                  20    
HELIX  248 BB5 GLY N    9  VAL N   29  1                                  21    
HELIX  249 BB6 ASP N   52  ILE N   60  1                                   9    
HELIX  250 BB7 ASP N   64  GLY N   86  1                                  23    
HELIX  251 BB8 GLY N   88  GLY N  110  1                                  23    
HELIX  252 BB9 ASN N  112  SER N  135  1                                  24    
HELIX  253 BC1 ASP N  140  ALA N  152  1                                  13    
HELIX  254 BC2 ASP N  155  GLY N  170  1                                  16    
HELIX  255 BC3 SER N  201  ILE N  205  5                                   5    
HELIX  256 BC4 MET N  233  GLY N  244  1                                  12    
HELIX  257 BC5 GLU N  255  GLY N  269  1                                  15    
HELIX  258 BC6 GLY N  282  GLY N  297  1                                  16    
HELIX  259 BC7 GLU N  338  ALA N  356  1                                  19    
HELIX  260 BC8 SER N  358  GLY N  375  1                                  18    
HELIX  261 BC9 THR N  385  GLY N  410  1                                  26    
HELIX  262 BD1 GLY N  416  LEU N  426  1                                  11    
HELIX  263 BD2 ASN N  433  MET N  447  1                                  15    
HELIX  264 BD3 GLU N  448  GLY N  459  1                                  12    
HELIX  265 BD4 GLU N  461  GLY N  472  1                                  12    
HELIX  266 BD5 THR N  497  THR N  516  1                                  20    
SHEET    1 AA1 4 LYS A   4  PHE A   8  0                                        
SHEET    2 AA1 4 THR A 517  ASP A 523 -1  O  THR A 522   N  ASP A   5           
SHEET    3 AA1 4 ASN G  37  LEU G  40  1  O  VAL G  39   N  VAL A 521           
SHEET    4 AA1 4 THR G  48  THR G  50 -1  O  THR G  48   N  LEU G  40           
SHEET    1 AA2 4 THR A  48  THR A  50  0                                        
SHEET    2 AA2 4 ASN A  37  LEU A  40 -1  N  LEU A  40   O  THR A  48           
SHEET    3 AA2 4 THR B 517  ASP B 523  1  O  VAL B 521   N  VAL A  39           
SHEET    4 AA2 4 LYS B   4  PHE B   8 -1  N  ASP B   5   O  THR B 522           
SHEET    1 AA3 3 VAL A 174  ASP A 179  0                                        
SHEET    2 AA3 3 VAL A 376  VAL A 381  1  O  ILE A 379   N  THR A 176           
SHEET    3 AA3 3 GLU A 186  VAL A 190 -1  N  VAL A 190   O  VAL A 376           
SHEET    1 AA4 6 MET A 193  PHE A 195  0                                        
SHEET    2 AA4 6 THR A 329  GLY A 335 -1  O  ILE A 332   N  MET A 193           
SHEET    3 AA4 6 GLY A 318  ASN A 326 -1  N  VAL A 324   O  THR A 331           
SHEET    4 AA4 6 PHE A 219  ASP A 224 -1  N  ILE A 220   O  GLY A 318           
SHEET    5 AA4 6 LEU A 247  ALA A 251  1  O  LEU A 248   N  LEU A 221           
SHEET    6 AA4 6 VAL A 273  LYS A 277  1  O  ALA A 274   N  ILE A 249           
SHEET    1 AA5 4 VAL A 213  GLU A 216  0                                        
SHEET    2 AA5 4 GLY A 318  ASN A 326 -1  O  ILE A 325   N  VAL A 213           
SHEET    3 AA5 4 PHE A 219  ASP A 224 -1  N  ILE A 220   O  GLY A 318           
SHEET    4 AA5 4 ILE A 301  SER A 302  1  O  ILE A 301   N  LEU A 222           
SHEET    1 AA6 2 LYS A 226  ILE A 227  0                                        
SHEET    2 AA6 2 ASP A 253  VAL A 254  1  O  ASP A 253   N  ILE A 227           
SHEET    1 AA7 2 VAL A 411  ALA A 413  0                                        
SHEET    2 AA7 2 LEU A 494  PRO A 496 -1  O  ASP A 495   N  VAL A 412           
SHEET    1 AA8 2 TYR A 476  ASN A 479  0                                        
SHEET    2 AA8 2 GLU A 484  ASN A 487 -1  O  GLY A 486   N  GLY A 477           
SHEET    1 AA9 4 THR B  48  THR B  50  0                                        
SHEET    2 AA9 4 ASN B  37  LEU B  40 -1  N  LEU B  40   O  THR B  48           
SHEET    3 AA9 4 THR C 517  ASP C 523  1  O  CYS C 519   N  VAL B  39           
SHEET    4 AA9 4 LYS C   4  PHE C   8 -1  N  ASP C   5   O  THR C 522           
SHEET    1 AB1 3 VAL B 174  ASP B 179  0                                        
SHEET    2 AB1 3 VAL B 376  VAL B 381  1  O  ILE B 379   N  THR B 176           
SHEET    3 AB1 3 GLU B 186  VAL B 190 -1  N  VAL B 190   O  VAL B 376           
SHEET    1 AB2 6 MET B 193  PHE B 195  0                                        
SHEET    2 AB2 6 THR B 329  GLY B 335 -1  O  ILE B 332   N  MET B 193           
SHEET    3 AB2 6 GLY B 318  ASN B 326 -1  N  VAL B 324   O  THR B 331           
SHEET    4 AB2 6 PHE B 219  ASP B 224 -1  N  ILE B 220   O  GLY B 318           
SHEET    5 AB2 6 LEU B 247  ALA B 251  1  O  LEU B 248   N  LEU B 221           
SHEET    6 AB2 6 VAL B 273  LYS B 277  1  O  ALA B 274   N  ILE B 249           
SHEET    1 AB3 4 VAL B 213  GLU B 216  0                                        
SHEET    2 AB3 4 GLY B 318  ASN B 326 -1  O  ILE B 325   N  VAL B 213           
SHEET    3 AB3 4 PHE B 219  ASP B 224 -1  N  ILE B 220   O  GLY B 318           
SHEET    4 AB3 4 ILE B 301  SER B 302  1  O  ILE B 301   N  LEU B 222           
SHEET    1 AB4 2 LYS B 226  ILE B 227  0                                        
SHEET    2 AB4 2 ASP B 253  VAL B 254  1  O  ASP B 253   N  ILE B 227           
SHEET    1 AB5 2 VAL B 411  ALA B 413  0                                        
SHEET    2 AB5 2 LEU B 494  PRO B 496 -1  O  ASP B 495   N  VAL B 412           
SHEET    1 AB6 2 TYR B 476  ASN B 479  0                                        
SHEET    2 AB6 2 GLU B 484  ASN B 487 -1  O  GLY B 486   N  GLY B 477           
SHEET    1 AB7 4 THR C  48  THR C  50  0                                        
SHEET    2 AB7 4 ASN C  37  LEU C  40 -1  N  LEU C  40   O  THR C  48           
SHEET    3 AB7 4 THR D 517  ASP D 523  1  O  VAL D 521   N  VAL C  39           
SHEET    4 AB7 4 LYS D   4  PHE D   8 -1  N  ASP D   5   O  THR D 522           
SHEET    1 AB8 3 VAL C 174  ASP C 179  0                                        
SHEET    2 AB8 3 VAL C 376  VAL C 381  1  O  ILE C 379   N  THR C 176           
SHEET    3 AB8 3 GLU C 186  VAL C 190 -1  N  VAL C 190   O  VAL C 376           
SHEET    1 AB9 6 MET C 193  PHE C 195  0                                        
SHEET    2 AB9 6 THR C 329  GLY C 335 -1  O  ILE C 332   N  MET C 193           
SHEET    3 AB9 6 GLY C 318  ASN C 326 -1  N  VAL C 324   O  THR C 331           
SHEET    4 AB9 6 PHE C 219  ASP C 224 -1  N  ILE C 220   O  GLY C 318           
SHEET    5 AB9 6 LEU C 247  ALA C 251  1  O  LEU C 248   N  LEU C 221           
SHEET    6 AB9 6 VAL C 273  LYS C 277  1  O  ALA C 274   N  ILE C 249           
SHEET    1 AC1 4 VAL C 213  GLU C 216  0                                        
SHEET    2 AC1 4 GLY C 318  ASN C 326 -1  O  ILE C 325   N  VAL C 213           
SHEET    3 AC1 4 PHE C 219  ASP C 224 -1  N  ILE C 220   O  GLY C 318           
SHEET    4 AC1 4 ILE C 301  SER C 302  1  O  ILE C 301   N  LEU C 222           
SHEET    1 AC2 2 LYS C 226  ILE C 227  0                                        
SHEET    2 AC2 2 ASP C 253  VAL C 254  1  O  ASP C 253   N  ILE C 227           
SHEET    1 AC3 2 VAL C 411  ALA C 413  0                                        
SHEET    2 AC3 2 LEU C 494  PRO C 496 -1  O  ASP C 495   N  VAL C 412           
SHEET    1 AC4 2 TYR C 476  ASN C 479  0                                        
SHEET    2 AC4 2 GLU C 484  ASN C 487 -1  O  GLY C 486   N  GLY C 477           
SHEET    1 AC5 4 THR D  48  THR D  50  0                                        
SHEET    2 AC5 4 ASN D  37  LEU D  40 -1  N  LEU D  40   O  THR D  48           
SHEET    3 AC5 4 THR E 517  ASP E 523  1  O  VAL E 521   N  VAL D  39           
SHEET    4 AC5 4 LYS E   4  PHE E   8 -1  N  ASP E   5   O  THR E 522           
SHEET    1 AC6 3 VAL D 174  ASP D 179  0                                        
SHEET    2 AC6 3 VAL D 376  VAL D 381  1  O  ILE D 379   N  THR D 176           
SHEET    3 AC6 3 GLU D 186  VAL D 190 -1  N  VAL D 190   O  VAL D 376           
SHEET    1 AC7 6 MET D 193  PHE D 195  0                                        
SHEET    2 AC7 6 THR D 329  GLY D 335 -1  O  ILE D 332   N  MET D 193           
SHEET    3 AC7 6 GLY D 318  ASN D 326 -1  N  VAL D 324   O  THR D 331           
SHEET    4 AC7 6 PHE D 219  ASP D 224 -1  N  ILE D 220   O  GLY D 318           
SHEET    5 AC7 6 LEU D 247  ALA D 251  1  O  LEU D 248   N  LEU D 221           
SHEET    6 AC7 6 VAL D 273  LYS D 277  1  O  ALA D 274   N  ILE D 249           
SHEET    1 AC8 4 VAL D 213  GLU D 216  0                                        
SHEET    2 AC8 4 GLY D 318  ASN D 326 -1  O  ILE D 325   N  VAL D 213           
SHEET    3 AC8 4 PHE D 219  ASP D 224 -1  N  ILE D 220   O  GLY D 318           
SHEET    4 AC8 4 ILE D 301  SER D 302  1  O  ILE D 301   N  LEU D 222           
SHEET    1 AC9 2 LYS D 226  ILE D 227  0                                        
SHEET    2 AC9 2 ASP D 253  VAL D 254  1  O  ASP D 253   N  ILE D 227           
SHEET    1 AD1 2 VAL D 411  ALA D 413  0                                        
SHEET    2 AD1 2 LEU D 494  PRO D 496 -1  O  ASP D 495   N  VAL D 412           
SHEET    1 AD2 2 TYR D 476  ASN D 479  0                                        
SHEET    2 AD2 2 GLU D 484  ASN D 487 -1  O  GLU D 484   N  ASN D 479           
SHEET    1 AD3 4 THR E  48  THR E  50  0                                        
SHEET    2 AD3 4 ASN E  37  LEU E  40 -1  N  LEU E  40   O  THR E  48           
SHEET    3 AD3 4 THR F 517  ASP F 523  1  O  CYS F 519   N  VAL E  39           
SHEET    4 AD3 4 LYS F   4  PHE F   8 -1  N  ASP F   5   O  THR F 522           
SHEET    1 AD4 3 VAL E 174  ASP E 179  0                                        
SHEET    2 AD4 3 VAL E 376  VAL E 381  1  O  ILE E 379   N  THR E 176           
SHEET    3 AD4 3 GLU E 186  VAL E 190 -1  N  VAL E 190   O  VAL E 376           
SHEET    1 AD5 6 MET E 193  PHE E 195  0                                        
SHEET    2 AD5 6 THR E 329  GLY E 335 -1  O  ILE E 332   N  MET E 193           
SHEET    3 AD5 6 GLY E 318  ASN E 326 -1  N  VAL E 324   O  THR E 331           
SHEET    4 AD5 6 PHE E 219  ASP E 224 -1  N  ILE E 220   O  GLY E 318           
SHEET    5 AD5 6 LEU E 247  ALA E 251  1  O  LEU E 248   N  LEU E 221           
SHEET    6 AD5 6 VAL E 273  LYS E 277  1  O  ALA E 274   N  ILE E 249           
SHEET    1 AD6 4 VAL E 213  GLU E 216  0                                        
SHEET    2 AD6 4 GLY E 318  ASN E 326 -1  O  ILE E 325   N  VAL E 213           
SHEET    3 AD6 4 PHE E 219  ASP E 224 -1  N  ILE E 220   O  GLY E 318           
SHEET    4 AD6 4 ILE E 301  SER E 302  1  O  ILE E 301   N  LEU E 222           
SHEET    1 AD7 2 LYS E 226  ILE E 227  0                                        
SHEET    2 AD7 2 ASP E 253  VAL E 254  1  O  ASP E 253   N  ILE E 227           
SHEET    1 AD8 2 VAL E 411  ALA E 413  0                                        
SHEET    2 AD8 2 LEU E 494  PRO E 496 -1  O  ASP E 495   N  VAL E 412           
SHEET    1 AD9 2 TYR E 476  ASN E 479  0                                        
SHEET    2 AD9 2 GLU E 484  ASN E 487 -1  O  GLY E 486   N  GLY E 477           
SHEET    1 AE1 4 THR F  48  THR F  50  0                                        
SHEET    2 AE1 4 ASN F  37  LEU F  40 -1  N  LEU F  40   O  THR F  48           
SHEET    3 AE1 4 THR G 517  ASP G 523  1  O  VAL G 521   N  VAL F  39           
SHEET    4 AE1 4 LYS G   4  PHE G   8 -1  N  ASP G   5   O  THR G 522           
SHEET    1 AE2 3 VAL F 174  ASP F 179  0                                        
SHEET    2 AE2 3 VAL F 376  VAL F 381  1  O  ILE F 379   N  THR F 176           
SHEET    3 AE2 3 GLU F 186  VAL F 190 -1  N  VAL F 190   O  VAL F 376           
SHEET    1 AE3 6 MET F 193  PHE F 195  0                                        
SHEET    2 AE3 6 THR F 329  GLY F 335 -1  O  ILE F 332   N  MET F 193           
SHEET    3 AE3 6 GLY F 318  ASN F 326 -1  N  VAL F 324   O  THR F 331           
SHEET    4 AE3 6 PHE F 219  ASP F 224 -1  N  ILE F 220   O  GLY F 318           
SHEET    5 AE3 6 LEU F 247  ALA F 251  1  O  LEU F 248   N  LEU F 221           
SHEET    6 AE3 6 VAL F 273  LYS F 277  1  O  ALA F 274   N  ILE F 249           
SHEET    1 AE4 4 VAL F 213  GLU F 216  0                                        
SHEET    2 AE4 4 GLY F 318  ASN F 326 -1  O  ILE F 325   N  VAL F 213           
SHEET    3 AE4 4 PHE F 219  ASP F 224 -1  N  ILE F 220   O  GLY F 318           
SHEET    4 AE4 4 ILE F 301  SER F 302  1  O  ILE F 301   N  LEU F 222           
SHEET    1 AE5 2 LYS F 226  ILE F 227  0                                        
SHEET    2 AE5 2 ASP F 253  VAL F 254  1  O  ASP F 253   N  ILE F 227           
SHEET    1 AE6 2 VAL F 411  ALA F 413  0                                        
SHEET    2 AE6 2 LEU F 494  PRO F 496 -1  O  ASP F 495   N  VAL F 412           
SHEET    1 AE7 2 TYR F 476  ASN F 479  0                                        
SHEET    2 AE7 2 GLU F 484  ASN F 487 -1  O  GLY F 486   N  GLY F 477           
SHEET    1 AE8 3 VAL G 174  ASP G 179  0                                        
SHEET    2 AE8 3 VAL G 376  VAL G 381  1  O  ILE G 379   N  THR G 176           
SHEET    3 AE8 3 GLU G 186  VAL G 190 -1  N  VAL G 190   O  VAL G 376           
SHEET    1 AE9 6 MET G 193  PHE G 195  0                                        
SHEET    2 AE9 6 THR G 329  GLY G 335 -1  O  ILE G 332   N  MET G 193           
SHEET    3 AE9 6 GLY G 318  ASN G 326 -1  N  VAL G 324   O  THR G 331           
SHEET    4 AE9 6 PHE G 219  ASP G 224 -1  N  ILE G 220   O  GLY G 318           
SHEET    5 AE9 6 LEU G 247  ALA G 251  1  O  LEU G 248   N  LEU G 221           
SHEET    6 AE9 6 VAL G 273  LYS G 277  1  O  ALA G 274   N  ILE G 249           
SHEET    1 AF1 4 VAL G 213  GLU G 216  0                                        
SHEET    2 AF1 4 GLY G 318  ASN G 326 -1  O  ILE G 325   N  VAL G 213           
SHEET    3 AF1 4 PHE G 219  ASP G 224 -1  N  ILE G 220   O  GLY G 318           
SHEET    4 AF1 4 ILE G 301  SER G 302  1  O  ILE G 301   N  LEU G 222           
SHEET    1 AF2 2 LYS G 226  ILE G 227  0                                        
SHEET    2 AF2 2 ASP G 253  VAL G 254  1  O  ASP G 253   N  ILE G 227           
SHEET    1 AF3 2 VAL G 411  ALA G 413  0                                        
SHEET    2 AF3 2 LEU G 494  PRO G 496 -1  O  ASP G 495   N  VAL G 412           
SHEET    1 AF4 2 TYR G 476  ASN G 479  0                                        
SHEET    2 AF4 2 GLU G 484  ASN G 487 -1  O  GLY G 486   N  GLY G 477           
SHEET    1 AF5 4 LYS H   4  PHE H   8  0                                        
SHEET    2 AF5 4 THR H 517  ASP H 523 -1  O  THR H 522   N  ASP H   5           
SHEET    3 AF5 4 ASN N  37  LEU N  40  1  O  VAL N  39   N  VAL H 521           
SHEET    4 AF5 4 THR N  48  THR N  50 -1  O  THR N  48   N  LEU N  40           
SHEET    1 AF6 4 THR H  48  THR H  50  0                                        
SHEET    2 AF6 4 ASN H  37  LEU H  40 -1  N  LEU H  40   O  THR H  48           
SHEET    3 AF6 4 THR I 517  ASP I 523  1  O  CYS I 519   N  VAL H  39           
SHEET    4 AF6 4 LYS I   4  PHE I   8 -1  N  ASP I   5   O  THR I 522           
SHEET    1 AF7 3 VAL H 174  ASP H 179  0                                        
SHEET    2 AF7 3 VAL H 376  VAL H 381  1  O  ILE H 379   N  THR H 176           
SHEET    3 AF7 3 GLU H 186  VAL H 190 -1  N  VAL H 190   O  VAL H 376           
SHEET    1 AF8 6 MET H 193  PHE H 195  0                                        
SHEET    2 AF8 6 THR H 329  GLY H 335 -1  O  ILE H 332   N  MET H 193           
SHEET    3 AF8 6 GLY H 318  ASN H 326 -1  N  VAL H 324   O  THR H 331           
SHEET    4 AF8 6 PHE H 219  ASP H 224 -1  N  ILE H 220   O  GLY H 318           
SHEET    5 AF8 6 LEU H 247  ALA H 251  1  O  LEU H 248   N  LEU H 221           
SHEET    6 AF8 6 VAL H 273  LYS H 277  1  O  ALA H 274   N  ILE H 249           
SHEET    1 AF9 4 VAL H 213  GLU H 216  0                                        
SHEET    2 AF9 4 GLY H 318  ASN H 326 -1  O  ILE H 325   N  VAL H 213           
SHEET    3 AF9 4 PHE H 219  ASP H 224 -1  N  ILE H 220   O  GLY H 318           
SHEET    4 AF9 4 ILE H 301  SER H 302  1  O  ILE H 301   N  LEU H 222           
SHEET    1 AG1 2 LYS H 226  ILE H 227  0                                        
SHEET    2 AG1 2 ASP H 253  VAL H 254  1  O  ASP H 253   N  ILE H 227           
SHEET    1 AG2 2 VAL H 411  ALA H 413  0                                        
SHEET    2 AG2 2 LEU H 494  PRO H 496 -1  O  ASP H 495   N  VAL H 412           
SHEET    1 AG3 2 TYR H 476  ASN H 479  0                                        
SHEET    2 AG3 2 GLU H 484  ASN H 487 -1  O  GLY H 486   N  GLY H 477           
SHEET    1 AG4 4 THR I  48  THR I  50  0                                        
SHEET    2 AG4 4 ASN I  37  LEU I  40 -1  N  LEU I  40   O  THR I  48           
SHEET    3 AG4 4 THR J 517  ASP J 523  1  O  VAL J 521   N  VAL I  39           
SHEET    4 AG4 4 LYS J   4  PHE J   8 -1  N  ASP J   5   O  THR J 522           
SHEET    1 AG5 3 VAL I 174  ASP I 179  0                                        
SHEET    2 AG5 3 VAL I 376  VAL I 381  1  O  ILE I 379   N  THR I 176           
SHEET    3 AG5 3 GLU I 186  VAL I 190 -1  N  VAL I 190   O  VAL I 376           
SHEET    1 AG6 6 MET I 193  PHE I 195  0                                        
SHEET    2 AG6 6 THR I 329  GLY I 335 -1  O  ILE I 332   N  MET I 193           
SHEET    3 AG6 6 GLY I 318  ASN I 326 -1  N  VAL I 324   O  THR I 331           
SHEET    4 AG6 6 PHE I 219  ASP I 224 -1  N  ILE I 220   O  GLY I 318           
SHEET    5 AG6 6 LEU I 247  ALA I 251  1  O  LEU I 248   N  LEU I 221           
SHEET    6 AG6 6 VAL I 273  LYS I 277  1  O  ALA I 274   N  ILE I 249           
SHEET    1 AG7 4 VAL I 213  GLU I 216  0                                        
SHEET    2 AG7 4 GLY I 318  ASN I 326 -1  O  ILE I 325   N  VAL I 213           
SHEET    3 AG7 4 PHE I 219  ASP I 224 -1  N  ILE I 220   O  GLY I 318           
SHEET    4 AG7 4 ILE I 301  SER I 302  1  O  ILE I 301   N  LEU I 222           
SHEET    1 AG8 2 LYS I 226  ILE I 227  0                                        
SHEET    2 AG8 2 ASP I 253  VAL I 254  1  O  ASP I 253   N  ILE I 227           
SHEET    1 AG9 2 VAL I 411  ALA I 413  0                                        
SHEET    2 AG9 2 LEU I 494  PRO I 496 -1  O  ASP I 495   N  VAL I 412           
SHEET    1 AH1 2 TYR I 476  ASN I 479  0                                        
SHEET    2 AH1 2 GLU I 484  ASN I 487 -1  O  GLY I 486   N  GLY I 477           
SHEET    1 AH2 4 THR J  48  THR J  50  0                                        
SHEET    2 AH2 4 ASN J  37  LEU J  40 -1  N  LEU J  40   O  THR J  48           
SHEET    3 AH2 4 THR K 517  ASP K 523  1  O  VAL K 521   N  VAL J  39           
SHEET    4 AH2 4 LYS K   4  PHE K   8 -1  N  ASP K   5   O  THR K 522           
SHEET    1 AH3 3 VAL J 174  ASP J 179  0                                        
SHEET    2 AH3 3 VAL J 376  VAL J 381  1  O  ILE J 379   N  THR J 176           
SHEET    3 AH3 3 GLU J 186  VAL J 190 -1  N  VAL J 190   O  VAL J 376           
SHEET    1 AH4 6 MET J 193  PHE J 195  0                                        
SHEET    2 AH4 6 THR J 329  GLY J 335 -1  O  ILE J 332   N  MET J 193           
SHEET    3 AH4 6 GLY J 318  ASN J 326 -1  N  VAL J 324   O  THR J 331           
SHEET    4 AH4 6 PHE J 219  ASP J 224 -1  N  ILE J 220   O  GLY J 318           
SHEET    5 AH4 6 LEU J 247  ALA J 251  1  O  LEU J 248   N  LEU J 221           
SHEET    6 AH4 6 VAL J 273  LYS J 277  1  O  ALA J 274   N  ILE J 249           
SHEET    1 AH5 4 VAL J 213  GLU J 216  0                                        
SHEET    2 AH5 4 GLY J 318  ASN J 326 -1  O  ILE J 325   N  VAL J 213           
SHEET    3 AH5 4 PHE J 219  ASP J 224 -1  N  ILE J 220   O  GLY J 318           
SHEET    4 AH5 4 ILE J 301  SER J 302  1  O  ILE J 301   N  LEU J 222           
SHEET    1 AH6 2 LYS J 226  ILE J 227  0                                        
SHEET    2 AH6 2 ASP J 253  VAL J 254  1  O  ASP J 253   N  ILE J 227           
SHEET    1 AH7 2 VAL J 411  ALA J 413  0                                        
SHEET    2 AH7 2 LEU J 494  PRO J 496 -1  O  ASP J 495   N  VAL J 412           
SHEET    1 AH8 2 TYR J 476  ASN J 479  0                                        
SHEET    2 AH8 2 GLU J 484  ASN J 487 -1  O  GLY J 486   N  GLY J 477           
SHEET    1 AH9 4 THR K  48  THR K  50  0                                        
SHEET    2 AH9 4 ASN K  37  LEU K  40 -1  N  LEU K  40   O  THR K  48           
SHEET    3 AH9 4 THR L 517  ASP L 523  1  O  VAL L 521   N  VAL K  39           
SHEET    4 AH9 4 LYS L   4  PHE L   8 -1  N  ASP L   5   O  THR L 522           
SHEET    1 AI1 3 VAL K 174  ASP K 179  0                                        
SHEET    2 AI1 3 VAL K 376  VAL K 381  1  O  ILE K 379   N  THR K 176           
SHEET    3 AI1 3 GLU K 186  VAL K 190 -1  N  VAL K 190   O  VAL K 376           
SHEET    1 AI2 6 MET K 193  PHE K 195  0                                        
SHEET    2 AI2 6 THR K 329  GLY K 335 -1  O  ILE K 332   N  MET K 193           
SHEET    3 AI2 6 GLY K 318  ASN K 326 -1  N  VAL K 324   O  THR K 331           
SHEET    4 AI2 6 PHE K 219  ASP K 224 -1  N  ILE K 220   O  GLY K 318           
SHEET    5 AI2 6 LEU K 247  ALA K 251  1  O  LEU K 248   N  LEU K 221           
SHEET    6 AI2 6 VAL K 273  LYS K 277  1  O  ALA K 274   N  ILE K 249           
SHEET    1 AI3 4 VAL K 213  GLU K 216  0                                        
SHEET    2 AI3 4 GLY K 318  ASN K 326 -1  O  ILE K 325   N  VAL K 213           
SHEET    3 AI3 4 PHE K 219  ASP K 224 -1  N  ILE K 220   O  GLY K 318           
SHEET    4 AI3 4 ILE K 301  SER K 302  1  O  ILE K 301   N  LEU K 222           
SHEET    1 AI4 2 LYS K 226  ILE K 227  0                                        
SHEET    2 AI4 2 ASP K 253  VAL K 254  1  O  ASP K 253   N  ILE K 227           
SHEET    1 AI5 2 VAL K 411  ALA K 413  0                                        
SHEET    2 AI5 2 LEU K 494  PRO K 496 -1  O  ASP K 495   N  VAL K 412           
SHEET    1 AI6 2 TYR K 476  ASN K 479  0                                        
SHEET    2 AI6 2 GLU K 484  ASN K 487 -1  O  GLY K 486   N  GLY K 477           
SHEET    1 AI7 4 THR L  48  THR L  50  0                                        
SHEET    2 AI7 4 ASN L  37  LEU L  40 -1  N  LEU L  40   O  THR L  48           
SHEET    3 AI7 4 THR M 517  ASP M 523  1  O  VAL M 521   N  VAL L  39           
SHEET    4 AI7 4 LYS M   4  PHE M   8 -1  N  ASP M   5   O  THR M 522           
SHEET    1 AI8 3 VAL L 174  ASP L 179  0                                        
SHEET    2 AI8 3 VAL L 376  VAL L 381  1  O  ILE L 379   N  THR L 176           
SHEET    3 AI8 3 GLU L 186  VAL L 190 -1  N  VAL L 190   O  VAL L 376           
SHEET    1 AI9 6 MET L 193  PHE L 195  0                                        
SHEET    2 AI9 6 THR L 329  GLY L 335 -1  O  ILE L 332   N  MET L 193           
SHEET    3 AI9 6 GLY L 318  ASN L 326 -1  N  VAL L 324   O  THR L 331           
SHEET    4 AI9 6 PHE L 219  ASP L 224 -1  N  ILE L 220   O  GLY L 318           
SHEET    5 AI9 6 LEU L 247  ALA L 251  1  O  LEU L 248   N  LEU L 221           
SHEET    6 AI9 6 VAL L 273  LYS L 277  1  O  ALA L 274   N  ILE L 249           
SHEET    1 AJ1 4 VAL L 213  GLU L 216  0                                        
SHEET    2 AJ1 4 GLY L 318  ASN L 326 -1  O  ILE L 325   N  VAL L 213           
SHEET    3 AJ1 4 PHE L 219  ASP L 224 -1  N  ILE L 220   O  GLY L 318           
SHEET    4 AJ1 4 ILE L 301  SER L 302  1  O  ILE L 301   N  LEU L 222           
SHEET    1 AJ2 2 LYS L 226  ILE L 227  0                                        
SHEET    2 AJ2 2 ASP L 253  VAL L 254  1  O  ASP L 253   N  ILE L 227           
SHEET    1 AJ3 2 VAL L 411  ALA L 413  0                                        
SHEET    2 AJ3 2 LEU L 494  PRO L 496 -1  O  ASP L 495   N  VAL L 412           
SHEET    1 AJ4 2 TYR L 476  ASN L 479  0                                        
SHEET    2 AJ4 2 GLU L 484  ASN L 487 -1  O  GLU L 484   N  ASN L 479           
SHEET    1 AJ5 4 THR M  48  THR M  50  0                                        
SHEET    2 AJ5 4 ASN M  37  LEU M  40 -1  N  LEU M  40   O  THR M  48           
SHEET    3 AJ5 4 THR N 517  ASP N 523  1  O  VAL N 521   N  VAL M  39           
SHEET    4 AJ5 4 LYS N   4  PHE N   8 -1  N  ASP N   5   O  THR N 522           
SHEET    1 AJ6 3 VAL M 174  ASP M 179  0                                        
SHEET    2 AJ6 3 VAL M 376  VAL M 381  1  O  ILE M 379   N  THR M 176           
SHEET    3 AJ6 3 GLU M 186  VAL M 190 -1  N  VAL M 190   O  VAL M 376           
SHEET    1 AJ7 6 MET M 193  PHE M 195  0                                        
SHEET    2 AJ7 6 THR M 329  GLY M 335 -1  O  ILE M 332   N  MET M 193           
SHEET    3 AJ7 6 GLY M 318  ASN M 326 -1  N  VAL M 324   O  THR M 331           
SHEET    4 AJ7 6 PHE M 219  ASP M 224 -1  N  ILE M 220   O  GLY M 318           
SHEET    5 AJ7 6 LEU M 247  ALA M 251  1  O  LEU M 248   N  LEU M 221           
SHEET    6 AJ7 6 VAL M 273  LYS M 277  1  O  ALA M 274   N  ILE M 249           
SHEET    1 AJ8 4 VAL M 213  GLU M 216  0                                        
SHEET    2 AJ8 4 GLY M 318  ASN M 326 -1  O  ILE M 325   N  VAL M 213           
SHEET    3 AJ8 4 PHE M 219  ASP M 224 -1  N  ILE M 220   O  GLY M 318           
SHEET    4 AJ8 4 ILE M 301  SER M 302  1  O  ILE M 301   N  LEU M 222           
SHEET    1 AJ9 2 LYS M 226  ILE M 227  0                                        
SHEET    2 AJ9 2 ASP M 253  VAL M 254  1  O  ASP M 253   N  ILE M 227           
SHEET    1 AK1 2 VAL M 411  ALA M 413  0                                        
SHEET    2 AK1 2 LEU M 494  PRO M 496 -1  O  ASP M 495   N  VAL M 412           
SHEET    1 AK2 2 TYR M 476  ASN M 479  0                                        
SHEET    2 AK2 2 GLU M 484  ASN M 487 -1  O  GLY M 486   N  GLY M 477           
SHEET    1 AK3 3 VAL N 174  ASP N 179  0                                        
SHEET    2 AK3 3 VAL N 376  VAL N 381  1  O  ILE N 379   N  THR N 176           
SHEET    3 AK3 3 GLU N 186  VAL N 190 -1  N  VAL N 190   O  VAL N 376           
SHEET    1 AK4 6 MET N 193  PHE N 195  0                                        
SHEET    2 AK4 6 THR N 329  GLY N 335 -1  O  ILE N 332   N  MET N 193           
SHEET    3 AK4 6 GLY N 318  ASN N 326 -1  N  VAL N 324   O  THR N 331           
SHEET    4 AK4 6 PHE N 219  ASP N 224 -1  N  ILE N 220   O  GLY N 318           
SHEET    5 AK4 6 LEU N 247  ALA N 251  1  O  LEU N 248   N  LEU N 221           
SHEET    6 AK4 6 VAL N 273  LYS N 277  1  O  ALA N 274   N  ILE N 249           
SHEET    1 AK5 4 VAL N 213  GLU N 216  0                                        
SHEET    2 AK5 4 GLY N 318  ASN N 326 -1  O  ILE N 325   N  VAL N 213           
SHEET    3 AK5 4 PHE N 219  ASP N 224 -1  N  ILE N 220   O  GLY N 318           
SHEET    4 AK5 4 ILE N 301  SER N 302  1  O  ILE N 301   N  LEU N 222           
SHEET    1 AK6 2 LYS N 226  ILE N 227  0                                        
SHEET    2 AK6 2 ASP N 253  VAL N 254  1  O  ASP N 253   N  ILE N 227           
SHEET    1 AK7 2 VAL N 411  ALA N 413  0                                        
SHEET    2 AK7 2 LEU N 494  PRO N 496 -1  O  ASP N 495   N  VAL N 412           
SHEET    1 AK8 2 TYR N 476  ASN N 479  0                                        
SHEET    2 AK8 2 GLU N 484  ASN N 487 -1  O  GLY N 486   N  GLY N 477           
SSBOND   1 CYS A  109    CYS M  109                          1555   1555  2.06  
SSBOND   2 CYS B  109    CYS L  109                          1555   1555  1.98  
SSBOND   3 CYS C  109    CYS K  109                          1555   1555  2.08  
SSBOND   4 CYS D  109    CYS J  109                          1555   1555  2.04  
SSBOND   5 CYS E  109    CYS I  109                          1555   1555  1.97  
SSBOND   6 CYS F  109    CYS H  109                          1555   1555  1.98  
SSBOND   7 CYS G  109    CYS N  109                          1555   1555  2.01  
CRYST1  135.695  262.047  149.213  90.00 100.81  90.00 P 1 21 1     28          
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      0.007369  0.000000  0.001407        0.00000                         
SCALE2      0.000000  0.003816  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006823        0.00000                         
ATOM      1  N   ALA A   2      35.786  12.568  -1.428  1.00 62.76           N  
ANISOU    1  N   ALA A   2     4656   5406  13785   1052  -1445   1977       N  
ATOM      2  CA  ALA A   2      34.957  12.123  -0.267  1.00 62.17           C  
ANISOU    2  CA  ALA A   2     4464   5229  13926   1017  -1302   1728       C  
ATOM      3  C   ALA A   2      35.600  12.525   1.056  1.00 60.77           C  
ANISOU    3  C   ALA A   2     4327   4958  13805    954  -1042   1593       C  
ATOM      4  O   ALA A   2      36.812  12.740   1.125  1.00 59.72           O  
ANISOU    4  O   ALA A   2     4334   4879  13477    916   -972   1645       O  
ATOM      5  CB  ALA A   2      34.749  10.616  -0.311  1.00 61.21           C  
ANISOU    5  CB  ALA A   2     4386   5267  13602    982  -1324   1594       C  
ATOM      6  N   ALA A   3      34.782  12.616   2.102  1.00 60.92           N  
ANISOU    6  N   ALA A   3     4217   4838  14091    947   -901   1411       N  
ATOM      7  CA  ALA A   3      35.273  12.941   3.439  1.00 60.02           C  
ANISOU    7  CA  ALA A   3     4141   4646  14017    899   -655   1246       C  
ATOM      8  C   ALA A   3      36.225  11.856   3.926  1.00 57.86           C  
ANISOU    8  C   ALA A   3     4053   4548  13384    824   -540   1151       C  
ATOM      9  O   ALA A   3      36.037  10.676   3.620  1.00 57.27           O  
ANISOU    9  O   ALA A   3     4015   4608  13135    804   -589   1127       O  
ATOM     10  CB  ALA A   3      34.118  13.105   4.411  1.00 61.04           C  
ANISOU   10  CB  ALA A   3     4100   4622  14469    915   -517   1065       C  
ATOM     11  N   LYS A   4      37.235  12.268   4.690  1.00 57.14           N  
ANISOU   11  N   LYS A   4     4064   4440  13204    786   -400   1088       N  
ATOM     12  CA  LYS A   4      38.330  11.388   5.090  1.00 55.40           C  
ANISOU   12  CA  LYS A   4     4027   4376  12643    721   -315   1024       C  
ATOM     13  C   LYS A   4      38.371  11.138   6.592  1.00 55.03           C  
ANISOU   13  C   LYS A   4     4015   4304  12587    687    -91    801       C  
ATOM     14  O   LYS A   4      37.867  11.935   7.385  1.00 56.29           O  
ANISOU   14  O   LYS A   4     4081   4318  12989    713     17    691       O  
ATOM     15  CB  LYS A   4      39.669  11.997   4.672  1.00 54.96           C  
ANISOU   15  CB  LYS A   4     4082   4346  12452    705   -355   1146       C  
ATOM     16  CG  LYS A   4      39.814  12.278   3.187  1.00 55.75           C  
ANISOU   16  CG  LYS A   4     4181   4495  12507    741   -551   1393       C  
ATOM     17  CD  LYS A   4      39.749  11.006   2.360  1.00 55.03           C  
ANISOU   17  CD  LYS A   4     4160   4601  12146    735   -662   1438       C  
ATOM     18  CE  LYS A   4      40.304  11.221   0.960  1.00 55.64           C  
ANISOU   18  CE  LYS A   4     4298   4778  12064    767   -825   1673       C  
ATOM     19  NZ  LYS A   4      39.494  12.186   0.166  1.00 57.89           N  
ANISOU   19  NZ  LYS A   4     4458   4956  12581    845   -971   1845       N  
ATOM     20  N   ASP A   5      38.981  10.015   6.961  1.00 53.67           N  
ANISOU   20  N   ASP A   5     3981   4281  12127    635    -27    737       N  
ATOM     21  CA  ASP A   5      39.301   9.690   8.344  1.00 53.30           C  
ANISOU   21  CA  ASP A   5     4017   4250  11981    605    171    556       C  
ATOM     22  C   ASP A   5      40.804   9.889   8.493  1.00 52.28           C  
ANISOU   22  C   ASP A   5     4044   4181  11638    572    167    563       C  
ATOM     23  O   ASP A   5      41.585   9.257   7.779  1.00 51.25           O  
ANISOU   23  O   ASP A   5     4010   4174  11287    541     73    663       O  
ATOM     24  CB  ASP A   5      38.918   8.234   8.646  1.00 52.68           C  
ANISOU   24  CB  ASP A   5     3978   4286  11751    572    236    499       C  
ATOM     25  CG  ASP A   5      38.784   7.947  10.137  1.00 52.89           C  
ANISOU   25  CG  ASP A   5     4049   4306  11738    560    465    325       C  
ATOM     26  OD1 ASP A   5      39.220   8.776  10.965  1.00 53.49           O  
ANISOU   26  OD1 ASP A   5     4166   4326  11832    575    560    225       O  
ATOM     27  OD2 ASP A   5      38.236   6.875  10.479  1.00 52.64           O  
ANISOU   27  OD2 ASP A   5     4012   4329  11659    540    550    289       O  
ATOM     28  N   VAL A   6      41.209  10.765   9.408  1.00 53.02           N  
ANISOU   28  N   VAL A   6     4151   4181  11811    581    266    446       N  
ATOM     29  CA  VAL A   6      42.623  11.094   9.592  1.00 52.49           C  
ANISOU   29  CA  VAL A   6     4202   4138  11601    553    252    436       C  
ATOM     30  C   VAL A   6      43.076  10.727  11.004  1.00 52.45           C  
ANISOU   30  C   VAL A   6     4310   4180  11436    538    399    232       C  
ATOM     31  O   VAL A   6      42.498  11.195  11.983  1.00 53.64           O  
ANISOU   31  O   VAL A   6     4417   4250  11712    571    523     74       O  
ATOM     32  CB  VAL A   6      42.884  12.595   9.343  1.00 53.78           C  
ANISOU   32  CB  VAL A   6     4277   4133  12023    581    201    479       C  
ATOM     33  CG1 VAL A   6      44.377  12.896   9.371  1.00 53.14           C  
ANISOU   33  CG1 VAL A   6     4296   4067  11826    547    171    491       C  
ATOM     34  CG2 VAL A   6      42.287  13.028   8.012  1.00 54.63           C  
ANISOU   34  CG2 VAL A   6     4268   4186  12300    611     60    695       C  
ATOM     35  N   LYS A   7      44.109   9.891  11.098  1.00 51.57           N  
ANISOU   35  N   LYS A   7     4347   4203  11045    496    383    236       N  
ATOM     36  CA  LYS A   7      44.696   9.508  12.385  1.00 51.75           C  
ANISOU   36  CA  LYS A   7     4497   4285  10880    487    491     65       C  
ATOM     37  C   LYS A   7      46.159   9.931  12.458  1.00 51.52           C  
ANISOU   37  C   LYS A   7     4553   4256  10765    466    422     44       C  
ATOM     38  O   LYS A   7      46.828  10.052  11.432  1.00 50.63           O  
ANISOU   38  O   LYS A   7     4431   4149  10654    441    308    193       O  
ATOM     39  CB  LYS A   7      44.565   8.002  12.609  1.00 50.95           C  
ANISOU   39  CB  LYS A   7     4488   4332  10536    458    541     74       C  
ATOM     40  CG  LYS A   7      43.155   7.570  12.972  1.00 52.15           C  
ANISOU   40  CG  LYS A   7     4560   4470  10785    479    660     40       C  
ATOM     41  CD  LYS A   7      43.095   6.106  13.371  1.00 51.75           C  
ANISOU   41  CD  LYS A   7     4599   4545  10516    450    732     44       C  
ATOM     42  CE  LYS A   7      41.676   5.695  13.734  1.00 53.30           C  
ANISOU   42  CE  LYS A   7     4694   4709  10847    467    869     19       C  
ATOM     43  NZ  LYS A   7      41.230   6.240  15.048  1.00 55.01           N  
ANISOU   43  NZ  LYS A   7     4917   4879  11103    510   1061   -138       N  
ATOM     44  N   PHE A   8      46.643  10.151  13.679  1.00 52.47           N  
ANISOU   44  N   PHE A   8     4752   4371  10811    481    494   -143       N  
ATOM     45  CA  PHE A   8      47.985  10.683  13.909  1.00 52.76           C  
ANISOU   45  CA  PHE A   8     4846   4380  10821    468    424   -205       C  
ATOM     46  C   PHE A   8      48.787   9.848  14.900  1.00 52.98           C  
ANISOU   46  C   PHE A   8     5037   4532  10558    459    450   -328       C  
ATOM     47  O   PHE A   8      48.225   9.202  15.785  1.00 53.29           O  
ANISOU   47  O   PHE A   8     5148   4650  10449    481    560   -420       O  
ATOM     48  CB  PHE A   8      47.897  12.113  14.447  1.00 54.24           C  
ANISOU   48  CB  PHE A   8     4944   4396  11268    510    442   -350       C  
ATOM     49  CG  PHE A   8      47.247  13.081  13.504  1.00 54.78           C  
ANISOU   49  CG  PHE A   8     4844   4314  11656    523    400   -221       C  
ATOM     50  CD1 PHE A   8      47.999  13.737  12.542  1.00 54.68           C  
ANISOU   50  CD1 PHE A   8     4772   4218  11786    499    289    -69       C  
ATOM     51  CD2 PHE A   8      45.888  13.345  13.585  1.00 55.65           C  
ANISOU   51  CD2 PHE A   8     4848   4359  11936    563    475   -241       C  
ATOM     52  CE1 PHE A   8      47.406  14.633  11.673  1.00 55.58           C  
ANISOU   52  CE1 PHE A   8     4737   4193  12188    518    245     75       C  
ATOM     53  CE2 PHE A   8      45.289  14.242  12.718  1.00 56.51           C  
ANISOU   53  CE2 PHE A   8     4798   4322  12349    583    418   -113       C  
ATOM     54  CZ  PHE A   8      46.049  14.888  11.760  1.00 56.49           C  
ANISOU   54  CZ  PHE A   8     4751   4243  12470    562    299     52       C  
ATOM     55  N   GLY A   9      50.108   9.887  14.745  1.00 53.55           N  
ANISOU   55  N   GLY A   9     5164   4616  10566    430    352   -321       N  
ATOM     56  CA  GLY A   9      51.045   9.331  15.718  1.00 54.50           C  
ANISOU   56  CA  GLY A   9     5427   4826  10452    430    340   -454       C  
ATOM     57  C   GLY A   9      50.725   7.933  16.214  1.00 54.91           C  
ANISOU   57  C   GLY A   9     5601   5036  10226    428    410   -442       C  
ATOM     58  O   GLY A   9      50.405   7.045  15.428  1.00 53.91           O  
ANISOU   58  O   GLY A   9     5465   4977  10040    394    406   -285       O  
ATOM     59  N   ASN A  10      50.810   7.748  17.529  1.00 57.11           N  
ANISOU   59  N   ASN A  10     5992   5371  10337    468    471   -610       N  
ATOM     60  CA  ASN A  10      50.634   6.439  18.160  1.00 57.56           C  
ANISOU   60  CA  ASN A  10     6178   5571  10120    471    544   -593       C  
ATOM     61  C   ASN A  10      49.329   5.770  17.750  1.00 57.40           C  
ANISOU   61  C   ASN A  10     6099   5576  10134    460    657   -470       C  
ATOM     62  O   ASN A  10      49.307   4.582  17.434  1.00 56.12           O  
ANISOU   62  O   ASN A  10     5977   5499   9846    426    659   -350       O  
ATOM     63  CB  ASN A  10      50.700   6.577  19.685  1.00 59.88           C  
ANISOU   63  CB  ASN A  10     6594   5915  10241    536    615   -794       C  
ATOM     64  CG  ASN A  10      50.952   5.251  20.383  1.00 60.58           C  
ANISOU   64  CG  ASN A  10     6845   6154  10019    540    651   -760       C  
ATOM     65  OD1 ASN A  10      50.116   4.347  20.346  1.00 60.68           O  
ANISOU   65  OD1 ASN A  10     6864   6224   9966    529    767   -648       O  
ATOM     66  ND2 ASN A  10      52.106   5.134  21.038  1.00 61.52           N  
ANISOU   66  ND2 ASN A  10     7084   6326   9964    559    546   -853       N  
ATOM     67  N   ASP A  11      48.250   6.546  17.753  1.00 58.98           N  
ANISOU   67  N   ASP A  11     6187   5687  10534    489    746   -508       N  
ATOM     68  CA  ASP A  11      46.934   6.064  17.338  1.00 59.40           C  
ANISOU   68  CA  ASP A  11     6149   5736  10683    483    845   -407       C  
ATOM     69  C   ASP A  11      46.970   5.471  15.923  1.00 57.32           C  
ANISOU   69  C   ASP A  11     5818   5484  10476    428    731   -215       C  
ATOM     70  O   ASP A  11      46.314   4.468  15.647  1.00 56.41           O  
ANISOU   70  O   ASP A  11     5686   5419  10328    408    775   -125       O  
ATOM     71  CB  ASP A  11      45.918   7.213  17.420  1.00 61.92           C  
ANISOU   71  CB  ASP A  11     6331   5928  11266    525    923   -486       C  
ATOM     72  CG  ASP A  11      44.483   6.757  17.210  1.00 63.47           C  
ANISOU   72  CG  ASP A  11     6423   6109  11583    528   1042   -415       C  
ATOM     73  OD1 ASP A  11      44.190   5.551  17.375  1.00 64.04           O  
ANISOU   73  OD1 ASP A  11     6547   6273  11511    507   1112   -346       O  
ATOM     74  OD2 ASP A  11      43.640   7.621  16.888  1.00 64.80           O  
ANISOU   74  OD2 ASP A  11     6443   6159  12018    553   1063   -430       O  
ATOM     75  N   ALA A  12      47.742   6.097  15.038  1.00 56.59           N  
ANISOU   75  N   ALA A  12     5685   5344  10472    408    590   -158       N  
ATOM     76  CA  ALA A  12      47.900   5.623  13.661  1.00 55.15           C  
ANISOU   76  CA  ALA A  12     5454   5190  10309    366    478     14       C  
ATOM     77  C   ALA A  12      48.869   4.447  13.547  1.00 53.51           C  
ANISOU   77  C   ALA A  12     5359   5100   9870    328    421     59       C  
ATOM     78  O   ALA A  12      48.661   3.557  12.726  1.00 52.56           O  
ANISOU   78  O   ALA A  12     5220   5040   9710    301    380    167       O  
ATOM     79  CB  ALA A  12      48.359   6.764  12.764  1.00 55.44           C  
ANISOU   79  CB  ALA A  12     5408   5134  10522    365    372     79       C  
ATOM     80  N   ARG A  13      49.929   4.453  14.355  1.00 53.40           N  
ANISOU   80  N   ARG A  13     5456   5115   9719    329    407    -35       N  
ATOM     81  CA  ARG A  13      50.954   3.401  14.295  1.00 52.20           C  
ANISOU   81  CA  ARG A  13     5403   5059   9369    297    343      0       C  
ATOM     82  C   ARG A  13      50.447   2.049  14.800  1.00 51.26           C  
ANISOU   82  C   ARG A  13     5350   5026   9097    292    421     20       C  
ATOM     83  O   ARG A  13      50.745   1.018  14.200  1.00 49.55           O  
ANISOU   83  O   ARG A  13     5149   4872   8806    258    369    105       O  
ATOM     84  CB  ARG A  13      52.214   3.812  15.070  1.00 53.01           C  
ANISOU   84  CB  ARG A  13     5593   5156   9390    306    289   -115       C  
ATOM     85  CG  ARG A  13      52.944   5.010  14.471  1.00 53.59           C  
ANISOU   85  CG  ARG A  13     5589   5132   9638    298    201   -116       C  
ATOM     86  CD  ARG A  13      54.292   5.277  15.132  1.00 54.05           C  
ANISOU   86  CD  ARG A  13     5715   5179   9640    301    124   -231       C  
ATOM     87  NE  ARG A  13      54.671   6.679  15.261  1.00 55.24           N  
ANISOU   87  NE  ARG A  13     5794   5199   9994    317     86   -322       N  
ATOM     88  CZ  ARG A  13      54.423   7.546  16.197  1.00 56.77           C  
ANISOU   88  CZ  ARG A  13     5986   5322  10260    362    115   -490       C  
ATOM     89  NH1 ARG A  13      53.661   7.301  17.227  1.00 57.34           N  
ANISOU   89  NH1 ARG A  13     6133   5448  10206    407    207   -599       N  
ATOM     90  NH2 ARG A  13      54.934   8.747  15.969  1.00 58.01           N  
ANISOU   90  NH2 ARG A  13     6047   5342  10651    361     56   -534       N  
ATOM     91  N   VAL A  14      49.682   2.055  15.891  1.00 52.14           N  
ANISOU   91  N   VAL A  14     5496   5137   9175    328    554    -57       N  
ATOM     92  CA  VAL A  14      49.099   0.813  16.421  1.00 52.27           C  
ANISOU   92  CA  VAL A  14     5564   5220   9075    325    657    -15       C  
ATOM     93  C   VAL A  14      48.118   0.171  15.436  1.00 51.57           C  
ANISOU   93  C   VAL A  14     5356   5116   9122    295    666     99       C  
ATOM     94  O   VAL A  14      47.960  -1.049  15.428  1.00 51.51           O  
ANISOU   94  O   VAL A  14     5369   5154   9048    272    691    164       O  
ATOM     95  CB  VAL A  14      48.392   0.998  17.791  1.00 54.08           C  
ANISOU   95  CB  VAL A  14     5851   5457   9239    376    831   -109       C  
ATOM     96  CG1 VAL A  14      49.382   1.469  18.851  1.00 54.80           C  
ANISOU   96  CG1 VAL A  14     6081   5586   9155    416    803   -241       C  
ATOM     97  CG2 VAL A  14      47.192   1.936  17.692  1.00 55.29           C  
ANISOU   97  CG2 VAL A  14     5874   5521   9611    402    926   -150       C  
ATOM     98  N   LYS A  15      47.462   0.991  14.617  1.00 51.42           N  
ANISOU   98  N   LYS A  15     5206   5025   9305    299    636    119       N  
ATOM     99  CA  LYS A  15      46.586   0.484  13.563  1.00 50.97           C  
ANISOU   99  CA  LYS A  15     5027   4954   9383    279    601    214       C  
ATOM    100  C   LYS A  15      47.380  -0.270  12.500  1.00 49.45           C  
ANISOU  100  C   LYS A  15     4851   4826   9111    241    456    293       C  
ATOM    101  O   LYS A  15      46.974  -1.346  12.075  1.00 48.99           O  
ANISOU  101  O   LYS A  15     4758   4797   9057    219    442    342       O  
ATOM    102  CB  LYS A  15      45.790   1.620  12.912  1.00 51.87           C  
ANISOU  102  CB  LYS A  15     5005   4979   9725    302    575    224       C  
ATOM    103  CG  LYS A  15      44.672   2.177  13.779  1.00 53.55           C  
ANISOU  103  CG  LYS A  15     5155   5116  10073    340    732    148       C  
ATOM    104  CD  LYS A  15      43.509   1.205  13.889  1.00 54.16           C  
ANISOU  104  CD  LYS A  15     5159   5191  10228    332    834    182       C  
ATOM    105  CE  LYS A  15      42.292   1.870  14.504  1.00 56.05           C  
ANISOU  105  CE  LYS A  15     5296   5341  10659    371    988    117       C  
ATOM    106  NZ  LYS A  15      41.209   0.887  14.775  1.00 57.15           N  
ANISOU  106  NZ  LYS A  15     5360   5469  10884    360   1119    148       N  
ATOM    107  N   MET A  16      48.511   0.291  12.080  1.00 48.83           N  
ANISOU  107  N   MET A  16     4815   4762   8975    235    354    297       N  
ATOM    108  CA  MET A  16      49.372  -0.372  11.099  1.00 47.79           C  
ANISOU  108  CA  MET A  16     4702   4698   8755    204    235    360       C  
ATOM    109  C   MET A  16      49.986  -1.648  11.668  1.00 47.17           C  
ANISOU  109  C   MET A  16     4721   4684   8517    182    249    343       C  
ATOM    110  O   MET A  16      50.032  -2.671  10.986  1.00 46.32           O  
ANISOU  110  O   MET A  16     4595   4622   8381    159    195    386       O  
ATOM    111  CB  MET A  16      50.488   0.559  10.628  1.00 47.62           C  
ANISOU  111  CB  MET A  16     4698   4668   8727    202    153    373       C  
ATOM    112  CG  MET A  16      50.010   1.753   9.824  1.00 48.20           C  
ANISOU  112  CG  MET A  16     4671   4676   8966    223    118    431       C  
ATOM    113  SD  MET A  16      51.374   2.714   9.141  1.00 48.33           S  
ANISOU  113  SD  MET A  16     4694   4674   8995    213     38    485       S  
ATOM    114  CE  MET A  16      52.054   3.452  10.625  1.00 49.12           C  
ANISOU  114  CE  MET A  16     4856   4698   9108    222     92    340       C  
ATOM    115  N   LEU A  17      50.459  -1.574  12.912  1.00 47.70           N  
ANISOU  115  N   LEU A  17     4888   4751   8482    195    313    276       N  
ATOM    116  CA  LEU A  17      51.017  -2.733  13.614  1.00 47.85           C  
ANISOU  116  CA  LEU A  17     5009   4823   8349    184    328    272       C  
ATOM    117  C   LEU A  17      50.004  -3.863  13.673  1.00 48.42           C  
ANISOU  117  C   LEU A  17     5040   4896   8458    172    404    325       C  
ATOM    118  O   LEU A  17      50.332  -5.019  13.399  1.00 47.89           O  
ANISOU  118  O   LEU A  17     4985   4860   8348    147    362    365       O  
ATOM    119  CB  LEU A  17      51.449  -2.348  15.033  1.00 48.91           C  
ANISOU  119  CB  LEU A  17     5260   4962   8362    217    388    190       C  
ATOM    120  CG  LEU A  17      52.050  -3.443  15.925  1.00 49.13           C  
ANISOU  120  CG  LEU A  17     5411   5045   8212    220    399    198       C  
ATOM    121  CD1 LEU A  17      53.297  -4.056  15.302  1.00 48.01           C  
ANISOU  121  CD1 LEU A  17     5288   4932   8019    190    259    223       C  
ATOM    122  CD2 LEU A  17      52.364  -2.882  17.305  1.00 50.30           C  
ANISOU  122  CD2 LEU A  17     5678   5209   8223    270    447    104       C  
ATOM    123  N   ARG A  18      48.771  -3.527  14.035  1.00 50.08           N  
ANISOU  123  N   ARG A  18     5188   5061   8776    191    521    320       N  
ATOM    124  CA  ARG A  18      47.704  -4.514  14.057  1.00 51.34           C  
ANISOU  124  CA  ARG A  18     5278   5199   9028    177    605    371       C  
ATOM    125  C   ARG A  18      47.503  -5.169  12.697  1.00 50.07           C  
ANISOU  125  C   ARG A  18     5011   5039   8973    147    484    413       C  
ATOM    126  O   ARG A  18      47.279  -6.376  12.613  1.00 49.92           O  
ANISOU  126  O   ARG A  18     4966   5018   8983    123    491    448       O  
ATOM    127  CB  ARG A  18      46.382  -3.907  14.495  1.00 53.54           C  
ANISOU  127  CB  ARG A  18     5475   5416   9451    203    746    352       C  
ATOM    128  CG  ARG A  18      45.297  -4.999  14.466  1.00 55.35           C  
ANISOU  128  CG  ARG A  18     5608   5606   9815    182    834    411       C  
ATOM    129  CD  ARG A  18      43.934  -4.481  15.142  1.00 57.81           C  
ANISOU  129  CD  ARG A  18     5834   5849  10280    210   1022    391       C  
ATOM    130  NE  ARG A  18      43.742  -4.921  16.541  1.00 60.13           N  
ANISOU  130  NE  ARG A  18     6221   6160  10466    227   1228    407       N  
ATOM    131  CZ  ARG A  18      44.439  -4.437  17.573  1.00 61.42           C  
ANISOU  131  CZ  ARG A  18     6541   6383  10410    264   1287    357       C  
ATOM    132  NH1 ARG A  18      45.391  -3.523  17.383  1.00 60.74           N  
ANISOU  132  NH1 ARG A  18     6524   6327  10226    279   1155    282       N  
ATOM    133  NH2 ARG A  18      44.197  -4.875  18.805  1.00 63.32           N  
ANISOU  133  NH2 ARG A  18     6873   6654  10530    289   1477    384       N  
ATOM    134  N   GLY A  19      47.538  -4.350  11.651  1.00 49.07           N  
ANISOU  134  N   GLY A  19     4820   4912   8910    153    375    410       N  
ATOM    135  CA  GLY A  19      47.325  -4.812  10.288  1.00 48.15           C  
ANISOU  135  CA  GLY A  19     4611   4817   8866    140    247    438       C  
ATOM    136  C   GLY A  19      48.405  -5.746   9.782  1.00 46.83           C  
ANISOU  136  C   GLY A  19     4500   4717   8575    116    150    440       C  
ATOM    137  O   GLY A  19      48.102  -6.791   9.212  1.00 46.79           O  
ANISOU  137  O   GLY A  19     4436   4720   8620    100     99    440       O  
ATOM    138  N   VAL A  20      49.664  -5.364   9.982  1.00 45.77           N  
ANISOU  138  N   VAL A  20     4466   4621   8301    114    120    430       N  
ATOM    139  CA  VAL A  20      50.799  -6.193   9.555  1.00 44.80           C  
ANISOU  139  CA  VAL A  20     4392   4556   8071     94     37    424       C  
ATOM    140  C   VAL A  20      50.921  -7.472  10.378  1.00 44.15           C  
ANISOU  140  C   VAL A  20     4355   4462   7956     77     85    423       C  
ATOM    141  O   VAL A  20      51.410  -8.478   9.874  1.00 43.65           O  
ANISOU  141  O   VAL A  20     4284   4424   7876     59     17    415       O  
ATOM    142  CB  VAL A  20      52.147  -5.417   9.552  1.00 44.84           C  
ANISOU  142  CB  VAL A  20     4473   4590   7972     96     -6    414       C  
ATOM    143  CG1 VAL A  20      52.070  -4.213   8.626  1.00 45.15           C  
ANISOU  143  CG1 VAL A  20     4459   4632   8062    112    -51    445       C  
ATOM    144  CG2 VAL A  20      52.566  -4.994  10.955  1.00 45.42           C  
ANISOU  144  CG2 VAL A  20     4642   4633   7983    107     65    380       C  
ATOM    145  N   ASN A  21      50.473  -7.440  11.630  1.00 44.16           N  
ANISOU  145  N   ASN A  21     4405   4424   7950     86    208    433       N  
ATOM    146  CA  ASN A  21      50.426  -8.656  12.443  1.00 44.25           C  
ANISOU  146  CA  ASN A  21     4454   4416   7940     75    273    466       C  
ATOM    147  C   ASN A  21      49.470  -9.698  11.860  1.00 44.21           C  
ANISOU  147  C   ASN A  21     4327   4368   8101     53    275    489       C  
ATOM    148  O   ASN A  21      49.794 -10.881  11.827  1.00 44.64           O  
ANISOU  148  O   ASN A  21     4379   4410   8170     33    246    505       O  
ATOM    149  CB  ASN A  21      50.049  -8.341  13.897  1.00 45.33           C  
ANISOU  149  CB  ASN A  21     4674   4535   8014    100    424    484       C  
ATOM    150  CG  ASN A  21      51.209  -7.770  14.697  1.00 45.49           C  
ANISOU  150  CG  ASN A  21     4835   4597   7850    124    398    448       C  
ATOM    151  OD1 ASN A  21      52.377  -8.007  14.385  1.00 45.08           O  
ANISOU  151  OD1 ASN A  21     4825   4575   7726    114    282    431       O  
ATOM    152  ND2 ASN A  21      50.890  -7.020  15.745  1.00 46.57           N  
ANISOU  152  ND2 ASN A  21     5038   4735   7919    160    504    421       N  
ATOM    153  N   VAL A  22      48.306  -9.258  11.385  1.00 44.04           N  
ANISOU  153  N   VAL A  22     4193   4312   8227     58    297    482       N  
ATOM    154  CA  VAL A  22      47.327 -10.172  10.788  1.00 44.13           C  
ANISOU  154  CA  VAL A  22     4065   4270   8430     40    279    483       C  
ATOM    155  C   VAL A  22      47.872 -10.792   9.499  1.00 43.37           C  
ANISOU  155  C   VAL A  22     3925   4219   8334     29    106    432       C  
ATOM    156  O   VAL A  22      47.676 -11.981   9.250  1.00 43.74           O  
ANISOU  156  O   VAL A  22     3904   4228   8487      9     75    418       O  
ATOM    157  CB  VAL A  22      45.974  -9.475  10.514  1.00 44.78           C  
ANISOU  157  CB  VAL A  22     4023   4302   8686     55    317    475       C  
ATOM    158  CG1 VAL A  22      45.032 -10.391   9.743  1.00 45.38           C  
ANISOU  158  CG1 VAL A  22     3938   4321   8981     39    256    453       C  
ATOM    159  CG2 VAL A  22      45.325  -9.046  11.823  1.00 45.71           C  
ANISOU  159  CG2 VAL A  22     4169   4371   8828     67    516    512       C  
ATOM    160  N   LEU A  23      48.557  -9.989   8.689  1.00 42.62           N  
ANISOU  160  N   LEU A  23     3864   4202   8127     46      3    405       N  
ATOM    161  CA  LEU A  23      49.201 -10.495   7.475  1.00 42.27           C  
ANISOU  161  CA  LEU A  23     3798   4224   8036     45   -142    354       C  
ATOM    162  C   LEU A  23      50.344 -11.445   7.819  1.00 41.67           C  
ANISOU  162  C   LEU A  23     3795   4159   7878     25   -151    342       C  
ATOM    163  O   LEU A  23      50.383 -12.577   7.345  1.00 41.70           O  
ANISOU  163  O   LEU A  23     3741   4151   7949     13   -213    296       O  
ATOM    164  CB  LEU A  23      49.737  -9.345   6.616  1.00 41.78           C  
ANISOU  164  CB  LEU A  23     3767   4245   7862     70   -217    356       C  
ATOM    165  CG  LEU A  23      50.598  -9.739   5.407  1.00 41.51           C  
ANISOU  165  CG  LEU A  23     3737   4304   7728     77   -339    311       C  
ATOM    166  CD1 LEU A  23      49.866 -10.700   4.484  1.00 42.26           C  
ANISOU  166  CD1 LEU A  23     3726   4410   7919     85   -438    240       C  
ATOM    167  CD2 LEU A  23      51.034  -8.506   4.636  1.00 41.44           C  
ANISOU  167  CD2 LEU A  23     3758   4370   7617    103   -380    350       C  
ATOM    168  N   ALA A  24      51.268 -10.966   8.646  1.00 41.10           N  
ANISOU  168  N   ALA A  24     3839   4101   7675     26   -102    373       N  
ATOM    169  CA  ALA A  24      52.457 -11.728   9.018  1.00 40.68           C  
ANISOU  169  CA  ALA A  24     3858   4056   7542     14   -125    366       C  
ATOM    170  C   ALA A  24      52.117 -13.055   9.689  1.00 41.28           C  
ANISOU  170  C   ALA A  24     3913   4056   7715     -3    -79    395       C  
ATOM    171  O   ALA A  24      52.675 -14.091   9.327  1.00 41.72           O  
ANISOU  171  O   ALA A  24     3944   4102   7805    -14   -146    362       O  
ATOM    172  CB  ALA A  24      53.349 -10.897   9.927  1.00 40.36           C  
ANISOU  172  CB  ALA A  24     3937   4031   7366     25    -88    389       C  
ATOM    173  N   ASP A  25      51.206 -13.023  10.660  1.00 41.90           N  
ANISOU  173  N   ASP A  25     3994   4074   7850     -3     44    459       N  
ATOM    174  CA  ASP A  25      50.828 -14.231  11.399  1.00 42.92           C  
ANISOU  174  CA  ASP A  25     4104   4120   8082    -19    117    522       C  
ATOM    175  C   ASP A  25      50.166 -15.270  10.491  1.00 43.54           C  
ANISOU  175  C   ASP A  25     4030   4140   8373    -41     56    477       C  
ATOM    176  O   ASP A  25      50.342 -16.474  10.691  1.00 43.98           O  
ANISOU  176  O   ASP A  25     4056   4127   8526    -58     52    499       O  
ATOM    177  CB  ASP A  25      49.881 -13.897  12.563  1.00 43.83           C  
ANISOU  177  CB  ASP A  25     4246   4191   8214    -10    292    607       C  
ATOM    178  CG  ASP A  25      50.532 -13.027  13.633  1.00 43.75           C  
ANISOU  178  CG  ASP A  25     4396   4237   7989     19    351    634       C  
ATOM    179  OD1 ASP A  25      51.778 -12.959  13.691  1.00 43.53           O  
ANISOU  179  OD1 ASP A  25     4459   4257   7821     27    261    610       O  
ATOM    180  OD2 ASP A  25      49.788 -12.401  14.420  1.00 44.33           O  
ANISOU  180  OD2 ASP A  25     4495   4303   8043     38    487    666       O  
ATOM    181  N   ALA A  26      49.405 -14.801   9.504  1.00 43.49           N  
ANISOU  181  N   ALA A  26     3922   4152   8449    -36     -1    410       N  
ATOM    182  CA  ALA A  26      48.756 -15.683   8.531  1.00 44.05           C  
ANISOU  182  CA  ALA A  26     3841   4177   8718    -47    -92    333       C  
ATOM    183  C   ALA A  26      49.760 -16.315   7.573  1.00 43.36           C  
ANISOU  183  C   ALA A  26     3752   4145   8577    -44   -239    234       C  
ATOM    184  O   ALA A  26      49.610 -17.470   7.180  1.00 43.92           O  
ANISOU  184  O   ALA A  26     3725   4153   8808    -57   -298    173       O  
ATOM    185  CB  ALA A  26      47.701 -14.916   7.748  1.00 44.50           C  
ANISOU  185  CB  ALA A  26     3800   4252   8852    -30   -136    287       C  
ATOM    186  N   VAL A  27      50.778 -15.549   7.200  1.00 42.37           N  
ANISOU  186  N   VAL A  27     3723   4130   8245    -25   -289    213       N  
ATOM    187  CA  VAL A  27      51.779 -15.997   6.238  1.00 42.05           C  
ANISOU  187  CA  VAL A  27     3684   4159   8133    -16   -407    116       C  
ATOM    188  C   VAL A  27      52.881 -16.830   6.902  1.00 41.76           C  
ANISOU  188  C   VAL A  27     3705   4081   8078    -31   -393    135       C  
ATOM    189  O   VAL A  27      53.310 -17.840   6.344  1.00 41.96           O  
ANISOU  189  O   VAL A  27     3673   4090   8177    -34   -470     49       O  
ATOM    190  CB  VAL A  27      52.387 -14.791   5.483  1.00 41.52           C  
ANISOU  190  CB  VAL A  27     3680   4221   7873      9   -451    100       C  
ATOM    191  CG1 VAL A  27      53.589 -15.201   4.646  1.00 41.37           C  
ANISOU  191  CG1 VAL A  27     3678   4281   7760     20   -532     15       C  
ATOM    192  CG2 VAL A  27      51.333 -14.144   4.596  1.00 42.05           C  
ANISOU  192  CG2 VAL A  27     3675   4331   7969     33   -503     75       C  
ATOM    193  N   LYS A  28      53.325 -16.423   8.091  1.00 41.39           N  
ANISOU  193  N   LYS A  28     3768   4016   7940    -35   -305    238       N  
ATOM    194  CA  LYS A  28      54.507 -17.030   8.716  1.00 41.16           C  
ANISOU  194  CA  LYS A  28     3810   3962   7864    -39   -317    262       C  
ATOM    195  C   LYS A  28      54.309 -18.459   9.239  1.00 42.05           C  
ANISOU  195  C   LYS A  28     3871   3955   8151    -56   -302    300       C  
ATOM    196  O   LYS A  28      55.290 -19.140   9.534  1.00 42.34           O  
ANISOU  196  O   LYS A  28     3938   3961   8185    -55   -341    306       O  
ATOM    197  CB  LYS A  28      55.081 -16.124   9.821  1.00 40.67           C  
ANISOU  197  CB  LYS A  28     3887   3927   7639    -27   -255    346       C  
ATOM    198  CG  LYS A  28      54.333 -16.114  11.151  1.00 41.33           C  
ANISOU  198  CG  LYS A  28     4024   3949   7727    -26   -131    462       C  
ATOM    199  CD  LYS A  28      54.694 -14.907  11.998  1.00 41.16           C  
ANISOU  199  CD  LYS A  28     4129   3981   7526     -3    -83    497       C  
ATOM    200  CE  LYS A  28      54.234 -15.083  13.441  1.00 42.34           C  
ANISOU  200  CE  LYS A  28     4362   4089   7634     10     37    608       C  
ATOM    201  NZ  LYS A  28      54.849 -14.071  14.346  1.00 42.51           N  
ANISOU  201  NZ  LYS A  28     4522   4168   7462     42     52    612       N  
ATOM    202  N   VAL A  29      53.063 -18.915   9.348  1.00 43.11           N  
ANISOU  202  N   VAL A  29     3913   4007   8458    -71   -246    330       N  
ATOM    203  CA  VAL A  29      52.794 -20.312   9.727  1.00 44.49           C  
ANISOU  203  CA  VAL A  29     4009   4044   8849    -91   -228    371       C  
ATOM    204  C   VAL A  29      53.236 -21.311   8.650  1.00 44.98           C  
ANISOU  204  C   VAL A  29     3961   4080   9048    -95   -362    225       C  
ATOM    205  O   VAL A  29      53.482 -22.478   8.954  1.00 45.96           O  
ANISOU  205  O   VAL A  29     4036   4090   9335   -107   -374    248       O  
ATOM    206  CB  VAL A  29      51.306 -20.575  10.087  1.00 45.65           C  
ANISOU  206  CB  VAL A  29     4058   4089   9195   -111   -123    440       C  
ATOM    207  CG1 VAL A  29      50.906 -19.785  11.326  1.00 45.88           C  
ANISOU  207  CG1 VAL A  29     4199   4133   9099   -103     37    589       C  
ATOM    208  CG2 VAL A  29      50.375 -20.273   8.917  1.00 45.63           C  
ANISOU  208  CG2 VAL A  29     3925   4112   9300   -111   -193    311       C  
ATOM    209  N   THR A  30      53.342 -20.854   7.403  1.00 44.70           N  
ANISOU  209  N   THR A  30     3889   4150   8945    -78   -460     77       N  
ATOM    210  CA  THR A  30      53.754 -21.719   6.292  1.00 45.27           C  
ANISOU  210  CA  THR A  30     3862   4224   9112    -70   -585    -92       C  
ATOM    211  C   THR A  30      55.273 -21.887   6.168  1.00 45.05           C  
ANISOU  211  C   THR A  30     3901   4245   8968    -56   -633   -136       C  
ATOM    212  O   THR A  30      55.741 -22.716   5.387  1.00 45.61           O  
ANISOU  212  O   THR A  30     3893   4307   9129    -47   -721   -278       O  
ATOM    213  CB  THR A  30      53.230 -21.181   4.944  1.00 45.20           C  
ANISOU  213  CB  THR A  30     3794   4328   9049    -46   -673   -236       C  
ATOM    214  OG1 THR A  30      53.809 -19.898   4.674  1.00 43.89           O  
ANISOU  214  OG1 THR A  30     3742   4312   8620    -24   -662   -213       O  
ATOM    215  CG2 THR A  30      51.710 -21.064   4.960  1.00 45.99           C  
ANISOU  215  CG2 THR A  30     3801   4368   9303    -55   -651   -216       C  
ATOM    216  N   LEU A  31      56.036 -21.106   6.932  1.00 44.58           N  
ANISOU  216  N   LEU A  31     3976   4235   8727    -53   -580    -29       N  
ATOM    217  CA  LEU A  31      57.493 -21.062   6.788  1.00 44.24           C  
ANISOU  217  CA  LEU A  31     3988   4244   8577    -38   -626    -73       C  
ATOM    218  C   LEU A  31      58.172 -22.322   7.320  1.00 45.07           C  
ANISOU  218  C   LEU A  31     4062   4225   8837    -44   -658    -59       C  
ATOM    219  O   LEU A  31      57.799 -22.842   8.371  1.00 45.79           O  
ANISOU  219  O   LEU A  31     4168   4203   9025    -57   -610     73       O  
ATOM    220  CB  LEU A  31      58.053 -19.833   7.513  1.00 43.36           C  
ANISOU  220  CB  LEU A  31     4013   4200   8260    -32   -574     28       C  
ATOM    221  CG  LEU A  31      59.528 -19.494   7.290  1.00 42.93           C  
ANISOU  221  CG  LEU A  31     4004   4208   8097    -18   -617    -19       C  
ATOM    222  CD1 LEU A  31      59.775 -19.025   5.864  1.00 42.82           C  
ANISOU  222  CD1 LEU A  31     3945   4314   8007     -4   -648   -145       C  
ATOM    223  CD2 LEU A  31      59.976 -18.434   8.283  1.00 42.39           C  
ANISOU  223  CD2 LEU A  31     4059   4164   7882    -14   -576     84       C  
ATOM    224  N   GLY A  32      59.173 -22.798   6.584  1.00 45.47           N  
ANISOU  224  N   GLY A  32     4066   4296   8912    -30   -733   -190       N  
ATOM    225  CA  GLY A  32      59.979 -23.943   7.001  1.00 46.61           C  
ANISOU  225  CA  GLY A  32     4172   4321   9215    -29   -779   -190       C  
ATOM    226  C   GLY A  32      59.443 -25.271   6.498  1.00 48.29           C  
ANISOU  226  C   GLY A  32     4235   4416   9697    -35   -827   -292       C  
ATOM    227  O   GLY A  32      58.323 -25.338   5.992  1.00 48.67           O  
ANISOU  227  O   GLY A  32     4211   4462   9819    -44   -824   -345       O  
ATOM    228  N   PRO A  33      60.249 -26.341   6.631  1.00 49.70           N  
ANISOU  228  N   PRO A  33     4352   4482  10047    -29   -883   -327       N  
ATOM    229  CA  PRO A  33      59.854 -27.671   6.168  1.00 51.42           C  
ANISOU  229  CA  PRO A  33     4410   4562  10562    -34   -938   -441       C  
ATOM    230  C   PRO A  33      58.743 -28.299   7.011  1.00 52.70           C  
ANISOU  230  C   PRO A  33     4528   4561  10934    -64   -888   -285       C  
ATOM    231  O   PRO A  33      58.035 -29.179   6.520  1.00 54.53           O  
ANISOU  231  O   PRO A  33     4610   4683  11422    -75   -924   -386       O  
ATOM    232  CB  PRO A  33      61.148 -28.483   6.282  1.00 51.91           C  
ANISOU  232  CB  PRO A  33     4437   4542  10744    -17  -1001   -486       C  
ATOM    233  CG  PRO A  33      61.918 -27.811   7.360  1.00 51.03           C  
ANISOU  233  CG  PRO A  33     4473   4459  10455    -12   -969   -300       C  
ATOM    234  CD  PRO A  33      61.583 -26.352   7.260  1.00 49.71           C  
ANISOU  234  CD  PRO A  33     4421   4466   9998    -15   -907   -266       C  
ATOM    235  N   LYS A  34      58.595 -27.856   8.259  1.00 52.59           N  
ANISOU  235  N   LYS A  34     4635   4528  10816    -74   -802    -49       N  
ATOM    236  CA  LYS A  34      57.476 -28.280   9.105  1.00 53.75           C  
ANISOU  236  CA  LYS A  34     4756   4544  11122   -100   -712    126       C  
ATOM    237  C   LYS A  34      56.375 -27.215   9.106  1.00 52.71           C  
ANISOU  237  C   LYS A  34     4672   4514  10842   -112   -624    165       C  
ATOM    238  O   LYS A  34      55.669 -27.041  10.104  1.00 52.90           O  
ANISOU  238  O   LYS A  34     4749   4491  10858   -125   -508    358       O  
ATOM    239  CB  LYS A  34      57.949 -28.540  10.539  1.00 54.67           C  
ANISOU  239  CB  LYS A  34     4982   4579  11209    -93   -660    374       C  
ATOM    240  CG  LYS A  34      59.182 -29.423  10.667  1.00 55.77           C  
ANISOU  240  CG  LYS A  34     5097   4627  11465    -73   -758    361       C  
ATOM    241  CD  LYS A  34      58.911 -30.874  10.306  1.00 57.67           C  
ANISOU  241  CD  LYS A  34     5150   4664  12098    -88   -804    303       C  
ATOM    242  CE  LYS A  34      60.126 -31.743  10.607  1.00 58.72           C  
ANISOU  242  CE  LYS A  34     5262   4685  12364    -64   -896    325       C  
ATOM    243  NZ  LYS A  34      60.357 -31.926  12.070  1.00 59.79           N  
ANISOU  243  NZ  LYS A  34     5519   4746  12453    -50   -850    624       N  
ATOM    244  N   GLY A  35      56.229 -26.507   7.986  1.00 51.39           N  
ANISOU  244  N   GLY A  35     4483   4485  10557   -102   -675    -12       N  
ATOM    245  CA  GLY A  35      55.256 -25.426   7.869  1.00 50.18           C  
ANISOU  245  CA  GLY A  35     4366   4431  10268   -106   -613     10       C  
ATOM    246  C   GLY A  35      53.829 -25.931   7.906  1.00 50.57           C  
ANISOU  246  C   GLY A  35     4284   4358  10570   -132   -568     33       C  
ATOM    247  O   GLY A  35      53.546 -27.050   7.478  1.00 51.60           O  
ANISOU  247  O   GLY A  35     4262   4358  10984   -144   -628    -58       O  
ATOM    248  N   ARG A  36      52.934 -25.095   8.423  1.00 49.68           N  
ANISOU  248  N   ARG A  36     4220   4279  10376   -141   -461    148       N  
ATOM    249  CA  ARG A  36      51.539 -25.465   8.619  1.00 50.63           C  
ANISOU  249  CA  ARG A  36     4215   4275  10746   -168   -389    198       C  
ATOM    250  C   ARG A  36      50.678 -25.038   7.438  1.00 50.52           C  
ANISOU  250  C   ARG A  36     4093   4324  10779   -161   -474     21       C  
ATOM    251  O   ARG A  36      51.060 -24.174   6.648  1.00 49.72           O  
ANISOU  251  O   ARG A  36     4054   4387  10448   -132   -551    -87       O  
ATOM    252  CB  ARG A  36      51.001 -24.841   9.910  1.00 50.65           C  
ANISOU  252  CB  ARG A  36     4321   4270  10652   -176   -207    424       C  
ATOM    253  CG  ARG A  36      51.849 -25.118  11.145  1.00 50.98           C  
ANISOU  253  CG  ARG A  36     4503   4282  10583   -168   -132    611       C  
ATOM    254  CD  ARG A  36      51.908 -26.600  11.485  1.00 52.68           C  
ANISOU  254  CD  ARG A  36     4618   4306  11092   -187   -130    687       C  
ATOM    255  NE  ARG A  36      52.785 -26.865  12.624  1.00 53.07           N  
ANISOU  255  NE  ARG A  36     4810   4337  11018   -169    -84    873       N  
ATOM    256  CZ  ARG A  36      52.467 -26.649  13.901  1.00 54.08           C  
ANISOU  256  CZ  ARG A  36     5052   4456  11038   -161     74   1101       C  
ATOM    257  NH1 ARG A  36      51.280 -26.150  14.241  1.00 54.55           N  
ANISOU  257  NH1 ARG A  36     5094   4518  11115   -173    226   1174       N  
ATOM    258  NH2 ARG A  36      53.351 -26.932  14.852  1.00 54.85           N  
ANISOU  258  NH2 ARG A  36     5284   4549  11006   -133     79   1256       N  
ATOM    259  N   ASN A  37      49.509 -25.661   7.336  1.00 51.74           N  
ANISOU  259  N   ASN A  37     4078   4337  11241   -184   -461      2       N  
ATOM    260  CA  ASN A  37      48.572 -25.419   6.242  1.00 51.93           C  
ANISOU  260  CA  ASN A  37     3972   4393  11364   -173   -566   -173       C  
ATOM    261  C   ASN A  37      47.708 -24.186   6.498  1.00 51.44           C  
ANISOU  261  C   ASN A  37     3955   4406  11182   -169   -478    -87       C  
ATOM    262  O   ASN A  37      47.384 -23.872   7.645  1.00 51.41           O  
ANISOU  262  O   ASN A  37     4014   4356  11164   -188   -303    108       O  
ATOM    263  CB  ASN A  37      47.687 -26.662   6.042  1.00 53.77           C  
ANISOU  263  CB  ASN A  37     3978   4418  12034   -201   -605   -245       C  
ATOM    264  CG  ASN A  37      48.282 -27.665   5.068  1.00 54.29           C  
ANISOU  264  CG  ASN A  37     3945   4453  12228   -186   -782   -471       C  
ATOM    265  OD1 ASN A  37      48.444 -28.825   5.412  1.00 55.28           O  
ANISOU  265  OD1 ASN A  37     3975   4401  12626   -210   -772   -452       O  
ATOM    266  ND2 ASN A  37      48.603 -27.229   3.852  1.00 53.85           N  
ANISOU  266  ND2 ASN A  37     3911   4569  11981   -141   -938   -684       N  
ATOM    267  N   VAL A  38      47.352 -23.487   5.422  1.00 51.21           N  
ANISOU  267  N   VAL A  38     3898   4497  11061   -138   -601   -234       N  
ATOM    268  CA  VAL A  38      46.438 -22.347   5.486  1.00 51.06           C  
ANISOU  268  CA  VAL A  38     3887   4533  10978   -128   -549   -179       C  
ATOM    269  C   VAL A  38      45.292 -22.596   4.511  1.00 52.52           C  
ANISOU  269  C   VAL A  38     3878   4670  11405   -117   -685   -339       C  
ATOM    270  O   VAL A  38      45.526 -22.832   3.326  1.00 52.64           O  
ANISOU  270  O   VAL A  38     3851   4764  11384    -83   -873   -533       O  
ATOM    271  CB  VAL A  38      47.143 -21.023   5.126  1.00 49.59           C  
ANISOU  271  CB  VAL A  38     3870   4552  10420    -90   -577   -176       C  
ATOM    272  CG1 VAL A  38      46.180 -19.848   5.245  1.00 49.50           C  
ANISOU  272  CG1 VAL A  38     3856   4574  10376    -79   -522   -113       C  
ATOM    273  CG2 VAL A  38      48.357 -20.799   6.019  1.00 48.54           C  
ANISOU  273  CG2 VAL A  38     3914   4462  10064    -98   -475    -51       C  
ATOM    274  N   VAL A  39      44.060 -22.547   5.012  1.00 53.78           N  
ANISOU  274  N   VAL A  39     3918   4704  11811   -140   -591   -265       N  
ATOM    275  CA  VAL A  39      42.877 -22.818   4.195  1.00 55.52           C  
ANISOU  275  CA  VAL A  39     3927   4848  12316   -132   -724   -414       C  
ATOM    276  C   VAL A  39      42.294 -21.506   3.677  1.00 55.50           C  
ANISOU  276  C   VAL A  39     3951   4974  12163    -90   -783   -432       C  
ATOM    277  O   VAL A  39      41.824 -20.677   4.457  1.00 55.24           O  
ANISOU  277  O   VAL A  39     3958   4928  12100   -100   -624   -282       O  
ATOM    278  CB  VAL A  39      41.801 -23.587   4.987  1.00 57.18           C  
ANISOU  278  CB  VAL A  39     3953   4821  12952   -183   -589   -327       C  
ATOM    279  CG1 VAL A  39      40.669 -24.022   4.069  1.00 59.05           C  
ANISOU  279  CG1 VAL A  39     3944   4958  13532   -174   -762   -517       C  
ATOM    280  CG2 VAL A  39      42.406 -24.805   5.668  1.00 57.73           C  
ANISOU  280  CG2 VAL A  39     4015   4754  13167   -224   -501   -252       C  
ATOM    281  N   LEU A  40      42.334 -21.326   2.359  1.00 56.22           N  
ANISOU  281  N   LEU A  40     4020   5187  12153    -38  -1010   -616       N  
ATOM    282  CA  LEU A  40      41.823 -20.122   1.712  1.00 56.42           C  
ANISOU  282  CA  LEU A  40     4067   5338  12031     11  -1101   -633       C  
ATOM    283  C   LEU A  40      40.479 -20.422   1.059  1.00 59.19           C  
ANISOU  283  C   LEU A  40     4190   5591  12705     28  -1255   -770       C  
ATOM    284  O   LEU A  40      40.386 -21.282   0.185  1.00 60.61           O  
ANISOU  284  O   LEU A  40     4260   5757  13013     49  -1447   -969       O  
ATOM    285  CB  LEU A  40      42.816 -19.625   0.660  1.00 55.27           C  
ANISOU  285  CB  LEU A  40     4069   5416  11513     69  -1249   -719       C  
ATOM    286  CG  LEU A  40      44.250 -19.392   1.144  1.00 53.27           C  
ANISOU  286  CG  LEU A  40     4019   5257  10962     55  -1129   -618       C  
ATOM    287  CD1 LEU A  40      45.150 -19.036  -0.028  1.00 52.87           C  
ANISOU  287  CD1 LEU A  40     4077   5414  10595    113  -1272   -720       C  
ATOM    288  CD2 LEU A  40      44.303 -18.309   2.210  1.00 52.07           C  
ANISOU  288  CD2 LEU A  40     3984   5107  10691     34   -934   -410       C  
ATOM    289  N   ASP A  41      39.445 -19.704   1.485  1.00 60.65           N  
ANISOU  289  N   ASP A  41     4301   5708  13036     23  -1176   -677       N  
ATOM    290  CA  ASP A  41      38.082 -19.943   1.015  1.00 63.75           C  
ANISOU  290  CA  ASP A  41     4454   5978  13787     35  -1305   -791       C  
ATOM    291  C   ASP A  41      37.871 -19.395  -0.396  1.00 65.55           C  
ANISOU  291  C   ASP A  41     4675   6365  13864    119  -1593   -948       C  
ATOM    292  O   ASP A  41      38.561 -18.472  -0.825  1.00 64.30           O  
ANISOU  292  O   ASP A  41     4701   6402  13327    165  -1632   -903       O  
ATOM    293  CB  ASP A  41      37.077 -19.297   1.980  1.00 64.01           C  
ANISOU  293  CB  ASP A  41     4408   5887  14026      6  -1105   -632       C  
ATOM    294  CG  ASP A  41      35.654 -19.810   1.795  1.00 66.14           C  
ANISOU  294  CG  ASP A  41     4388   5963  14777     -3  -1179   -728       C  
ATOM    295  OD1 ASP A  41      35.474 -20.963   1.349  1.00 67.69           O  
ANISOU  295  OD1 ASP A  41     4432   6057  15230    -15  -1309   -882       O  
ATOM    296  OD2 ASP A  41      34.713 -19.056   2.113  1.00 66.22           O  
ANISOU  296  OD2 ASP A  41     4311   5913  14934      1  -1106   -658       O  
ATOM    297  N   LYS A  42      36.917 -19.989  -1.106  1.00 69.44           N  
ANISOU  297  N   LYS A  42     4952   6768  14663    142  -1797  -1131       N  
ATOM    298  CA  LYS A  42      36.483 -19.512  -2.416  1.00 72.17           C  
ANISOU  298  CA  LYS A  42     5265   7248  14908    231  -2091  -1284       C  
ATOM    299  C   LYS A  42      34.961 -19.458  -2.441  1.00 75.37           C  
ANISOU  299  C   LYS A  42     5417   7485  15735    236  -2175  -1334       C  
ATOM    300  O   LYS A  42      34.296 -20.227  -1.742  1.00 76.84           O  
ANISOU  300  O   LYS A  42     5411   7441  16342    171  -2062  -1333       O  
ATOM    301  CB  LYS A  42      36.974 -20.451  -3.513  1.00 73.68           C  
ANISOU  301  CB  LYS A  42     5444   7527  15024    276  -2334  -1533       C  
ATOM    302  CG  LYS A  42      38.471 -20.398  -3.770  1.00 72.34           C  
ANISOU  302  CG  LYS A  42     5516   7556  14411    293  -2295  -1515       C  
ATOM    303  CD  LYS A  42      38.969 -21.649  -4.484  1.00 73.96           C  
ANISOU  303  CD  LYS A  42     5673   7776  14652    311  -2453  -1762       C  
ATOM    304  CE  LYS A  42      38.139 -21.991  -5.715  1.00 76.77           C  
ANISOU  304  CE  LYS A  42     5873   8163  15129    391  -2782  -2031       C  
ATOM    305  NZ  LYS A  42      38.689 -23.164  -6.449  1.00 78.19           N  
ANISOU  305  NZ  LYS A  42     6018   8375  15316    419  -2939  -2300       N  
ATOM    306  N   SER A  43      34.412 -18.555  -3.247  1.00 77.45           N  
ANISOU  306  N   SER A  43     5670   7855  15900    314  -2370  -1367       N  
ATOM    307  CA  SER A  43      32.958 -18.393  -3.343  1.00 80.45           C  
ANISOU  307  CA  SER A  43     5804   8082  16682    329  -2476  -1419       C  
ATOM    308  C   SER A  43      32.286 -19.646  -3.913  1.00 82.91           C  
ANISOU  308  C   SER A  43     5865   8253  17381    333  -2696  -1677       C  
ATOM    309  O   SER A  43      31.251 -20.084  -3.405  1.00 84.15           O  
ANISOU  309  O   SER A  43     5773   8170  18028    285  -2639  -1694       O  
ATOM    310  CB  SER A  43      32.604 -17.166  -4.190  1.00 81.39           C  
ANISOU  310  CB  SER A  43     5977   8358  16586    426  -2677  -1402       C  
ATOM    311  OG  SER A  43      33.189 -17.245  -5.479  1.00 82.60           O  
ANISOU  311  OG  SER A  43     6248   8735  16399    514  -2954  -1550       O  
ATOM    312  N   PHE A  44      32.882 -20.215  -4.961  1.00 83.48           N  
ANISOU  312  N   PHE A  44     6000   8472  17245    390  -2939  -1882       N  
ATOM    313  CA  PHE A  44      32.387 -21.449  -5.573  1.00 85.69           C  
ANISOU  313  CA  PHE A  44     6057   8633  17866    401  -3172  -2165       C  
ATOM    314  C   PHE A  44      33.329 -22.614  -5.272  1.00 83.67           C  
ANISOU  314  C   PHE A  44     5843   8330  17617    343  -3063  -2228       C  
ATOM    315  O   PHE A  44      34.551 -22.443  -5.231  1.00 81.70           O  
ANISOU  315  O   PHE A  44     5839   8252  16952    345  -2958  -2148       O  
ATOM    316  CB  PHE A  44      32.243 -21.278  -7.090  1.00 88.31           C  
ANISOU  316  CB  PHE A  44     6405   9167  17979    528  -3572  -2401       C  
ATOM    317  CG  PHE A  44      31.170 -20.301  -7.496  1.00 90.43           C  
ANISOU  317  CG  PHE A  44     6584   9450  18326    596  -3743  -2373       C  
ATOM    318  CD1 PHE A  44      29.850 -20.719  -7.653  1.00 93.31           C  
ANISOU  318  CD1 PHE A  44     6636   9607  19208    602  -3924  -2531       C  
ATOM    319  CD2 PHE A  44      31.477 -18.963  -7.731  1.00 89.53           C  
ANISOU  319  CD2 PHE A  44     6680   9542  17792    655  -3730  -2189       C  
ATOM    320  CE1 PHE A  44      28.860 -19.821  -8.029  1.00 94.79           C  
ANISOU  320  CE1 PHE A  44     6729   9798  19488    668  -4096  -2508       C  
ATOM    321  CE2 PHE A  44      30.491 -18.062  -8.107  1.00 91.03           C  
ANISOU  321  CE2 PHE A  44     6780   9733  18072    721  -3897  -2154       C  
ATOM    322  CZ  PHE A  44      29.181 -18.492  -8.257  1.00 93.61           C  
ANISOU  322  CZ  PHE A  44     6799   9858  18909    730  -4084  -2316       C  
ATOM    323  N   GLY A  45      32.750 -23.793  -5.055  1.00 83.91           N  
ANISOU  323  N   GLY A  45     5619   8112  18149    292  -3088  -2368       N  
ATOM    324  CA  GLY A  45      33.523 -25.015  -4.841  1.00 82.55           C  
ANISOU  324  CA  GLY A  45     5441   7857  18065    242  -3021  -2452       C  
ATOM    325  C   GLY A  45      34.122 -25.133  -3.452  1.00 79.34           C  
ANISOU  325  C   GLY A  45     5131   7344  17668    141  -2635  -2169       C  
ATOM    326  O   GLY A  45      33.743 -24.403  -2.533  1.00 78.27           O  
ANISOU  326  O   GLY A  45     5020   7152  17567     98  -2400  -1922       O  
ATOM    327  N   ALA A  46      35.062 -26.066  -3.308  1.00 77.53           N  
ANISOU  327  N   ALA A  46     4957   7090  17408    110  -2579  -2214       N  
ATOM    328  CA  ALA A  46      35.711 -26.343  -2.027  1.00 74.84           C  
ANISOU  328  CA  ALA A  46     4709   6647  17079     22  -2245  -1961       C  
ATOM    329  C   ALA A  46      36.887 -25.393  -1.795  1.00 71.32           C  
ANISOU  329  C   ALA A  46     4590   6450  16058     41  -2111  -1782       C  
ATOM    330  O   ALA A  46      37.406 -24.813  -2.749  1.00 70.96           O  
ANISOU  330  O   ALA A  46     4692   6647  15622    118  -2284  -1887       O  
ATOM    331  CB  ALA A  46      36.182 -27.788  -1.984  1.00 75.71           C  
ANISOU  331  CB  ALA A  46     4715   6599  17450    -15  -2262  -2087       C  
ATOM    332  N   PRO A  47      37.320 -25.237  -0.528  1.00 68.88           N  
ANISOU  332  N   PRO A  47     4392   6080  15698    -25  -1802  -1509       N  
ATOM    333  CA  PRO A  47      38.416 -24.312  -0.231  1.00 65.57           C  
ANISOU  333  CA  PRO A  47     4264   5874  14772    -10  -1676  -1344       C  
ATOM    334  C   PRO A  47      39.776 -24.814  -0.703  1.00 63.72           C  
ANISOU  334  C   PRO A  47     4176   5770  14263     11  -1748  -1445       C  
ATOM    335  O   PRO A  47      39.936 -25.999  -0.992  1.00 64.68           O  
ANISOU  335  O   PRO A  47     4178   5783  14612      0  -1840  -1607       O  
ATOM    336  CB  PRO A  47      38.400 -24.209   1.305  1.00 64.92           C  
ANISOU  336  CB  PRO A  47     4227   5662  14777    -85  -1344  -1057       C  
ATOM    337  CG  PRO A  47      37.150 -24.884   1.755  1.00 67.42           C  
ANISOU  337  CG  PRO A  47     4274   5712  15627   -134  -1281  -1049       C  
ATOM    338  CD  PRO A  47      36.822 -25.886   0.696  1.00 69.63           C  
ANISOU  338  CD  PRO A  47     4351   5912  16191   -112  -1555  -1337       C  
ATOM    339  N   THR A  48      40.741 -23.900  -0.766  1.00 60.93           N  
ANISOU  339  N   THR A  48     4067   5635  13449     40  -1698  -1350       N  
ATOM    340  CA  THR A  48      42.107 -24.214  -1.172  1.00 59.34           C  
ANISOU  340  CA  THR A  48     4015   5570  12958     63  -1736  -1423       C  
ATOM    341  C   THR A  48      42.997 -24.361   0.057  1.00 57.25           C  
ANISOU  341  C   THR A  48     3876   5246  12628      3  -1492  -1207       C  
ATOM    342  O   THR A  48      43.159 -23.415   0.825  1.00 55.83           O  
ANISOU  342  O   THR A  48     3834   5118  12258    -12  -1324   -996       O  
ATOM    343  CB  THR A  48      42.687 -23.103  -2.071  1.00 58.21           C  
ANISOU  343  CB  THR A  48     4057   5708  12352    137  -1835  -1449       C  
ATOM    344  OG1 THR A  48      41.806 -22.869  -3.177  1.00 59.83           O  
ANISOU  344  OG1 THR A  48     4162   5983  12587    204  -2070  -1623       O  
ATOM    345  CG2 THR A  48      44.064 -23.488  -2.598  1.00 57.56           C  
ANISOU  345  CG2 THR A  48     4103   5765  12000    164  -1873  -1550       C  
ATOM    346  N   ILE A  49      43.565 -25.550   0.241  1.00 57.12           N  
ANISOU  346  N   ILE A  49     3808   5116  12778    -24  -1484  -1269       N  
ATOM    347  CA  ILE A  49      44.532 -25.796   1.309  1.00 55.30           C  
ANISOU  347  CA  ILE A  49     3701   4838  12471    -69  -1292  -1081       C  
ATOM    348  C   ILE A  49      45.927 -25.604   0.719  1.00 53.64           C  
ANISOU  348  C   ILE A  49     3660   4824  11897    -28  -1355  -1160       C  
ATOM    349  O   ILE A  49      46.246 -26.197  -0.311  1.00 54.32           O  
ANISOU  349  O   ILE A  49     3691   4962  11985     11  -1526  -1396       O  
ATOM    350  CB  ILE A  49      44.383 -27.221   1.883  1.00 56.62           C  
ANISOU  350  CB  ILE A  49     3706   4749  13055   -121  -1244  -1078       C  
ATOM    351  CG1 ILE A  49      42.940 -27.463   2.343  1.00 58.09           C  
ANISOU  351  CG1 ILE A  49     3692   4731  13648   -162  -1181  -1016       C  
ATOM    352  CG2 ILE A  49      45.339 -27.435   3.048  1.00 55.52           C  
ANISOU  352  CG2 ILE A  49     3705   4565  12826   -159  -1052   -855       C  
ATOM    353  CD1 ILE A  49      42.610 -28.917   2.599  1.00 60.15           C  
ANISOU  353  CD1 ILE A  49     3739   4723  14389   -207  -1179  -1060       C  
ATOM    354  N   THR A  50      46.752 -24.780   1.363  1.00 51.63           N  
ANISOU  354  N   THR A  50     3602   4673  11340    -34  -1215   -975       N  
ATOM    355  CA  THR A  50      48.070 -24.436   0.816  1.00 50.58           C  
ANISOU  355  CA  THR A  50     3625   4728  10864      2  -1255  -1032       C  
ATOM    356  C   THR A  50      49.114 -24.098   1.883  1.00 48.95           C  
ANISOU  356  C   THR A  50     3583   4532  10483    -25  -1088   -829       C  
ATOM    357  O   THR A  50      48.776 -23.652   2.981  1.00 48.41           O  
ANISOU  357  O   THR A  50     3564   4398  10432    -59   -939   -626       O  
ATOM    358  CB  THR A  50      47.966 -23.247  -0.166  1.00 50.22           C  
ANISOU  358  CB  THR A  50     3662   4902  10515     61  -1346  -1086       C  
ATOM    359  OG1 THR A  50      49.248 -22.985  -0.749  1.00 49.45           O  
ANISOU  359  OG1 THR A  50     3698   4979  10111     97  -1369  -1140       O  
ATOM    360  CG2 THR A  50      47.464 -21.987   0.540  1.00 49.16           C  
ANISOU  360  CG2 THR A  50     3611   4793  10274     46  -1221   -875       C  
ATOM    361  N   LYS A  51      50.382 -24.314   1.534  1.00 48.45           N  
ANISOU  361  N   LYS A  51     3599   4555  10252     -5  -1121   -899       N  
ATOM    362  CA  LYS A  51      51.517 -23.902   2.359  1.00 47.25           C  
ANISOU  362  CA  LYS A  51     3605   4439   9907    -20  -1003   -742       C  
ATOM    363  C   LYS A  51      52.352 -22.840   1.630  1.00 46.09           C  
ANISOU  363  C   LYS A  51     3590   4511   9409     20  -1028   -774       C  
ATOM    364  O   LYS A  51      53.538 -22.670   1.917  1.00 45.24           O  
ANISOU  364  O   LYS A  51     3584   4450   9153     20   -979   -726       O  
ATOM    365  CB  LYS A  51      52.392 -25.113   2.706  1.00 48.06           C  
ANISOU  365  CB  LYS A  51     3673   4425  10162    -36  -1005   -772       C  
ATOM    366  CG  LYS A  51      51.661 -26.223   3.445  1.00 49.64           C  
ANISOU  366  CG  LYS A  51     3739   4392  10731    -78   -969   -713       C  
ATOM    367  CD  LYS A  51      52.617 -27.296   3.948  1.00 50.31           C  
ANISOU  367  CD  LYS A  51     3809   4352  10953    -92   -959   -692       C  
ATOM    368  CE  LYS A  51      51.931 -28.264   4.905  1.00 51.91           C  
ANISOU  368  CE  LYS A  51     3904   4314  11503   -136   -883   -555       C  
ATOM    369  NZ  LYS A  51      52.910 -29.175   5.562  1.00 52.62           N  
ANISOU  369  NZ  LYS A  51     4007   4284  11701   -146   -864   -477       N  
ATOM    370  N   ASP A  52      51.726 -22.130   0.691  1.00 46.36           N  
ANISOU  370  N   ASP A  52     3614   4669   9328     58  -1105   -847       N  
ATOM    371  CA  ASP A  52      52.400 -21.110  -0.109  1.00 45.84           C  
ANISOU  371  CA  ASP A  52     3662   4809   8944    101  -1124   -862       C  
ATOM    372  C   ASP A  52      52.095 -19.728   0.465  1.00 45.00           C  
ANISOU  372  C   ASP A  52     3654   4744   8700     91  -1029   -670       C  
ATOM    373  O   ASP A  52      50.968 -19.243   0.368  1.00 45.72           O  
ANISOU  373  O   ASP A  52     3698   4825   8846     99  -1053   -642       O  
ATOM    374  CB  ASP A  52      51.938 -21.197  -1.570  1.00 47.14           C  
ANISOU  374  CB  ASP A  52     3764   5098   9045    162  -1281  -1057       C  
ATOM    375  CG  ASP A  52      52.780 -20.346  -2.517  1.00 46.85           C  
ANISOU  375  CG  ASP A  52     3844   5283   8674    215  -1292  -1076       C  
ATOM    376  OD1 ASP A  52      53.579 -19.508  -2.048  1.00 45.68           O  
ANISOU  376  OD1 ASP A  52     3812   5180   8365    199  -1177   -925       O  
ATOM    377  OD2 ASP A  52      52.636 -20.517  -3.745  1.00 48.05           O  
ANISOU  377  OD2 ASP A  52     3968   5564   8724    276  -1415  -1244       O  
ATOM    378  N   GLY A  53      53.105 -19.098   1.055  1.00 44.03           N  
ANISOU  378  N   GLY A  53     3653   4657   8417     78   -930   -552       N  
ATOM    379  CA  GLY A  53      52.949 -17.777   1.659  1.00 43.42           C  
ANISOU  379  CA  GLY A  53     3669   4608   8221     70   -839   -387       C  
ATOM    380  C   GLY A  53      52.565 -16.680   0.681  1.00 43.94           C  
ANISOU  380  C   GLY A  53     3755   4812   8125    113   -890   -387       C  
ATOM    381  O   GLY A  53      51.970 -15.677   1.075  1.00 43.78           O  
ANISOU  381  O   GLY A  53     3763   4783   8087    110   -841   -272       O  
ATOM    382  N   VAL A  54      52.913 -16.862  -0.592  1.00 44.83           N  
ANISOU  382  N   VAL A  54     3858   5055   8119    158   -987   -511       N  
ATOM    383  CA  VAL A  54      52.547 -15.909  -1.638  1.00 45.64           C  
ANISOU  383  CA  VAL A  54     3985   5303   8050    211  -1051   -502       C  
ATOM    384  C   VAL A  54      51.041 -15.967  -1.900  1.00 46.83           C  
ANISOU  384  C   VAL A  54     4035   5412   8346    229  -1151   -541       C  
ATOM    385  O   VAL A  54      50.389 -14.932  -2.032  1.00 46.77           O  
ANISOU  385  O   VAL A  54     4041   5436   8291    249  -1159   -445       O  
ATOM    386  CB  VAL A  54      53.311 -16.184  -2.953  1.00 46.54           C  
ANISOU  386  CB  VAL A  54     4122   5584   7974    266  -1123   -632       C  
ATOM    387  CG1 VAL A  54      52.829 -15.258  -4.064  1.00 47.70           C  
ANISOU  387  CG1 VAL A  54     4300   5890   7931    331  -1199   -606       C  
ATOM    388  CG2 VAL A  54      54.808 -16.021  -2.740  1.00 45.61           C  
ANISOU  388  CG2 VAL A  54     4089   5505   7735    249  -1015   -588       C  
ATOM    389  N   SER A  55      50.504 -17.183  -1.981  1.00 48.06           N  
ANISOU  389  N   SER A  55     4075   5482   8703    222  -1231   -684       N  
ATOM    390  CA  SER A  55      49.073 -17.390  -2.194  1.00 49.49           C  
ANISOU  390  CA  SER A  55     4129   5594   9079    235  -1334   -743       C  
ATOM    391  C   SER A  55      48.255 -16.894  -1.005  1.00 49.04           C  
ANISOU  391  C   SER A  55     4044   5391   9196    187  -1218   -586       C  
ATOM    392  O   SER A  55      47.189 -16.304  -1.183  1.00 49.79           O  
ANISOU  392  O   SER A  55     4081   5474   9363    207  -1266   -557       O  
ATOM    393  CB  SER A  55      48.778 -18.871  -2.435  1.00 50.80           C  
ANISOU  393  CB  SER A  55     4160   5668   9472    229  -1432   -936       C  
ATOM    394  OG  SER A  55      49.579 -19.386  -3.483  1.00 51.65           O  
ANISOU  394  OG  SER A  55     4292   5909   9422    277  -1528  -1106       O  
ATOM    395  N   VAL A  56      48.761 -17.137   0.203  1.00 48.10           N  
ANISOU  395  N   VAL A  56     3968   5167   9140    131  -1067   -488       N  
ATOM    396  CA  VAL A  56      48.099 -16.687   1.425  1.00 47.78           C  
ANISOU  396  CA  VAL A  56     3922   5003   9227     92   -928   -339       C  
ATOM    397  C   VAL A  56      48.103 -15.163   1.492  1.00 47.35           C  
ANISOU  397  C   VAL A  56     3961   5030   8998    112   -877   -218       C  
ATOM    398  O   VAL A  56      47.062 -14.549   1.719  1.00 48.01           O  
ANISOU  398  O   VAL A  56     3989   5063   9187    116   -857   -163       O  
ATOM    399  CB  VAL A  56      48.770 -17.268   2.691  1.00 47.00           C  
ANISOU  399  CB  VAL A  56     3877   4801   9178     41   -786   -256       C  
ATOM    400  CG1 VAL A  56      48.235 -16.601   3.954  1.00 46.63           C  
ANISOU  400  CG1 VAL A  56     3864   4672   9179     14   -625    -97       C  
ATOM    401  CG2 VAL A  56      48.554 -18.772   2.762  1.00 47.87           C  
ANISOU  401  CG2 VAL A  56     3869   4787   9533     17   -821   -346       C  
ATOM    402  N   ALA A  57      49.277 -14.564   1.295  1.00 46.63           N  
ANISOU  402  N   ALA A  57     3997   5050   8671    123   -855   -178       N  
ATOM    403  CA  ALA A  57      49.428 -13.109   1.342  1.00 46.14           C  
ANISOU  403  CA  ALA A  57     4018   5050   8461    140   -805    -61       C  
ATOM    404  C   ALA A  57      48.454 -12.410   0.402  1.00 47.25           C  
ANISOU  404  C   ALA A  57     4100   5248   8604    189   -913    -65       C  
ATOM    405  O   ALA A  57      47.775 -11.466   0.800  1.00 47.60           O  
ANISOU  405  O   ALA A  57     4134   5247   8705    193   -867     26       O  
ATOM    406  CB  ALA A  57      50.857 -12.714   1.003  1.00 45.55           C  
ANISOU  406  CB  ALA A  57     4057   5085   8163    149   -787    -40       C  
ATOM    407  N   ARG A  58      48.369 -12.899  -0.833  1.00 48.56           N  
ANISOU  407  N   ARG A  58     4226   5512   8713    233  -1065   -180       N  
ATOM    408  CA  ARG A  58      47.501 -12.310  -1.860  1.00 49.95           C  
ANISOU  408  CA  ARG A  58     4354   5764   8861    294  -1205   -191       C  
ATOM    409  C   ARG A  58      46.063 -12.093  -1.379  1.00 49.88           C  
ANISOU  409  C   ARG A  58     4224   5623   9102    287  -1213   -166       C  
ATOM    410  O   ARG A  58      45.444 -11.081  -1.704  1.00 50.43           O  
ANISOU  410  O   ARG A  58     4282   5716   9163    325  -1258    -90       O  
ATOM    411  CB  ARG A  58      47.488 -13.187  -3.119  1.00 52.15           C  
ANISOU  411  CB  ARG A  58     4589   6151   9071    345  -1381   -363       C  
ATOM    412  CG  ARG A  58      47.130 -12.438  -4.394  1.00 54.37           C  
ANISOU  412  CG  ARG A  58     4890   6587   9178    429  -1530   -354       C  
ATOM    413  CD  ARG A  58      46.710 -13.374  -5.522  1.00 57.01           C  
ANISOU  413  CD  ARG A  58     5153   7007   9500    488  -1735   -559       C  
ATOM    414  NE  ARG A  58      47.523 -14.590  -5.599  1.00 57.73           N  
ANISOU  414  NE  ARG A  58     5245   7110   9577    469  -1725   -715       N  
ATOM    415  CZ  ARG A  58      48.767 -14.659  -6.079  1.00 58.27           C  
ANISOU  415  CZ  ARG A  58     5422   7315   9400    487  -1677   -734       C  
ATOM    416  NH1 ARG A  58      49.393 -13.574  -6.535  1.00 58.38           N  
ANISOU  416  NH1 ARG A  58     5558   7469   9152    521  -1624   -592       N  
ATOM    417  NH2 ARG A  58      49.400 -15.829  -6.096  1.00 58.66           N  
ANISOU  417  NH2 ARG A  58     5447   7349   9490    470  -1675   -893       N  
ATOM    418  N   GLU A  59      45.545 -13.042  -0.602  1.00 49.31           N  
ANISOU  418  N   GLU A  59     4057   5407   9269    240  -1163   -220       N  
ATOM    419  CA  GLU A  59      44.162 -12.991  -0.123  1.00 49.57           C  
ANISOU  419  CA  GLU A  59     3953   5301   9580    229  -1150   -208       C  
ATOM    420  C   GLU A  59      43.923 -11.972   0.995  1.00 48.20           C  
ANISOU  420  C   GLU A  59     3816   5048   9447    203   -972    -56       C  
ATOM    421  O   GLU A  59      42.787 -11.546   1.198  1.00 49.05           O  
ANISOU  421  O   GLU A  59     3819   5070   9746    211   -965    -31       O  
ATOM    422  CB  GLU A  59      43.720 -14.376   0.372  1.00 50.18           C  
ANISOU  422  CB  GLU A  59     3908   5237   9922    184  -1128   -299       C  
ATOM    423  CG  GLU A  59      43.725 -15.465  -0.691  1.00 51.37           C  
ANISOU  423  CG  GLU A  59     3979   5429  10110    211  -1319   -488       C  
ATOM    424  CD  GLU A  59      42.737 -15.209  -1.814  1.00 53.14           C  
ANISOU  424  CD  GLU A  59     4099   5704  10388    276  -1533   -585       C  
ATOM    425  OE1 GLU A  59      41.623 -14.709  -1.540  1.00 53.76           O  
ANISOU  425  OE1 GLU A  59     4074   5689  10663    278  -1528   -535       O  
ATOM    426  OE2 GLU A  59      43.074 -15.517  -2.976  1.00 54.14           O  
ANISOU  426  OE2 GLU A  59     4245   5967  10359    332  -1709   -717       O  
ATOM    427  N   ILE A  60      44.975 -11.586   1.716  1.00 46.11           N  
ANISOU  427  N   ILE A  60     3692   4808   9018    177   -834     28       N  
ATOM    428  CA  ILE A  60      44.824 -10.766   2.920  1.00 45.08           C  
ANISOU  428  CA  ILE A  60     3603   4599   8925    153   -657    141       C  
ATOM    429  C   ILE A  60      44.384  -9.336   2.607  1.00 45.37           C  
ANISOU  429  C   ILE A  60     3639   4661   8937    193   -681    212       C  
ATOM    430  O   ILE A  60      45.115  -8.564   1.984  1.00 45.05           O  
ANISOU  430  O   ILE A  60     3686   4724   8705    221   -733    256       O  
ATOM    431  CB  ILE A  60      46.121 -10.725   3.761  1.00 43.54           C  
ANISOU  431  CB  ILE A  60     3556   4426   8557    122   -533    194       C  
ATOM    432  CG1 ILE A  60      46.513 -12.133   4.237  1.00 43.42           C  
ANISOU  432  CG1 ILE A  60     3538   4362   8597     83   -499    146       C  
ATOM    433  CG2 ILE A  60      45.969  -9.791   4.956  1.00 43.03           C  
ANISOU  433  CG2 ILE A  60     3543   4298   8505    110   -370    284       C  
ATOM    434  CD1 ILE A  60      45.515 -12.813   5.153  1.00 44.19           C  
ANISOU  434  CD1 ILE A  60     3538   4316   8935     52   -391    163       C  
ATOM    435  N   GLU A  61      43.174  -9.009   3.053  1.00 46.32           N  
ANISOU  435  N   GLU A  61     3649   4673   9274    195   -632    230       N  
ATOM    436  CA  GLU A  61      42.631  -7.655   3.001  1.00 46.61           C  
ANISOU  436  CA  GLU A  61     3666   4693   9351    230   -628    301       C  
ATOM    437  C   GLU A  61      41.757  -7.483   4.241  1.00 46.83           C  
ANISOU  437  C   GLU A  61     3623   4580   9589    206   -449    323       C  
ATOM    438  O   GLU A  61      40.904  -8.327   4.514  1.00 47.57           O  
ANISOU  438  O   GLU A  61     3595   4583   9893    186   -419    277       O  
ATOM    439  CB  GLU A  61      41.805  -7.458   1.727  1.00 48.02           C  
ANISOU  439  CB  GLU A  61     3735   4906   9601    286   -835    271       C  
ATOM    440  CG  GLU A  61      41.277  -6.043   1.523  1.00 48.68           C  
ANISOU  440  CG  GLU A  61     3792   4971   9733    331   -859    359       C  
ATOM    441  CD  GLU A  61      40.297  -5.932   0.364  1.00 50.21           C  
ANISOU  441  CD  GLU A  61     3862   5182  10029    393  -1077    333       C  
ATOM    442  OE1 GLU A  61      40.308  -6.810  -0.525  1.00 50.80           O  
ANISOU  442  OE1 GLU A  61     3914   5336  10049    413  -1238    244       O  
ATOM    443  OE2 GLU A  61      39.513  -4.958   0.343  1.00 50.88           O  
ANISOU  443  OE2 GLU A  61     3871   5202  10256    428  -1097    392       O  
ATOM    444  N   LEU A  62      41.973  -6.406   4.992  1.00 46.36           N  
ANISOU  444  N   LEU A  62     3633   4498   9483    209   -322    387       N  
ATOM    445  CA  LEU A  62      41.285  -6.203   6.269  1.00 46.87           C  
ANISOU  445  CA  LEU A  62     3658   4450   9700    193   -122    399       C  
ATOM    446  C   LEU A  62      40.154  -5.181   6.157  1.00 48.13           C  
ANISOU  446  C   LEU A  62     3692   4530  10064    231   -124    412       C  
ATOM    447  O   LEU A  62      40.160  -4.327   5.269  1.00 48.16           O  
ANISOU  447  O   LEU A  62     3684   4570  10042    272   -264    442       O  
ATOM    448  CB  LEU A  62      42.286  -5.767   7.339  1.00 45.92           C  
ANISOU  448  CB  LEU A  62     3699   4353   9394    177     27    429       C  
ATOM    449  CG  LEU A  62      43.563  -6.608   7.450  1.00 44.80           C  
ANISOU  449  CG  LEU A  62     3689   4289   9042    146     14    424       C  
ATOM    450  CD1 LEU A  62      44.435  -6.087   8.579  1.00 44.33           C  
ANISOU  450  CD1 LEU A  62     3774   4242   8825    140    146    444       C  
ATOM    451  CD2 LEU A  62      43.250  -8.081   7.665  1.00 45.13           C  
ANISOU  451  CD2 LEU A  62     3677   4292   9178    113     42    398       C  
ATOM    452  N   GLU A  63      39.189  -5.279   7.070  1.00 49.25           N  
ANISOU  452  N   GLU A  63     3738   4558  10414    220     39    399       N  
ATOM    453  CA  GLU A  63      38.019  -4.399   7.063  1.00 50.61           C  
ANISOU  453  CA  GLU A  63     3764   4633  10829    255     56    398       C  
ATOM    454  C   GLU A  63      38.382  -2.995   7.515  1.00 49.98           C  
ANISOU  454  C   GLU A  63     3764   4550  10673    283    130    429       C  
ATOM    455  O   GLU A  63      38.012  -2.017   6.865  1.00 50.63           O  
ANISOU  455  O   GLU A  63     3780   4609  10847    326     21    453       O  
ATOM    456  CB  GLU A  63      36.915  -4.948   7.968  1.00 52.33           C  
ANISOU  456  CB  GLU A  63     3850   4728  11303    234    244    373       C  
ATOM    457  CG  GLU A  63      35.606  -4.173   7.871  1.00 54.40           C  
ANISOU  457  CG  GLU A  63     3925   4875  11869    271    253    358       C  
ATOM    458  CD  GLU A  63      34.488  -4.775   8.703  1.00 56.42           C  
ANISOU  458  CD  GLU A  63     4027   5002  12406    249    453    335       C  
ATOM    459  OE1 GLU A  63      34.760  -5.676   9.526  1.00 56.87           O  
ANISOU  459  OE1 GLU A  63     4147   5063  12398    206    622    352       O  
ATOM    460  OE2 GLU A  63      33.329  -4.340   8.535  1.00 58.20           O  
ANISOU  460  OE2 GLU A  63     4062   5118  12932    276    447    311       O  
ATOM    461  N   ASP A  64      39.087  -2.903   8.640  1.00 48.92           N  
ANISOU  461  N   ASP A  64     3766   4436  10386    263    307    424       N  
ATOM    462  CA  ASP A  64      39.539  -1.615   9.158  1.00 48.50           C  
ANISOU  462  CA  ASP A  64     3792   4374  10260    288    375    425       C  
ATOM    463  C   ASP A  64      40.469  -0.971   8.139  1.00 47.69           C  
ANISOU  463  C   ASP A  64     3760   4345  10013    303    189    474       C  
ATOM    464  O   ASP A  64      41.464  -1.567   7.731  1.00 46.83           O  
ANISOU  464  O   ASP A  64     3755   4333   9703    281    110    492       O  
ATOM    465  CB  ASP A  64      40.245  -1.788  10.506  1.00 47.85           C  
ANISOU  465  CB  ASP A  64     3859   4321  10001    269    565    396       C  
ATOM    466  CG  ASP A  64      40.611  -0.462  11.155  1.00 47.78           C  
ANISOU  466  CG  ASP A  64     3914   4288   9950    300    639    360       C  
ATOM    467  OD1 ASP A  64      41.390   0.309  10.558  1.00 47.08           O  
ANISOU  467  OD1 ASP A  64     3875   4227   9786    311    513    382       O  
ATOM    468  OD2 ASP A  64      40.132  -0.199  12.276  1.00 48.58           O  
ANISOU  468  OD2 ASP A  64     4015   4343  10100    315    832    305       O  
ATOM    469  N   LYS A  65      40.133   0.250   7.738  1.00 48.47           N  
ANISOU  469  N   LYS A  65     3795   4389  10232    344    132    503       N  
ATOM    470  CA  LYS A  65      40.825   0.934   6.648  1.00 48.30           C  
ANISOU  470  CA  LYS A  65     3813   4421  10115    366    -39    582       C  
ATOM    471  C   LYS A  65      42.300   1.183   6.956  1.00 46.78           C  
ANISOU  471  C   LYS A  65     3786   4296   9692    344     -8    592       C  
ATOM    472  O   LYS A  65      43.156   1.020   6.086  1.00 46.03           O  
ANISOU  472  O   LYS A  65     3758   4293   9437    338   -126    650       O  
ATOM    473  CB  LYS A  65      40.139   2.267   6.346  1.00 49.94           C  
ANISOU  473  CB  LYS A  65     3912   4529  10532    416    -81    624       C  
ATOM    474  CG  LYS A  65      38.723   2.144   5.802  1.00 51.65           C  
ANISOU  474  CG  LYS A  65     3947   4677  10997    449   -164    627       C  
ATOM    475  CD  LYS A  65      38.720   1.715   4.344  1.00 52.12           C  
ANISOU  475  CD  LYS A  65     3988   4829  10984    471   -400    695       C  
ATOM    476  CE  LYS A  65      37.397   2.045   3.667  1.00 54.19           C  
ANISOU  476  CE  LYS A  65     4067   5011  11509    525   -534    716       C  
ATOM    477  NZ  LYS A  65      37.580   2.314   2.214  1.00 55.06           N  
ANISOU  477  NZ  LYS A  65     4191   5210  11517    575   -778    822       N  
ATOM    478  N   PHE A  66      42.585   1.578   8.194  1.00 46.40           N  
ANISOU  478  N   PHE A  66     3798   4202   9629    335    149    527       N  
ATOM    479  CA  PHE A  66      43.952   1.869   8.622  1.00 45.31           C  
ANISOU  479  CA  PHE A  66     3802   4108   9305    317    173    514       C  
ATOM    480  C   PHE A  66      44.770   0.591   8.767  1.00 44.18           C  
ANISOU  480  C   PHE A  66     3767   4067   8950    277    172    499       C  
ATOM    481  O   PHE A  66      45.939   0.555   8.381  1.00 43.30           O  
ANISOU  481  O   PHE A  66     3743   4022   8685    261    103    527       O  
ATOM    482  CB  PHE A  66      43.953   2.644   9.942  1.00 45.73           C  
ANISOU  482  CB  PHE A  66     3885   4086   9401    331    326    422       C  
ATOM    483  CG  PHE A  66      43.306   3.994   9.848  1.00 46.84           C  
ANISOU  483  CG  PHE A  66     3918   4110   9767    372    327    422       C  
ATOM    484  CD1 PHE A  66      43.991   5.068   9.300  1.00 46.96           C  
ANISOU  484  CD1 PHE A  66     3935   4089   9816    385    238    477       C  
ATOM    485  CD2 PHE A  66      42.012   4.192  10.302  1.00 48.06           C  
ANISOU  485  CD2 PHE A  66     3957   4178  10126    399    425    372       C  
ATOM    486  CE1 PHE A  66      43.398   6.315   9.210  1.00 48.19           C  
ANISOU  486  CE1 PHE A  66     3981   4118  10208    424    235    485       C  
ATOM    487  CE2 PHE A  66      41.412   5.435  10.213  1.00 49.29           C  
ANISOU  487  CE2 PHE A  66     3999   4212  10514    441    422    366       C  
ATOM    488  CZ  PHE A  66      42.105   6.498   9.667  1.00 49.34           C  
ANISOU  488  CZ  PHE A  66     4012   4177  10556    454    321    424       C  
ATOM    489  N   GLU A  67      44.156  -0.451   9.323  1.00 44.16           N  
ANISOU  489  N   GLU A  67     3749   4067   8963    260    256    461       N  
ATOM    490  CA  GLU A  67      44.823  -1.747   9.456  1.00 43.27           C  
ANISOU  490  CA  GLU A  67     3721   4031   8689    224    252    455       C  
ATOM    491  C   GLU A  67      45.139  -2.329   8.086  1.00 42.79           C  
ANISOU  491  C   GLU A  67     3637   4043   8578    216     82    499       C  
ATOM    492  O   GLU A  67      46.221  -2.871   7.875  1.00 41.90           O  
ANISOU  492  O   GLU A  67     3613   4004   8299    194     34    501       O  
ATOM    493  CB  GLU A  67      43.969  -2.730  10.258  1.00 43.78           C  
ANISOU  493  CB  GLU A  67     3748   4060   8824    210    382    430       C  
ATOM    494  CG  GLU A  67      43.785  -2.339  11.716  1.00 44.61           C  
ANISOU  494  CG  GLU A  67     3909   4126   8913    224    574    384       C  
ATOM    495  CD  GLU A  67      42.839  -3.253  12.468  1.00 45.76           C  
ANISOU  495  CD  GLU A  67     4006   4233   9147    213    732    387       C  
ATOM    496  OE1 GLU A  67      42.512  -4.346  11.959  1.00 45.71           O  
ANISOU  496  OE1 GLU A  67     3934   4225   9208    186    686    421       O  
ATOM    497  OE2 GLU A  67      42.426  -2.878  13.587  1.00 47.07           O  
ANISOU  497  OE2 GLU A  67     4196   4368   9320    235    910    352       O  
ATOM    498  N   ASN A  68      44.198  -2.202   7.154  1.00 43.62           N  
ANISOU  498  N   ASN A  68     3619   4128   8824    239    -12    525       N  
ATOM    499  CA  ASN A  68      44.408  -2.679   5.791  1.00 43.61           C  
ANISOU  499  CA  ASN A  68     3599   4212   8758    246   -184    553       C  
ATOM    500  C   ASN A  68      45.616  -2.002   5.156  1.00 43.20           C  
ANISOU  500  C   ASN A  68     3639   4235   8539    254   -253    611       C  
ATOM    501  O   ASN A  68      46.486  -2.673   4.609  1.00 42.63           O  
ANISOU  501  O   ASN A  68     3630   4256   8309    240   -315    608       O  
ATOM    502  CB  ASN A  68      43.166  -2.444   4.929  1.00 44.75           C  
ANISOU  502  CB  ASN A  68     3598   4323   9080    285   -294    571       C  
ATOM    503  CG  ASN A  68      43.272  -3.102   3.565  1.00 44.90           C  
ANISOU  503  CG  ASN A  68     3600   4444   9013    302   -481    573       C  
ATOM    504  OD1 ASN A  68      43.564  -4.292   3.463  1.00 44.45           O  
ANISOU  504  OD1 ASN A  68     3563   4436   8889    276   -503    514       O  
ATOM    505  ND2 ASN A  68      43.042  -2.329   2.508  1.00 45.78           N  
ANISOU  505  ND2 ASN A  68     3677   4591   9124    352   -618    642       N  
ATOM    506  N   MET A  69      45.669  -0.676   5.247  1.00 43.90           N  
ANISOU  506  N   MET A  69     3724   4271   8684    277   -232    662       N  
ATOM    507  CA  MET A  69      46.804   0.090   4.727  1.00 43.86           C  
ANISOU  507  CA  MET A  69     3790   4310   8566    281   -273    733       C  
ATOM    508  C   MET A  69      48.125  -0.469   5.248  1.00 42.62           C  
ANISOU  508  C   MET A  69     3748   4204   8241    242   -222    690       C  
ATOM    509  O   MET A  69      49.078  -0.630   4.486  1.00 42.26           O  
ANISOU  509  O   MET A  69     3751   4241   8061    236   -281    730       O  
ATOM    510  CB  MET A  69      46.679   1.568   5.103  1.00 44.74           C  
ANISOU  510  CB  MET A  69     3870   4315   8813    303   -225    773       C  
ATOM    511  CG  MET A  69      45.608   2.314   4.326  1.00 46.30           C  
ANISOU  511  CG  MET A  69     3952   4463   9174    351   -308    852       C  
ATOM    512  SD  MET A  69      45.091   3.828   5.151  1.00 47.80           S  
ANISOU  512  SD  MET A  69     4072   4484   9606    375   -219    846       S  
ATOM    513  CE  MET A  69      46.502   4.885   4.841  1.00 47.59           C  
ANISOU  513  CE  MET A  69     4114   4449   9519    369   -231    937       C  
ATOM    514  N   GLY A  70      48.167  -0.770   6.544  1.00 42.19           N  
ANISOU  514  N   GLY A  70     3735   4101   8192    219   -110    610       N  
ATOM    515  CA  GLY A  70      49.332  -1.397   7.161  1.00 41.35           C  
ANISOU  515  CA  GLY A  70     3735   4036   7939    188    -75    564       C  
ATOM    516  C   GLY A  70      49.747  -2.667   6.446  1.00 40.89           C  
ANISOU  516  C   GLY A  70     3694   4070   7770    170   -147    559       C  
ATOM    517  O   GLY A  70      50.901  -2.819   6.049  1.00 40.35           O  
ANISOU  517  O   GLY A  70     3682   4061   7586    157   -186    569       O  
ATOM    518  N   ALA A  71      48.788  -3.569   6.267  1.00 41.47           N  
ANISOU  518  N   ALA A  71     3704   4145   7906    169   -164    536       N  
ATOM    519  CA  ALA A  71      49.036  -4.857   5.627  1.00 41.32           C  
ANISOU  519  CA  ALA A  71     3683   4197   7820    155   -237    505       C  
ATOM    520  C   ALA A  71      49.395  -4.713   4.150  1.00 41.60           C  
ANISOU  520  C   ALA A  71     3704   4329   7772    179   -362    538       C  
ATOM    521  O   ALA A  71      50.287  -5.398   3.660  1.00 41.29           O  
ANISOU  521  O   ALA A  71     3708   4366   7612    170   -405    512       O  
ATOM    522  CB  ALA A  71      47.821  -5.762   5.786  1.00 42.02           C  
ANISOU  522  CB  ALA A  71     3681   4239   8045    151   -228    466       C  
ATOM    523  N   GLN A  72      48.704  -3.821   3.447  1.00 42.83           N  
ANISOU  523  N   GLN A  72     3802   4483   7988    216   -418    599       N  
ATOM    524  CA  GLN A  72      48.917  -3.637   2.008  1.00 43.80           C  
ANISOU  524  CA  GLN A  72     3920   4713   8009    253   -538    650       C  
ATOM    525  C   GLN A  72      50.266  -2.984   1.704  1.00 44.15           C  
ANISOU  525  C   GLN A  72     4045   4809   7919    249   -510    719       C  
ATOM    526  O   GLN A  72      50.824  -3.189   0.627  1.00 44.21           O  
ANISOU  526  O   GLN A  72     4078   4930   7787    270   -572    746       O  
ATOM    527  CB  GLN A  72      47.772  -2.824   1.381  1.00 44.80           C  
ANISOU  527  CB  GLN A  72     3961   4815   8244    301   -615    716       C  
ATOM    528  CG  GLN A  72      46.384  -3.442   1.549  1.00 45.24           C  
ANISOU  528  CG  GLN A  72     3908   4811   8468    309   -655    645       C  
ATOM    529  CD  GLN A  72      46.204  -4.724   0.746  1.00 45.51           C  
ANISOU  529  CD  GLN A  72     3912   4930   8449    317   -773    557       C  
ATOM    530  OE1 GLN A  72      47.143  -5.235   0.140  1.00 45.11           O  
ANISOU  530  OE1 GLN A  72     3931   4989   8219    317   -812    535       O  
ATOM    531  NE2 GLN A  72      44.984  -5.240   0.727  1.00 46.44           N  
ANISOU  531  NE2 GLN A  72     3913   4990   8741    327   -831    494       N  
ATOM    532  N   MET A  73      50.781  -2.201   2.651  1.00 44.90           N  
ANISOU  532  N   MET A  73     4174   4819   8064    226   -412    740       N  
ATOM    533  CA  MET A  73      52.106  -1.587   2.513  1.00 45.42           C  
ANISOU  533  CA  MET A  73     4298   4904   8053    214   -377    794       C  
ATOM    534  C   MET A  73      53.200  -2.650   2.518  1.00 44.99           C  
ANISOU  534  C   MET A  73     4301   4919   7872    185   -370    725       C  
ATOM    535  O   MET A  73      53.962  -2.758   1.558  1.00 45.53           O  
ANISOU  535  O   MET A  73     4389   5082   7828    195   -396    761       O  
ATOM    536  CB  MET A  73      52.366  -0.574   3.634  1.00 45.50           C  
ANISOU  536  CB  MET A  73     4320   4793   8175    197   -292    795       C  
ATOM    537  CG  MET A  73      51.854   0.824   3.340  1.00 46.70           C  
ANISOU  537  CG  MET A  73     4416   4873   8454    227   -295    896       C  
ATOM    538  SD  MET A  73      52.287   1.983   4.650  1.00 47.37           S  
ANISOU  538  SD  MET A  73     4507   4809   8681    211   -205    856       S  
ATOM    539  CE  MET A  73      51.038   1.596   5.864  1.00 47.09           C  
ANISOU  539  CE  MET A  73     4454   4710   8727    215   -151    738       C  
ATOM    540  N   VAL A  74      53.275  -3.414   3.608  1.00 44.52           N  
ANISOU  540  N   VAL A  74     4267   4812   7834    155   -330    632       N  
ATOM    541  CA  VAL A  74      54.239  -4.514   3.735  1.00 44.37           C  
ANISOU  541  CA  VAL A  74     4293   4838   7727    130   -332    562       C  
ATOM    542  C   VAL A  74      54.097  -5.568   2.634  1.00 45.11           C  
ANISOU  542  C   VAL A  74     4359   5034   7744    144   -408    523       C  
ATOM    543  O   VAL A  74      55.094  -6.115   2.157  1.00 44.92           O  
ANISOU  543  O   VAL A  74     4360   5077   7628    139   -420    492       O  
ATOM    544  CB  VAL A  74      54.189  -5.195   5.157  1.00 43.85           C  
ANISOU  544  CB  VAL A  74     4262   4698   7699    103   -281    490       C  
ATOM    545  CG1 VAL A  74      54.654  -6.645   5.129  1.00 43.43           C  
ANISOU  545  CG1 VAL A  74     4222   4681   7597     86   -310    423       C  
ATOM    546  CG2 VAL A  74      55.064  -4.387   6.098  1.00 43.84           C  
ANISOU  546  CG2 VAL A  74     4315   4637   7701     91   -230    490       C  
ATOM    547  N   LYS A  75      52.860  -5.841   2.237  1.00 46.55           N  
ANISOU  547  N   LYS A  75     4483   5223   7979    167   -464    511       N  
ATOM    548  CA  LYS A  75      52.585  -6.849   1.220  1.00 47.87           C  
ANISOU  548  CA  LYS A  75     4615   5480   8091    188   -558    444       C  
ATOM    549  C   LYS A  75      53.141  -6.459  -0.149  1.00 49.44           C  
ANISOU  549  C   LYS A  75     4835   5813   8136    228   -609    490       C  
ATOM    550  O   LYS A  75      53.561  -7.326  -0.916  1.00 49.95           O  
ANISOU  550  O   LYS A  75     4904   5975   8100    242   -658    414       O  
ATOM    551  CB  LYS A  75      51.080  -7.117   1.121  1.00 48.55           C  
ANISOU  551  CB  LYS A  75     4616   5529   8300    206   -620    415       C  
ATOM    552  CG  LYS A  75      50.744  -8.381   0.349  1.00 49.28           C  
ANISOU  552  CG  LYS A  75     4657   5681   8385    222   -725    302       C  
ATOM    553  CD  LYS A  75      49.281  -8.769   0.481  1.00 49.83           C  
ANISOU  553  CD  LYS A  75     4621   5676   8635    228   -778    257       C  
ATOM    554  CE  LYS A  75      48.367  -7.786  -0.223  1.00 50.78           C  
ANISOU  554  CE  LYS A  75     4694   5820   8777    278   -858    323       C  
ATOM    555  NZ  LYS A  75      47.117  -8.415  -0.734  1.00 51.92           N  
ANISOU  555  NZ  LYS A  75     4721   5947   9056    305   -984    238       N  
ATOM    556  N   GLU A  76      53.145  -5.162  -0.452  1.00 51.21           N  
ANISOU  556  N   GLU A  76     5071   6041   8346    249   -589    617       N  
ATOM    557  CA  GLU A  76      53.649  -4.673  -1.734  1.00 53.69           C  
ANISOU  557  CA  GLU A  76     5410   6481   8505    292   -615    701       C  
ATOM    558  C   GLU A  76      55.161  -4.864  -1.849  1.00 53.94           C  
ANISOU  558  C   GLU A  76     5493   6563   8439    270   -537    694       C  
ATOM    559  O   GLU A  76      55.640  -5.427  -2.832  1.00 55.43           O  
ANISOU  559  O   GLU A  76     5700   6883   8477    298   -561    659       O  
ATOM    560  CB  GLU A  76      53.298  -3.196  -1.932  1.00 55.33           C  
ANISOU  560  CB  GLU A  76     5609   6651   8761    317   -601    864       C  
ATOM    561  CG  GLU A  76      53.561  -2.679  -3.342  1.00 57.99           C  
ANISOU  561  CG  GLU A  76     5973   7127   8933    375   -635    986       C  
ATOM    562  CD  GLU A  76      53.563  -1.161  -3.438  1.00 59.79           C  
ANISOU  562  CD  GLU A  76     6193   7291   9231    389   -592   1177       C  
ATOM    563  OE1 GLU A  76      53.125  -0.487  -2.480  1.00 60.03           O  
ANISOU  563  OE1 GLU A  76     6186   7170   9453    363   -560   1193       O  
ATOM    564  OE2 GLU A  76      54.010  -0.637  -4.481  1.00 61.70           O  
ANISOU  564  OE2 GLU A  76     6468   7635   9341    430   -582   1315       O  
ATOM    565  N   VAL A  77      55.904  -4.389  -0.852  1.00 53.46           N  
ANISOU  565  N   VAL A  77     5448   6396   8467    224   -447    717       N  
ATOM    566  CA  VAL A  77      57.371  -4.508  -0.857  1.00 53.45           C  
ANISOU  566  CA  VAL A  77     5476   6415   8418    199   -376    708       C  
ATOM    567  C   VAL A  77      57.856  -5.952  -0.715  1.00 52.73           C  
ANISOU  567  C   VAL A  77     5388   6355   8289    182   -396    559       C  
ATOM    568  O   VAL A  77      58.922  -6.299  -1.224  1.00 53.62           O  
ANISOU  568  O   VAL A  77     5510   6535   8326    183   -360    533       O  
ATOM    569  CB  VAL A  77      58.049  -3.640   0.232  1.00 53.09           C  
ANISOU  569  CB  VAL A  77     5435   6235   8501    158   -301    747       C  
ATOM    570  CG1 VAL A  77      57.821  -2.160  -0.048  1.00 54.25           C  
ANISOU  570  CG1 VAL A  77     5563   6340   8709    174   -271    898       C  
ATOM    571  CG2 VAL A  77      57.567  -4.007   1.630  1.00 52.17           C  
ANISOU  571  CG2 VAL A  77     5325   6007   8487    129   -310    658       C  
ATOM    572  N   ALA A  78      57.083  -6.784  -0.024  1.00 51.71           N  
ANISOU  572  N   ALA A  78     5244   6170   8232    169   -443    467       N  
ATOM    573  CA  ALA A  78      57.422  -8.195   0.126  1.00 51.60           C  
ANISOU  573  CA  ALA A  78     5222   6165   8218    155   -471    335       C  
ATOM    574  C   ALA A  78      57.360  -8.921  -1.218  1.00 53.00           C  
ANISOU  574  C   ALA A  78     5379   6480   8276    197   -534    261       C  
ATOM    575  O   ALA A  78      58.157  -9.824  -1.475  1.00 53.10           O  
ANISOU  575  O   ALA A  78     5387   6533   8255    194   -532    163       O  
ATOM    576  CB  ALA A  78      56.496  -8.859   1.133  1.00 51.20           C  
ANISOU  576  CB  ALA A  78     5151   6012   8290    133   -496    282       C  
ATOM    577  N   SER A  79      56.414  -8.526  -2.068  1.00 54.47           N  
ANISOU  577  N   SER A  79     5552   6741   8401    242   -597    299       N  
ATOM    578  CA  SER A  79      56.270  -9.121  -3.399  1.00 56.14           C  
ANISOU  578  CA  SER A  79     5755   7105   8469    297   -675    221       C  
ATOM    579  C   SER A  79      57.354  -8.643  -4.371  1.00 57.69           C  
ANISOU  579  C   SER A  79     5998   7436   8484    328   -607    283       C  
ATOM    580  O   SER A  79      57.646  -9.325  -5.353  1.00 58.92           O  
ANISOU  580  O   SER A  79     6159   7727   8498    371   -638    186       O  
ATOM    581  CB  SER A  79      54.885  -8.824  -3.978  1.00 56.71           C  
ANISOU  581  CB  SER A  79     5798   7215   8532    345   -786    243       C  
ATOM    582  OG  SER A  79      54.789  -7.482  -4.411  1.00 57.22           O  
ANISOU  582  OG  SER A  79     5896   7321   8524    374   -762    416       O  
ATOM    583  N   LYS A  80      57.935  -7.473  -4.106  1.00 58.22           N  
ANISOU  583  N   LYS A  80     6092   7463   8564    309   -509    439       N  
ATOM    584  CA  LYS A  80      59.058  -6.969  -4.903  1.00 59.85           C  
ANISOU  584  CA  LYS A  80     6330   7770   8639    328   -410    522       C  
ATOM    585  C   LYS A  80      60.299  -7.838  -4.721  1.00 59.67           C  
ANISOU  585  C   LYS A  80     6295   7745   8628    300   -345    404       C  
ATOM    586  O   LYS A  80      61.066  -8.036  -5.664  1.00 61.06           O  
ANISOU  586  O   LYS A  80     6484   8051   8664    333   -287    387       O  
ATOM    587  CB  LYS A  80      59.392  -5.522  -4.538  1.00 60.26           C  
ANISOU  587  CB  LYS A  80     6388   7737   8769    305   -319    713       C  
ATOM    588  CG  LYS A  80      58.301  -4.524  -4.881  1.00 61.64           C  
ANISOU  588  CG  LYS A  80     6568   7916   8935    342   -371    855       C  
ATOM    589  CD  LYS A  80      58.795  -3.096  -4.728  1.00 62.54           C  
ANISOU  589  CD  LYS A  80     6678   7951   9132    326   -271   1047       C  
ATOM    590  CE  LYS A  80      57.657  -2.098  -4.866  1.00 63.78           C  
ANISOU  590  CE  LYS A  80     6825   8070   9337    358   -331   1183       C  
ATOM    591  NZ  LYS A  80      58.157  -0.728  -5.165  1.00 65.26           N  
ANISOU  591  NZ  LYS A  80     7006   8217   9571    362   -237   1397       N  
ATOM    592  N   ALA A  81      60.494  -8.345  -3.505  1.00 58.29           N  
ANISOU  592  N   ALA A  81     6098   7427   8622    244   -352    327       N  
ATOM    593  CA  ALA A  81      61.566  -9.298  -3.229  1.00 58.22           C  
ANISOU  593  CA  ALA A  81     6067   7394   8657    220   -321    205       C  
ATOM    594  C   ALA A  81      61.375 -10.577  -4.043  1.00 59.04           C  
ANISOU  594  C   ALA A  81     6152   7605   8675    259   -387     37       C  
ATOM    595  O   ALA A  81      62.343 -11.170  -4.519  1.00 59.89           O  
ANISOU  595  O   ALA A  81     6242   7772   8740    270   -339    -51       O  
ATOM    596  CB  ALA A  81      61.620  -9.621  -1.742  1.00 56.86           C  
ANISOU  596  CB  ALA A  81     5884   7053   8666    165   -342    169       C  
ATOM    597  N   ASN A  82      60.119 -10.991  -4.194  1.00 59.12           N  
ANISOU  597  N   ASN A  82     6151   7628   8681    282   -498    -18       N  
ATOM    598  CA  ASN A  82      59.775 -12.164  -4.993  1.00 60.17           C  
ANISOU  598  CA  ASN A  82     6254   7852   8753    325   -587   -197       C  
ATOM    599  C   ASN A  82      59.969 -11.914  -6.489  1.00 61.89           C  
ANISOU  599  C   ASN A  82     6507   8281   8725    399   -576   -203       C  
ATOM    600  O   ASN A  82      60.405 -12.806  -7.212  1.00 63.00           O  
ANISOU  600  O   ASN A  82     6632   8520   8782    436   -587   -363       O  
ATOM    601  CB  ASN A  82      58.329 -12.597  -4.712  1.00 59.96           C  
ANISOU  601  CB  ASN A  82     6189   7764   8827    327   -714   -251       C  
ATOM    602  CG  ASN A  82      58.130 -14.097  -4.844  1.00 60.27           C  
ANISOU  602  CG  ASN A  82     6163   7783   8952    334   -803   -462       C  
ATOM    603  OD1 ASN A  82      58.050 -14.813  -3.843  1.00 59.17           O  
ANISOU  603  OD1 ASN A  82     5981   7491   9009    284   -811   -504       O  
ATOM    604  ND2 ASN A  82      58.059 -14.581  -6.079  1.00 61.91           N  
ANISOU  604  ND2 ASN A  82     6362   8143   9015    399   -871   -598       N  
ATOM    605  N   ASP A  83      59.639 -10.708  -6.947  1.00 62.54           N  
ANISOU  605  N   ASP A  83     6637   8433   8689    428   -551    -27       N  
ATOM    606  CA  ASP A  83      59.838 -10.333  -8.351  1.00 64.65           C  
ANISOU  606  CA  ASP A  83     6957   8913   8693    506   -526     13       C  
ATOM    607  C   ASP A  83      61.321 -10.247  -8.698  1.00 64.61           C  
ANISOU  607  C   ASP A  83     6965   8969   8612    503   -358     36       C  
ATOM    608  O   ASP A  83      61.732 -10.651  -9.785  1.00 66.03           O  
ANISOU  608  O   ASP A  83     7169   9327   8590    566   -328    -45       O  
ATOM    609  CB  ASP A  83      59.163  -8.991  -8.670  1.00 65.79           C  
ANISOU  609  CB  ASP A  83     7146   9092   8758    535   -534    235       C  
ATOM    610  CG  ASP A  83      57.650  -9.053  -8.566  1.00 66.44           C  
ANISOU  610  CG  ASP A  83     7204   9138   8899    555   -705    206       C  
ATOM    611  OD1 ASP A  83      57.061 -10.113  -8.865  1.00 67.72           O  
ANISOU  611  OD1 ASP A  83     7334   9341   9054    584   -834     12       O  
ATOM    612  OD2 ASP A  83      57.041  -8.032  -8.188  1.00 66.70           O  
ANISOU  612  OD2 ASP A  83     7240   9093   9009    544   -712    371       O  
ATOM    613  N   ALA A  84      62.114  -9.717  -7.769  1.00 62.97           N  
ANISOU  613  N   ALA A  84     6737   8616   8572    433   -251    136       N  
ATOM    614  CA  ALA A  84      63.541  -9.506  -7.993  1.00 63.35           C  
ANISOU  614  CA  ALA A  84     6774   8689   8604    421    -85    175       C  
ATOM    615  C   ALA A  84      64.327 -10.814  -7.983  1.00 63.08           C  
ANISOU  615  C   ALA A  84     6692   8658   8617    416    -74    -43       C  
ATOM    616  O   ALA A  84      65.062 -11.105  -8.926  1.00 64.64           O  
ANISOU  616  O   ALA A  84     6891   8997   8670    461     17   -102       O  
ATOM    617  CB  ALA A  84      64.101  -8.554  -6.947  1.00 62.09           C  
ANISOU  617  CB  ALA A  84     6591   8353   8647    349     -5    325       C  
ATOM    618  N   ALA A  85      64.160 -11.596  -6.918  1.00 61.22           N  
ANISOU  618  N   ALA A  85     6411   8264   8585    366   -162   -157       N  
ATOM    619  CA  ALA A  85      64.974 -12.793  -6.684  1.00 60.67           C  
ANISOU  619  CA  ALA A  85     6281   8146   8624    351   -157   -343       C  
ATOM    620  C   ALA A  85      64.256 -14.125  -6.940  1.00 60.89           C  
ANISOU  620  C   ALA A  85     6279   8197   8656    382   -292   -559       C  
ATOM    621  O   ALA A  85      64.897 -15.177  -6.944  1.00 61.11           O  
ANISOU  621  O   ALA A  85     6251   8200   8769    383   -292   -729       O  
ATOM    622  CB  ALA A  85      65.519 -12.765  -5.266  1.00 58.90           C  
ANISOU  622  CB  ALA A  85     6021   7713   8643    276   -153   -306       C  
ATOM    623  N   GLY A  86      62.941 -14.086  -7.145  1.00 60.90           N  
ANISOU  623  N   GLY A  86     6305   8233   8599    407   -412   -560       N  
ATOM    624  CA  GLY A  86      62.163 -15.302  -7.397  1.00 60.97           C  
ANISOU  624  CA  GLY A  86     6270   8248   8648    436   -553   -768       C  
ATOM    625  C   GLY A  86      61.666 -16.018  -6.149  1.00 58.91           C  
ANISOU  625  C   GLY A  86     5951   7776   8654    374   -636   -808       C  
ATOM    626  O   GLY A  86      61.015 -17.060  -6.251  1.00 59.44           O  
ANISOU  626  O   GLY A  86     5960   7810   8812    387   -749   -972       O  
ATOM    627  N   ASP A  87      61.955 -15.460  -4.974  1.00 56.73           N  
ANISOU  627  N   ASP A  87     5689   7356   8507    310   -580   -658       N  
ATOM    628  CA  ASP A  87      61.583 -16.077  -3.699  1.00 55.19           C  
ANISOU  628  CA  ASP A  87     5458   6971   8541    255   -633   -664       C  
ATOM    629  C   ASP A  87      61.766 -15.070  -2.559  1.00 52.96           C  
ANISOU  629  C   ASP A  87     5223   6583   8316    204   -570   -475       C  
ATOM    630  O   ASP A  87      62.470 -14.068  -2.716  1.00 52.81           O  
ANISOU  630  O   ASP A  87     5243   6612   8211    203   -482   -369       O  
ATOM    631  CB  ASP A  87      62.444 -17.326  -3.444  1.00 55.85           C  
ANISOU  631  CB  ASP A  87     5476   6974   8768    243   -640   -811       C  
ATOM    632  CG  ASP A  87      61.871 -18.236  -2.360  1.00 55.61           C  
ANISOU  632  CG  ASP A  87     5400   6762   8966    203   -714   -833       C  
ATOM    633  OD1 ASP A  87      60.639 -18.356  -2.250  1.00 56.49           O  
ANISOU  633  OD1 ASP A  87     5496   6841   9124    201   -782   -828       O  
ATOM    634  OD2 ASP A  87      62.653 -18.851  -1.617  1.00 55.65           O  
ANISOU  634  OD2 ASP A  87     5377   6650   9115    175   -702   -849       O  
ATOM    635  N   GLY A  88      61.127 -15.338  -1.423  1.00 51.50           N  
ANISOU  635  N   GLY A  88     5031   6254   8280    166   -610   -438       N  
ATOM    636  CA  GLY A  88      61.362 -14.579  -0.192  1.00 50.13           C  
ANISOU  636  CA  GLY A  88     4904   5974   8167    123   -560   -298       C  
ATOM    637  C   GLY A  88      60.252 -13.636   0.239  1.00 49.64           C  
ANISOU  637  C   GLY A  88     4878   5888   8093    116   -559   -179       C  
ATOM    638  O   GLY A  88      60.509 -12.683   0.975  1.00 49.09           O  
ANISOU  638  O   GLY A  88     4854   5770   8028     95   -507    -69       O  
ATOM    639  N   THR A  89      59.022 -13.891  -0.207  1.00 49.85           N  
ANISOU  639  N   THR A  89     4875   5941   8125    136   -621   -212       N  
ATOM    640  CA  THR A  89      57.865 -13.105   0.226  1.00 48.99           C  
ANISOU  640  CA  THR A  89     4777   5792   8042    131   -622   -113       C  
ATOM    641  C   THR A  89      57.595 -13.368   1.701  1.00 47.42           C  
ANISOU  641  C   THR A  89     4589   5445   7981     89   -592    -68       C  
ATOM    642  O   THR A  89      57.495 -12.434   2.498  1.00 46.85           O  
ANISOU  642  O   THR A  89     4565   5327   7909     74   -537     33       O  
ATOM    643  CB  THR A  89      56.599 -13.456  -0.581  1.00 50.22           C  
ANISOU  643  CB  THR A  89     4877   5996   8207    164   -713   -178       C  
ATOM    644  OG1 THR A  89      56.837 -13.222  -1.975  1.00 51.75           O  
ANISOU  644  OG1 THR A  89     5078   6350   8231    216   -749   -218       O  
ATOM    645  CG2 THR A  89      55.405 -12.614  -0.130  1.00 50.16           C  
ANISOU  645  CG2 THR A  89     4866   5936   8255    160   -709    -75       C  
ATOM    646  N   THR A  90      57.475 -14.647   2.050  1.00 46.55           N  
ANISOU  646  N   THR A  90     4434   5262   7989     75   -625   -146       N  
ATOM    647  CA  THR A  90      57.252 -15.065   3.430  1.00 45.13           C  
ANISOU  647  CA  THR A  90     4270   4949   7928     43   -589    -91       C  
ATOM    648  C   THR A  90      58.340 -14.507   4.340  1.00 43.89           C  
ANISOU  648  C   THR A  90     4194   4763   7717     28   -537    -20       C  
ATOM    649  O   THR A  90      58.041 -13.872   5.347  1.00 42.77           O  
ANISOU  649  O   THR A  90     4107   4570   7572     17   -488     67       O  
ATOM    650  CB  THR A  90      57.227 -16.601   3.547  1.00 45.40           C  
ANISOU  650  CB  THR A  90     4237   4903   8108     32   -633   -176       C  
ATOM    651  OG1 THR A  90      56.319 -17.139   2.579  1.00 46.00           O  
ANISOU  651  OG1 THR A  90     4222   5007   8248     51   -704   -277       O  
ATOM    652  CG2 THR A  90      56.798 -17.043   4.944  1.00 45.18           C  
ANISOU  652  CG2 THR A  90     4226   4741   8199      4   -584    -85       C  
ATOM    653  N   THR A  91      59.598 -14.732   3.963  1.00 43.70           N  
ANISOU  653  N   THR A  91     4171   4773   7657     32   -552    -72       N  
ATOM    654  CA  THR A  91      60.749 -14.290   4.759  1.00 43.08           C  
ANISOU  654  CA  THR A  91     4150   4659   7557     21   -528    -28       C  
ATOM    655  C   THR A  91      60.747 -12.774   4.994  1.00 42.22           C  
ANISOU  655  C   THR A  91     4095   4574   7372     21   -480     55       C  
ATOM    656  O   THR A  91      61.018 -12.315   6.106  1.00 41.96           O  
ANISOU  656  O   THR A  91     4120   4480   7343     12   -465    105       O  
ATOM    657  CB  THR A  91      62.081 -14.691   4.090  1.00 43.43           C  
ANISOU  657  CB  THR A  91     4160   4741   7598     28   -545   -108       C  
ATOM    658  OG1 THR A  91      61.996 -16.040   3.614  1.00 44.04           O  
ANISOU  658  OG1 THR A  91     4171   4806   7756     35   -592   -213       O  
ATOM    659  CG2 THR A  91      63.241 -14.576   5.074  1.00 43.29           C  
ANISOU  659  CG2 THR A  91     4179   4652   7616     16   -550    -82       C  
ATOM    660  N   ALA A  92      60.439 -12.010   3.947  1.00 41.52           N  
ANISOU  660  N   ALA A  92     3986   4572   7215     36   -464     70       N  
ATOM    661  CA  ALA A  92      60.386 -10.551   4.038  1.00 40.56           C  
ANISOU  661  CA  ALA A  92     3898   4460   7053     37   -420    156       C  
ATOM    662  C   ALA A  92      59.264 -10.068   4.957  1.00 39.93           C  
ANISOU  662  C   ALA A  92     3846   4316   7007     34   -400    211       C  
ATOM    663  O   ALA A  92      59.419  -9.062   5.648  1.00 39.78           O  
ANISOU  663  O   ALA A  92     3866   4255   6991     30   -367    259       O  
ATOM    664  CB  ALA A  92      60.227  -9.942   2.653  1.00 40.98           C  
ANISOU  664  CB  ALA A  92     3923   4621   7026     62   -409    181       C  
ATOM    665  N   THR A  93      58.141 -10.784   4.956  1.00 39.74           N  
ANISOU  665  N   THR A  93     3793   4279   7025     36   -416    193       N  
ATOM    666  CA  THR A  93      56.982 -10.425   5.778  1.00 39.33           C  
ANISOU  666  CA  THR A  93     3752   4166   7024     35   -377    242       C  
ATOM    667  C   THR A  93      57.256 -10.637   7.273  1.00 38.94           C  
ANISOU  667  C   THR A  93     3770   4037   6988     22   -338    261       C  
ATOM    668  O   THR A  93      56.856  -9.808   8.093  1.00 39.03           O  
ANISOU  668  O   THR A  93     3823   4014   6992     27   -286    300       O  
ATOM    669  CB  THR A  93      55.725 -11.215   5.344  1.00 39.67           C  
ANISOU  669  CB  THR A  93     3724   4204   7144     39   -403    214       C  
ATOM    670  OG1 THR A  93      55.533 -11.073   3.930  1.00 39.74           O  
ANISOU  670  OG1 THR A  93     3682   4305   7111     63   -464    182       O  
ATOM    671  CG2 THR A  93      54.466 -10.724   6.071  1.00 39.84           C  
ANISOU  671  CG2 THR A  93     3737   4163   7238     39   -345    267       C  
ATOM    672  N   VAL A  94      57.940 -11.727   7.626  1.00 38.57           N  
ANISOU  672  N   VAL A  94     3735   3964   6956     13   -367    230       N  
ATOM    673  CA  VAL A  94      58.271 -11.988   9.046  1.00 38.40           C  
ANISOU  673  CA  VAL A  94     3790   3878   6920     12   -346    262       C  
ATOM    674  C   VAL A  94      59.365 -11.036   9.533  1.00 38.04           C  
ANISOU  674  C   VAL A  94     3808   3838   6807     19   -361    257       C  
ATOM    675  O   VAL A  94      59.329 -10.587  10.680  1.00 38.00           O  
ANISOU  675  O   VAL A  94     3878   3801   6757     31   -336    279       O  
ATOM    676  CB  VAL A  94      58.608 -13.483   9.388  1.00 38.54           C  
ANISOU  676  CB  VAL A  94     3799   3847   6995      5   -380    254       C  
ATOM    677  CG1 VAL A  94      58.545 -14.408   8.181  1.00 38.68           C  
ANISOU  677  CG1 VAL A  94     3718   3883   7093     -2   -429    185       C  
ATOM    678  CG2 VAL A  94      59.954 -13.628  10.096  1.00 38.50           C  
ANISOU  678  CG2 VAL A  94     3857   3820   6948     12   -429    249       C  
ATOM    679  N   LEU A  95      60.323 -10.724   8.661  1.00 37.78           N  
ANISOU  679  N   LEU A  95     3739   3842   6772     15   -399    220       N  
ATOM    680  CA  LEU A  95      61.357  -9.739   8.975  1.00 37.83           C  
ANISOU  680  CA  LEU A  95     3775   3838   6761     18   -414    210       C  
ATOM    681  C   LEU A  95      60.753  -8.352   9.189  1.00 37.94           C  
ANISOU  681  C   LEU A  95     3805   3843   6766     25   -367    241       C  
ATOM    682  O   LEU A  95      61.120  -7.654  10.135  1.00 38.30           O  
ANISOU  682  O   LEU A  95     3902   3848   6801     35   -374    226       O  
ATOM    683  CB  LEU A  95      62.419  -9.683   7.870  1.00 37.96           C  
ANISOU  683  CB  LEU A  95     3728   3893   6801      9   -435    179       C  
ATOM    684  CG  LEU A  95      63.394 -10.861   7.815  1.00 38.29           C  
ANISOU  684  CG  LEU A  95     3747   3923   6878      6   -488    125       C  
ATOM    685  CD1 LEU A  95      64.150 -10.871   6.495  1.00 38.65           C  
ANISOU  685  CD1 LEU A  95     3717   4028   6939      3   -474     90       C  
ATOM    686  CD2 LEU A  95      64.367 -10.824   8.983  1.00 38.52           C  
ANISOU  686  CD2 LEU A  95     3823   3884   6927     11   -546    108       C  
ATOM    687  N   ALA A  96      59.832  -7.959   8.310  1.00 37.86           N  
ANISOU  687  N   ALA A  96     3746   3869   6768     26   -331    275       N  
ATOM    688  CA  ALA A  96      59.158  -6.664   8.426  1.00 38.00           C  
ANISOU  688  CA  ALA A  96     3764   3866   6807     36   -288    310       C  
ATOM    689  C   ALA A  96      58.413  -6.562   9.751  1.00 38.26           C  
ANISOU  689  C   ALA A  96     3856   3850   6830     48   -247    302       C  
ATOM    690  O   ALA A  96      58.541  -5.571  10.466  1.00 38.83           O  
ANISOU  690  O   ALA A  96     3962   3883   6908     61   -231    284       O  
ATOM    691  CB  ALA A  96      58.199  -6.443   7.267  1.00 38.07           C  
ANISOU  691  CB  ALA A  96     3709   3922   6833     42   -275    355       C  
ATOM    692  N   GLN A  97      57.648  -7.599  10.077  1.00 38.36           N  
ANISOU  692  N   GLN A  97     3877   3863   6833     48   -225    313       N  
ATOM    693  CA  GLN A  97      56.904  -7.649  11.335  1.00 38.91           C  
ANISOU  693  CA  GLN A  97     4007   3897   6880     63   -158    321       C  
ATOM    694  C   GLN A  97      57.814  -7.430  12.543  1.00 39.46           C  
ANISOU  694  C   GLN A  97     4176   3950   6867     81   -179    286       C  
ATOM    695  O   GLN A  97      57.484  -6.659  13.444  1.00 39.92           O  
ANISOU  695  O   GLN A  97     4288   3991   6889    105   -133    263       O  
ATOM    696  CB  GLN A  97      56.188  -8.996  11.476  1.00 38.98           C  
ANISOU  696  CB  GLN A  97     4001   3897   6913     54   -129    353       C  
ATOM    697  CG  GLN A  97      55.280  -9.073  12.694  1.00 39.60           C  
ANISOU  697  CG  GLN A  97     4130   3942   6970     71    -25    387       C  
ATOM    698  CD  GLN A  97      54.618 -10.401  12.894  1.00 39.90           C  
ANISOU  698  CD  GLN A  97     4144   3951   7064     59     18    439       C  
ATOM    699  OE1 GLN A  97      53.474 -10.452  13.345  1.00 40.57           O  
ANISOU  699  OE1 GLN A  97     4208   4005   7199     63    124    478       O  
ATOM    700  NE2 GLN A  97      55.288 -11.473  12.515  1.00 39.68           N  
ANISOU  700  NE2 GLN A  97     4098   3919   7057     42    -55    439       N  
ATOM    701  N   ALA A  98      58.957  -8.112  12.548  1.00 39.76           N  
ANISOU  701  N   ALA A  98     4234   3993   6879     74   -258    268       N  
ATOM    702  CA  ALA A  98      59.893  -8.067  13.673  1.00 40.40           C  
ANISOU  702  CA  ALA A  98     4406   4059   6883     97   -313    231       C  
ATOM    703  C   ALA A  98      60.519  -6.687  13.862  1.00 40.66           C  
ANISOU  703  C   ALA A  98     4444   4072   6931    109   -347    163       C  
ATOM    704  O   ALA A  98      60.671  -6.224  14.994  1.00 41.70           O  
ANISOU  704  O   ALA A  98     4659   4193   6990    143   -361    114       O  
ATOM    705  CB  ALA A  98      60.981  -9.116  13.494  1.00 40.30           C  
ANISOU  705  CB  ALA A  98     4387   4044   6881     88   -402    227       C  
ATOM    706  N   ILE A  99      60.885  -6.041  12.758  1.00 40.11           N  
ANISOU  706  N   ILE A  99     4286   3997   6957     85   -360    161       N  
ATOM    707  CA  ILE A  99      61.481  -4.706  12.815  1.00 40.61           C  
ANISOU  707  CA  ILE A  99     4326   4016   7085     89   -385    109       C  
ATOM    708  C   ILE A  99      60.424  -3.687  13.240  1.00 41.09           C  
ANISOU  708  C   ILE A  99     4398   4054   7158    110   -314     98       C  
ATOM    709  O   ILE A  99      60.694  -2.809  14.061  1.00 42.05           O  
ANISOU  709  O   ILE A  99     4553   4134   7289    134   -336     19       O  
ATOM    710  CB  ILE A  99      62.096  -4.287  11.461  1.00 40.39           C  
ANISOU  710  CB  ILE A  99     4195   3987   7164     59   -391    142       C  
ATOM    711  CG1 ILE A  99      63.210  -5.255  11.050  1.00 40.27           C  
ANISOU  711  CG1 ILE A  99     4158   3991   7152     43   -449    133       C  
ATOM    712  CG2 ILE A  99      62.672  -2.876  11.544  1.00 41.03           C  
ANISOU  712  CG2 ILE A  99     4235   3997   7355     60   -405    105       C  
ATOM    713  CD1 ILE A  99      63.573  -5.188   9.582  1.00 40.14           C  
ANISOU  713  CD1 ILE A  99     4048   4007   7195     19   -419    181       C  
ATOM    714  N   ILE A 100      59.226  -3.815  12.676  1.00 40.80           N  
ANISOU  714  N   ILE A 100     4324   4039   7137    103   -237    163       N  
ATOM    715  CA  ILE A 100      58.120  -2.907  12.973  1.00 41.27           C  
ANISOU  715  CA  ILE A 100     4373   4069   7237    123   -161    157       C  
ATOM    716  C   ILE A 100      57.676  -3.014  14.432  1.00 42.14           C  
ANISOU  716  C   ILE A 100     4584   4181   7246    160   -115     99       C  
ATOM    717  O   ILE A 100      57.494  -2.000  15.100  1.00 42.76           O  
ANISOU  717  O   ILE A 100     4681   4223   7343    188    -91     25       O  
ATOM    718  CB  ILE A 100      56.918  -3.167  12.036  1.00 41.05           C  
ANISOU  718  CB  ILE A 100     4274   4063   7260    111   -105    238       C  
ATOM    719  CG1 ILE A 100      57.266  -2.740  10.605  1.00 40.77           C  
ANISOU  719  CG1 ILE A 100     4151   4037   7301     91   -144    296       C  
ATOM    720  CG2 ILE A 100      55.681  -2.417  12.513  1.00 41.70           C  
ANISOU  720  CG2 ILE A 100     4340   4106   7395    136    -20    227       C  
ATOM    721  CD1 ILE A 100      56.391  -3.368   9.540  1.00 40.72           C  
ANISOU  721  CD1 ILE A 100     4086   4080   7305     84   -138    363       C  
ATOM    722  N   THR A 101      57.500  -4.241  14.918  1.00 42.46           N  
ANISOU  722  N   THR A 101     4687   4263   7183    163    -96    133       N  
ATOM    723  CA  THR A 101      57.025  -4.470  16.285  1.00 43.62           C  
ANISOU  723  CA  THR A 101     4940   4428   7203    203    -29    109       C  
ATOM    724  C   THR A 101      57.938  -3.812  17.321  1.00 44.90           C  
ANISOU  724  C   THR A 101     5193   4588   7275    244   -101      0       C  
ATOM    725  O   THR A 101      57.473  -3.050  18.167  1.00 45.76           O  
ANISOU  725  O   THR A 101     5351   4695   7338    286    -45    -76       O  
ATOM    726  CB  THR A 101      56.905  -5.977  16.593  1.00 43.46           C  
ANISOU  726  CB  THR A 101     4970   4442   7100    198    -10    192       C  
ATOM    727  OG1 THR A 101      56.057  -6.600  15.619  1.00 42.78           O  
ANISOU  727  OG1 THR A 101     4784   4347   7121    162     39    269       O  
ATOM    728  CG2 THR A 101      56.319  -6.204  17.981  1.00 44.84           C  
ANISOU  728  CG2 THR A 101     5260   4645   7132    245     88    199       C  
ATOM    729  N   GLU A 102      59.232  -4.110  17.241  1.00 45.25           N  
ANISOU  729  N   GLU A 102     5252   4631   7308    236   -230    -24       N  
ATOM    730  CA  GLU A 102      60.224  -3.558  18.169  1.00 46.54           C  
ANISOU  730  CA  GLU A 102     5489   4787   7407    276   -336   -143       C  
ATOM    731  C   GLU A 102      60.544  -2.097  17.869  1.00 46.72           C  
ANISOU  731  C   GLU A 102     5433   4740   7579    272   -370   -242       C  
ATOM    732  O   GLU A 102      60.907  -1.342  18.773  1.00 48.02           O  
ANISOU  732  O   GLU A 102     5649   4885   7708    316   -425   -373       O  
ATOM    733  CB  GLU A 102      61.503  -4.399  18.138  1.00 46.78           C  
ANISOU  733  CB  GLU A 102     5536   4822   7414    267   -471   -133       C  
ATOM    734  CG  GLU A 102      61.298  -5.842  18.576  1.00 47.39           C  
ANISOU  734  CG  GLU A 102     5694   4950   7361    278   -453    -35       C  
ATOM    735  CD  GLU A 102      60.766  -5.951  19.993  1.00 49.31           C  
ANISOU  735  CD  GLU A 102     6085   5247   7401    343   -403    -44       C  
ATOM    736  OE1 GLU A 102      61.452  -5.474  20.920  1.00 50.91           O  
ANISOU  736  OE1 GLU A 102     6375   5466   7502    396   -503   -150       O  
ATOM    737  OE2 GLU A 102      59.663  -6.510  20.177  1.00 49.61           O  
ANISOU  737  OE2 GLU A 102     6150   5313   7384    344   -264     50       O  
ATOM    738  N   GLY A 103      60.407  -1.702  16.605  1.00 45.86           N  
ANISOU  738  N   GLY A 103     5199   4589   7635    225   -342   -180       N  
ATOM    739  CA  GLY A 103      60.608  -0.312  16.207  1.00 46.36           C  
ANISOU  739  CA  GLY A 103     5172   4570   7873    217   -355   -236       C  
ATOM    740  C   GLY A 103      59.547   0.611  16.777  1.00 47.58           C  
ANISOU  740  C   GLY A 103     5334   4696   8046    253   -270   -298       C  
ATOM    741  O   GLY A 103      59.867   1.607  17.424  1.00 48.32           O  
ANISOU  741  O   GLY A 103     5431   4732   8195    283   -312   -432       O  
ATOM    742  N   LEU A 104      58.280   0.267  16.545  1.00 48.00           N  
ANISOU  742  N   LEU A 104     5381   4783   8072    251   -153   -216       N  
ATOM    743  CA  LEU A 104      57.149   1.073  17.019  1.00 49.10           C  
ANISOU  743  CA  LEU A 104     5511   4893   8251    284    -50   -269       C  
ATOM    744  C   LEU A 104      57.061   1.088  18.542  1.00 50.88           C  
ANISOU  744  C   LEU A 104     5866   5159   8305    347    -27   -398       C  
ATOM    745  O   LEU A 104      56.584   2.059  19.127  1.00 52.23           O  
ANISOU  745  O   LEU A 104     6033   5291   8519    387     20   -512       O  
ATOM    746  CB  LEU A 104      55.830   0.563  16.430  1.00 48.59           C  
ANISOU  746  CB  LEU A 104     5398   4852   8210    268     63   -150       C  
ATOM    747  CG  LEU A 104      55.679   0.620  14.907  1.00 47.82           C  
ANISOU  747  CG  LEU A 104     5179   4731   8256    223     41    -29       C  
ATOM    748  CD1 LEU A 104      54.367  -0.024  14.490  1.00 47.57           C  
ANISOU  748  CD1 LEU A 104     5107   4728   8237    216    129     59       C  
ATOM    749  CD2 LEU A 104      55.757   2.047  14.387  1.00 48.42           C  
ANISOU  749  CD2 LEU A 104     5159   4713   8525    223     20    -46       C  
ATOM    750  N   LYS A 105      57.509   0.007  19.176  1.00 51.58           N  
ANISOU  750  N   LYS A 105     6070   5329   8199    361    -59   -379       N  
ATOM    751  CA  LYS A 105      57.664  -0.019  20.630  1.00 53.62           C  
ANISOU  751  CA  LYS A 105     6474   5645   8253    430    -66   -495       C  
ATOM    752  C   LYS A 105      58.669   1.034  21.090  1.00 54.58           C  
ANISOU  752  C   LYS A 105     6599   5715   8424    462   -204   -676       C  
ATOM    753  O   LYS A 105      58.408   1.770  22.041  1.00 56.23           O  
ANISOU  753  O   LYS A 105     6866   5930   8569    524   -183   -829       O  
ATOM    754  CB  LYS A 105      58.088  -1.411  21.117  1.00 54.14           C  
ANISOU  754  CB  LYS A 105     6657   5798   8115    440   -100   -410       C  
ATOM    755  CG  LYS A 105      56.954  -2.204  21.738  1.00 55.21           C  
ANISOU  755  CG  LYS A 105     6872   6004   8099    465     67   -319       C  
ATOM    756  CD  LYS A 105      57.366  -3.621  22.081  1.00 55.39           C  
ANISOU  756  CD  LYS A 105     6989   6089   7965    467     34   -200       C  
ATOM    757  CE  LYS A 105      58.368  -3.687  23.214  1.00 56.83           C  
ANISOU  757  CE  LYS A 105     7321   6330   7939    534    -94   -288       C  
ATOM    758  NZ  LYS A 105      58.626  -5.098  23.614  1.00 57.20           N  
ANISOU  758  NZ  LYS A 105     7463   6432   7836    544   -111   -145       N  
ATOM    759  N   ALA A 106      59.805   1.106  20.400  1.00 54.11           N  
ANISOU  759  N   ALA A 106     6466   5599   8493    420   -341   -668       N  
ATOM    760  CA  ALA A 106      60.847   2.089  20.712  1.00 55.32           C  
ANISOU  760  CA  ALA A 106     6588   5676   8755    439   -485   -836       C  
ATOM    761  C   ALA A 106      60.407   3.530  20.430  1.00 56.17           C  
ANISOU  761  C   ALA A 106     6580   5670   9089    437   -442   -922       C  
ATOM    762  O   ALA A 106      60.920   4.464  21.042  1.00 57.62           O  
ANISOU  762  O   ALA A 106     6753   5789   9348    474   -532  -1107       O  
ATOM    763  CB  ALA A 106      62.123   1.770  19.946  1.00 54.40           C  
ANISOU  763  CB  ALA A 106     6396   5515   8758    388   -614   -785       C  
ATOM    764  N   VAL A 107      59.470   3.710  19.503  1.00 55.71           N  
ANISOU  764  N   VAL A 107     6429   5582   9157    398   -318   -794       N  
ATOM    765  CA  VAL A 107      58.894   5.030  19.239  1.00 56.66           C  
ANISOU  765  CA  VAL A 107     6438   5589   9499    402   -267   -851       C  
ATOM    766  C   VAL A 107      57.991   5.455  20.400  1.00 59.06           C  
ANISOU  766  C   VAL A 107     6818   5920   9699    475   -181  -1003       C  
ATOM    767  O   VAL A 107      58.022   6.615  20.816  1.00 60.90           O  
ANISOU  767  O   VAL A 107     7004   6061  10071    509   -206  -1170       O  
ATOM    768  CB  VAL A 107      58.124   5.054  17.899  1.00 55.25           C  
ANISOU  768  CB  VAL A 107     6143   5378   9471    350   -175   -659       C  
ATOM    769  CG1 VAL A 107      57.401   6.377  17.688  1.00 56.02           C  
ANISOU  769  CG1 VAL A 107     6127   5355   9800    362   -119   -701       C  
ATOM    770  CG2 VAL A 107      59.082   4.823  16.742  1.00 54.14           C  
ANISOU  770  CG2 VAL A 107     5924   5211   9434    288   -250   -531       C  
ATOM    771  N   ALA A 108      57.199   4.518  20.921  1.00 59.95           N  
ANISOU  771  N   ALA A 108     7042   6153   9582    500    -71   -947       N  
ATOM    772  CA  ALA A 108      56.347   4.771  22.091  1.00 62.37           C  
ANISOU  772  CA  ALA A 108     7439   6512   9745    575     39  -1079       C  
ATOM    773  C   ALA A 108      57.176   5.013  23.356  1.00 64.75           C  
ANISOU  773  C   ALA A 108     7868   6860   9872    648    -72  -1292       C  
ATOM    774  O   ALA A 108      56.770   5.771  24.241  1.00 67.25           O  
ANISOU  774  O   ALA A 108     8223   7177  10149    718    -28  -1481       O  
ATOM    775  CB  ALA A 108      55.388   3.612  22.304  1.00 62.12           C  
ANISOU  775  CB  ALA A 108     7487   6593   9521    578    193   -938       C  
ATOM    776  N   CYS A 109      58.325   4.348  23.431  1.00 64.72           N  
ANISOU  776  N   CYS A 109     7928   6897   9764    637   -224  -1270       N  
ATOM    777  CA  CYS A 109      59.341   4.589  24.457  1.00 67.16           C  
ANISOU  777  CA  CYS A 109     8336   7235   9945    702   -391  -1470       C  
ATOM    778  C   CYS A 109      59.743   6.059  24.601  1.00 68.00           C  
ANISOU  778  C   CYS A 109     8342   7208  10285    725   -487  -1701       C  
ATOM    779  O   CYS A 109      60.055   6.510  25.708  1.00 70.54           O  
ANISOU  779  O   CYS A 109     8754   7562  10483    808   -572  -1932       O  
ATOM    780  CB  CYS A 109      60.567   3.729  24.137  1.00 67.34           C  
ANISOU  780  CB  CYS A 109     8376   7275   9934    665   -553  -1381       C  
ATOM    781  SG  CYS A 109      60.352   1.964  24.513  1.00 68.73           S  
ANISOU  781  SG  CYS A 109     8717   7615   9781    676   -494  -1184       S  
ATOM    782  N   GLY A 110      59.706   6.801  23.494  1.00 66.32           N  
ANISOU  782  N   GLY A 110     7944   6845  10407    657   -473  -1638       N  
ATOM    783  CA  GLY A 110      60.107   8.209  23.463  1.00 66.97           C  
ANISOU  783  CA  GLY A 110     7896   6763  10784    664   -559  -1822       C  
ATOM    784  C   GLY A 110      61.319   8.472  22.583  1.00 65.52           C  
ANISOU  784  C   GLY A 110     7575   6453  10866    595   -700  -1768       C  
ATOM    785  O   GLY A 110      61.794   9.607  22.508  1.00 66.72           O  
ANISOU  785  O   GLY A 110     7600   6447  11303    592   -782  -1904       O  
ATOM    786  N   MET A 111      61.817   7.435  21.911  1.00 62.92           N  
ANISOU  786  N   MET A 111     7259   6182  10463    539   -720  -1572       N  
ATOM    787  CA  MET A 111      63.015   7.554  21.082  1.00 61.57           C  
ANISOU  787  CA  MET A 111     6963   5909  10521    475   -834  -1511       C  
ATOM    788  C   MET A 111      62.675   8.124  19.712  1.00 59.79           C  
ANISOU  788  C   MET A 111     6570   5570  10577    403   -732  -1330       C  
ATOM    789  O   MET A 111      61.546   7.998  19.239  1.00 58.52           O  
ANISOU  789  O   MET A 111     6407   5446  10378    393   -587  -1197       O  
ATOM    790  CB  MET A 111      63.694   6.195  20.915  1.00 60.43           C  
ANISOU  790  CB  MET A 111     6897   5874  10188    451   -889  -1385       C  
ATOM    791  CG  MET A 111      64.035   5.501  22.223  1.00 61.71           C  
ANISOU  791  CG  MET A 111     7238   6159  10049    526   -997  -1517       C  
ATOM    792  SD  MET A 111      64.923   3.961  21.951  1.00 60.77           S  
ANISOU  792  SD  MET A 111     7179   6132   9779    496  -1079  -1362       S  
ATOM    793  CE  MET A 111      64.648   3.128  23.512  1.00 62.27           C  
ANISOU  793  CE  MET A 111     7613   6495   9550    599  -1122  -1446       C  
ATOM    794  N   ASN A 112      63.672   8.742  19.087  1.00 59.53           N  
ANISOU  794  N   ASN A 112     6392   5396  10829    358   -811  -1321       N  
ATOM    795  CA  ASN A 112      63.504   9.423  17.807  1.00 58.87           C  
ANISOU  795  CA  ASN A 112     6146   5194  11028    297   -725  -1144       C  
ATOM    796  C   ASN A 112      63.300   8.421  16.670  1.00 56.74           C  
ANISOU  796  C   ASN A 112     5888   5029  10641    245   -634   -880       C  
ATOM    797  O   ASN A 112      64.161   7.576  16.441  1.00 56.39           O  
ANISOU  797  O   ASN A 112     5867   5043  10512    219   -689   -829       O  
ATOM    798  CB  ASN A 112      64.733  10.296  17.528  1.00 60.07           C  
ANISOU  798  CB  ASN A 112     6139   5165  11517    265   -827  -1202       C  
ATOM    799  CG  ASN A 112      64.497  11.325  16.435  1.00 60.43           C  
ANISOU  799  CG  ASN A 112     6012   5055  11893    220   -736  -1047       C  
ATOM    800  OD1 ASN A 112      63.639  11.156  15.570  1.00 59.52           O  
ANISOU  800  OD1 ASN A 112     5893   4989  11731    199   -611   -841       O  
ATOM    801  ND2 ASN A 112      65.270  12.401  16.470  1.00 62.22           N  
ANISOU  801  ND2 ASN A 112     6089   5084  12467    207   -808  -1144       N  
ATOM    802  N   PRO A 113      62.159   8.507  15.955  1.00 56.12           N  
ANISOU  802  N   PRO A 113     5786   4971  10564    234   -506   -726       N  
ATOM    803  CA  PRO A 113      61.914   7.604  14.824  1.00 54.70           C  
ANISOU  803  CA  PRO A 113     5612   4892  10278    192   -433   -496       C  
ATOM    804  C   PRO A 113      62.936   7.719  13.692  1.00 54.71           C  
ANISOU  804  C   PRO A 113     5503   4838  10444    136   -446   -356       C  
ATOM    805  O   PRO A 113      63.240   6.722  13.039  1.00 53.99           O  
ANISOU  805  O   PRO A 113     5442   4851  10219    108   -431   -238       O  
ATOM    806  CB  PRO A 113      60.530   8.031  14.319  1.00 54.58           C  
ANISOU  806  CB  PRO A 113     5560   4867  10308    201   -323   -392       C  
ATOM    807  CG  PRO A 113      59.886   8.704  15.475  1.00 55.89           C  
ANISOU  807  CG  PRO A 113     5755   4983  10494    256   -316   -585       C  
ATOM    808  CD  PRO A 113      61.000   9.382  16.212  1.00 57.18           C  
ANISOU  808  CD  PRO A 113     5890   5043  10790    269   -431   -776       C  
ATOM    809  N   MET A 114      63.455   8.922  13.467  1.00 56.40           N  
ANISOU  809  N   MET A 114     5584   4885  10957    121   -465   -371       N  
ATOM    810  CA  MET A 114      64.414   9.158  12.388  1.00 57.10           C  
ANISOU  810  CA  MET A 114     5554   4907  11232     69   -448   -221       C  
ATOM    811  C   MET A 114      65.761   8.504  12.686  1.00 56.33           C  
ANISOU  811  C   MET A 114     5466   4828  11108     51   -537   -304       C  
ATOM    812  O   MET A 114      66.423   8.001  11.777  1.00 55.82           O  
ANISOU  812  O   MET A 114     5361   4802  11043     12   -500   -166       O  
ATOM    813  CB  MET A 114      64.602  10.662  12.151  1.00 60.18           C  
ANISOU  813  CB  MET A 114     5786   5087  11991     59   -437   -209       C  
ATOM    814  CG  MET A 114      63.331  11.411  11.754  1.00 61.45           C  
ANISOU  814  CG  MET A 114     5912   5203  12232     78   -355   -107       C  
ATOM    815  SD  MET A 114      62.449  10.715  10.336  1.00 61.52           S  
ANISOU  815  SD  MET A 114     5959   5368  12048     65   -244    186       S  
ATOM    816  CE  MET A 114      63.725  10.751   9.077  1.00 62.08           C  
ANISOU  816  CE  MET A 114     5932   5413  12243     11   -201    390       C  
ATOM    817  N   ASP A 115      66.166   8.522  13.954  1.00 56.31           N  
ANISOU  817  N   ASP A 115     5514   4799  11082     86   -659   -536       N  
ATOM    818  CA  ASP A 115      67.392   7.845  14.389  1.00 55.62           C  
ANISOU  818  CA  ASP A 115     5443   4731  10958     81   -775   -635       C  
ATOM    819  C   ASP A 115      67.218   6.326  14.406  1.00 53.58           C  
ANISOU  819  C   ASP A 115     5324   4661  10370     88   -769   -577       C  
ATOM    820  O   ASP A 115      68.135   5.594  14.041  1.00 53.21           O  
ANISOU  820  O   ASP A 115     5257   4645  10314     62   -801   -536       O  
ATOM    821  CB  ASP A 115      67.827   8.340  15.775  1.00 57.03           C  
ANISOU  821  CB  ASP A 115     5643   4833  11191    130   -932   -910       C  
ATOM    822  CG  ASP A 115      68.381   9.757  15.748  1.00 58.57           C  
ANISOU  822  CG  ASP A 115     5664   4807  11783    115   -973   -997       C  
ATOM    823  OD1 ASP A 115      69.035  10.132  14.752  1.00 58.42           O  
ANISOU  823  OD1 ASP A 115     5494   4684  12018     58   -916   -853       O  
ATOM    824  OD2 ASP A 115      68.176  10.493  16.737  1.00 59.78           O  
ANISOU  824  OD2 ASP A 115     5826   4887  11999    163  -1058  -1214       O  
ATOM    825  N   LEU A 116      66.049   5.856  14.838  1.00 52.53           N  
ANISOU  825  N   LEU A 116     5320   4642   9995    123   -724   -577       N  
ATOM    826  CA  LEU A 116      65.744   4.425  14.818  1.00 51.11           C  
ANISOU  826  CA  LEU A 116     5260   4623   9534    127   -703   -505       C  
ATOM    827  C   LEU A 116      65.860   3.860  13.404  1.00 50.33           C  
ANISOU  827  C   LEU A 116     5101   4573   9446     77   -616   -306       C  
ATOM    828  O   LEU A 116      66.421   2.784  13.211  1.00 50.01           O  
ANISOU  828  O   LEU A 116     5091   4607   9301     64   -644   -276       O  
ATOM    829  CB  LEU A 116      64.342   4.151  15.377  1.00 50.51           C  
ANISOU  829  CB  LEU A 116     5301   4637   9252    166   -634   -511       C  
ATOM    830  CG  LEU A 116      64.179   4.249  16.896  1.00 51.51           C  
ANISOU  830  CG  LEU A 116     5542   4782   9245    231   -705   -705       C  
ATOM    831  CD1 LEU A 116      62.707   4.317  17.274  1.00 51.61           C  
ANISOU  831  CD1 LEU A 116     5627   4852   9131    265   -590   -697       C  
ATOM    832  CD2 LEU A 116      64.850   3.081  17.600  1.00 51.54           C  
ANISOU  832  CD2 LEU A 116     5660   4878   9043    254   -805   -748       C  
ATOM    833  N   LYS A 117      65.334   4.591  12.425  1.00 50.52           N  
ANISOU  833  N   LYS A 117     5040   4557   9596     54   -517   -175       N  
ATOM    834  CA  LYS A 117      65.412   4.182  11.023  1.00 50.18           C  
ANISOU  834  CA  LYS A 117     4946   4573   9547     18   -432     11       C  
ATOM    835  C   LYS A 117      66.852   4.150  10.519  1.00 51.26           C  
ANISOU  835  C   LYS A 117     4989   4660   9827    -16   -452     30       C  
ATOM    836  O   LYS A 117      67.251   3.216   9.824  1.00 50.96           O  
ANISOU  836  O   LYS A 117     4955   4712   9693    -34   -423    103       O  
ATOM    837  CB  LYS A 117      64.583   5.123  10.145  1.00 50.59           C  
ANISOU  837  CB  LYS A 117     4928   4584   9709     13   -337    153       C  
ATOM    838  CG  LYS A 117      64.728   4.881   8.649  1.00 50.50           C  
ANISOU  838  CG  LYS A 117     4864   4636   9684    -12   -253    350       C  
ATOM    839  CD  LYS A 117      63.936   5.894   7.838  1.00 51.58           C  
ANISOU  839  CD  LYS A 117     4937   4726   9932     -7   -179    503       C  
ATOM    840  CE  LYS A 117      64.508   6.059   6.438  1.00 52.37           C  
ANISOU  840  CE  LYS A 117     4963   4849  10085    -30    -98    698       C  
ATOM    841  NZ  LYS A 117      64.516   4.781   5.672  1.00 51.53           N  
ANISOU  841  NZ  LYS A 117     4919   4920   9739    -30    -75    753       N  
ATOM    842  N   ARG A 118      67.624   5.177  10.864  1.00 53.21           N  
ANISOU  842  N   ARG A 118     5138   4755  10325    -25   -497    -45       N  
ATOM    843  CA  ARG A 118      69.012   5.295  10.407  1.00 54.19           C  
ANISOU  843  CA  ARG A 118     5142   4800  10646    -61   -505    -28       C  
ATOM    844  C   ARG A 118      69.882   4.181  10.993  1.00 53.01           C  
ANISOU  844  C   ARG A 118     5041   4705  10395    -55   -611   -144       C  
ATOM    845  O   ARG A 118      70.783   3.674  10.324  1.00 53.07           O  
ANISOU  845  O   ARG A 118     4982   4725  10455    -83   -581    -89       O  
ATOM    846  CB  ARG A 118      69.576   6.671  10.776  1.00 56.73           C  
ANISOU  846  CB  ARG A 118     5333   4920  11298    -70   -545   -106       C  
ATOM    847  CG  ARG A 118      70.745   7.135   9.918  1.00 58.81           C  
ANISOU  847  CG  ARG A 118     5428   5074  11841   -118   -483     -8       C  
ATOM    848  CD  ARG A 118      70.994   8.631  10.088  1.00 61.72           C  
ANISOU  848  CD  ARG A 118     5652   5225  12572   -131   -490    -38       C  
ATOM    849  NE  ARG A 118      69.824   9.439   9.731  1.00 62.66           N  
ANISOU  849  NE  ARG A 118     5778   5322  12706   -119   -407     76       N  
ATOM    850  CZ  ARG A 118      69.698  10.748   9.961  1.00 64.65           C  
ANISOU  850  CZ  ARG A 118     5923   5388  13253   -119   -415     45       C  
ATOM    851  NH1 ARG A 118      70.675  11.440  10.548  1.00 66.24           N  
ANISOU  851  NH1 ARG A 118     5996   5402  13769   -133   -505   -106       N  
ATOM    852  NH2 ARG A 118      68.582  11.374   9.597  1.00 64.71           N  
ANISOU  852  NH2 ARG A 118     5940   5383  13262   -103   -341    160       N  
ATOM    853  N   GLY A 119      69.601   3.805  12.239  1.00 51.87           N  
ANISOU  853  N   GLY A 119     5012   4592  10104    -13   -728   -300       N  
ATOM    854  CA  GLY A 119      70.274   2.683  12.887  1.00 50.89           C  
ANISOU  854  CA  GLY A 119     4956   4528   9852      4   -843   -394       C  
ATOM    855  C   GLY A 119      69.941   1.349  12.242  1.00 48.88           C  
ANISOU  855  C   GLY A 119     4768   4419   9385     -3   -776   -279       C  
ATOM    856  O   GLY A 119      70.815   0.500  12.080  1.00 48.62           O  
ANISOU  856  O   GLY A 119     4711   4405   9354    -13   -818   -288       O  
ATOM    857  N   ILE A 120      68.672   1.165  11.881  1.00 47.34           N  
ANISOU  857  N   ILE A 120     4645   4314   9028      2   -679   -183       N  
ATOM    858  CA  ILE A 120      68.225  -0.045  11.184  1.00 45.29           C  
ANISOU  858  CA  ILE A 120     4434   4183   8589     -4   -616    -83       C  
ATOM    859  C   ILE A 120      68.919  -0.164   9.831  1.00 44.80           C  
ANISOU  859  C   ILE A 120     4265   4134   8624    -41   -533     20       C  
ATOM    860  O   ILE A 120      69.431  -1.225   9.485  1.00 43.98           O  
ANISOU  860  O   ILE A 120     4159   4089   8459    -48   -540     24       O  
ATOM    861  CB  ILE A 120      66.689  -0.058  10.986  1.00 44.26           C  
ANISOU  861  CB  ILE A 120     4373   4127   8316      8   -533     -7       C  
ATOM    862  CG1 ILE A 120      65.980  -0.246  12.329  1.00 44.17           C  
ANISOU  862  CG1 ILE A 120     4481   4131   8167     49   -587   -103       C  
ATOM    863  CG2 ILE A 120      66.270  -1.172  10.034  1.00 43.22           C  
ANISOU  863  CG2 ILE A 120     4258   4112   8051     -2   -471     91       C  
ATOM    864  CD1 ILE A 120      64.537   0.210  12.332  1.00 43.96           C  
ANISOU  864  CD1 ILE A 120     4488   4126   8086     64   -503    -59       C  
ATOM    865  N   ASP A 121      68.937   0.933   9.078  1.00 45.26           N  
ANISOU  865  N   ASP A 121     4230   4132   8834    -62   -448    108       N  
ATOM    866  CA  ASP A 121      69.543   0.949   7.746  1.00 45.60           C  
ANISOU  866  CA  ASP A 121     4176   4197   8950    -90   -339    231       C  
ATOM    867  C   ASP A 121      71.041   0.651   7.794  1.00 46.00           C  
ANISOU  867  C   ASP A 121     4138   4187   9153   -110   -375    165       C  
ATOM    868  O   ASP A 121      71.558  -0.071   6.941  1.00 45.69           O  
ANISOU  868  O   ASP A 121     4062   4217   9080   -122   -308    214       O  
ATOM    869  CB  ASP A 121      69.303   2.298   7.055  1.00 46.73           C  
ANISOU  869  CB  ASP A 121     4238   4268   9249   -104   -242    358       C  
ATOM    870  CG  ASP A 121      67.839   2.535   6.707  1.00 46.49           C  
ANISOU  870  CG  ASP A 121     4274   4307   9080    -82   -195    452       C  
ATOM    871  OD1 ASP A 121      67.079   1.551   6.564  1.00 45.88           O  
ANISOU  871  OD1 ASP A 121     4287   4358   8784    -65   -200    455       O  
ATOM    872  OD2 ASP A 121      67.451   3.715   6.571  1.00 47.30           O  
ANISOU  872  OD2 ASP A 121     4326   4322   9321    -83   -158    522       O  
ATOM    873  N   LYS A 122      71.733   1.212   8.786  1.00 46.56           N  
ANISOU  873  N   LYS A 122     4165   4126   9400   -110   -485     40       N  
ATOM    874  CA  LYS A 122      73.167   0.966   8.962  1.00 47.03           C  
ANISOU  874  CA  LYS A 122     4125   4106   9639   -125   -547    -42       C  
ATOM    875  C   LYS A 122      73.441  -0.499   9.294  1.00 45.95           C  
ANISOU  875  C   LYS A 122     4058   4056   9342   -106   -629   -113       C  
ATOM    876  O   LYS A 122      74.414  -1.076   8.812  1.00 46.07           O  
ANISOU  876  O   LYS A 122     3990   4067   9445   -121   -610   -116       O  
ATOM    877  CB  LYS A 122      73.748   1.866  10.057  1.00 48.15           C  
ANISOU  877  CB  LYS A 122     4210   4086   9997   -118   -685   -189       C  
ATOM    878  CG  LYS A 122      75.261   1.761  10.192  1.00 49.34           C  
ANISOU  878  CG  LYS A 122     4226   4129  10393   -136   -759   -277       C  
ATOM    879  CD  LYS A 122      75.820   2.763  11.188  1.00 50.77           C  
ANISOU  879  CD  LYS A 122     4331   4138  10819   -127   -907   -434       C  
ATOM    880  CE  LYS A 122      77.329   2.624  11.316  1.00 51.87           C  
ANISOU  880  CE  LYS A 122     4318   4160  11230   -143   -995   -530       C  
ATOM    881  NZ  LYS A 122      77.898   3.578  12.306  1.00 53.48           N  
ANISOU  881  NZ  LYS A 122     4439   4190  11690   -130  -1168   -711       N  
ATOM    882  N   ALA A 123      72.580  -1.088  10.121  1.00 44.89           N  
ANISOU  882  N   ALA A 123     4072   3994   8991    -71   -712   -162       N  
ATOM    883  CA  ALA A 123      72.688  -2.501  10.479  1.00 44.02           C  
ANISOU  883  CA  ALA A 123     4037   3959   8729    -50   -787   -205       C  
ATOM    884  C   ALA A 123      72.451  -3.405   9.273  1.00 43.10           C  
ANISOU  884  C   ALA A 123     3910   3952   8513    -66   -665   -107       C  
ATOM    885  O   ALA A 123      73.122  -4.422   9.118  1.00 43.17           O  
ANISOU  885  O   ALA A 123     3891   3980   8529    -64   -695   -140       O  
ATOM    886  CB  ALA A 123      71.708  -2.840  11.589  1.00 43.60           C  
ANISOU  886  CB  ALA A 123     4141   3954   8468    -10   -869   -248       C  
ATOM    887  N   VAL A 124      71.498  -3.029   8.424  1.00 42.57           N  
ANISOU  887  N   VAL A 124     3860   3955   8359    -74   -538      2       N  
ATOM    888  CA  VAL A 124      71.199  -3.790   7.211  1.00 42.10           C  
ANISOU  888  CA  VAL A 124     3794   4012   8188    -79   -430     81       C  
ATOM    889  C   VAL A 124      72.333  -3.668   6.194  1.00 42.71           C  
ANISOU  889  C   VAL A 124     3742   4078   8407   -102   -334    114       C  
ATOM    890  O   VAL A 124      72.750  -4.667   5.613  1.00 42.76           O  
ANISOU  890  O   VAL A 124     3724   4149   8373    -99   -304     94       O  
ATOM    891  CB  VAL A 124      69.864  -3.344   6.573  1.00 41.98           C  
ANISOU  891  CB  VAL A 124     3831   4077   8043    -74   -342    188       C  
ATOM    892  CG1 VAL A 124      69.676  -3.966   5.194  1.00 41.96           C  
ANISOU  892  CG1 VAL A 124     3809   4199   7933    -72   -239    260       C  
ATOM    893  CG2 VAL A 124      68.700  -3.720   7.477  1.00 41.23           C  
ANISOU  893  CG2 VAL A 124     3853   4006   7805    -51   -410    155       C  
ATOM    894  N   THR A 125      72.829  -2.451   5.983  1.00 43.41           N  
ANISOU  894  N   THR A 125     3739   4076   8676   -123   -277    164       N  
ATOM    895  CA  THR A 125      73.950  -2.228   5.067  1.00 44.42           C  
ANISOU  895  CA  THR A 125     3730   4178   8968   -146   -160    211       C  
ATOM    896  C   THR A 125      75.151  -3.079   5.467  1.00 44.73           C  
ANISOU  896  C   THR A 125     3701   4165   9127   -149   -238     87       C  
ATOM    897  O   THR A 125      75.797  -3.694   4.618  1.00 44.80           O  
ANISOU  897  O   THR A 125     3642   4226   9154   -153   -143     96       O  
ATOM    898  CB  THR A 125      74.376  -0.745   5.031  1.00 45.52           C  
ANISOU  898  CB  THR A 125     3764   4182   9348   -173   -106    277       C  
ATOM    899  OG1 THR A 125      73.224   0.085   4.838  1.00 45.35           O  
ANISOU  899  OG1 THR A 125     3805   4184   9241   -166    -63    384       O  
ATOM    900  CG2 THR A 125      75.365  -0.492   3.902  1.00 46.84           C  
ANISOU  900  CG2 THR A 125     3792   4339   9665   -197     64    373       C  
ATOM    901  N   ALA A 126      75.443  -3.101   6.766  1.00 45.11           N  
ANISOU  901  N   ALA A 126     3769   4114   9255   -140   -415    -32       N  
ATOM    902  CA  ALA A 126      76.524  -3.921   7.316  1.00 45.84           C  
ANISOU  902  CA  ALA A 126     3805   4146   9463   -132   -532   -154       C  
ATOM    903  C   ALA A 126      76.229  -5.409   7.163  1.00 44.87           C  
ANISOU  903  C   ALA A 126     3757   4132   9157   -109   -554   -179       C  
ATOM    904  O   ALA A 126      77.116  -6.189   6.824  1.00 45.38           O  
ANISOU  904  O   ALA A 126     3738   4189   9316   -109   -546   -229       O  
ATOM    905  CB  ALA A 126      76.749  -3.584   8.783  1.00 46.29           C  
ANISOU  905  CB  ALA A 126     3895   4092   9598   -113   -738   -272       C  
ATOM    906  N   ALA A 127      74.980  -5.790   7.416  1.00 43.83           N  
ANISOU  906  N   ALA A 127     3769   4090   8792    -90   -578   -150       N  
ATOM    907  CA  ALA A 127      74.551  -7.183   7.296  1.00 43.01           C  
ANISOU  907  CA  ALA A 127     3732   4075   8534    -70   -600   -169       C  
ATOM    908  C   ALA A 127      74.685  -7.710   5.870  1.00 43.38           C  
ANISOU  908  C   ALA A 127     3714   4217   8550    -77   -448   -136       C  
ATOM    909  O   ALA A 127      75.117  -8.840   5.668  1.00 43.55           O  
ANISOU  909  O   ALA A 127     3705   4256   8585    -65   -468   -200       O  
ATOM    910  CB  ALA A 127      73.118  -7.342   7.785  1.00 41.82           C  
ANISOU  910  CB  ALA A 127     3728   3989   8171    -53   -630   -131       C  
ATOM    911  N   VAL A 128      74.322  -6.889   4.888  1.00 43.95           N  
ANISOU  911  N   VAL A 128     3768   4351   8579    -90   -300    -39       N  
ATOM    912  CA  VAL A 128      74.414  -7.286   3.480  1.00 44.65           C  
ANISOU  912  CA  VAL A 128     3812   4556   8597    -85   -148     -4       C  
ATOM    913  C   VAL A 128      75.867  -7.533   3.064  1.00 46.20           C  
ANISOU  913  C   VAL A 128     3865   4704   8984    -94    -85    -59       C  
ATOM    914  O   VAL A 128      76.145  -8.467   2.315  1.00 46.43           O  
ANISOU  914  O   VAL A 128     3860   4810   8969    -78    -22   -110       O  
ATOM    915  CB  VAL A 128      73.753  -6.242   2.549  1.00 44.87           C  
ANISOU  915  CB  VAL A 128     3856   4661   8531    -88     -8    136       C  
ATOM    916  CG1 VAL A 128      74.070  -6.527   1.085  1.00 45.82           C  
ANISOU  916  CG1 VAL A 128     3926   4908   8573    -74    158    175       C  
ATOM    917  CG2 VAL A 128      72.246  -6.227   2.761  1.00 43.76           C  
ANISOU  917  CG2 VAL A 128     3842   4585   8199    -72    -61    176       C  
ATOM    918  N   GLU A 129      76.784  -6.693   3.543  1.00 47.59           N  
ANISOU  918  N   GLU A 129     3946   4745   9389   -118   -102    -60       N  
ATOM    919  CA  GLU A 129      78.213  -6.878   3.269  1.00 49.07           C  
ANISOU  919  CA  GLU A 129     3975   4858   9810   -129    -50   -118       C  
ATOM    920  C   GLU A 129      78.743  -8.142   3.933  1.00 49.00           C  
ANISOU  920  C   GLU A 129     3949   4802   9863   -110   -199   -259       C  
ATOM    921  O   GLU A 129      79.534  -8.873   3.339  1.00 50.23           O  
ANISOU  921  O   GLU A 129     4007   4970  10108   -103   -131   -320       O  
ATOM    922  CB  GLU A 129      79.025  -5.665   3.733  1.00 50.12           C  
ANISOU  922  CB  GLU A 129     3995   4832  10214   -160    -60    -98       C  
ATOM    923  CG  GLU A 129      78.765  -4.402   2.928  1.00 51.22           C  
ANISOU  923  CG  GLU A 129     4106   4989  10366   -182    118     59       C  
ATOM    924  CD  GLU A 129      79.070  -4.576   1.450  1.00 52.40           C  
ANISOU  924  CD  GLU A 129     4195   5257  10455   -179    357    145       C  
ATOM    925  OE1 GLU A 129      80.193  -5.013   1.117  1.00 53.29           O  
ANISOU  925  OE1 GLU A 129     4177   5335  10736   -184    429     86       O  
ATOM    926  OE2 GLU A 129      78.184  -4.259   0.624  1.00 52.58           O  
ANISOU  926  OE2 GLU A 129     4303   5412  10262   -166    471    272       O  
ATOM    927  N   GLU A 130      78.301  -8.394   5.163  1.00 48.11           N  
ANISOU  927  N   GLU A 130     3935   4638   9706    -97   -397   -304       N  
ATOM    928  CA  GLU A 130      78.687  -9.602   5.894  1.00 47.78           C  
ANISOU  928  CA  GLU A 130     3899   4548   9707    -72   -557   -408       C  
ATOM    929  C   GLU A 130      78.076 -10.842   5.242  1.00 47.13           C  
ANISOU  929  C   GLU A 130     3866   4579   9460    -51   -509   -425       C  
ATOM    930  O   GLU A 130      78.648 -11.929   5.297  1.00 47.05           O  
ANISOU  930  O   GLU A 130     3800   4536   9539    -34   -567   -510       O  
ATOM    931  CB  GLU A 130      78.247  -9.505   7.359  1.00 47.12           C  
ANISOU  931  CB  GLU A 130     3931   4402   9569    -54   -764   -425       C  
ATOM    932  CG  GLU A 130      79.110 -10.306   8.321  1.00 47.85           C  
ANISOU  932  CG  GLU A 130     3990   4392   9799    -27   -959   -520       C  
ATOM    933  CD  GLU A 130      80.475  -9.680   8.555  1.00 49.51           C  
ANISOU  933  CD  GLU A 130     4044   4466  10301    -38  -1016   -589       C  
ATOM    934  OE1 GLU A 130      80.556  -8.440   8.696  1.00 49.93           O  
ANISOU  934  OE1 GLU A 130     4070   4471  10431    -59   -996   -571       O  
ATOM    935  OE2 GLU A 130      81.473 -10.431   8.603  1.00 50.66           O  
ANISOU  935  OE2 GLU A 130     4079   4539  10628    -24  -1084   -666       O  
ATOM    936  N   LEU A 131      76.910 -10.660   4.627  1.00 46.78           N  
ANISOU  936  N   LEU A 131     3917   4660   9197    -52   -414   -351       N  
ATOM    937  CA  LEU A 131      76.215 -11.725   3.904  1.00 46.52           C  
ANISOU  937  CA  LEU A 131     3926   4740   9009    -32   -368   -377       C  
ATOM    938  C   LEU A 131      76.949 -12.106   2.613  1.00 47.59           C  
ANISOU  938  C   LEU A 131     3947   4942   9191    -24   -213   -429       C  
ATOM    939  O   LEU A 131      76.949 -13.271   2.219  1.00 47.49           O  
ANISOU  939  O   LEU A 131     3915   4968   9160     -1   -218   -521       O  
ATOM    940  CB  LEU A 131      74.777 -11.284   3.588  1.00 45.65           C  
ANISOU  940  CB  LEU A 131     3935   4738   8671    -31   -322   -288       C  
ATOM    941  CG  LEU A 131      73.725 -12.354   3.305  1.00 45.17           C  
ANISOU  941  CG  LEU A 131     3945   4761   8456     -9   -347   -320       C  
ATOM    942  CD1 LEU A 131      73.397 -13.151   4.558  1.00 44.47           C  
ANISOU  942  CD1 LEU A 131     3918   4584   8393     -3   -509   -345       C  
ATOM    943  CD2 LEU A 131      72.466 -11.701   2.757  1.00 44.81           C  
ANISOU  943  CD2 LEU A 131     3982   4824   8220     -8   -280   -230       C  
ATOM    944  N   LYS A 132      77.561 -11.121   1.957  1.00 48.73           N  
ANISOU  944  N   LYS A 132     4014   5098   9402    -41    -66   -371       N  
ATOM    945  CA  LYS A 132      78.361 -11.366   0.753  1.00 50.30           C  
ANISOU  945  CA  LYS A 132     4101   5365   9645    -31    112   -409       C  
ATOM    946  C   LYS A 132      79.643 -12.132   1.066  1.00 50.92           C  
ANISOU  946  C   LYS A 132     4041   5328   9979    -27     65   -536       C  
ATOM    947  O   LYS A 132      80.111 -12.923   0.246  1.00 51.57           O  
ANISOU  947  O   LYS A 132     4047   5467  10079     -4    163   -628       O  
ATOM    948  CB  LYS A 132      78.710 -10.048   0.051  1.00 51.81           C  
ANISOU  948  CB  LYS A 132     4240   5581   9864    -51    295   -282       C  
ATOM    949  CG  LYS A 132      77.540  -9.399  -0.667  1.00 52.20           C  
ANISOU  949  CG  LYS A 132     4405   5775   9651    -41    383   -152       C  
ATOM    950  CD  LYS A 132      77.923  -8.045  -1.239  1.00 54.11           C  
ANISOU  950  CD  LYS A 132     4590   6012   9955    -62    555      2       C  
ATOM    951  CE  LYS A 132      76.713  -7.333  -1.827  1.00 54.54           C  
ANISOU  951  CE  LYS A 132     4764   6191   9766    -48    610    148       C  
ATOM    952  NZ  LYS A 132      77.049  -5.958  -2.292  1.00 56.27           N  
ANISOU  952  NZ  LYS A 132     4927   6380  10072    -69    766    326       N  
ATOM    953  N   ALA A 133      80.219 -11.875   2.238  1.00 50.76           N  
ANISOU  953  N   ALA A 133     3982   5146  10158    -44    -90   -552       N  
ATOM    954  CA  ALA A 133      81.419 -12.586   2.688  1.00 51.71           C  
ANISOU  954  CA  ALA A 133     3968   5136  10544    -36   -179   -669       C  
ATOM    955  C   ALA A 133      81.118 -14.057   2.958  1.00 51.05           C  
ANISOU  955  C   ALA A 133     3924   5055  10417     -3   -302   -766       C  
ATOM    956  O   ALA A 133      81.911 -14.934   2.616  1.00 51.87           O  
ANISOU  956  O   ALA A 133     3909   5123  10675     15   -282   -876       O  
ATOM    957  CB  ALA A 133      81.986 -11.927   3.937  1.00 51.97           C  
ANISOU  957  CB  ALA A 133     3969   5003  10771    -52   -352   -664       C  
ATOM    958  N   LEU A 134      79.964 -14.309   3.569  1.00 49.81           N  
ANISOU  958  N   LEU A 134     3923   4930  10071      3   -421   -721       N  
ATOM    959  CA  LEU A 134      79.500 -15.667   3.854  1.00 49.35           C  
ANISOU  959  CA  LEU A 134     3910   4865   9974     31   -532   -784       C  
ATOM    960  C   LEU A 134      79.094 -16.424   2.582  1.00 49.48           C  
ANISOU  960  C   LEU A 134     3908   5009   9880     49   -393   -855       C  
ATOM    961  O   LEU A 134      79.149 -17.652   2.542  1.00 49.39           O  
ANISOU  961  O   LEU A 134     3860   4967   9938     74   -451   -954       O  
ATOM    962  CB  LEU A 134      78.308 -15.609   4.813  1.00 48.21           C  
ANISOU  962  CB  LEU A 134     3934   4724   9659     30   -662   -698       C  
ATOM    963  CG  LEU A 134      77.789 -16.939   5.372  1.00 48.00           C  
ANISOU  963  CG  LEU A 134     3959   4657   9620     55   -794   -725       C  
ATOM    964  CD1 LEU A 134      78.239 -17.139   6.812  1.00 48.32           C  
ANISOU  964  CD1 LEU A 134     4027   4561   9770     69   -998   -700       C  
ATOM    965  CD2 LEU A 134      76.273 -17.001   5.284  1.00 47.01           C  
ANISOU  965  CD2 LEU A 134     3967   4626   9265     51   -769   -658       C  
ATOM    966  N   SER A 135      78.692 -15.684   1.551  1.00 49.70           N  
ANISOU  966  N   SER A 135     3962   5179   9741     43   -217   -806       N  
ATOM    967  CA  SER A 135      78.219 -16.268   0.295  1.00 50.17           C  
ANISOU  967  CA  SER A 135     4025   5390   9646     71    -91   -877       C  
ATOM    968  C   SER A 135      79.259 -17.150  -0.400  1.00 51.26           C  
ANISOU  968  C   SER A 135     4016   5519   9939     98    -10  -1034       C  
ATOM    969  O   SER A 135      80.395 -16.726  -0.630  1.00 52.81           O  
ANISOU  969  O   SER A 135     4092   5674  10296     90     90  -1045       O  
ATOM    970  CB  SER A 135      77.777 -15.158  -0.666  1.00 50.83           C  
ANISOU  970  CB  SER A 135     4160   5626   9524     67     82   -773       C  
ATOM    971  OG  SER A 135      77.256 -15.695  -1.871  1.00 51.87           O  
ANISOU  971  OG  SER A 135     4314   5925   9467    106    183   -846       O  
ATOM    972  N   VAL A 136      78.848 -18.371  -0.737  1.00 63.11           N  
ANISOU  972  N   VAL A 136     6782   7295   9902    469   -682   -448       N  
ATOM    973  CA  VAL A 136      79.656 -19.292  -1.530  1.00 63.76           C  
ANISOU  973  CA  VAL A 136     6719   7384  10120    572   -715   -554       C  
ATOM    974  C   VAL A 136      79.273 -19.109  -3.002  1.00 63.41           C  
ANISOU  974  C   VAL A 136     6653   7414  10026    614   -587   -660       C  
ATOM    975  O   VAL A 136      78.093 -19.192  -3.339  1.00 62.48           O  
ANISOU  975  O   VAL A 136     6623   7256   9859    622   -556   -654       O  
ATOM    976  CB  VAL A 136      79.398 -20.757  -1.123  1.00 64.28           C  
ANISOU  976  CB  VAL A 136     6812   7296  10313    638   -877   -547       C  
ATOM    977  CG1 VAL A 136      80.318 -21.699  -1.888  1.00 65.87           C  
ANISOU  977  CG1 VAL A 136     6875   7489  10663    809   -952   -700       C  
ATOM    978  CG2 VAL A 136      79.577 -20.940   0.379  1.00 64.72           C  
ANISOU  978  CG2 VAL A 136     6955   7254  10379    548  -1026   -417       C  
ATOM    979  N   PRO A 137      80.258 -18.842  -3.886  1.00 64.35           N  
ANISOU  979  N   PRO A 137     6644   7671  10135    615   -513   -766       N  
ATOM    980  CA  PRO A 137      79.932 -18.630  -5.306  1.00 64.34           C  
ANISOU  980  CA  PRO A 137     6648   7746  10052    610   -395   -861       C  
ATOM    981  C   PRO A 137      79.312 -19.847  -5.989  1.00 64.33           C  
ANISOU  981  C   PRO A 137     6625   7666  10150    745   -420   -950       C  
ATOM    982  O   PRO A 137      79.436 -20.967  -5.492  1.00 64.87           O  
ANISOU  982  O   PRO A 137     6656   7628  10361    852   -547   -968       O  
ATOM    983  CB  PRO A 137      81.292 -18.308  -5.942  1.00 65.94           C  
ANISOU  983  CB  PRO A 137     6676   8167  10209    541   -319   -974       C  
ATOM    984  CG  PRO A 137      82.142 -17.826  -4.821  1.00 66.34           C  
ANISOU  984  CG  PRO A 137     6681   8261  10263    463   -379   -894       C  
ATOM    985  CD  PRO A 137      81.682 -18.580  -3.610  1.00 65.68           C  
ANISOU  985  CD  PRO A 137     6655   7978  10322    574   -527   -802       C  
ATOM    986  N   CYS A 138      78.653 -19.606  -7.122  1.00 63.85           N  
ANISOU  986  N   CYS A 138     6628   7634   9999    726   -330   -998       N  
ATOM    987  CA  CYS A 138      78.053 -20.663  -7.934  1.00 63.96           C  
ANISOU  987  CA  CYS A 138     6640   7583  10077    827   -343  -1087       C  
ATOM    988  C   CYS A 138      78.447 -20.451  -9.399  1.00 64.62           C  
ANISOU  988  C   CYS A 138     6667   7808  10074    801   -219  -1228       C  
ATOM    989  O   CYS A 138      77.651 -19.979 -10.214  1.00 63.75           O  
ANISOU  989  O   CYS A 138     6680   7694   9848    739   -164  -1215       O  
ATOM    990  CB  CYS A 138      76.533 -20.654  -7.761  1.00 62.92           C  
ANISOU  990  CB  CYS A 138     6657   7351   9900    805   -372   -993       C  
ATOM    991  SG  CYS A 138      75.660 -21.973  -8.635  1.00 63.50           S  
ANISOU  991  SG  CYS A 138     6763   7334  10030    876   -415  -1068       S  
ATOM    992  N   SER A 139      79.691 -20.804  -9.718  1.00 66.36           N  
ANISOU  992  N   SER A 139     6694   8180  10338    846   -187  -1379       N  
ATOM    993  CA  SER A 139      80.291 -20.489 -11.017  1.00 67.80           C  
ANISOU  993  CA  SER A 139     6782   8586  10390    759    -41  -1533       C  
ATOM    994  C   SER A 139      80.187 -21.640 -12.020  1.00 68.96           C  
ANISOU  994  C   SER A 139     6862   8734  10604    913    -33  -1725       C  
ATOM    995  O   SER A 139      79.466 -21.539 -13.014  1.00 68.70           O  
ANISOU  995  O   SER A 139     6950   8683  10470    849     31  -1736       O  
ATOM    996  CB  SER A 139      81.760 -20.087 -10.835  1.00 69.68           C  
ANISOU  996  CB  SER A 139     6794   9094  10587    680     17  -1629       C  
ATOM    997  OG  SER A 139      81.872 -18.896 -10.063  1.00 69.01           O  
ANISOU  997  OG  SER A 139     6816   9008  10394    489     13  -1449       O  
ATOM    998  N   ASP A 140      80.906 -22.731 -11.755  1.00 70.51           N  
ANISOU  998  N   ASP A 140     6889   8934  10968   1132   -128  -1884       N  
ATOM    999  CA  ASP A 140      80.992 -23.853 -12.700  1.00 72.06           C  
ANISOU  999  CA  ASP A 140     7019   9135  11225   1319   -145  -2116       C  
ATOM   1000  C   ASP A 140      79.672 -24.619 -12.822  1.00 70.53           C  
ANISOU 1000  C   ASP A 140     7070   8637  11087   1377   -256  -2021       C  
ATOM   1001  O   ASP A 140      78.798 -24.509 -11.960  1.00 68.54           O  
ANISOU 1001  O   ASP A 140     6988   8189  10864   1312   -347  -1802       O  
ATOM   1002  CB  ASP A 140      82.140 -24.807 -12.323  1.00 74.80           C  
ANISOU 1002  CB  ASP A 140     7137   9542  11739   1593   -276  -2343       C  
ATOM   1003  CG  ASP A 140      81.962 -25.445 -10.951  1.00 74.45           C  
ANISOU 1003  CG  ASP A 140     7216   9194  11878   1729   -535  -2203       C  
ATOM   1004  OD1 ASP A 140      81.312 -24.833 -10.078  1.00 72.40           O  
ANISOU 1004  OD1 ASP A 140     7116   8804  11589   1558   -551  -1936       O  
ATOM   1005  OD2 ASP A 140      82.486 -26.559 -10.744  1.00 76.65           O  
ANISOU 1005  OD2 ASP A 140     7444   9364  12313   2008   -741  -2375       O  
ATOM   1006  N   SER A 141      79.545 -25.394 -13.897  1.00 71.62           N  
ANISOU 1006  N   SER A 141     7216   8772  11221   1480   -243  -2203       N  
ATOM   1007  CA  SER A 141      78.302 -26.110 -14.205  1.00 70.77           C  
ANISOU 1007  CA  SER A 141     7343   8414  11132   1491   -338  -2127       C  
ATOM   1008  C   SER A 141      78.012 -27.281 -13.259  1.00 71.21           C  
ANISOU 1008  C   SER A 141     7538   8167  11351   1634   -604  -2070       C  
ATOM   1009  O   SER A 141      76.885 -27.780 -13.227  1.00 70.67           O  
ANISOU 1009  O   SER A 141     7681   7897  11270   1561   -700  -1946       O  
ATOM   1010  CB  SER A 141      78.304 -26.597 -15.658  1.00 72.18           C  
ANISOU 1010  CB  SER A 141     7512   8671  11239   1545   -256  -2344       C  
ATOM   1011  OG  SER A 141      79.439 -27.397 -15.927  1.00 75.04           O  
ANISOU 1011  OG  SER A 141     7690   9134  11686   1791   -300  -2642       O  
ATOM   1012  N   LYS A 142      79.017 -27.722 -12.504  1.00 72.71           N  
ANISOU 1012  N   LYS A 142     7622   8331  11671   1812   -744  -2160       N  
ATOM   1013  CA  LYS A 142      78.805 -28.706 -11.443  1.00 73.53           C  
ANISOU 1013  CA  LYS A 142     7916   8118  11902   1899  -1042  -2066       C  
ATOM   1014  C   LYS A 142      77.977 -28.088 -10.319  1.00 71.11           C  
ANISOU 1014  C   LYS A 142     7733   7739  11544   1651  -1045  -1756       C  
ATOM   1015  O   LYS A 142      76.996 -28.678  -9.865  1.00 70.83           O  
ANISOU 1015  O   LYS A 142     7929   7490  11492   1536  -1190  -1604       O  
ATOM   1016  CB  LYS A 142      80.143 -29.206 -10.886  1.00 76.27           C  
ANISOU 1016  CB  LYS A 142     8117   8463  12396   2167  -1219  -2246       C  
ATOM   1017  CG  LYS A 142      80.014 -30.339  -9.876  1.00 77.88           C  
ANISOU 1017  CG  LYS A 142     8586   8284  12720   2271  -1596  -2169       C  
ATOM   1018  CD  LYS A 142      81.322 -30.596  -9.146  1.00 80.41           C  
ANISOU 1018  CD  LYS A 142     8757   8611  13185   2528  -1793  -2313       C  
ATOM   1019  CE  LYS A 142      81.129 -31.584  -8.007  1.00 81.92           C  
ANISOU 1019  CE  LYS A 142     9283   8380  13462   2565  -2203  -2177       C  
ATOM   1020  NZ  LYS A 142      82.384 -31.805  -7.236  1.00 84.42           N  
ANISOU 1020  NZ  LYS A 142     9470   8682  13924   2828  -2438  -2308       N  
ATOM   1021  N   ALA A 143      78.387 -26.901  -9.876  1.00 69.70           N  
ANISOU 1021  N   ALA A 143     7401   7762  11319   1552   -890  -1679       N  
ATOM   1022  CA  ALA A 143      77.682 -26.175  -8.819  1.00 67.69           C  
ANISOU 1022  CA  ALA A 143     7234   7482  11001   1346   -873  -1429       C  
ATOM   1023  C   ALA A 143      76.286 -25.734  -9.258  1.00 66.02           C  
ANISOU 1023  C   ALA A 143     7132   7295  10658   1173   -761  -1316       C  
ATOM   1024  O   ALA A 143      75.358 -25.714  -8.449  1.00 65.22           O  
ANISOU 1024  O   ALA A 143     7141   7129  10507   1031   -816  -1152       O  
ATOM   1025  CB  ALA A 143      78.498 -24.970  -8.375  1.00 67.07           C  
ANISOU 1025  CB  ALA A 143     6991   7604  10888   1293   -746  -1399       C  
ATOM   1026  N   ILE A 144      76.146 -25.378 -10.534  1.00 65.86           N  
ANISOU 1026  N   ILE A 144     7065   7393  10563   1180   -610  -1419       N  
ATOM   1027  CA  ILE A 144      74.851 -24.998 -11.104  1.00 64.70           C  
ANISOU 1027  CA  ILE A 144     7013   7269  10298   1057   -536  -1345       C  
ATOM   1028  C   ILE A 144      73.868 -26.170 -11.051  1.00 65.37           C  
ANISOU 1028  C   ILE A 144     7248   7186  10401   1020   -683  -1304       C  
ATOM   1029  O   ILE A 144      72.686 -25.981 -10.757  1.00 64.59           O  
ANISOU 1029  O   ILE A 144     7208   7113  10217    878   -685  -1186       O  
ATOM   1030  CB  ILE A 144      75.001 -24.480 -12.556  1.00 64.76           C  
ANISOU 1030  CB  ILE A 144     6981   7411  10213   1059   -381  -1470       C  
ATOM   1031  CG1 ILE A 144      75.693 -23.112 -12.552  1.00 64.21           C  
ANISOU 1031  CG1 ILE A 144     6833   7513  10050    983   -249  -1454       C  
ATOM   1032  CG2 ILE A 144      73.647 -24.365 -13.246  1.00 64.11           C  
ANISOU 1032  CG2 ILE A 144     7014   7311  10031    973   -365  -1419       C  
ATOM   1033  CD1 ILE A 144      76.177 -22.645 -13.910  1.00 65.02           C  
ANISOU 1033  CD1 ILE A 144     6904   7771  10028    927   -110  -1586       C  
ATOM   1034  N   ALA A 145      74.363 -27.373 -11.329  1.00 67.35           N  
ANISOU 1034  N   ALA A 145     7562   7281  10747   1144   -822  -1417       N  
ATOM   1035  CA  ALA A 145      73.550 -28.585 -11.250  1.00 68.76           C  
ANISOU 1035  CA  ALA A 145     7947   7253  10923   1077  -1012  -1370       C  
ATOM   1036  C   ALA A 145      73.123 -28.885  -9.811  1.00 69.22           C  
ANISOU 1036  C   ALA A 145     8121   7210  10968    912  -1169  -1183       C  
ATOM   1037  O   ALA A 145      71.969 -29.237  -9.567  1.00 69.53           O  
ANISOU 1037  O   ALA A 145     8281   7233  10903    695  -1227  -1064       O  
ATOM   1038  CB  ALA A 145      74.309 -29.769 -11.831  1.00 71.06           C  
ANISOU 1038  CB  ALA A 145     8323   7360  11316   1289  -1173  -1560       C  
ATOM   1039  N   GLN A 146      74.055 -28.745  -8.869  1.00 69.75           N  
ANISOU 1039  N   GLN A 146     8144   7239  11119    985  -1238  -1163       N  
ATOM   1040  CA  GLN A 146      73.781 -28.991  -7.447  1.00 70.11           C  
ANISOU 1040  CA  GLN A 146     8314   7189  11133    807  -1393   -985       C  
ATOM   1041  C   GLN A 146      72.696 -28.069  -6.890  1.00 68.22           C  
ANISOU 1041  C   GLN A 146     8005   7171  10745    569  -1234   -840       C  
ATOM   1042  O   GLN A 146      71.829 -28.513  -6.135  1.00 68.70           O  
ANISOU 1042  O   GLN A 146     8190   7216  10694    321  -1330   -710       O  
ATOM   1043  CB  GLN A 146      75.062 -28.845  -6.614  1.00 70.91           C  
ANISOU 1043  CB  GLN A 146     8354   7236  11353    950  -1482  -1003       C  
ATOM   1044  CG  GLN A 146      76.048 -29.990  -6.787  1.00 73.73           C  
ANISOU 1044  CG  GLN A 146     8813   7345  11855   1197  -1745  -1152       C  
ATOM   1045  CD  GLN A 146      77.371 -29.737  -6.081  1.00 74.78           C  
ANISOU 1045  CD  GLN A 146     8814   7487  12111   1376  -1823  -1209       C  
ATOM   1046  OE1 GLN A 146      78.050 -28.746  -6.351  1.00 73.90           O  
ANISOU 1046  OE1 GLN A 146     8433   7626  12020   1459  -1605  -1290       O  
ATOM   1047  NE2 GLN A 146      77.752 -30.641  -5.182  1.00 77.15           N  
ANISOU 1047  NE2 GLN A 146     9326   7508  12477   1414  -2160  -1166       N  
ATOM   1048  N   VAL A 147      72.747 -26.791  -7.263  1.00 66.38           N  
ANISOU 1048  N   VAL A 147     7582   7152  10486    637  -1008   -879       N  
ATOM   1049  CA  VAL A 147      71.753 -25.812  -6.814  1.00 65.14           C  
ANISOU 1049  CA  VAL A 147     7348   7208  10194    495   -878   -799       C  
ATOM   1050  C   VAL A 147      70.385 -26.103  -7.434  1.00 65.28           C  
ANISOU 1050  C   VAL A 147     7383   7319  10098    373   -856   -803       C  
ATOM   1051  O   VAL A 147      69.362 -26.031  -6.750  1.00 65.59           O  
ANISOU 1051  O   VAL A 147     7400   7510  10010    183   -854   -734       O  
ATOM   1052  CB  VAL A 147      72.187 -24.365  -7.144  1.00 63.73           C  
ANISOU 1052  CB  VAL A 147     7033   7174  10005    618   -702   -849       C  
ATOM   1053  CG1 VAL A 147      71.056 -23.378  -6.878  1.00 62.96           C  
ANISOU 1053  CG1 VAL A 147     6880   7272   9769    547   -612   -819       C  
ATOM   1054  CG2 VAL A 147      73.415 -23.983  -6.329  1.00 63.66           C  
ANISOU 1054  CG2 VAL A 147     6988   7127  10070    673   -721   -822       C  
ATOM   1055  N   GLY A 148      70.373 -26.424  -8.725  1.00 65.24           N  
ANISOU 1055  N   GLY A 148     7401   7260  10126    471   -837   -901       N  
ATOM   1056  CA  GLY A 148      69.144 -26.811  -9.415  1.00 65.51           C  
ANISOU 1056  CA  GLY A 148     7461   7366  10060    355   -841   -910       C  
ATOM   1057  C   GLY A 148      68.542 -28.087  -8.853  1.00 67.12           C  
ANISOU 1057  C   GLY A 148     7826   7474  10202    117  -1019   -819       C  
ATOM   1058  O   GLY A 148      67.323 -28.206  -8.742  1.00 67.60           O  
ANISOU 1058  O   GLY A 148     7857   7709  10117    -97  -1015   -777       O  
ATOM   1059  N   THR A 149      69.404 -29.036  -8.492  1.00 68.33           N  
ANISOU 1059  N   THR A 149     8158   7357  10445    144  -1199   -800       N  
ATOM   1060  CA  THR A 149      68.981 -30.303  -7.894  1.00 70.40           C  
ANISOU 1060  CA  THR A 149     8671   7449  10629   -109  -1437   -694       C  
ATOM   1061  C   THR A 149      68.313 -30.085  -6.536  1.00 70.86           C  
ANISOU 1061  C   THR A 149     8707   7684  10531   -417  -1441   -548       C  
ATOM   1062  O   THR A 149      67.251 -30.644  -6.265  1.00 72.32           O  
ANISOU 1062  O   THR A 149     8974   7972  10533   -753  -1507   -466       O  
ATOM   1063  CB  THR A 149      70.178 -31.264  -7.727  1.00 71.95           C  
ANISOU 1063  CB  THR A 149     9092   7277  10967     51  -1684   -727       C  
ATOM   1064  OG1 THR A 149      70.763 -31.528  -9.009  1.00 72.05           O  
ANISOU 1064  OG1 THR A 149     9099   7177  11099    336  -1671   -907       O  
ATOM   1065  CG2 THR A 149      69.749 -32.584  -7.091  1.00 74.60           C  
ANISOU 1065  CG2 THR A 149     9783   7367  11195   -236  -1998   -599       C  
ATOM   1066  N   ILE A 150      68.941 -29.271  -5.692  1.00 69.99           N  
ANISOU 1066  N   ILE A 150     8482   7640  10471   -330  -1365   -526       N  
ATOM   1067  CA  ILE A 150      68.402 -28.961  -4.365  1.00 70.50           C  
ANISOU 1067  CA  ILE A 150     8508   7899  10379   -603  -1346   -414       C  
ATOM   1068  C   ILE A 150      67.076 -28.203  -4.471  1.00 70.09           C  
ANISOU 1068  C   ILE A 150     8214   8258  10157   -729  -1147   -458       C  
ATOM   1069  O   ILE A 150      66.132 -28.487  -3.731  1.00 71.67           O  
ANISOU 1069  O   ILE A 150     8403   8677  10148  -1073  -1164   -395       O  
ATOM   1070  CB  ILE A 150      69.410 -28.142  -3.525  1.00 69.49           C  
ANISOU 1070  CB  ILE A 150     8304   7752  10346   -448  -1299   -398       C  
ATOM   1071  CG1 ILE A 150      70.626 -29.006  -3.169  1.00 70.60           C  
ANISOU 1071  CG1 ILE A 150     8672   7525  10627   -360  -1548   -357       C  
ATOM   1072  CG2 ILE A 150      68.759 -27.621  -2.248  1.00 69.89           C  
ANISOU 1072  CG2 ILE A 150     8275   8065  10213   -707  -1229   -319       C  
ATOM   1073  CD1 ILE A 150      71.849 -28.213  -2.762  1.00 69.45           C  
ANISOU 1073  CD1 ILE A 150     8412   7349  10626   -120  -1498   -387       C  
ATOM   1074  N   SER A 151      67.012 -27.248  -5.397  1.00 68.41           N  
ANISOU 1074  N   SER A 151     7811   8163  10017   -457   -979   -582       N  
ATOM   1075  CA  SER A 151      65.811 -26.433  -5.596  1.00 68.32           C  
ANISOU 1075  CA  SER A 151     7564   8521   9872   -478   -831   -668       C  
ATOM   1076  C   SER A 151      64.625 -27.238  -6.126  1.00 69.78           C  
ANISOU 1076  C   SER A 151     7745   8849   9916   -716   -878   -674       C  
ATOM   1077  O   SER A 151      63.472 -26.866  -5.899  1.00 70.64           O  
ANISOU 1077  O   SER A 151     7644   9338   9858   -848   -799   -736       O  
ATOM   1078  CB  SER A 151      66.108 -25.276  -6.551  1.00 66.65           C  
ANISOU 1078  CB  SER A 151     7238   8319   9766   -131   -709   -785       C  
ATOM   1079  OG  SER A 151      67.209 -24.509  -6.099  1.00 65.63           O  
ANISOU 1079  OG  SER A 151     7121   8076   9737     41   -670   -773       O  
ATOM   1080  N   ALA A 152      64.912 -28.336  -6.826  1.00 70.27           N  
ANISOU 1080  N   ALA A 152     8033   8627  10039   -764  -1016   -631       N  
ATOM   1081  CA  ALA A 152      63.877 -29.209  -7.375  1.00 71.87           C  
ANISOU 1081  CA  ALA A 152     8291   8913  10101  -1023  -1092   -619       C  
ATOM   1082  C   ALA A 152      63.633 -30.453  -6.508  1.00 74.31           C  
ANISOU 1082  C   ALA A 152     8849   9136  10249  -1460  -1289   -468       C  
ATOM   1083  O   ALA A 152      63.256 -31.506  -7.022  1.00 75.84           O  
ANISOU 1083  O   ALA A 152     9253   9192  10368  -1666  -1442   -421       O  
ATOM   1084  CB  ALA A 152      64.252 -29.614  -8.791  1.00 71.34           C  
ANISOU 1084  CB  ALA A 152     8352   8583  10168   -814  -1137   -680       C  
ATOM   1085  N   ASN A 153      63.839 -30.320  -5.198  1.00 74.88           N  
ANISOU 1085  N   ASN A 153     8932   9276  10244  -1627  -1303   -386       N  
ATOM   1086  CA  ASN A 153      63.591 -31.399  -4.239  1.00 77.69           C  
ANISOU 1086  CA  ASN A 153     9557   9565  10396  -2107  -1506   -223       C  
ATOM   1087  C   ASN A 153      64.410 -32.664  -4.532  1.00 78.91           C  
ANISOU 1087  C   ASN A 153    10165   9166  10649  -2107  -1816   -130       C  
ATOM   1088  O   ASN A 153      63.862 -33.757  -4.691  1.00 81.48           O  
ANISOU 1088  O   ASN A 153    10762   9382  10812  -2453  -2016    -44       O  
ATOM   1089  CB  ASN A 153      62.089 -31.713  -4.173  1.00 80.08           C  
ANISOU 1089  CB  ASN A 153     9731  10303  10391  -2567  -1465   -218       C  
ATOM   1090  CG  ASN A 153      61.697 -32.451  -2.904  1.00 83.20           C  
ANISOU 1090  CG  ASN A 153    10318  10804  10489  -3154  -1602    -59       C  
ATOM   1091  OD1 ASN A 153      62.188 -32.146  -1.816  1.00 83.19           O  
ANISOU 1091  OD1 ASN A 153    10342  10799  10467  -3202  -1599     -2       O  
ATOM   1092  ND2 ASN A 153      60.797 -33.420  -3.035  1.00 86.14           N  
ANISOU 1092  ND2 ASN A 153    10843  11280  10603  -3646  -1732     20       N  
ATOM   1093  N   SER A 154      65.728 -32.490  -4.604  1.00 77.54           N  
ANISOU 1093  N   SER A 154    10070   8659  10731  -1710  -1869   -167       N  
ATOM   1094  CA  SER A 154      66.683 -33.591  -4.803  1.00 78.96           C  
ANISOU 1094  CA  SER A 154    10645   8314  11040  -1592  -2185   -138       C  
ATOM   1095  C   SER A 154      66.471 -34.379  -6.104  1.00 79.86           C  
ANISOU 1095  C   SER A 154    10921   8230  11189  -1510  -2291   -214       C  
ATOM   1096  O   SER A 154      66.721 -35.586  -6.150  1.00 82.45           O  
ANISOU 1096  O   SER A 154    11664   8165  11496  -1603  -2622   -163       O  
ATOM   1097  CB  SER A 154      66.665 -34.542  -3.598  1.00 81.85           C  
ANISOU 1097  CB  SER A 154    11397   8474  11226  -2011  -2497     51       C  
ATOM   1098  OG  SER A 154      66.807 -33.827  -2.384  1.00 81.28           O  
ANISOU 1098  OG  SER A 154    11182   8605  11094  -2122  -2394    120       O  
ATOM   1099  N   ASP A 155      66.023 -33.693  -7.153  1.00 78.09           N  
ANISOU 1099  N   ASP A 155    10406   8252  11010  -1332  -2038   -339       N  
ATOM   1100  CA  ASP A 155      65.869 -34.300  -8.475  1.00 78.67           C  
ANISOU 1100  CA  ASP A 155    10601   8163  11124  -1221  -2101   -430       C  
ATOM   1101  C   ASP A 155      67.067 -33.904  -9.337  1.00 76.96           C  
ANISOU 1101  C   ASP A 155    10291   7779  11172   -698  -2019   -610       C  
ATOM   1102  O   ASP A 155      67.190 -32.751  -9.750  1.00 74.78           O  
ANISOU 1102  O   ASP A 155     9692   7745  10973   -479  -1748   -700       O  
ATOM   1103  CB  ASP A 155      64.559 -33.841  -9.126  1.00 78.30           C  
ANISOU 1103  CB  ASP A 155    10306   8511  10931  -1393  -1900   -455       C  
ATOM   1104  CG  ASP A 155      64.236 -34.596 -10.413  1.00 79.44           C  
ANISOU 1104  CG  ASP A 155    10624   8491  11067  -1378  -1995   -517       C  
ATOM   1105  OD1 ASP A 155      65.139 -35.227 -11.001  1.00 79.97           O  
ANISOU 1105  OD1 ASP A 155    10930   8173  11282  -1118  -2147   -598       O  
ATOM   1106  OD2 ASP A 155      63.065 -34.551 -10.844  1.00 80.07           O  
ANISOU 1106  OD2 ASP A 155    10584   8851  10985  -1617  -1920   -506       O  
ATOM   1107  N   GLU A 156      67.945 -34.868  -9.604  1.00 78.49           N  
ANISOU 1107  N   GLU A 156    10777   7565  11479   -509  -2274   -677       N  
ATOM   1108  CA  GLU A 156      69.166 -34.616 -10.372  1.00 77.59           C  
ANISOU 1108  CA  GLU A 156    10553   7338  11589    -30  -2210   -886       C  
ATOM   1109  C   GLU A 156      68.899 -34.354 -11.857  1.00 76.53           C  
ANISOU 1109  C   GLU A 156    10286   7322  11469    118  -2024  -1036       C  
ATOM   1110  O   GLU A 156      69.729 -33.752 -12.538  1.00 75.26           O  
ANISOU 1110  O   GLU A 156     9924   7234  11437    438  -1856  -1205       O  
ATOM   1111  CB  GLU A 156      70.146 -35.781 -10.216  1.00 80.40           C  
ANISOU 1111  CB  GLU A 156    11246   7249  12053    168  -2572   -965       C  
ATOM   1112  CG  GLU A 156      70.649 -35.968  -8.793  1.00 81.58           C  
ANISOU 1112  CG  GLU A 156    11535   7243  12215     86  -2784   -837       C  
ATOM   1113  CD  GLU A 156      71.742 -37.014  -8.681  1.00 84.71           C  
ANISOU 1113  CD  GLU A 156    12243   7191  12749    382  -3176   -959       C  
ATOM   1114  OE1 GLU A 156      71.826 -37.896  -9.562  1.00 86.83           O  
ANISOU 1114  OE1 GLU A 156    12738   7209  13043    543  -3364  -1105       O  
ATOM   1115  OE2 GLU A 156      72.517 -36.957  -7.703  1.00 85.42           O  
ANISOU 1115  OE2 GLU A 156    12359   7176  12921    473  -3320   -926       O  
ATOM   1116  N   THR A 157      67.749 -34.810 -12.352  1.00 77.27           N  
ANISOU 1116  N   THR A 157    10497   7453  11406   -149  -2060   -972       N  
ATOM   1117  CA  THR A 157      67.361 -34.590 -13.745  1.00 76.62           C  
ANISOU 1117  CA  THR A 157    10319   7481  11312    -57  -1906  -1092       C  
ATOM   1118  C   THR A 157      67.098 -33.112 -14.039  1.00 74.01           C  
ANISOU 1118  C   THR A 157     9609   7526  10984     13  -1578  -1113       C  
ATOM   1119  O   THR A 157      67.377 -32.637 -15.140  1.00 73.19           O  
ANISOU 1119  O   THR A 157     9396   7484  10926    213  -1429  -1250       O  
ATOM   1120  CB  THR A 157      66.094 -35.391 -14.108  1.00 78.21           C  
ANISOU 1120  CB  THR A 157    10726   7665  11324   -408  -2037   -998       C  
ATOM   1121  OG1 THR A 157      66.190 -36.715 -13.569  1.00 81.10           O  
ANISOU 1121  OG1 THR A 157    11511   7669  11632   -575  -2391   -921       O  
ATOM   1122  CG2 THR A 157      65.921 -35.473 -15.621  1.00 78.21           C  
ANISOU 1122  CG2 THR A 157    10730   7657  11328   -272  -1961  -1143       C  
ATOM   1123  N   VAL A 158      66.556 -32.396 -13.055  1.00 73.07           N  
ANISOU 1123  N   VAL A 158     9319   7648  10794   -159  -1490   -987       N  
ATOM   1124  CA  VAL A 158      66.254 -30.971 -13.205  1.00 70.95           C  
ANISOU 1124  CA  VAL A 158     8741   7700  10516    -75  -1240  -1012       C  
ATOM   1125  C   VAL A 158      67.544 -30.150 -13.218  1.00 69.73           C  
ANISOU 1125  C   VAL A 158     8467   7516  10509    224  -1117  -1100       C  
ATOM   1126  O   VAL A 158      67.693 -29.234 -14.028  1.00 68.50           O  
ANISOU 1126  O   VAL A 158     8178   7483  10365    370   -954  -1184       O  
ATOM   1127  CB  VAL A 158      65.318 -30.464 -12.085  1.00 70.73           C  
ANISOU 1127  CB  VAL A 158     8558   7958  10359   -316  -1196   -894       C  
ATOM   1128  CG1 VAL A 158      65.091 -28.962 -12.205  1.00 68.94           C  
ANISOU 1128  CG1 VAL A 158     8051   8008  10132   -157   -991   -952       C  
ATOM   1129  CG2 VAL A 158      63.986 -31.201 -12.129  1.00 72.46           C  
ANISOU 1129  CG2 VAL A 158     8834   8306  10389   -666  -1291   -826       C  
ATOM   1130  N   GLY A 159      68.465 -30.478 -12.314  1.00 70.48           N  
ANISOU 1130  N   GLY A 159     8628   7455  10695    285  -1216  -1074       N  
ATOM   1131  CA  GLY A 159      69.778 -29.835 -12.275  1.00 69.83           C  
ANISOU 1131  CA  GLY A 159     8424   7362  10744    544  -1123  -1166       C  
ATOM   1132  C   GLY A 159      70.571 -30.069 -13.549  1.00 70.58           C  
ANISOU 1132  C   GLY A 159     8524   7382  10911    771  -1082  -1361       C  
ATOM   1133  O   GLY A 159      71.268 -29.175 -14.029  1.00 69.73           O  
ANISOU 1133  O   GLY A 159     8251   7414  10829    908   -909  -1455       O  
ATOM   1134  N   LYS A 160      70.459 -31.280 -14.090  1.00 72.72           N  
ANISOU 1134  N   LYS A 160     9001   7442  11187    785  -1251  -1428       N  
ATOM   1135  CA  LYS A 160      71.075 -31.637 -15.367  1.00 74.05           C  
ANISOU 1135  CA  LYS A 160     9185   7556  11395    992  -1219  -1646       C  
ATOM   1136  C   LYS A 160      70.506 -30.793 -16.511  1.00 72.79           C  
ANISOU 1136  C   LYS A 160     8914   7609  11131    935  -1001  -1677       C  
ATOM   1137  O   LYS A 160      71.253 -30.315 -17.365  1.00 72.79           O  
ANISOU 1137  O   LYS A 160     8800   7721  11136   1073   -850  -1835       O  
ATOM   1138  CB  LYS A 160      70.853 -33.130 -15.645  1.00 76.81           C  
ANISOU 1138  CB  LYS A 160     9837   7602  11742    995  -1486  -1697       C  
ATOM   1139  CG  LYS A 160      71.489 -33.664 -16.920  1.00 78.68           C  
ANISOU 1139  CG  LYS A 160    10114   7766  12012   1237  -1485  -1962       C  
ATOM   1140  CD  LYS A 160      71.129 -35.130 -17.123  1.00 81.56           C  
ANISOU 1140  CD  LYS A 160    10844   7788  12355   1223  -1793  -1995       C  
ATOM   1141  CE  LYS A 160      71.496 -35.622 -18.515  1.00 83.40           C  
ANISOU 1141  CE  LYS A 160    11128   7976  12581   1434  -1773  -2265       C  
ATOM   1142  NZ  LYS A 160      72.969 -35.721 -18.713  1.00 85.13           N  
ANISOU 1142  NZ  LYS A 160    11193   8222  12928   1827  -1763  -2567       N  
ATOM   1143  N   LEU A 161      69.186 -30.616 -16.519  1.00 72.12           N  
ANISOU 1143  N   LEU A 161     8863   7601  10936    714   -999  -1534       N  
ATOM   1144  CA  LEU A 161      68.508 -29.825 -17.553  1.00 71.24           C  
ANISOU 1144  CA  LEU A 161     8679   7665  10723    662   -852  -1551       C  
ATOM   1145  C   LEU A 161      68.914 -28.353 -17.532  1.00 69.66           C  
ANISOU 1145  C   LEU A 161     8298   7660  10509    725   -670  -1549       C  
ATOM   1146  O   LEU A 161      69.184 -27.765 -18.580  1.00 69.73           O  
ANISOU 1146  O   LEU A 161     8288   7746  10459    767   -554  -1641       O  
ATOM   1147  CB  LEU A 161      66.984 -29.928 -17.405  1.00 71.22           C  
ANISOU 1147  CB  LEU A 161     8705   7748  10608    432   -918  -1416       C  
ATOM   1148  CG  LEU A 161      66.319 -31.172 -17.995  1.00 72.94           C  
ANISOU 1148  CG  LEU A 161     9131   7818  10764    299  -1072  -1423       C  
ATOM   1149  CD1 LEU A 161      64.918 -31.348 -17.428  1.00 73.38           C  
ANISOU 1149  CD1 LEU A 161     9170   8014  10695     12  -1152  -1274       C  
ATOM   1150  CD2 LEU A 161      66.278 -31.088 -19.514  1.00 73.17           C  
ANISOU 1150  CD2 LEU A 161     9204   7849  10747    370  -1000  -1549       C  
ATOM   1151  N   ILE A 162      68.946 -27.765 -16.338  1.00 68.60           N  
ANISOU 1151  N   ILE A 162     8067   7595  10402    702   -662  -1441       N  
ATOM   1152  CA  ILE A 162      69.283 -26.350 -16.183  1.00 67.26           C  
ANISOU 1152  CA  ILE A 162     7776   7574  10203    746   -531  -1424       C  
ATOM   1153  C   ILE A 162      70.754 -26.105 -16.523  1.00 67.79           C  
ANISOU 1153  C   ILE A 162     7793   7644  10318    864   -436  -1542       C  
ATOM   1154  O   ILE A 162      71.078 -25.142 -17.218  1.00 67.63           O  
ANISOU 1154  O   ILE A 162     7751   7733  10212    852   -322  -1583       O  
ATOM   1155  CB  ILE A 162      68.970 -25.842 -14.757  1.00 66.31           C  
ANISOU 1155  CB  ILE A 162     7575   7527  10093    696   -555  -1297       C  
ATOM   1156  CG1 ILE A 162      67.461 -25.893 -14.499  1.00 66.37           C  
ANISOU 1156  CG1 ILE A 162     7562   7647  10008    563   -614  -1224       C  
ATOM   1157  CG2 ILE A 162      69.471 -24.412 -14.567  1.00 65.31           C  
ANISOU 1157  CG2 ILE A 162     7375   7503   9935    757   -453  -1288       C  
ATOM   1158  CD1 ILE A 162      67.078 -25.807 -13.036  1.00 66.35           C  
ANISOU 1158  CD1 ILE A 162     7480   7738   9989    468   -650  -1126       C  
ATOM   1159  N   ALA A 163      71.633 -26.980 -16.038  1.00 68.93           N  
ANISOU 1159  N   ALA A 163     7926   7684  10579    962   -506  -1606       N  
ATOM   1160  CA  ALA A 163      73.068 -26.878 -16.318  1.00 69.96           C  
ANISOU 1160  CA  ALA A 163     7946   7879  10756   1093   -425  -1765       C  
ATOM   1161  C   ALA A 163      73.354 -26.929 -17.820  1.00 71.16           C  
ANISOU 1161  C   ALA A 163     8099   8117  10820   1112   -316  -1944       C  
ATOM   1162  O   ALA A 163      74.136 -26.129 -18.334  1.00 71.41           O  
ANISOU 1162  O   ALA A 163     8027   8335  10770   1083   -165  -2030       O  
ATOM   1163  CB  ALA A 163      73.830 -27.982 -15.598  1.00 71.42           C  
ANISOU 1163  CB  ALA A 163     8132   7913  11090   1248   -582  -1838       C  
ATOM   1164  N   GLU A 164      72.711 -27.867 -18.513  1.00 72.23           N  
ANISOU 1164  N   GLU A 164     8369   8127  10945   1122   -397  -1997       N  
ATOM   1165  CA  GLU A 164      72.842 -27.993 -19.969  1.00 73.56           C  
ANISOU 1165  CA  GLU A 164     8569   8368  11011   1120   -302  -2167       C  
ATOM   1166  C   GLU A 164      72.252 -26.790 -20.707  1.00 72.53           C  
ANISOU 1166  C   GLU A 164     8473   8372  10710    938   -181  -2080       C  
ATOM   1167  O   GLU A 164      72.790 -26.359 -21.728  1.00 73.46           O  
ANISOU 1167  O   GLU A 164     8573   8636  10700    880    -48  -2205       O  
ATOM   1168  CB  GLU A 164      72.169 -29.277 -20.465  1.00 74.87           C  
ANISOU 1168  CB  GLU A 164     8916   8333  11196   1155   -450  -2220       C  
ATOM   1169  CG  GLU A 164      72.938 -30.551 -20.143  1.00 77.15           C  
ANISOU 1169  CG  GLU A 164     9242   8451  11618   1377   -608  -2386       C  
ATOM   1170  CD  GLU A 164      72.191 -31.814 -20.539  1.00 78.66           C  
ANISOU 1170  CD  GLU A 164     9691   8389  11807   1378   -805  -2406       C  
ATOM   1171  OE1 GLU A 164      71.175 -31.717 -21.263  1.00 78.35           O  
ANISOU 1171  OE1 GLU A 164     9757   8357  11653   1206   -776  -2327       O  
ATOM   1172  OE2 GLU A 164      72.621 -32.911 -20.124  1.00 80.46           O  
ANISOU 1172  OE2 GLU A 164    10040   8393  12138   1548  -1020  -2503       O  
ATOM   1173  N   ALA A 165      71.145 -26.261 -20.192  1.00 71.07           N  
ANISOU 1173  N   ALA A 165     8348   8148  10507    845   -247  -1882       N  
ATOM   1174  CA  ALA A 165      70.487 -25.099 -20.792  1.00 70.41           C  
ANISOU 1174  CA  ALA A 165     8333   8145  10273    721   -207  -1803       C  
ATOM   1175  C   ALA A 165      71.356 -23.849 -20.696  1.00 70.23           C  
ANISOU 1175  C   ALA A 165     8266   8248  10167    666   -103  -1793       C  
ATOM   1176  O   ALA A 165      71.504 -23.115 -21.676  1.00 70.88           O  
ANISOU 1176  O   ALA A 165     8443   8405  10080    542    -41  -1824       O  
ATOM   1177  CB  ALA A 165      69.140 -24.854 -20.131  1.00 69.36           C  
ANISOU 1177  CB  ALA A 165     8221   7980  10151    693   -324  -1644       C  
ATOM   1178  N   MET A 166      71.930 -23.617 -19.517  1.00 69.71           N  
ANISOU 1178  N   MET A 166     8088   8201  10197    721   -100  -1741       N  
ATOM   1179  CA  MET A 166      72.815 -22.470 -19.299  1.00 69.88           C  
ANISOU 1179  CA  MET A 166     8076   8340  10133    642    -16  -1721       C  
ATOM   1180  C   MET A 166      74.139 -22.633 -20.042  1.00 71.54           C  
ANISOU 1180  C   MET A 166     8186   8720  10275    592    126  -1905       C  
ATOM   1181  O   MET A 166      74.772 -21.645 -20.408  1.00 72.03           O  
ANISOU 1181  O   MET A 166     8272   8925  10168    420    213  -1908       O  
ATOM   1182  CB  MET A 166      73.075 -22.261 -17.802  1.00 68.99           C  
ANISOU 1182  CB  MET A 166     7865   8204  10141    711    -58  -1622       C  
ATOM   1183  CG  MET A 166      71.829 -21.896 -17.012  1.00 67.80           C  
ANISOU 1183  CG  MET A 166     7776   7972  10012    735   -171  -1472       C  
ATOM   1184  SD  MET A 166      72.163 -21.510 -15.281  1.00 66.90           S  
ANISOU 1184  SD  MET A 166     7569   7856   9992    777   -204  -1364       S  
ATOM   1185  CE  MET A 166      72.409 -19.741 -15.377  1.00 66.76           C  
ANISOU 1185  CE  MET A 166     7674   7887   9804    689   -188  -1305       C  
ATOM   1186  N   ASP A 167      74.553 -23.877 -20.262  1.00 72.81           N  
ANISOU 1186  N   ASP A 167     8241   8879  10543    733    136  -2073       N  
ATOM   1187  CA  ASP A 167      75.752 -24.161 -21.047  1.00 75.27           C  
ANISOU 1187  CA  ASP A 167     8407   9409  10783    730    274  -2318       C  
ATOM   1188  C   ASP A 167      75.568 -23.768 -22.520  1.00 76.48           C  
ANISOU 1188  C   ASP A 167     8683   9675  10699    529    377  -2388       C  
ATOM   1189  O   ASP A 167      76.524 -23.362 -23.178  1.00 78.31           O  
ANISOU 1189  O   ASP A 167     8818  10175  10758    378    531  -2534       O  
ATOM   1190  CB  ASP A 167      76.118 -25.646 -20.935  1.00 76.71           C  
ANISOU 1190  CB  ASP A 167     8485   9516  11143    994    202  -2512       C  
ATOM   1191  CG  ASP A 167      77.505 -25.953 -21.469  1.00 79.46           C  
ANISOU 1191  CG  ASP A 167     8594  10145  11449   1074    330  -2823       C  
ATOM   1192  OD1 ASP A 167      78.463 -25.245 -21.092  1.00 79.90           O  
ANISOU 1192  OD1 ASP A 167     8463  10437  11456    998    429  -2854       O  
ATOM   1193  OD2 ASP A 167      77.638 -26.915 -22.255  1.00 81.55           O  
ANISOU 1193  OD2 ASP A 167     8847  10417  11721   1215    326  -3055       O  
ATOM   1194  N   LYS A 168      74.339 -23.892 -23.026  1.00 75.75           N  
ANISOU 1194  N   LYS A 168     8798   9403  10579    501    285  -2287       N  
ATOM   1195  CA  LYS A 168      74.020 -23.538 -24.416  1.00 76.74           C  
ANISOU 1195  CA  LYS A 168     9091   9588  10477    303    340  -2327       C  
ATOM   1196  C   LYS A 168      74.013 -22.028 -24.656  1.00 76.35           C  
ANISOU 1196  C   LYS A 168     9203   9602  10205     36    351  -2183       C  
ATOM   1197  O   LYS A 168      74.802 -21.520 -25.452  1.00 78.22           O  
ANISOU 1197  O   LYS A 168     9456  10051  10210   -200    479  -2277       O  
ATOM   1198  CB  LYS A 168      72.661 -24.123 -24.831  1.00 76.19           C  
ANISOU 1198  CB  LYS A 168     9194   9303  10450    357    205  -2255       C  
ATOM   1199  CG  LYS A 168      72.724 -25.525 -25.416  1.00 77.80           C  
ANISOU 1199  CG  LYS A 168     9371   9468  10721    489    209  -2450       C  
ATOM   1200  CD  LYS A 168      73.269 -25.516 -26.838  1.00 80.30           C  
ANISOU 1200  CD  LYS A 168     9723   9970  10817    344    355  -2650       C  
ATOM   1201  CE  LYS A 168      72.906 -26.786 -27.593  1.00 81.73           C  
ANISOU 1201  CE  LYS A 168     9977  10047  11027    457    311  -2809       C  
ATOM   1202  NZ  LYS A 168      73.463 -28.011 -26.955  1.00 82.76           N  
ANISOU 1202  NZ  LYS A 168     9971  10105  11370    750    254  -2977       N  
ATOM   1203  N   VAL A 169      73.122 -21.321 -23.963  1.00 74.33           N  
ANISOU 1203  N   VAL A 169     9078   9166   9995     65    198  -1971       N  
ATOM   1204  CA  VAL A 169      72.898 -19.888 -24.208  1.00 74.44           C  
ANISOU 1204  CA  VAL A 169     9337   9147   9797   -141    119  -1828       C  
ATOM   1205  C   VAL A 169      73.689 -18.952 -23.283  1.00 74.33           C  
ANISOU 1205  C   VAL A 169     9289   9198   9755   -215    136  -1749       C  
ATOM   1206  O   VAL A 169      73.594 -17.732 -23.412  1.00 74.62           O  
ANISOU 1206  O   VAL A 169     9575   9174   9601   -394     38  -1630       O  
ATOM   1207  CB  VAL A 169      71.395 -19.519 -24.121  1.00 73.20           C  
ANISOU 1207  CB  VAL A 169     9371   8768   9674    -38    -98  -1684       C  
ATOM   1208  CG1 VAL A 169      70.594 -20.289 -25.164  1.00 73.69           C  
ANISOU 1208  CG1 VAL A 169     9505   8777   9715    -27   -132  -1745       C  
ATOM   1209  CG2 VAL A 169      70.838 -19.754 -22.719  1.00 71.37           C  
ANISOU 1209  CG2 VAL A 169     8984   8455   9677    201   -176  -1605       C  
ATOM   1210  N   GLY A 170      74.465 -19.517 -22.360  1.00 74.17           N  
ANISOU 1210  N   GLY A 170     8995   9274   9912    -82    228  -1812       N  
ATOM   1211  CA  GLY A 170      75.241 -18.722 -21.406  1.00 74.10           C  
ANISOU 1211  CA  GLY A 170     8930   9333   9891   -147    242  -1738       C  
ATOM   1212  C   GLY A 170      74.530 -18.607 -20.073  1.00 72.13           C  
ANISOU 1212  C   GLY A 170     8671   8896   9837     65    106  -1596       C  
ATOM   1213  O   GLY A 170      73.381 -19.030 -19.936  1.00 71.06           O  
ANISOU 1213  O   GLY A 170     8575   8609   9813    228      1  -1551       O  
ATOM   1214  N   LYS A 171      75.218 -18.032 -19.091  1.00 72.16           N  
ANISOU 1214  N   LYS A 171     8613   8945   9860     37    114  -1533       N  
ATOM   1215  CA  LYS A 171      74.681 -17.903 -17.737  1.00 70.62           C  
ANISOU 1215  CA  LYS A 171     8392   8613   9828    215      6  -1416       C  
ATOM   1216  C   LYS A 171      73.597 -16.830 -17.677  1.00 70.09           C  
ANISOU 1216  C   LYS A 171     8594   8378   9658    224   -163  -1294       C  
ATOM   1217  O   LYS A 171      72.546 -17.041 -17.075  1.00 68.70           O  
ANISOU 1217  O   LYS A 171     8394   8106   9600    413   -260  -1257       O  
ATOM   1218  CB  LYS A 171      75.797 -17.585 -16.738  1.00 70.82           C  
ANISOU 1218  CB  LYS A 171     8283   8737   9888    172     57  -1394       C  
ATOM   1219  CG  LYS A 171      76.920 -18.611 -16.723  1.00 71.90           C  
ANISOU 1219  CG  LYS A 171     8124   9056  10136    220    185  -1552       C  
ATOM   1220  CD  LYS A 171      77.674 -18.607 -15.403  1.00 71.64           C  
ANISOU 1220  CD  LYS A 171     7929   9060  10231    285    172  -1514       C  
ATOM   1221  CE  LYS A 171      78.912 -19.486 -15.467  1.00 73.46           C  
ANISOU 1221  CE  LYS A 171     7860   9500  10551    352    265  -1708       C  
ATOM   1222  NZ  LYS A 171      79.853 -19.199 -14.348  1.00 73.71           N  
ANISOU 1222  NZ  LYS A 171     7743   9619  10642    346    251  -1675       N  
ATOM   1223  N   GLU A 172      73.862 -15.694 -18.322  1.00 71.57           N  
ANISOU 1223  N   GLU A 172     9043   8546   9603     11   -217  -1250       N  
ATOM   1224  CA  GLU A 172      72.918 -14.573 -18.392  1.00 72.04           C  
ANISOU 1224  CA  GLU A 172     9424   8411   9538     41   -441  -1161       C  
ATOM   1225  C   GLU A 172      71.957 -14.672 -19.590  1.00 71.99           C  
ANISOU 1225  C   GLU A 172     9586   8319   9447     53   -541  -1192       C  
ATOM   1226  O   GLU A 172      71.173 -13.752 -19.828  1.00 72.66           O  
ANISOU 1226  O   GLU A 172     9959   8232   9413     96   -769  -1145       O  
ATOM   1227  CB  GLU A 172      73.689 -13.246 -18.466  1.00 74.31           C  
ANISOU 1227  CB  GLU A 172    10002   8657   9572   -223   -518  -1077       C  
ATOM   1228  CG  GLU A 172      74.696 -13.022 -17.342  1.00 74.62           C  
ANISOU 1228  CG  GLU A 172     9902   8790   9660   -279   -435  -1037       C  
ATOM   1229  CD  GLU A 172      74.045 -12.893 -15.973  1.00 73.63           C  
ANISOU 1229  CD  GLU A 172     9712   8550   9713      4   -534   -993       C  
ATOM   1230  OE1 GLU A 172      73.142 -12.042 -15.814  1.00 74.08           O  
ANISOU 1230  OE1 GLU A 172    10023   8419   9703    131   -750   -958       O  
ATOM   1231  OE2 GLU A 172      74.446 -13.638 -15.051  1.00 72.93           O  
ANISOU 1231  OE2 GLU A 172     9324   8566   9817    103   -411  -1011       O  
ATOM   1232  N   GLY A 173      72.007 -15.781 -20.330  1.00 71.24           N  
ANISOU 1232  N   GLY A 173     9326   8327   9412     35   -402  -1284       N  
ATOM   1233  CA  GLY A 173      71.139 -15.988 -21.495  1.00 71.25           C  
ANISOU 1233  CA  GLY A 173     9475   8262   9336     27   -485  -1316       C  
ATOM   1234  C   GLY A 173      69.692 -16.264 -21.140  1.00 69.68           C  
ANISOU 1234  C   GLY A 173     9222   7969   9281    300   -635  -1311       C  
ATOM   1235  O   GLY A 173      69.367 -16.491 -19.971  1.00 68.27           O  
ANISOU 1235  O   GLY A 173     8853   7814   9272    484   -638  -1298       O  
ATOM   1236  N   VAL A 174      68.826 -16.252 -22.157  1.00 69.91           N  
ANISOU 1236  N   VAL A 174     9411   7926   9223    299   -761  -1329       N  
ATOM   1237  CA  VAL A 174      67.389 -16.446 -21.961  1.00 69.23           C  
ANISOU 1237  CA  VAL A 174     9257   7808   9238    535   -921  -1348       C  
ATOM   1238  C   VAL A 174      67.039 -17.936 -21.991  1.00 68.06           C  
ANISOU 1238  C   VAL A 174     8841   7766   9251    578   -787  -1404       C  
ATOM   1239  O   VAL A 174      67.416 -18.644 -22.921  1.00 68.45           O  
ANISOU 1239  O   VAL A 174     8911   7833   9261    445   -682  -1449       O  
ATOM   1240  CB  VAL A 174      66.561 -15.707 -23.040  1.00 70.89           C  
ANISOU 1240  CB  VAL A 174     9776   7882   9275    529  -1169  -1347       C  
ATOM   1241  CG1 VAL A 174      65.069 -15.877 -22.782  1.00 70.97           C  
ANISOU 1241  CG1 VAL A 174     9651   7923   9389    797  -1342  -1402       C  
ATOM   1242  CG2 VAL A 174      66.921 -14.226 -23.081  1.00 72.28           C  
ANISOU 1242  CG2 VAL A 174    10317   7889   9255    458  -1364  -1282       C  
ATOM   1243  N   ILE A 175      66.312 -18.397 -20.974  1.00 66.88           N  
ANISOU 1243  N   ILE A 175     8463   7691   9256    743   -805  -1408       N  
ATOM   1244  CA  ILE A 175      65.852 -19.787 -20.890  1.00 66.34           C  
ANISOU 1244  CA  ILE A 175     8192   7700   9311    747   -732  -1438       C  
ATOM   1245  C   ILE A 175      64.357 -19.806 -20.583  1.00 66.59           C  
ANISOU 1245  C   ILE A 175     8107   7829   9362    870   -880  -1459       C  
ATOM   1246  O   ILE A 175      63.891 -19.058 -19.722  1.00 66.47           O  
ANISOU 1246  O   ILE A 175     8021   7882   9353   1009   -967  -1466       O  
ATOM   1247  CB  ILE A 175      66.598 -20.581 -19.792  1.00 65.34           C  
ANISOU 1247  CB  ILE A 175     7877   7616   9332    743   -591  -1421       C  
ATOM   1248  CG1 ILE A 175      68.112 -20.518 -20.019  1.00 65.43           C  
ANISOU 1248  CG1 ILE A 175     7937   7595   9327    653   -451  -1440       C  
ATOM   1249  CG2 ILE A 175      66.139 -22.039 -19.772  1.00 65.44           C  
ANISOU 1249  CG2 ILE A 175     7775   7652   9437    710   -570  -1440       C  
ATOM   1250  CD1 ILE A 175      68.936 -21.047 -18.862  1.00 64.79           C  
ANISOU 1250  CD1 ILE A 175     7689   7539   9387    688   -362  -1427       C  
ATOM   1251  N   THR A 176      63.617 -20.663 -21.288  1.00 67.11           N  
ANISOU 1251  N   THR A 176     8141   7931   9423    817   -909  -1487       N  
ATOM   1252  CA  THR A 176      62.178 -20.812 -21.078  1.00 67.96           C  
ANISOU 1252  CA  THR A 176     8089   8203   9530    891  -1039  -1526       C  
ATOM   1253  C   THR A 176      61.799 -22.283 -20.913  1.00 68.02           C  
ANISOU 1253  C   THR A 176     7952   8295   9595    748   -971  -1513       C  
ATOM   1254  O   THR A 176      62.435 -23.166 -21.492  1.00 67.95           O  
ANISOU 1254  O   THR A 176     8048   8160   9608    630   -888  -1499       O  
ATOM   1255  CB  THR A 176      61.369 -20.233 -22.258  1.00 69.37           C  
ANISOU 1255  CB  THR A 176     8415   8347   9594    946  -1227  -1573       C  
ATOM   1256  OG1 THR A 176      61.948 -18.993 -22.695  1.00 69.67           O  
ANISOU 1256  OG1 THR A 176     8719   8214   9536    999  -1314  -1560       O  
ATOM   1257  CG2 THR A 176      59.922 -19.997 -21.843  1.00 70.67           C  
ANISOU 1257  CG2 THR A 176     8361   8740   9751   1099  -1392  -1657       C  
ATOM   1258  N   VAL A 177      60.755 -22.534 -20.127  1.00 68.66           N  
ANISOU 1258  N   VAL A 177     7803   8603   9679    749  -1023  -1533       N  
ATOM   1259  CA  VAL A 177      60.243 -23.885 -19.902  1.00 69.38           C  
ANISOU 1259  CA  VAL A 177     7790   8792   9776    549  -1002  -1504       C  
ATOM   1260  C   VAL A 177      58.894 -24.040 -20.600  1.00 71.15           C  
ANISOU 1260  C   VAL A 177     7926   9199   9908    508  -1132  -1561       C  
ATOM   1261  O   VAL A 177      58.053 -23.143 -20.530  1.00 72.03           O  
ANISOU 1261  O   VAL A 177     7894   9503   9971    668  -1242  -1649       O  
ATOM   1262  CB  VAL A 177      60.072 -24.184 -18.398  1.00 69.43           C  
ANISOU 1262  CB  VAL A 177     7594   8981   9806    474   -953  -1473       C  
ATOM   1263  CG1 VAL A 177      59.953 -25.684 -18.161  1.00 70.11           C  
ANISOU 1263  CG1 VAL A 177     7702   9051   9882    202   -945  -1401       C  
ATOM   1264  CG2 VAL A 177      61.239 -23.619 -17.603  1.00 68.04           C  
ANISOU 1264  CG2 VAL A 177     7465   8675   9711    577   -861  -1436       C  
ATOM   1265  N   GLU A 178      58.698 -25.176 -21.270  1.00 72.01           N  
ANISOU 1265  N   GLU A 178     8124   9244   9990    312  -1142  -1528       N  
ATOM   1266  CA  GLU A 178      57.448 -25.476 -21.977  1.00 73.92           C  
ANISOU 1266  CA  GLU A 178     8289   9662  10135    224  -1268  -1570       C  
ATOM   1267  C   GLU A 178      56.955 -26.884 -21.659  1.00 75.06           C  
ANISOU 1267  C   GLU A 178     8389   9900  10228    -86  -1271  -1511       C  
ATOM   1268  O   GLU A 178      57.683 -27.689 -21.077  1.00 74.40           O  
ANISOU 1268  O   GLU A 178     8415   9660  10191   -213  -1202  -1434       O  
ATOM   1269  CB  GLU A 178      57.650 -25.349 -23.488  1.00 74.09           C  
ANISOU 1269  CB  GLU A 178     8562   9463  10123    260  -1325  -1586       C  
ATOM   1270  CG  GLU A 178      57.862 -23.924 -23.968  1.00 73.95           C  
ANISOU 1270  CG  GLU A 178     8641   9366  10091    499  -1397  -1635       C  
ATOM   1271  CD  GLU A 178      57.905 -23.813 -25.482  1.00 74.62           C  
ANISOU 1271  CD  GLU A 178     8989   9268  10094    471  -1479  -1644       C  
ATOM   1272  OE1 GLU A 178      57.917 -24.853 -26.175  1.00 75.02           O  
ANISOU 1272  OE1 GLU A 178     9145   9240  10117    291  -1445  -1623       O  
ATOM   1273  OE2 GLU A 178      57.925 -22.676 -25.986  1.00 74.95           O  
ANISOU 1273  OE2 GLU A 178     9166   9228  10081    618  -1597  -1672       O  
ATOM   1274  N   ASP A 179      55.715 -27.172 -22.051  1.00 77.01           N  
ANISOU 1274  N   ASP A 179     8498  10396  10364   -217  -1381  -1548       N  
ATOM   1275  CA  ASP A 179      55.151 -28.513 -21.908  1.00 78.59           C  
ANISOU 1275  CA  ASP A 179     8708  10685  10467   -579  -1418  -1479       C  
ATOM   1276  C   ASP A 179      55.839 -29.465 -22.884  1.00 78.32           C  
ANISOU 1276  C   ASP A 179     9045  10256  10454   -676  -1433  -1419       C  
ATOM   1277  O   ASP A 179      56.073 -29.115 -24.040  1.00 77.72           O  
ANISOU 1277  O   ASP A 179     9122  10011  10397   -534  -1452  -1463       O  
ATOM   1278  CB  ASP A 179      53.641 -28.506 -22.177  1.00 81.08           C  
ANISOU 1278  CB  ASP A 179     8754  11414  10638   -706  -1536  -1552       C  
ATOM   1279  CG  ASP A 179      52.860 -27.696 -21.154  1.00 82.31           C  
ANISOU 1279  CG  ASP A 179     8487  12041  10745   -613  -1527  -1668       C  
ATOM   1280  OD1 ASP A 179      53.247 -27.679 -19.966  1.00 81.74           O  
ANISOU 1280  OD1 ASP A 179     8329  12038  10689   -657  -1424  -1639       O  
ATOM   1281  OD2 ASP A 179      51.843 -27.081 -21.540  1.00 84.28           O  
ANISOU 1281  OD2 ASP A 179     8482  12607  10932   -484  -1637  -1807       O  
ATOM   1282  N   GLY A 180      56.164 -30.666 -22.411  1.00 78.99           N  
ANISOU 1282  N   GLY A 180     9297  10192  10522   -919  -1445  -1331       N  
ATOM   1283  CA  GLY A 180      56.805 -31.678 -23.246  1.00 79.30           C  
ANISOU 1283  CA  GLY A 180     9700   9853  10576   -983  -1490  -1310       C  
ATOM   1284  C   GLY A 180      55.833 -32.356 -24.191  1.00 81.33           C  
ANISOU 1284  C   GLY A 180    10045  10163  10693  -1214  -1620  -1303       C  
ATOM   1285  O   GLY A 180      54.616 -32.236 -24.039  1.00 82.80           O  
ANISOU 1285  O   GLY A 180     9991  10711  10757  -1391  -1684  -1297       O  
ATOM   1286  N   THR A 181      56.384 -33.076 -25.165  1.00 81.77           N  
ANISOU 1286  N   THR A 181    10431   9880  10756  -1209  -1659  -1324       N  
ATOM   1287  CA  THR A 181      55.590 -33.802 -26.156  1.00 83.71           C  
ANISOU 1287  CA  THR A 181    10831  10109  10866  -1431  -1792  -1316       C  
ATOM   1288  C   THR A 181      55.724 -35.324 -25.998  1.00 85.45           C  
ANISOU 1288  C   THR A 181    11391  10062  11011  -1706  -1933  -1249       C  
ATOM   1289  O   THR A 181      55.363 -36.079 -26.902  1.00 87.04           O  
ANISOU 1289  O   THR A 181    11830  10128  11110  -1866  -2052  -1252       O  
ATOM   1290  CB  THR A 181      56.000 -33.405 -27.590  1.00 83.21           C  
ANISOU 1290  CB  THR A 181    10924   9865  10824  -1226  -1756  -1414       C  
ATOM   1291  OG1 THR A 181      57.382 -33.720 -27.802  1.00 82.52           O  
ANISOU 1291  OG1 THR A 181    11078   9435  10838  -1040  -1671  -1485       O  
ATOM   1292  CG2 THR A 181      55.782 -31.915 -27.820  1.00 82.00           C  
ANISOU 1292  CG2 THR A 181    10523   9926  10707   -995  -1690  -1464       C  
ATOM   1293  N   GLY A 182      56.230 -35.771 -24.849  1.00 85.45           N  
ANISOU 1293  N   GLY A 182    11451   9963  11051  -1766  -1950  -1186       N  
ATOM   1294  CA  GLY A 182      56.425 -37.198 -24.602  1.00 87.66           C  
ANISOU 1294  CA  GLY A 182    12125   9927  11255  -2012  -2145  -1117       C  
ATOM   1295  C   GLY A 182      57.112 -37.488 -23.281  1.00 87.76           C  
ANISOU 1295  C   GLY A 182    12202   9810  11329  -2020  -2176  -1052       C  
ATOM   1296  O   GLY A 182      57.102 -36.659 -22.371  1.00 86.23           O  
ANISOU 1296  O   GLY A 182    11696   9880  11187  -1962  -2045  -1025       O  
ATOM   1297  N   LEU A 183      57.705 -38.675 -23.180  1.00 89.87           N  
ANISOU 1297  N   LEU A 183    12906   9652  11586  -2082  -2379  -1036       N  
ATOM   1298  CA  LEU A 183      58.388 -39.108 -21.959  1.00 90.68           C  
ANISOU 1298  CA  LEU A 183    13159   9558  11736  -2101  -2482   -969       C  
ATOM   1299  C   LEU A 183      59.713 -38.377 -21.769  1.00 88.45           C  
ANISOU 1299  C   LEU A 183    12738   9166  11700  -1612  -2314  -1096       C  
ATOM   1300  O   LEU A 183      59.986 -37.845 -20.693  1.00 87.32           O  
ANISOU 1300  O   LEU A 183    12401   9155  11619  -1579  -2235  -1039       O  
ATOM   1301  CB  LEU A 183      58.643 -40.620 -21.994  1.00 93.92           C  
ANISOU 1301  CB  LEU A 183    14142   9484  12056  -2272  -2820   -935       C  
ATOM   1302  CG  LEU A 183      59.317 -41.234 -20.756  1.00 95.27           C  
ANISOU 1302  CG  LEU A 183    14576   9371  12249  -2322  -3022   -853       C  
ATOM   1303  CD1 LEU A 183      58.316 -41.999 -19.903  1.00 98.18           C  
ANISOU 1303  CD1 LEU A 183    15154   9815  12334  -2960  -3250   -622       C  
ATOM   1304  CD2 LEU A 183      60.464 -42.150 -21.160  1.00 96.87           C  
ANISOU 1304  CD2 LEU A 183    15234   8998  12571  -1987  -3256  -1004       C  
ATOM   1305  N   GLN A 184      60.534 -38.366 -22.815  1.00 88.18           N  
ANISOU 1305  N   GLN A 184    12801   8919  11783  -1261  -2260  -1277       N  
ATOM   1306  CA  GLN A 184      61.885 -37.813 -22.732  1.00 86.65           C  
ANISOU 1306  CA  GLN A 184    12497   8632  11793   -830  -2116  -1425       C  
ATOM   1307  C   GLN A 184      61.888 -36.291 -22.827  1.00 83.55           C  
ANISOU 1307  C   GLN A 184    11678   8597  11467   -673  -1822  -1446       C  
ATOM   1308  O   GLN A 184      61.040 -35.698 -23.497  1.00 82.77           O  
ANISOU 1308  O   GLN A 184    11427   8737  11285   -766  -1733  -1428       O  
ATOM   1309  CB  GLN A 184      62.768 -38.410 -23.829  1.00 88.09           C  
ANISOU 1309  CB  GLN A 184    12922   8514  12035   -542  -2163  -1650       C  
ATOM   1310  CG  GLN A 184      62.943 -39.917 -23.715  1.00 91.58           C  
ANISOU 1310  CG  GLN A 184    13843   8523  12430   -604  -2508  -1672       C  
ATOM   1311  CD  GLN A 184      63.860 -40.490 -24.781  1.00 93.45           C  
ANISOU 1311  CD  GLN A 184    14290   8489  12726   -254  -2556  -1954       C  
ATOM   1312  OE1 GLN A 184      64.074 -39.877 -25.828  1.00 92.59           O  
ANISOU 1312  OE1 GLN A 184    14001   8550  12628    -90  -2327  -2105       O  
ATOM   1313  NE2 GLN A 184      64.404 -41.675 -24.520  1.00 96.49           N  
ANISOU 1313  NE2 GLN A 184    15076   8454  13131   -141  -2875  -2043       N  
ATOM   1314  N   ASP A 185      62.855 -35.670 -22.154  1.00 81.96           N  
ANISOU 1314  N   ASP A 185    11318   8412  11408   -435  -1706  -1485       N  
ATOM   1315  CA  ASP A 185      63.012 -34.216 -22.164  1.00 79.42           C  
ANISOU 1315  CA  ASP A 185    10660   8371  11143   -281  -1463  -1504       C  
ATOM   1316  C   ASP A 185      63.635 -33.752 -23.476  1.00 79.15           C  
ANISOU 1316  C   ASP A 185    10619   8323  11128    -62  -1321  -1675       C  
ATOM   1317  O   ASP A 185      64.175 -34.558 -24.238  1.00 80.76           O  
ANISOU 1317  O   ASP A 185    11034   8315  11336     33  -1380  -1816       O  
ATOM   1318  CB  ASP A 185      63.899 -33.760 -21.000  1.00 78.09           C  
ANISOU 1318  CB  ASP A 185    10360   8210  11101   -133  -1402  -1484       C  
ATOM   1319  CG  ASP A 185      63.317 -34.113 -19.641  1.00 78.55           C  
ANISOU 1319  CG  ASP A 185    10419   8313  11110   -382  -1525  -1312       C  
ATOM   1320  OD1 ASP A 185      62.102 -33.913 -19.435  1.00 78.67           O  
ANISOU 1320  OD1 ASP A 185    10316   8578  10995   -640  -1528  -1207       O  
ATOM   1321  OD2 ASP A 185      64.081 -34.585 -18.773  1.00 79.05           O  
ANISOU 1321  OD2 ASP A 185    10594   8188  11252   -327  -1625  -1294       O  
ATOM   1322  N   GLU A 186      63.544 -32.451 -23.740  1.00 77.73           N  
ANISOU 1322  N   GLU A 186    10219   8373  10939      2  -1152  -1673       N  
ATOM   1323  CA  GLU A 186      64.175 -31.846 -24.913  1.00 77.75           C  
ANISOU 1323  CA  GLU A 186    10224   8398  10919    144  -1010  -1814       C  
ATOM   1324  C   GLU A 186      64.811 -30.509 -24.554  1.00 76.23           C  
ANISOU 1324  C   GLU A 186     9832   8362  10769    268   -849  -1811       C  
ATOM   1325  O   GLU A 186      64.470 -29.895 -23.543  1.00 75.17           O  
ANISOU 1325  O   GLU A 186     9546   8344  10671    251   -850  -1695       O  
ATOM   1326  CB  GLU A 186      63.159 -31.630 -26.039  1.00 78.29           C  
ANISOU 1326  CB  GLU A 186    10350   8545  10849     10  -1037  -1799       C  
ATOM   1327  CG  GLU A 186      62.457 -32.888 -26.526  1.00 80.22           C  
ANISOU 1327  CG  GLU A 186    10812   8648  11020   -152  -1201  -1794       C  
ATOM   1328  CD  GLU A 186      61.530 -32.616 -27.697  1.00 80.79           C  
ANISOU 1328  CD  GLU A 186    10932   8808  10955   -276  -1227  -1788       C  
ATOM   1329  OE1 GLU A 186      60.333 -32.958 -27.608  1.00 81.60           O  
ANISOU 1329  OE1 GLU A 186    11030   8992  10981   -481  -1361  -1683       O  
ATOM   1330  OE2 GLU A 186      61.994 -32.051 -28.707  1.00 80.72           O  
ANISOU 1330  OE2 GLU A 186    10965   8807  10896   -193  -1122  -1890       O  
ATOM   1331  N   LEU A 187      65.735 -30.069 -25.401  1.00 76.46           N  
ANISOU 1331  N   LEU A 187     9875   8408  10766    367   -714  -1949       N  
ATOM   1332  CA  LEU A 187      66.403 -28.781 -25.241  1.00 75.29           C  
ANISOU 1332  CA  LEU A 187     9596   8400  10610    426   -573  -1948       C  
ATOM   1333  C   LEU A 187      66.796 -28.262 -26.617  1.00 76.06           C  
ANISOU 1333  C   LEU A 187     9781   8559  10559    380   -466  -2061       C  
ATOM   1334  O   LEU A 187      67.597 -28.890 -27.310  1.00 77.79           O  
ANISOU 1334  O   LEU A 187    10051   8754  10751    423   -393  -2241       O  
ATOM   1335  CB  LEU A 187      67.641 -28.930 -24.352  1.00 75.15           C  
ANISOU 1335  CB  LEU A 187     9468   8367  10718    568   -507  -2011       C  
ATOM   1336  CG  LEU A 187      68.524 -27.695 -24.136  1.00 74.28           C  
ANISOU 1336  CG  LEU A 187     9229   8405  10588    600   -361  -2019       C  
ATOM   1337  CD1 LEU A 187      67.738 -26.552 -23.513  1.00 72.75           C  
ANISOU 1337  CD1 LEU A 187     8986   8284  10368    543   -398  -1841       C  
ATOM   1338  CD2 LEU A 187      69.720 -28.054 -23.269  1.00 74.59           C  
ANISOU 1338  CD2 LEU A 187     9144   8436  10760    745   -323  -2100       C  
ATOM   1339  N   ASP A 188      66.226 -27.124 -27.008  1.00 75.31           N  
ANISOU 1339  N   ASP A 188     9716   8545  10351    291   -478  -1970       N  
ATOM   1340  CA  ASP A 188      66.452 -26.545 -28.331  1.00 76.22           C  
ANISOU 1340  CA  ASP A 188     9975   8704  10279    178   -417  -2040       C  
ATOM   1341  C   ASP A 188      66.688 -25.041 -28.232  1.00 75.42           C  
ANISOU 1341  C   ASP A 188     9892   8681  10082    125   -398  -1959       C  
ATOM   1342  O   ASP A 188      66.023 -24.353 -27.457  1.00 74.44           O  
ANISOU 1342  O   ASP A 188     9718   8554  10010    183   -508  -1830       O  
ATOM   1343  CB  ASP A 188      65.244 -26.800 -29.240  1.00 77.11           C  
ANISOU 1343  CB  ASP A 188    10240   8760  10296     79   -553  -2000       C  
ATOM   1344  CG  ASP A 188      65.101 -28.257 -29.662  1.00 78.44           C  
ANISOU 1344  CG  ASP A 188    10481   8827  10494     76   -580  -2097       C  
ATOM   1345  OD1 ASP A 188      66.099 -29.012 -29.629  1.00 79.46           O  
ANISOU 1345  OD1 ASP A 188    10590   8924  10675    163   -484  -2250       O  
ATOM   1346  OD2 ASP A 188      63.975 -28.641 -30.054  1.00 79.03           O  
ANISOU 1346  OD2 ASP A 188    10640   8856  10528     -7   -720  -2033       O  
ATOM   1347  N   VAL A 189      67.631 -24.539 -29.027  1.00 76.24           N  
ANISOU 1347  N   VAL A 189    10080   8866  10022      0   -271  -2048       N  
ATOM   1348  CA  VAL A 189      67.883 -23.103 -29.129  1.00 76.12           C  
ANISOU 1348  CA  VAL A 189    10179   8892   9851   -126   -288  -1964       C  
ATOM   1349  C   VAL A 189      67.166 -22.579 -30.372  1.00 77.08           C  
ANISOU 1349  C   VAL A 189    10579   8950   9756   -296   -417  -1923       C  
ATOM   1350  O   VAL A 189      67.267 -23.170 -31.448  1.00 78.47           O  
ANISOU 1350  O   VAL A 189    10851   9148   9813   -415   -354  -2029       O  
ATOM   1351  CB  VAL A 189      69.392 -22.793 -29.221  1.00 77.18           C  
ANISOU 1351  CB  VAL A 189    10249   9194   9880   -245    -81  -2074       C  
ATOM   1352  CG1 VAL A 189      69.632 -21.288 -29.221  1.00 77.49           C  
ANISOU 1352  CG1 VAL A 189    10459   9247   9734   -426   -136  -1955       C  
ATOM   1353  CG2 VAL A 189      70.145 -23.449 -28.070  1.00 76.39           C  
ANISOU 1353  CG2 VAL A 189     9870   9151  10002    -51     20  -2142       C  
ATOM   1354  N   VAL A 190      66.443 -21.473 -30.216  1.00 76.46           N  
ANISOU 1354  N   VAL A 190    10646   8781   9621   -290   -619  -1784       N  
ATOM   1355  CA  VAL A 190      65.642 -20.901 -31.301  1.00 77.50           C  
ANISOU 1355  CA  VAL A 190    11073   8811   9560   -413   -820  -1732       C  
ATOM   1356  C   VAL A 190      65.853 -19.396 -31.400  1.00 78.25           C  
ANISOU 1356  C   VAL A 190    11441   8826   9463   -534   -970  -1633       C  
ATOM   1357  O   VAL A 190      66.401 -18.776 -30.487  1.00 77.50           O  
ANISOU 1357  O   VAL A 190    11281   8749   9414   -485   -939  -1591       O  
ATOM   1358  CB  VAL A 190      64.134 -21.195 -31.119  1.00 76.95           C  
ANISOU 1358  CB  VAL A 190    10944   8673   9619   -225  -1041  -1682       C  
ATOM   1359  CG1 VAL A 190      63.862 -22.683 -31.270  1.00 76.64           C  
ANISOU 1359  CG1 VAL A 190    10745   8676   9696   -198   -940  -1759       C  
ATOM   1360  CG2 VAL A 190      63.630 -20.695 -29.770  1.00 75.66           C  
ANISOU 1360  CG2 VAL A 190    10595   8523   9626     11  -1147  -1617       C  
ATOM   1361  N   GLU A 191      65.407 -18.821 -32.514  1.00 96.71           N  
ANISOU 1361  N   GLU A 191    13324  11777  11644    346  -1695   -764       N  
ATOM   1362  CA  GLU A 191      65.491 -17.381 -32.733  1.00 96.16           C  
ANISOU 1362  CA  GLU A 191    13103  11823  11609    292  -1545   -612       C  
ATOM   1363  C   GLU A 191      64.480 -16.678 -31.834  1.00 94.05           C  
ANISOU 1363  C   GLU A 191    12617  11515  11600    150  -1658   -474       C  
ATOM   1364  O   GLU A 191      63.271 -16.834 -32.011  1.00 94.31           O  
ANISOU 1364  O   GLU A 191    12700  11469  11662     52  -1887   -407       O  
ATOM   1365  CB  GLU A 191      65.207 -17.037 -34.201  1.00 98.57           C  
ANISOU 1365  CB  GLU A 191    13651  12170  11630    276  -1575   -547       C  
ATOM   1366  CG  GLU A 191      66.193 -17.628 -35.202  1.00101.22           C  
ANISOU 1366  CG  GLU A 191    14232  12567  11657    416  -1399   -699       C  
ATOM   1367  CD  GLU A 191      67.603 -17.084 -35.053  1.00101.44           C  
ANISOU 1367  CD  GLU A 191    14072  12725  11744    514  -1029   -719       C  
ATOM   1368  OE1 GLU A 191      67.755 -15.891 -34.718  1.00100.37           O  
ANISOU 1368  OE1 GLU A 191    13711  12652  11772    436   -913   -560       O  
ATOM   1369  OE2 GLU A 191      68.563 -17.850 -35.282  1.00103.16           O  
ANISOU 1369  OE2 GLU A 191    14355  12967  11873    669   -858   -900       O  
ATOM   1370  N   GLY A 192      64.976 -15.911 -30.867  1.00 92.26           N  
ANISOU 1370  N   GLY A 192    12140  11337  11575    140  -1495   -448       N  
ATOM   1371  CA  GLY A 192      64.112 -15.244 -29.898  1.00 90.67           C  
ANISOU 1371  CA  GLY A 192    11734  11098  11618     26  -1544   -364       C  
ATOM   1372  C   GLY A 192      64.780 -14.064 -29.224  1.00 89.67           C  
ANISOU 1372  C   GLY A 192    11385  11028  11654     15  -1342   -342       C  
ATOM   1373  O   GLY A 192      65.933 -13.738 -29.514  1.00 90.10           O  
ANISOU 1373  O   GLY A 192    11416  11157  11661     79  -1173   -369       O  
ATOM   1374  N   MET A 193      64.042 -13.428 -28.320  1.00 88.67           N  
ANISOU 1374  N   MET A 193    11091  10860  11737    -71  -1351   -304       N  
ATOM   1375  CA  MET A 193      64.514 -12.231 -27.638  1.00 88.14           C  
ANISOU 1375  CA  MET A 193    10834  10810  11844   -100  -1188   -305       C  
ATOM   1376  C   MET A 193      63.733 -11.998 -26.350  1.00 87.16           C  
ANISOU 1376  C   MET A 193    10575  10643  11898   -178  -1190   -345       C  
ATOM   1377  O   MET A 193      62.591 -12.442 -26.218  1.00 87.18           O  
ANISOU 1377  O   MET A 193    10583  10596  11944   -226  -1297   -312       O  
ATOM   1378  CB  MET A 193      64.316 -11.021 -28.559  1.00 89.38           C  
ANISOU 1378  CB  MET A 193    10962  10931  12063   -117  -1145   -165       C  
ATOM   1379  CG  MET A 193      65.392  -9.954 -28.458  1.00 89.93           C  
ANISOU 1379  CG  MET A 193    10916  11024  12228   -125   -953   -159       C  
ATOM   1380  SD  MET A 193      65.015  -8.493 -29.460  1.00 91.71           S  
ANISOU 1380  SD  MET A 193    11127  11155  12562   -166   -925     52       S  
ATOM   1381  CE  MET A 193      63.872  -7.568 -28.433  1.00 91.35           C  
ANISOU 1381  CE  MET A 193    10887  10958  12861   -215   -965     41       C  
ATOM   1382  N   GLN A 194      64.358 -11.292 -25.411  1.00 86.65           N  
ANISOU 1382  N   GLN A 194    10388  10598  11934   -203  -1062   -423       N  
ATOM   1383  CA  GLN A 194      63.705 -10.879 -24.171  1.00 86.34           C  
ANISOU 1383  CA  GLN A 194    10246  10528  12032   -277  -1009   -489       C  
ATOM   1384  C   GLN A 194      64.069  -9.427 -23.868  1.00 86.82           C  
ANISOU 1384  C   GLN A 194    10174  10542  12271   -302   -876   -526       C  
ATOM   1385  O   GLN A 194      65.204  -9.010 -24.098  1.00 87.15           O  
ANISOU 1385  O   GLN A 194    10194  10612  12307   -288   -824   -541       O  
ATOM   1386  CB  GLN A 194      64.129 -11.787 -23.010  1.00 85.85           C  
ANISOU 1386  CB  GLN A 194    10244  10530  11845   -301  -1031   -593       C  
ATOM   1387  CG  GLN A 194      63.537 -11.394 -21.663  1.00 85.99           C  
ANISOU 1387  CG  GLN A 194    10203  10543  11927   -390   -941   -677       C  
ATOM   1388  CD  GLN A 194      63.845 -12.394 -20.563  1.00 85.93           C  
ANISOU 1388  CD  GLN A 194    10309  10598  11739   -432   -992   -732       C  
ATOM   1389  OE1 GLN A 194      63.723 -13.604 -20.755  1.00 85.77           O  
ANISOU 1389  OE1 GLN A 194    10402  10578  11608   -419  -1111   -670       O  
ATOM   1390  NE2 GLN A 194      64.232 -11.891 -19.396  1.00 86.46           N  
ANISOU 1390  NE2 GLN A 194    10373  10705  11773   -490   -922   -846       N  
ATOM   1391  N   PHE A 195      63.104  -8.665 -23.355  1.00 87.36           N  
ANISOU 1391  N   PHE A 195    10140  10525  12527   -339   -812   -549       N  
ATOM   1392  CA  PHE A 195      63.337  -7.268 -22.969  1.00 88.23           C  
ANISOU 1392  CA  PHE A 195    10140  10542  12840   -362   -690   -615       C  
ATOM   1393  C   PHE A 195      62.522  -6.880 -21.733  1.00 89.07           C  
ANISOU 1393  C   PHE A 195    10177  10602  13062   -403   -578   -760       C  
ATOM   1394  O   PHE A 195      61.459  -7.446 -21.474  1.00 89.20           O  
ANISOU 1394  O   PHE A 195    10173  10632  13084   -410   -575   -745       O  
ATOM   1395  CB  PHE A 195      63.046  -6.317 -24.137  1.00 89.05           C  
ANISOU 1395  CB  PHE A 195    10188  10521  13122   -327   -705   -454       C  
ATOM   1396  CG  PHE A 195      61.680  -6.484 -24.744  1.00 89.49           C  
ANISOU 1396  CG  PHE A 195    10212  10514  13275   -291   -804   -325       C  
ATOM   1397  CD1 PHE A 195      61.456  -7.432 -25.735  1.00 89.18           C  
ANISOU 1397  CD1 PHE A 195    10286  10539  13058   -269   -963   -196       C  
ATOM   1398  CD2 PHE A 195      60.623  -5.679 -24.344  1.00 90.68           C  
ANISOU 1398  CD2 PHE A 195    10208  10528  13716   -276   -751   -345       C  
ATOM   1399  CE1 PHE A 195      60.200  -7.582 -26.303  1.00 90.05           C  
ANISOU 1399  CE1 PHE A 195    10353  10587  13276   -254  -1107    -75       C  
ATOM   1400  CE2 PHE A 195      59.365  -5.824 -24.909  1.00 91.59           C  
ANISOU 1400  CE2 PHE A 195    10241  10583  13976   -241   -870   -215       C  
ATOM   1401  CZ  PHE A 195      59.153  -6.777 -25.889  1.00 91.24           C  
ANISOU 1401  CZ  PHE A 195    10306  10610  13750   -241  -1069    -72       C  
ATOM   1402  N   ASP A 196      63.033  -5.907 -20.980  1.00 90.06           N  
ANISOU 1402  N   ASP A 196    10265  10669  13282   -440   -474   -909       N  
ATOM   1403  CA  ASP A 196      62.487  -5.561 -19.663  1.00 91.21           C  
ANISOU 1403  CA  ASP A 196    10399  10793  13463   -483   -334  -1106       C  
ATOM   1404  C   ASP A 196      61.279  -4.629 -19.754  1.00 92.61           C  
ANISOU 1404  C   ASP A 196    10430  10803  13955   -431   -214  -1116       C  
ATOM   1405  O   ASP A 196      61.354  -3.459 -19.377  1.00 93.94           O  
ANISOU 1405  O   ASP A 196    10548  10825  14320   -428   -109  -1248       O  
ATOM   1406  CB  ASP A 196      63.577  -4.925 -18.790  1.00 92.07           C  
ANISOU 1406  CB  ASP A 196    10560  10898  13524   -552   -304  -1296       C  
ATOM   1407  CG  ASP A 196      64.779  -5.838 -18.587  1.00 91.24           C  
ANISOU 1407  CG  ASP A 196    10555  10951  13158   -589   -444  -1291       C  
ATOM   1408  OD1 ASP A 196      64.609  -7.077 -18.597  1.00 90.34           O  
ANISOU 1408  OD1 ASP A 196    10521  10957  12846   -573   -519  -1210       O  
ATOM   1409  OD2 ASP A 196      65.898  -5.312 -18.413  1.00 91.93           O  
ANISOU 1409  OD2 ASP A 196    10628  11028  13274   -635   -491  -1365       O  
ATOM   1410  N   ARG A 197      60.168  -5.166 -20.252  1.00 92.64           N  
ANISOU 1410  N   ARG A 197    10355  10811  14033   -390   -247   -981       N  
ATOM   1411  CA  ARG A 197      58.905  -4.432 -20.348  1.00 94.41           C  
ANISOU 1411  CA  ARG A 197    10388  10883  14601   -321   -155   -971       C  
ATOM   1412  C   ARG A 197      57.748  -5.396 -20.105  1.00 94.84           C  
ANISOU 1412  C   ARG A 197    10362  11025  14646   -339   -128   -927       C  
ATOM   1413  O   ARG A 197      57.472  -6.253 -20.941  1.00 93.78           O  
ANISOU 1413  O   ARG A 197    10237  10945  14449   -345   -314   -742       O  
ATOM   1414  CB  ARG A 197      58.749  -3.794 -21.731  1.00 94.62           C  
ANISOU 1414  CB  ARG A 197    10334  10760  14857   -243   -313   -754       C  
ATOM   1415  CG  ARG A 197      59.715  -2.662 -22.045  1.00 95.00           C  
ANISOU 1415  CG  ARG A 197    10422  10672  15001   -239   -311   -758       C  
ATOM   1416  CD  ARG A 197      59.458  -1.433 -21.186  1.00 97.15           C  
ANISOU 1416  CD  ARG A 197    10601  10750  15559   -211   -128   -967       C  
ATOM   1417  NE  ARG A 197      60.073  -0.233 -21.755  1.00 98.17           N  
ANISOU 1417  NE  ARG A 197    10730  10669  15901   -202   -167   -902       N  
ATOM   1418  CZ  ARG A 197      59.987   0.988 -21.230  1.00100.35           C  
ANISOU 1418  CZ  ARG A 197    10946  10707  16473   -175    -47  -1064       C  
ATOM   1419  NH1 ARG A 197      59.307   1.200 -20.107  1.00101.87           N  
ANISOU 1419  NH1 ARG A 197    11080  10858  16766   -138    147  -1330       N  
ATOM   1420  NH2 ARG A 197      60.589   2.007 -21.835  1.00101.43           N  
ANISOU 1420  NH2 ARG A 197    11095  10634  16806   -191   -106   -962       N  
ATOM   1421  N   GLY A 198      57.078  -5.257 -18.964  1.00 96.75           N  
ANISOU 1421  N   GLY A 198    10533  11279  14946   -361    113  -1103       N  
ATOM   1422  CA  GLY A 198      55.971  -6.143 -18.601  1.00 97.87           C  
ANISOU 1422  CA  GLY A 198    10573  11511  15102   -408    194  -1061       C  
ATOM   1423  C   GLY A 198      54.640  -5.738 -19.211  1.00 99.97           C  
ANISOU 1423  C   GLY A 198    10533  11646  15804   -322    192   -954       C  
ATOM   1424  O   GLY A 198      54.568  -4.805 -20.015  1.00100.54           O  
ANISOU 1424  O   GLY A 198    10496  11548  16154   -212     85   -882       O  
ATOM   1425  N   TYR A 199      53.587  -6.455 -18.826  1.00101.53           N  
ANISOU 1425  N   TYR A 199    10581  11916  16079   -380    296   -924       N  
ATOM   1426  CA  TYR A 199      52.225  -6.165 -19.295  1.00104.10           C  
ANISOU 1426  CA  TYR A 199    10550  12131  16870   -306    292   -824       C  
ATOM   1427  C   TYR A 199      51.741  -4.802 -18.799  1.00107.09           C  
ANISOU 1427  C   TYR A 199    10717  12346  17623   -167    559  -1005       C  
ATOM   1428  O   TYR A 199      52.139  -4.350 -17.726  1.00107.77           O  
ANISOU 1428  O   TYR A 199    10922  12455  17570   -176    848  -1256       O  
ATOM   1429  CB  TYR A 199      51.237  -7.269 -18.873  1.00105.35           C  
ANISOU 1429  CB  TYR A 199    10567  12410  17048   -431    382   -761       C  
ATOM   1430  CG  TYR A 199      51.264  -7.633 -17.398  1.00106.31           C  
ANISOU 1430  CG  TYR A 199    10797  12679  16917   -543    756   -946       C  
ATOM   1431  CD1 TYR A 199      50.672  -6.811 -16.441  1.00109.29           C  
ANISOU 1431  CD1 TYR A 199    11007  13026  17492   -486   1160  -1162       C  
ATOM   1432  CD2 TYR A 199      51.868  -8.813 -16.963  1.00104.72           C  
ANISOU 1432  CD2 TYR A 199    10882  12635  16269   -703    707   -903       C  
ATOM   1433  CE1 TYR A 199      50.695  -7.146 -15.096  1.00110.69           C  
ANISOU 1433  CE1 TYR A 199    11331  13355  17370   -602   1514  -1329       C  
ATOM   1434  CE2 TYR A 199      51.895  -9.155 -15.622  1.00106.04           C  
ANISOU 1434  CE2 TYR A 199    11189  12938  16162   -819   1022  -1037       C  
ATOM   1435  CZ  TYR A 199      51.307  -8.319 -14.693  1.00109.05           C  
ANISOU 1435  CZ  TYR A 199    11430  13314  16689   -778   1431  -1249       C  
ATOM   1436  OH  TYR A 199      51.329  -8.659 -13.361  1.00110.82           O  
ANISOU 1436  OH  TYR A 199    11838  13689  16577   -907   1758  -1381       O  
ATOM   1437  N   LEU A 200      50.882  -4.159 -19.589  1.00109.33           N  
ANISOU 1437  N   LEU A 200    10702  12453  18386    -36    439   -884       N  
ATOM   1438  CA  LEU A 200      50.349  -2.835 -19.250  1.00112.66           C  
ANISOU 1438  CA  LEU A 200    10888  12663  19253    134    661  -1041       C  
ATOM   1439  C   LEU A 200      49.108  -2.889 -18.351  1.00116.61           C  
ANISOU 1439  C   LEU A 200    11061  13192  20052    159   1030  -1182       C  
ATOM   1440  O   LEU A 200      48.689  -1.860 -17.817  1.00119.73           O  
ANISOU 1440  O   LEU A 200    11280  13427  20781    306   1309  -1389       O  
ATOM   1441  CB  LEU A 200      50.040  -2.036 -20.524  1.00113.50           C  
ANISOU 1441  CB  LEU A 200    10824  12531  19768    285    338   -822       C  
ATOM   1442  CG  LEU A 200      51.249  -1.392 -21.208  1.00111.40           C  
ANISOU 1442  CG  LEU A 200    10845  12158  19323    303    125   -752       C  
ATOM   1443  CD1 LEU A 200      50.909  -0.982 -22.632  1.00112.20           C  
ANISOU 1443  CD1 LEU A 200    10842  12087  19703    397   -261   -441       C  
ATOM   1444  CD2 LEU A 200      51.751  -0.192 -20.417  1.00112.65           C  
ANISOU 1444  CD2 LEU A 200    11069  12147  19586    381    393  -1023       C  
ATOM   1445  N   SER A 201      48.522  -4.076 -18.188  1.00117.01           N  
ANISOU 1445  N   SER A 201    11025  13431  20002     15   1048  -1078       N  
ATOM   1446  CA  SER A 201      47.382  -4.259 -17.288  1.00120.97           C  
ANISOU 1446  CA  SER A 201    11214  13998  20749     -2   1448  -1193       C  
ATOM   1447  C   SER A 201      47.316  -5.699 -16.762  1.00120.30           C  
ANISOU 1447  C   SER A 201    11256  14167  20284   -245   1525  -1119       C  
ATOM   1448  O   SER A 201      47.498  -6.643 -17.532  1.00118.12           O  
ANISOU 1448  O   SER A 201    11078  13949  19850   -359   1158   -885       O  
ATOM   1449  CB  SER A 201      46.076  -3.899 -18.002  1.00124.31           C  
ANISOU 1449  CB  SER A 201    11117  14263  21852    135   1337  -1044       C  
ATOM   1450  OG  SER A 201      44.957  -4.086 -17.152  1.00128.32           O  
ANISOU 1450  OG  SER A 201    11265  14843  22645    116   1758  -1151       O  
ATOM   1451  N   PRO A 202      47.054  -5.873 -15.449  1.00122.67           N  
ANISOU 1451  N   PRO A 202    11580  14605  20423   -330   2005  -1319       N  
ATOM   1452  CA  PRO A 202      46.937  -7.211 -14.850  1.00122.63           C  
ANISOU 1452  CA  PRO A 202    11704  14822  20067   -577   2113  -1226       C  
ATOM   1453  C   PRO A 202      45.889  -8.140 -15.480  1.00123.99           C  
ANISOU 1453  C   PRO A 202    11536  15013  20560   -689   1938   -955       C  
ATOM   1454  O   PRO A 202      46.038  -9.360 -15.396  1.00122.85           O  
ANISOU 1454  O   PRO A 202    11571  14994  20110   -902   1827   -802       O  
ATOM   1455  CB  PRO A 202      46.552  -6.912 -13.398  1.00126.30           C  
ANISOU 1455  CB  PRO A 202    12159  15393  20435   -607   2722  -1494       C  
ATOM   1456  CG  PRO A 202      47.116  -5.566 -13.128  1.00126.55           C  
ANISOU 1456  CG  PRO A 202    12308  15287  20487   -410   2847  -1780       C  
ATOM   1457  CD  PRO A 202      47.016  -4.813 -14.422  1.00125.49           C  
ANISOU 1457  CD  PRO A 202    11934  14911  20836   -210   2468  -1657       C  
ATOM   1458  N   TYR A 203      44.851  -7.579 -16.102  1.00126.85           N  
ANISOU 1458  N   TYR A 203    11411  15232  21551   -551   1883   -890       N  
ATOM   1459  CA  TYR A 203      43.745  -8.385 -16.640  1.00129.06           C  
ANISOU 1459  CA  TYR A 203    11305  15521  22210   -668   1716   -649       C  
ATOM   1460  C   TYR A 203      44.043  -9.106 -17.968  1.00126.15           C  
ANISOU 1460  C   TYR A 203    11064  15099  21768   -738   1076   -381       C  
ATOM   1461  O   TYR A 203      43.158  -9.762 -18.521  1.00127.91           O  
ANISOU 1461  O   TYR A 203    10986  15303  22308   -845    854   -184       O  
ATOM   1462  CB  TYR A 203      42.475  -7.535 -16.775  1.00133.82           C  
ANISOU 1462  CB  TYR A 203    11292  15990  23562   -490   1878   -678       C  
ATOM   1463  CG  TYR A 203      41.969  -6.992 -15.457  1.00137.89           C  
ANISOU 1463  CG  TYR A 203    11624  16571  24197   -437   2571   -952       C  
ATOM   1464  CD1 TYR A 203      41.338  -7.830 -14.544  1.00140.73           C  
ANISOU 1464  CD1 TYR A 203    11862  17122  24486   -656   2987   -946       C  
ATOM   1465  CD2 TYR A 203      42.117  -5.646 -15.118  1.00139.34           C  
ANISOU 1465  CD2 TYR A 203    11774  16614  24553   -176   2826  -1221       C  
ATOM   1466  CE1 TYR A 203      40.869  -7.352 -13.332  1.00144.93           C  
ANISOU 1466  CE1 TYR A 203    12255  17736  25075   -615   3668  -1207       C  
ATOM   1467  CE2 TYR A 203      41.649  -5.158 -13.907  1.00143.52           C  
ANISOU 1467  CE2 TYR A 203    12168  17200  25162   -120   3486  -1512       C  
ATOM   1468  CZ  TYR A 203      41.026  -6.015 -13.019  1.00146.34           C  
ANISOU 1468  CZ  TYR A 203    12416  17779  25406   -338   3919  -1508       C  
ATOM   1469  OH  TYR A 203      40.561  -5.536 -11.816  1.00150.93           O  
ANISOU 1469  OH  TYR A 203    12888  18436  26019   -287   4617  -1807       O  
ATOM   1470  N   PHE A 204      45.270  -8.988 -18.480  1.00122.09           N  
ANISOU 1470  N   PHE A 204    10986  14558  20843   -685    789   -385       N  
ATOM   1471  CA  PHE A 204      45.714  -9.812 -19.609  1.00119.29           C  
ANISOU 1471  CA  PHE A 204    10855  14187  20282   -770    255   -175       C  
ATOM   1472  C   PHE A 204      46.197 -11.192 -19.152  1.00117.57           C  
ANISOU 1472  C   PHE A 204    10966  14113  19592  -1005    257   -130       C  
ATOM   1473  O   PHE A 204      46.352 -12.097 -19.974  1.00116.13           O  
ANISOU 1473  O   PHE A 204    10929  13911  19281  -1105   -139     29       O  
ATOM   1474  CB  PHE A 204      46.842  -9.125 -20.385  1.00116.08           C  
ANISOU 1474  CB  PHE A 204    10763  13697  19645   -616    -14   -189       C  
ATOM   1475  CG  PHE A 204      46.459  -7.796 -20.976  1.00117.71           C  
ANISOU 1475  CG  PHE A 204    10706  13720  20298   -391    -94   -182       C  
ATOM   1476  CD1 PHE A 204      45.377  -7.690 -21.839  1.00120.43           C  
ANISOU 1476  CD1 PHE A 204    10668  13949  21138   -344   -382      1       C  
ATOM   1477  CD2 PHE A 204      47.197  -6.654 -20.688  1.00116.83           C  
ANISOU 1477  CD2 PHE A 204    10735  13528  20126   -234     77   -347       C  
ATOM   1478  CE1 PHE A 204      45.027  -6.468 -22.390  1.00122.37           C  
ANISOU 1478  CE1 PHE A 204    10681  14000  21814   -126   -493     37       C  
ATOM   1479  CE2 PHE A 204      46.854  -5.431 -21.237  1.00118.71           C  
ANISOU 1479  CE2 PHE A 204    10749  13556  20798    -28    -12   -321       C  
ATOM   1480  CZ  PHE A 204      45.767  -5.338 -22.089  1.00121.52           C  
ANISOU 1480  CZ  PHE A 204    10730  13795  21647     34   -299   -119       C  
ATOM   1481  N   ILE A 205      46.434 -11.348 -17.848  1.00118.10           N  
ANISOU 1481  N   ILE A 205    11170  14307  19392  -1089    691   -272       N  
ATOM   1482  CA  ILE A 205      46.984 -12.588 -17.293  1.00116.80           C  
ANISOU 1482  CA  ILE A 205    11357  14261  18758  -1299    700   -219       C  
ATOM   1483  C   ILE A 205      45.991 -13.741 -17.447  1.00119.25           C  
ANISOU 1483  C   ILE A 205    11457  14573  19279  -1521    606    -17       C  
ATOM   1484  O   ILE A 205      44.855 -13.658 -16.977  1.00123.12           O  
ANISOU 1484  O   ILE A 205    11549  15087  20144  -1591    897      0       O  
ATOM   1485  CB  ILE A 205      47.363 -12.427 -15.799  1.00117.52           C  
ANISOU 1485  CB  ILE A 205    11648  14492  18512  -1351   1186   -400       C  
ATOM   1486  CG1 ILE A 205      48.478 -11.389 -15.634  1.00115.21           C  
ANISOU 1486  CG1 ILE A 205    11611  14184  17977  -1168   1219   -608       C  
ATOM   1487  CG2 ILE A 205      47.826 -13.754 -15.203  1.00116.84           C  
ANISOU 1487  CG2 ILE A 205    11910  14509  17973  -1578   1170   -295       C  
ATOM   1488  CD1 ILE A 205      48.688 -10.938 -14.204  1.00116.92           C  
ANISOU 1488  CD1 ILE A 205    11976  14516  17933  -1190   1693   -835       C  
ATOM   1489  N   ASN A 206      46.432 -14.805 -18.116  1.00117.46           N  
ANISOU 1489  N   ASN A 206    11489  14306  18832  -1631    205    124       N  
ATOM   1490  CA  ASN A 206      45.643 -16.034 -18.267  1.00119.66           C  
ANISOU 1490  CA  ASN A 206    11649  14554  19263  -1877     60    313       C  
ATOM   1491  C   ASN A 206      46.276 -17.242 -17.562  1.00118.99           C  
ANISOU 1491  C   ASN A 206    11969  14520  18722  -2073    104    371       C  
ATOM   1492  O   ASN A 206      45.766 -18.360 -17.659  1.00120.63           O  
ANISOU 1492  O   ASN A 206    12152  14670  19010  -2297    -36    535       O  
ATOM   1493  CB  ASN A 206      45.401 -16.340 -19.753  1.00119.12           C  
ANISOU 1493  CB  ASN A 206    11511  14344  19403  -1860   -502    438       C  
ATOM   1494  CG  ASN A 206      46.680 -16.348 -20.573  1.00115.13           C  
ANISOU 1494  CG  ASN A 206    11447  13798  18497  -1719   -843    392       C  
ATOM   1495  OD1 ASN A 206      47.785 -16.331 -20.031  1.00112.62           O  
ANISOU 1495  OD1 ASN A 206    11479  13548  17761  -1661   -702    290       O  
ATOM   1496  ND2 ASN A 206      46.533 -16.365 -21.890  1.00115.00           N  
ANISOU 1496  ND2 ASN A 206    11409  13676  18609  -1666  -1294    468       N  
ATOM   1497  N   LYS A 207      47.384 -17.008 -16.858  1.00117.01           N  
ANISOU 1497  N   LYS A 207    12086  14355  18016  -1994    270    246       N  
ATOM   1498  CA  LYS A 207      48.044 -18.031 -16.049  1.00116.82           C  
ANISOU 1498  CA  LYS A 207    12455  14379  17551  -2153    322    306       C  
ATOM   1499  C   LYS A 207      48.285 -17.454 -14.651  1.00117.97           C  
ANISOU 1499  C   LYS A 207    12706  14685  17432  -2154    808    172       C  
ATOM   1500  O   LYS A 207      49.385 -16.984 -14.353  1.00115.78           O  
ANISOU 1500  O   LYS A 207    12722  14458  16810  -2020    805     33       O  
ATOM   1501  CB  LYS A 207      49.371 -18.450 -16.689  1.00113.17           C  
ANISOU 1501  CB  LYS A 207    12405  13851  16743  -2044    -69    290       C  
ATOM   1502  CG  LYS A 207      49.237 -19.150 -18.033  1.00112.40           C  
ANISOU 1502  CG  LYS A 207    12305  13596  16803  -2054   -542    394       C  
ATOM   1503  CD  LYS A 207      48.751 -20.583 -17.879  1.00114.43           C  
ANISOU 1503  CD  LYS A 207    12635  13759  17082  -2314   -660    573       C  
ATOM   1504  CE  LYS A 207      48.708 -21.299 -19.220  1.00113.87           C  
ANISOU 1504  CE  LYS A 207    12627  13513  17122  -2322  -1157    630       C  
ATOM   1505  NZ  LYS A 207      48.262 -22.713 -19.085  1.00116.11           N  
ANISOU 1505  NZ  LYS A 207    13003  13660  17453  -2586  -1301    793       N  
ATOM   1506  N   PRO A 208      47.253 -17.490 -13.784  1.00121.85           N  
ANISOU 1506  N   PRO A 208    12956  15260  18080  -2315   1231    208       N  
ATOM   1507  CA  PRO A 208      47.346 -16.851 -12.466  1.00123.62           C  
ANISOU 1507  CA  PRO A 208    13275  15647  18048  -2314   1739     48       C  
ATOM   1508  C   PRO A 208      48.300 -17.526 -11.469  1.00123.11           C  
ANISOU 1508  C   PRO A 208    13733  15673  17368  -2437   1783     82       C  
ATOM   1509  O   PRO A 208      48.614 -16.930 -10.438  1.00124.10           O  
ANISOU 1509  O   PRO A 208    14033  15934  17185  -2416   2121    -81       O  
ATOM   1510  CB  PRO A 208      45.903 -16.903 -11.949  1.00128.57           C  
ANISOU 1510  CB  PRO A 208    13479  16333  19037  -2477   2172    112       C  
ATOM   1511  CG  PRO A 208      45.293 -18.069 -12.641  1.00129.32           C  
ANISOU 1511  CG  PRO A 208    13425  16314  19396  -2678   1867    381       C  
ATOM   1512  CD  PRO A 208      45.945 -18.141 -13.991  1.00125.21           C  
ANISOU 1512  CD  PRO A 208    13005  15637  18931  -2519   1268    394       C  
ATOM   1513  N   GLU A 209      48.750 -18.746 -11.767  1.00121.82           N  
ANISOU 1513  N   GLU A 209    13828  15423  17034  -2560   1427    286       N  
ATOM   1514  CA  GLU A 209      49.719 -19.439 -10.914  1.00121.59           C  
ANISOU 1514  CA  GLU A 209    14296  15444  16455  -2653   1380    353       C  
ATOM   1515  C   GLU A 209      51.062 -18.714 -10.956  1.00118.10           C  
ANISOU 1515  C   GLU A 209    14118  15032  15722  -2420   1202    151       C  
ATOM   1516  O   GLU A 209      51.576 -18.283  -9.924  1.00119.01           O  
ANISOU 1516  O   GLU A 209    14474  15279  15464  -2421   1417     31       O  
ATOM   1517  CB  GLU A 209      49.897 -20.903 -11.342  1.00121.30           C  
ANISOU 1517  CB  GLU A 209    14450  15252  16384  -2803    999    611       C  
ATOM   1518  CG  GLU A 209      48.726 -21.818 -10.996  1.00125.47           C  
ANISOU 1518  CG  GLU A 209    14821  15749  17102  -3111   1185    853       C  
ATOM   1519  CD  GLU A 209      47.617 -21.819 -12.038  1.00126.21           C  
ANISOU 1519  CD  GLU A 209    14433  15732  17788  -3140   1081    899       C  
ATOM   1520  OE1 GLU A 209      47.565 -20.892 -12.876  1.00124.20           O  
ANISOU 1520  OE1 GLU A 209    13925  15464  17800  -2916    973    731       O  
ATOM   1521  OE2 GLU A 209      46.789 -22.754 -12.013  1.00129.12           O  
ANISOU 1521  OE2 GLU A 209    14677  16017  18365  -3403   1088   1120       O  
ATOM   1522  N   THR A 210      51.621 -18.586 -12.158  1.00114.40           N  
ANISOU 1522  N   THR A 210    13605  14442  15419  -2236    808    115       N  
ATOM   1523  CA  THR A 210      52.845 -17.812 -12.369  1.00111.18           C  
ANISOU 1523  CA  THR A 210    13362  14050  14831  -2017    646    -68       C  
ATOM   1524  C   THR A 210      52.560 -16.307 -12.348  1.00111.09           C  
ANISOU 1524  C   THR A 210    13103  14089  15015  -1868    908   -301       C  
ATOM   1525  O   THR A 210      53.440 -15.512 -12.022  1.00109.86           O  
ANISOU 1525  O   THR A 210    13099  13979  14662  -1749    924   -483       O  
ATOM   1526  CB  THR A 210      53.525 -18.174 -13.707  1.00107.90           C  
ANISOU 1526  CB  THR A 210    12980  13493  14523  -1876    186    -23       C  
ATOM   1527  OG1 THR A 210      52.551 -18.187 -14.758  1.00107.81           O  
ANISOU 1527  OG1 THR A 210    12649  13383  14930  -1873     92     43       O  
ATOM   1528  CG2 THR A 210      54.193 -19.543 -13.624  1.00107.63           C  
ANISOU 1528  CG2 THR A 210    13269  13386  14238  -1958    -92    140       C  
ATOM   1529  N   GLY A 211      51.332 -15.925 -12.698  1.00112.60           N  
ANISOU 1529  N   GLY A 211    12903  14250  15630  -1875   1091   -293       N  
ATOM   1530  CA  GLY A 211      50.939 -14.517 -12.753  1.00113.06           C  
ANISOU 1530  CA  GLY A 211    12686  14306  15962  -1713   1327   -501       C  
ATOM   1531  C   GLY A 211      51.519 -13.840 -13.977  1.00109.60           C  
ANISOU 1531  C   GLY A 211    12181  13749  15712  -1500    992   -549       C  
ATOM   1532  O   GLY A 211      52.102 -12.758 -13.882  1.00108.76           O  
ANISOU 1532  O   GLY A 211    12113  13633  15577  -1352   1054   -738       O  
ATOM   1533  N   ALA A 212      51.352 -14.485 -15.130  1.00107.83           N  
ANISOU 1533  N   ALA A 212    11875  13425  15670  -1500    639   -375       N  
ATOM   1534  CA  ALA A 212      51.951 -14.024 -16.377  1.00104.87           C  
ANISOU 1534  CA  ALA A 212    11497  12949  15397  -1326    302   -380       C  
ATOM   1535  C   ALA A 212      51.037 -14.298 -17.567  1.00105.20           C  
ANISOU 1535  C   ALA A 212    11272  12882  15814  -1328     53   -225       C  
ATOM   1536  O   ALA A 212      50.207 -15.207 -17.529  1.00106.94           O  
ANISOU 1536  O   ALA A 212    11384  13091  16155  -1492     29    -88       O  
ATOM   1537  CB  ALA A 212      53.298 -14.702 -16.581  1.00102.15           C  
ANISOU 1537  CB  ALA A 212    11526  12613  14671  -1310     29   -355       C  
ATOM   1538  N   VAL A 213      51.207 -13.508 -18.625  1.00103.88           N  
ANISOU 1538  N   VAL A 213    11014  12628  15825  -1162   -152   -236       N  
ATOM   1539  CA  VAL A 213      50.436 -13.675 -19.855  1.00104.41           C  
ANISOU 1539  CA  VAL A 213    10873  12590  16205  -1152   -460    -89       C  
ATOM   1540  C   VAL A 213      51.160 -14.677 -20.744  1.00102.34           C  
ANISOU 1540  C   VAL A 213    10914  12295  15675  -1180   -840      0       C  
ATOM   1541  O   VAL A 213      52.378 -14.605 -20.902  1.00 99.95           O  
ANISOU 1541  O   VAL A 213    10894  12016  15065  -1090   -907    -66       O  
ATOM   1542  CB  VAL A 213      50.277 -12.348 -20.629  1.00104.49           C  
ANISOU 1542  CB  VAL A 213    10683  12510  16507   -961   -531   -112       C  
ATOM   1543  CG1 VAL A 213      49.308 -12.523 -21.791  1.00106.03           C  
ANISOU 1543  CG1 VAL A 213    10641  12603  17040   -970   -867     58       C  
ATOM   1544  CG2 VAL A 213      49.802 -11.231 -19.709  1.00106.42           C  
ANISOU 1544  CG2 VAL A 213    10682  12757  16996   -883   -132   -259       C  
ATOM   1545  N   GLU A 214      50.404 -15.606 -21.324  1.00103.69           N  
ANISOU 1545  N   GLU A 214    11012  12401  15983  -1306  -1082    134       N  
ATOM   1546  CA  GLU A 214      50.968 -16.661 -22.161  1.00102.44           C  
ANISOU 1546  CA  GLU A 214    11152  12184  15587  -1340  -1437    190       C  
ATOM   1547  C   GLU A 214      50.101 -16.862 -23.402  1.00103.87           C  
ANISOU 1547  C   GLU A 214    11185  12257  16021  -1374  -1804    303       C  
ATOM   1548  O   GLU A 214      48.967 -17.336 -23.304  1.00106.44           O  
ANISOU 1548  O   GLU A 214    11261  12538  16642  -1533  -1853    398       O  
ATOM   1549  CB  GLU A 214      51.070 -17.961 -21.359  1.00103.02           C  
ANISOU 1549  CB  GLU A 214    11407  12259  15473  -1518  -1385    228       C  
ATOM   1550  CG  GLU A 214      51.855 -19.067 -22.049  1.00101.91           C  
ANISOU 1550  CG  GLU A 214    11622  12034  15063  -1520  -1705    241       C  
ATOM   1551  CD  GLU A 214      51.978 -20.320 -21.199  1.00102.77           C  
ANISOU 1551  CD  GLU A 214    11921  12106  15018  -1686  -1665    299       C  
ATOM   1552  OE1 GLU A 214      52.097 -20.200 -19.959  1.00103.08           O  
ANISOU 1552  OE1 GLU A 214    11966  12240  14959  -1742  -1358    294       O  
ATOM   1553  OE2 GLU A 214      51.967 -21.429 -21.777  1.00103.52           O  
ANISOU 1553  OE2 GLU A 214    12190  12065  15078  -1765  -1952    349       O  
ATOM   1554  N   LEU A 215      50.642 -16.496 -24.563  1.00102.57           N  
ANISOU 1554  N   LEU A 215    11178  12059  15736  -1238  -2064    299       N  
ATOM   1555  CA  LEU A 215      49.912 -16.573 -25.827  1.00104.45           C  
ANISOU 1555  CA  LEU A 215    11336  12204  16147  -1258  -2460    403       C  
ATOM   1556  C   LEU A 215      50.600 -17.545 -26.780  1.00103.78           C  
ANISOU 1556  C   LEU A 215    11652  12067  15712  -1269  -2781    381       C  
ATOM   1557  O   LEU A 215      51.812 -17.469 -26.978  1.00101.55           O  
ANISOU 1557  O   LEU A 215    11667  11830  15087  -1144  -2723    294       O  
ATOM   1558  CB  LEU A 215      49.827 -15.188 -26.475  1.00104.71           C  
ANISOU 1558  CB  LEU A 215    11220  12227  16335  -1088  -2502    439       C  
ATOM   1559  CG  LEU A 215      49.467 -14.007 -25.567  1.00105.23           C  
ANISOU 1559  CG  LEU A 215    10955  12321  16703  -1004  -2141    403       C  
ATOM   1560  CD1 LEU A 215      49.591 -12.697 -26.330  1.00105.36           C  
ANISOU 1560  CD1 LEU A 215    10912  12283  16836   -825  -2233    450       C  
ATOM   1561  CD2 LEU A 215      48.067 -14.161 -24.990  1.00108.37           C  
ANISOU 1561  CD2 LEU A 215    10924  12694  17554  -1124  -2051    461       C  
ATOM   1562  N   GLU A 216      49.819 -18.449 -27.373  1.00106.16           N  
ANISOU 1562  N   GLU A 216    11949  12266  16120  -1421  -3114    446       N  
ATOM   1563  CA  GLU A 216      50.344 -19.472 -28.280  1.00106.35           C  
ANISOU 1563  CA  GLU A 216    12369  12210  15829  -1444  -3430    391       C  
ATOM   1564  C   GLU A 216      50.101 -19.101 -29.742  1.00107.81           C  
ANISOU 1564  C   GLU A 216    12643  12357  15962  -1390  -3815    434       C  
ATOM   1565  O   GLU A 216      48.981 -18.766 -30.124  1.00110.27           O  
ANISOU 1565  O   GLU A 216    12672  12624  16602  -1465  -4042    552       O  
ATOM   1566  CB  GLU A 216      49.705 -20.829 -27.974  1.00108.42           C  
ANISOU 1566  CB  GLU A 216    12638  12348  16206  -1674  -3579    416       C  
ATOM   1567  CG  GLU A 216      50.046 -21.370 -26.594  1.00107.43           C  
ANISOU 1567  CG  GLU A 216    12526  12247  16044  -1745  -3237    401       C  
ATOM   1568  CD  GLU A 216      49.463 -22.747 -26.333  1.00109.79           C  
ANISOU 1568  CD  GLU A 216    12869  12391  16453  -1989  -3394    455       C  
ATOM   1569  OE1 GLU A 216      48.392 -23.068 -26.894  1.00112.69           O  
ANISOU 1569  OE1 GLU A 216    13058  12657  17100  -2154  -3687    532       O  
ATOM   1570  OE2 GLU A 216      50.077 -23.511 -25.560  1.00109.12           O  
ANISOU 1570  OE2 GLU A 216    12994  12272  16193  -2026  -3245    434       O  
ATOM   1571  N   SER A 217      51.159 -19.186 -30.548  1.00106.72           N  
ANISOU 1571  N   SER A 217    12900  12239  15407  -1262  -3886    343       N  
ATOM   1572  CA  SER A 217      51.138 -18.799 -31.963  1.00108.29           C  
ANISOU 1572  CA  SER A 217    13284  12429  15429  -1201  -4209    381       C  
ATOM   1573  C   SER A 217      50.497 -17.426 -32.196  1.00109.45           C  
ANISOU 1573  C   SER A 217    13122  12612  15853  -1138  -4241    543       C  
ATOM   1574  O   SER A 217      49.544 -17.308 -32.967  1.00112.35           O  
ANISOU 1574  O   SER A 217    13384  12913  16390  -1208  -4623    661       O  
ATOM   1575  CB  SER A 217      50.426 -19.870 -32.795  1.00111.24           C  
ANISOU 1575  CB  SER A 217    13816  12670  15777  -1364  -4674    368       C  
ATOM   1576  OG  SER A 217      51.094 -21.114 -32.696  1.00110.54           O  
ANISOU 1576  OG  SER A 217    14061  12509  15428  -1394  -4661    205       O  
ATOM   1577  N   PRO A 218      51.027 -16.379 -31.534  1.00107.63           N  
ANISOU 1577  N   PRO A 218    12747  12464  15684  -1004  -3869    549       N  
ATOM   1578  CA  PRO A 218      50.427 -15.055 -31.625  1.00108.92           C  
ANISOU 1578  CA  PRO A 218    12599  12616  16166   -927  -3868    692       C  
ATOM   1579  C   PRO A 218      50.968 -14.221 -32.782  1.00109.68           C  
ANISOU 1579  C   PRO A 218    12933  12727  16012   -805  -4012    781       C  
ATOM   1580  O   PRO A 218      52.094 -14.440 -33.236  1.00108.39           O  
ANISOU 1580  O   PRO A 218    13143  12628  15410   -747  -3932    700       O  
ATOM   1581  CB  PRO A 218      50.840 -14.415 -30.300  1.00106.57           C  
ANISOU 1581  CB  PRO A 218    12097  12378  16016   -855  -3383    616       C  
ATOM   1582  CG  PRO A 218      52.178 -15.008 -30.012  1.00103.80           C  
ANISOU 1582  CG  PRO A 218    12087  12103  15247   -821  -3176    466       C  
ATOM   1583  CD  PRO A 218      52.226 -16.363 -30.674  1.00104.57           C  
ANISOU 1583  CD  PRO A 218    12480  12161  15090   -915  -3460    418       C  
ATOM   1584  N   PHE A 219      50.158 -13.275 -33.250  1.00112.28           N  
ANISOU 1584  N   PHE A 219    13034  12990  16636   -768  -4218    961       N  
ATOM   1585  CA  PHE A 219      50.631 -12.217 -34.138  1.00113.24           C  
ANISOU 1585  CA  PHE A 219    13326  13108  16591   -649  -4288   1096       C  
ATOM   1586  C   PHE A 219      51.234 -11.107 -33.281  1.00111.49           C  
ANISOU 1586  C   PHE A 219    12936  12896  16529   -525  -3850   1069       C  
ATOM   1587  O   PHE A 219      50.869 -10.953 -32.114  1.00110.70           O  
ANISOU 1587  O   PHE A 219    12507  12781  16772   -522  -3587    986       O  
ATOM   1588  CB  PHE A 219      49.488 -11.655 -34.985  1.00117.09           C  
ANISOU 1588  CB  PHE A 219    13642  13488  17357   -656  -4742   1328       C  
ATOM   1589  CG  PHE A 219      49.073 -12.548 -36.122  1.00119.78           C  
ANISOU 1589  CG  PHE A 219    14259  13819  17432   -776  -5249   1372       C  
ATOM   1590  CD1 PHE A 219      49.752 -12.511 -37.333  1.00120.81           C  
ANISOU 1590  CD1 PHE A 219    14877  13995  17028   -756  -5434   1426       C  
ATOM   1591  CD2 PHE A 219      47.995 -13.414 -35.988  1.00121.68           C  
ANISOU 1591  CD2 PHE A 219    14281  14001  17951   -924  -5539   1355       C  
ATOM   1592  CE1 PHE A 219      49.369 -13.326 -38.386  1.00123.69           C  
ANISOU 1592  CE1 PHE A 219    15545  14349  17103   -871  -5912   1435       C  
ATOM   1593  CE2 PHE A 219      47.608 -14.232 -37.038  1.00124.50           C  
ANISOU 1593  CE2 PHE A 219    14909  14327  18065  -1052  -6045   1373       C  
ATOM   1594  CZ  PHE A 219      48.297 -14.189 -38.238  1.00125.52           C  
ANISOU 1594  CZ  PHE A 219    15563  14503  17624  -1020  -6239   1400       C  
ATOM   1595  N   ILE A 220      52.154 -10.340 -33.859  1.00111.47           N  
ANISOU 1595  N   ILE A 220    13171  12913  16267   -436  -3764   1134       N  
ATOM   1596  CA  ILE A 220      52.847  -9.276 -33.127  1.00109.98           C  
ANISOU 1596  CA  ILE A 220    12865  12712  16208   -338  -3376   1099       C  
ATOM   1597  C   ILE A 220      52.775  -7.960 -33.902  1.00112.37           C  
ANISOU 1597  C   ILE A 220    13169  12902  16622   -256  -3502   1330       C  
ATOM   1598  O   ILE A 220      53.426  -7.805 -34.937  1.00113.06           O  
ANISOU 1598  O   ILE A 220    13594  13026  16337   -255  -3606   1447       O  
ATOM   1599  CB  ILE A 220      54.323  -9.646 -32.849  1.00107.14           C  
ANISOU 1599  CB  ILE A 220    12780  12481  15445   -329  -3058    931       C  
ATOM   1600  CG1 ILE A 220      54.405 -10.953 -32.049  1.00105.42           C  
ANISOU 1600  CG1 ILE A 220    12576  12343  15136   -401  -2960    728       C  
ATOM   1601  CG2 ILE A 220      55.022  -8.528 -32.083  1.00105.72           C  
ANISOU 1601  CG2 ILE A 220    12469  12274  15423   -255  -2702    889       C  
ATOM   1602  CD1 ILE A 220      55.792 -11.552 -31.962  1.00103.37           C  
ANISOU 1602  CD1 ILE A 220    12598  12196  14479   -380  -2748    577       C  
ATOM   1603  N   LEU A 221      51.976  -7.021 -33.395  1.00114.04           N  
ANISOU 1603  N   LEU A 221    13009  12969  17352   -184  -3480   1400       N  
ATOM   1604  CA  LEU A 221      51.880  -5.683 -33.976  1.00116.56           C  
ANISOU 1604  CA  LEU A 221    13292  13127  17866    -89  -3587   1627       C  
ATOM   1605  C   LEU A 221      53.025  -4.815 -33.470  1.00114.93           C  
ANISOU 1605  C   LEU A 221    13157  12900  17608    -39  -3189   1552       C  
ATOM   1606  O   LEU A 221      53.287  -4.762 -32.266  1.00112.80           O  
ANISOU 1606  O   LEU A 221    12715  12649  17494    -24  -2842   1328       O  
ATOM   1607  CB  LEU A 221      50.544  -5.024 -33.618  1.00119.18           C  
ANISOU 1607  CB  LEU A 221    13165  13275  18840     -6  -3723   1713       C  
ATOM   1608  CG  LEU A 221      50.326  -3.597 -34.138  1.00121.98           C  
ANISOU 1608  CG  LEU A 221    13442  13405  19499    117  -3861   1959       C  
ATOM   1609  CD1 LEU A 221      50.334  -3.561 -35.658  1.00124.58           C  
ANISOU 1609  CD1 LEU A 221    14105  13724  19505     79  -4314   2263       C  
ATOM   1610  CD2 LEU A 221      49.024  -3.027 -33.603  1.00124.70           C  
ANISOU 1610  CD2 LEU A 221    13271  13562  20547    232  -3931   1985       C  
ATOM   1611  N   LEU A 222      53.692  -4.130 -34.395  1.00116.44           N  
ANISOU 1611  N   LEU A 222    13612  13051  17578    -30  -3252   1748       N  
ATOM   1612  CA  LEU A 222      54.803  -3.245 -34.062  1.00115.59           C  
ANISOU 1612  CA  LEU A 222    13572  12901  17444    -10  -2914   1716       C  
ATOM   1613  C   LEU A 222      54.501  -1.836 -34.558  1.00118.86           C  
ANISOU 1613  C   LEU A 222    13923  13064  18173     60  -3044   1986       C  
ATOM   1614  O   LEU A 222      54.334  -1.618 -35.760  1.00121.58           O  
ANISOU 1614  O   LEU A 222    14481  13368  18345     45  -3352   2276       O  
ATOM   1615  CB  LEU A 222      56.096  -3.763 -34.692  1.00114.40           C  
ANISOU 1615  CB  LEU A 222    13808  12939  16719    -89  -2792   1705       C  
ATOM   1616  CG  LEU A 222      56.477  -5.199 -34.320  1.00111.76           C  
ANISOU 1616  CG  LEU A 222    13575  12822  16066   -141  -2694   1454       C  
ATOM   1617  CD1 LEU A 222      57.642  -5.673 -35.167  1.00111.58           C  
ANISOU 1617  CD1 LEU A 222    13928  12962  15505   -186  -2609   1467       C  
ATOM   1618  CD2 LEU A 222      56.814  -5.317 -32.841  1.00108.90           C  
ANISOU 1618  CD2 LEU A 222    12987  12488  15900   -130  -2363   1180       C  
ATOM   1619  N   ALA A 223      54.427  -0.888 -33.625  1.00119.00           N  
ANISOU 1619  N   ALA A 223    13671  12899  18642    137  -2820   1888       N  
ATOM   1620  CA  ALA A 223      54.090   0.498 -33.943  1.00122.36           C  
ANISOU 1620  CA  ALA A 223    14000  13025  19465    226  -2930   2118       C  
ATOM   1621  C   ALA A 223      54.938   1.467 -33.126  1.00121.71           C  
ANISOU 1621  C   ALA A 223    13865  12804  19574    236  -2561   1975       C  
ATOM   1622  O   ALA A 223      54.979   1.383 -31.899  1.00119.80           O  
ANISOU 1622  O   ALA A 223    13426  12581  19510    259  -2278   1660       O  
ATOM   1623  CB  ALA A 223      52.614   0.749 -33.684  1.00124.85           C  
ANISOU 1623  CB  ALA A 223    13936  13161  20337    357  -3149   2152       C  
ATOM   1624  N   ASP A 224      55.609   2.388 -33.813  1.00123.70           N  
ANISOU 1624  N   ASP A 224    14313  12910  19778    201  -2574   2213       N  
ATOM   1625  CA  ASP A 224      56.415   3.409 -33.156  1.00123.72           C  
ANISOU 1625  CA  ASP A 224    14275  12733  20000    186  -2275   2110       C  
ATOM   1626  C   ASP A 224      55.532   4.628 -32.896  1.00126.81           C  
ANISOU 1626  C   ASP A 224    14415  12732  21033    336  -2373   2187       C  
ATOM   1627  O   ASP A 224      55.676   5.666 -33.544  1.00129.85           O  
ANISOU 1627  O   ASP A 224    14897  12852  21586    342  -2491   2473       O  
ATOM   1628  CB  ASP A 224      57.620   3.775 -34.032  1.00124.61           C  
ANISOU 1628  CB  ASP A 224    14710  12874  19761     48  -2214   2343       C  
ATOM   1629  CG  ASP A 224      58.549   4.780 -33.370  1.00124.86           C  
ANISOU 1629  CG  ASP A 224    14698  12721  20022     -9  -1919   2236       C  
ATOM   1630  OD1 ASP A 224      58.756   4.693 -32.140  1.00122.75           O  
ANISOU 1630  OD1 ASP A 224    14254  12477  19908      3  -1680   1873       O  
ATOM   1631  OD2 ASP A 224      59.077   5.655 -34.090  1.00127.52           O  
ANISOU 1631  OD2 ASP A 224    15193  12885  20372    -84  -1939   2523       O  
ATOM   1632  N   LYS A 225      54.617   4.497 -31.939  1.00126.41           N  
ANISOU 1632  N   LYS A 225    14040  12633  21355    460  -2307   1933       N  
ATOM   1633  CA  LYS A 225      53.630   5.554 -31.678  1.00129.89           C  
ANISOU 1633  CA  LYS A 225    14191  12702  22459    645  -2392   1971       C  
ATOM   1634  C   LYS A 225      52.826   5.276 -30.381  1.00129.16           C  
ANISOU 1634  C   LYS A 225    13741  12630  22703    759  -2164   1589       C  
ATOM   1635  O   LYS A 225      52.785   4.146 -29.878  1.00126.28           O  
ANISOU 1635  O   LYS A 225    13350  12574  22053    690  -2043   1381       O  
ATOM   1636  CB  LYS A 225      52.721   5.812 -32.910  1.00133.67           C  
ANISOU 1636  CB  LYS A 225    14661  13025  23102    730  -2871   2399       C  
ATOM   1637  CG  LYS A 225      51.372   5.189 -32.731  1.00134.59           C  
ANISOU 1637  CG  LYS A 225    14446  13200  23492    848  -3056   2344       C  
ATOM   1638  CD  LYS A 225      50.327   5.461 -33.817  1.00138.90           C  
ANISOU 1638  CD  LYS A 225    14904  13571  24298    952  -3581   2742       C  
ATOM   1639  CE  LYS A 225      49.243   6.469 -33.442  1.00143.05           C  
ANISOU 1639  CE  LYS A 225    15004  13708  25641   1198  -3663   2760       C  
ATOM   1640  NZ  LYS A 225      47.989   6.388 -34.236  1.00147.04           N  
ANISOU 1640  NZ  LYS A 225    15285  14116  26465   1312  -4183   3063       N  
ATOM   1641  N   LYS A 226      52.210   6.320 -29.832  1.00132.07           N  
ANISOU 1641  N   LYS A 226    13848  12656  23675    932  -2083   1495       N  
ATOM   1642  CA  LYS A 226      51.316   6.173 -28.679  1.00132.59           C  
ANISOU 1642  CA  LYS A 226    13555  12716  24105   1062  -1843   1153       C  
ATOM   1643  C   LYS A 226      49.885   5.883 -29.142  1.00135.44           C  
ANISOU 1643  C   LYS A 226    13587  13041  24832   1203  -2138   1334       C  
ATOM   1644  O   LYS A 226      49.246   6.731 -29.767  1.00139.42           O  
ANISOU 1644  O   LYS A 226    13946  13226  25799   1359  -2414   1588       O  
ATOM   1645  CB  LYS A 226      51.346   7.429 -27.801  1.00134.82           C  
ANISOU 1645  CB  LYS A 226    13711  12640  24874   1195  -1568    904       C  
ATOM   1646  CG  LYS A 226      52.646   7.614 -27.034  1.00132.15           C  
ANISOU 1646  CG  LYS A 226    13630  12361  24220   1044  -1245    624       C  
ATOM   1647  CD  LYS A 226      52.543   8.744 -26.022  1.00134.73           C  
ANISOU 1647  CD  LYS A 226    13828  12342  25020   1173   -964    296       C  
ATOM   1648  CE  LYS A 226      53.871   8.984 -25.323  1.00132.65           C  
ANISOU 1648  CE  LYS A 226    13833  12115  24452    998   -717     36       C  
ATOM   1649  NZ  LYS A 226      53.795  10.105 -24.347  1.00135.73           N  
ANISOU 1649  NZ  LYS A 226    14146  12145  25280   1110   -464   -314       N  
ATOM   1650  N   ILE A 227      49.396   4.682 -28.829  1.00133.75           N  
ANISOU 1650  N   ILE A 227    13247  13139  24430   1139  -2101   1215       N  
ATOM   1651  CA  ILE A 227      48.049   4.248 -29.210  1.00136.38           C  
ANISOU 1651  CA  ILE A 227    13235  13480  25104   1230  -2382   1366       C  
ATOM   1652  C   ILE A 227      47.061   4.564 -28.083  1.00139.02           C  
ANISOU 1652  C   ILE A 227    13095  13693  26033   1405  -2062   1074       C  
ATOM   1653  O   ILE A 227      46.924   3.794 -27.130  1.00137.06           O  
ANISOU 1653  O   ILE A 227    12744  13682  25648   1332  -1731    786       O  
ATOM   1654  CB  ILE A 227      48.009   2.732 -29.523  1.00133.57           C  
ANISOU 1654  CB  ILE A 227    12990  13505  24254   1042  -2528   1406       C  
ATOM   1655  CG1 ILE A 227      49.043   2.368 -30.603  1.00131.33           C  
ANISOU 1655  CG1 ILE A 227    13197  13361  23341    879  -2777   1642       C  
ATOM   1656  CG2 ILE A 227      46.609   2.319 -29.963  1.00136.75           C  
ANISOU 1656  CG2 ILE A 227    13015  13893  25048   1110  -2868   1576       C  
ATOM   1657  CD1 ILE A 227      49.305   0.883 -30.729  1.00128.15           C  
ANISOU 1657  CD1 ILE A 227    12983  13318  22387    693  -2819   1585       C  
ATOM   1658  N   SER A 228      46.378   5.701 -28.198  1.00143.83           N  
ANISOU 1658  N   SER A 228    13425  13923  27301   1639  -2150   1154       N  
ATOM   1659  CA  SER A 228      45.397   6.130 -27.196  1.00147.45           C  
ANISOU 1659  CA  SER A 228    13404  14224  28395   1848  -1824    871       C  
ATOM   1660  C   SER A 228      43.967   5.710 -27.549  1.00151.19           C  
ANISOU 1660  C   SER A 228    13380  14707  29357   1954  -2087   1037       C  
ATOM   1661  O   SER A 228      43.169   5.417 -26.656  1.00152.75           O  
ANISOU 1661  O   SER A 228    13183  14982  29873   2022  -1755    782       O  
ATOM   1662  CB  SER A 228      45.458   7.649 -27.015  1.00150.96           C  
ANISOU 1662  CB  SER A 228    13791  14206  29361   2073  -1728    810       C  
ATOM   1663  OG  SER A 228      46.738   8.055 -26.564  1.00148.15           O  
ANISOU 1663  OG  SER A 228    13846  13829  28614   1957  -1463    616       O  
ATOM   1664  N   ASN A 229      43.650   5.682 -28.843  1.00153.09           N  
ANISOU 1664  N   ASN A 229    13642  14873  29649   1957  -2681   1468       N  
ATOM   1665  CA  ASN A 229      42.310   5.334 -29.321  1.00157.17           C  
ANISOU 1665  CA  ASN A 229    13685  15373  30659   2046  -3045   1674       C  
ATOM   1666  C   ASN A 229      42.280   3.959 -29.979  1.00155.04           C  
ANISOU 1666  C   ASN A 229    13574  15462  29871   1789  -3378   1846       C  
ATOM   1667  O   ASN A 229      43.202   3.600 -30.713  1.00151.96           O  
ANISOU 1667  O   ASN A 229    13700  15209  28828   1610  -3596   2009       O  
ATOM   1668  CB  ASN A 229      41.829   6.381 -30.324  1.00161.96           C  
ANISOU 1668  CB  ASN A 229    14171  15583  31783   2258  -3560   2054       C  
ATOM   1669  CG  ASN A 229      41.797   7.777 -29.737  1.00165.10           C  
ANISOU 1669  CG  ASN A 229    14402  15557  32771   2534  -3274   1894       C  
ATOM   1670  OD1 ASN A 229      41.270   7.988 -28.644  1.00166.72           O  
ANISOU 1670  OD1 ASN A 229    14220  15703  33421   2686  -2802   1533       O  
ATOM   1671  ND2 ASN A 229      42.359   8.741 -30.460  1.00166.37           N  
ANISOU 1671  ND2 ASN A 229    14868  15409  32934   2593  -3545   2159       N  
ATOM   1672  N   ILE A 230      41.215   3.199 -29.718  1.00157.21           N  
ANISOU 1672  N   ILE A 230    13399  15875  30457   1770  -3403   1802       N  
ATOM   1673  CA  ILE A 230      41.038   1.872 -30.320  1.00155.87           C  
ANISOU 1673  CA  ILE A 230    13332  16002  29886   1524  -3749   1950       C  
ATOM   1674  C   ILE A 230      40.359   1.936 -31.697  1.00159.63           C  
ANISOU 1674  C   ILE A 230    13728  16351  30570   1553  -4514   2381       C  
ATOM   1675  O   ILE A 230      40.280   0.925 -32.397  1.00158.81           O  
ANISOU 1675  O   ILE A 230    13796  16455  30090   1346  -4900   2530       O  
ATOM   1676  CB  ILE A 230      40.252   0.916 -29.384  1.00156.29           C  
ANISOU 1676  CB  ILE A 230    12964  16277  30142   1430  -3423   1712       C  
ATOM   1677  CG1 ILE A 230      40.555  -0.548 -29.734  1.00153.02           C  
ANISOU 1677  CG1 ILE A 230    12854  16190  29094   1119  -3614   1756       C  
ATOM   1678  CG2 ILE A 230      38.752   1.193 -29.440  1.00162.35           C  
ANISOU 1678  CG2 ILE A 230    13010  16873  31801   1604  -3615   1820       C  
ATOM   1679  CD1 ILE A 230      40.081  -1.545 -28.701  1.00152.43           C  
ANISOU 1679  CD1 ILE A 230    12503  16346  29066    971  -3210   1513       C  
ATOM   1680  N   ARG A 231      39.878   3.117 -32.086  1.00163.97           N  
ANISOU 1680  N   ARG A 231    14042  16545  31711   1809  -4756   2580       N  
ATOM   1681  CA  ARG A 231      39.272   3.312 -33.408  1.00168.07           C  
ANISOU 1681  CA  ARG A 231    14522  16912  32424   1852  -5530   3026       C  
ATOM   1682  C   ARG A 231      40.254   3.006 -34.546  1.00165.55           C  
ANISOU 1682  C   ARG A 231    14924  16717  31260   1648  -5917   3284       C  
ATOM   1683  O   ARG A 231      39.847   2.562 -35.621  1.00167.88           O  
ANISOU 1683  O   ARG A 231    15317  17060  31410   1552  -6550   3589       O  
ATOM   1684  CB  ARG A 231      38.746   4.746 -33.544  1.00173.17           C  
ANISOU 1684  CB  ARG A 231    14845  17110  33839   2184  -5677   3194       C  
ATOM   1685  CG  ARG A 231      37.994   5.016 -34.838  1.00178.34           C  
ANISOU 1685  CG  ARG A 231    15396  17574  34790   2258  -6516   3679       C  
ATOM   1686  CD  ARG A 231      37.321   6.378 -34.822  1.00184.09           C  
ANISOU 1686  CD  ARG A 231    15693  17830  36420   2621  -6639   3823       C  
ATOM   1687  NE  ARG A 231      36.782   6.734 -36.133  1.00189.16           N  
ANISOU 1687  NE  ARG A 231    16349  18266  37255   2686  -7494   4341       N  
ATOM   1688  CZ  ARG A 231      36.087   7.841 -36.396  1.00195.16           C  
ANISOU 1688  CZ  ARG A 231    16744  18591  38817   3000  -7811   4583       C  
ATOM   1689  NH1 ARG A 231      35.829   8.726 -35.438  1.00196.98           N  
ANISOU 1689  NH1 ARG A 231    16549  18527  39765   3296  -7314   4322       N  
ATOM   1690  NH2 ARG A 231      35.644   8.064 -37.629  1.00199.80           N  
ANISOU 1690  NH2 ARG A 231    17406  19022  39485   3024  -8643   5085       N  
ATOM   1691  N   GLU A 232      41.540   3.241 -34.299  1.00161.24           N  
ANISOU 1691  N   GLU A 232    14874  16226  30161   1579  -5530   3149       N  
ATOM   1692  CA  GLU A 232      42.592   2.991 -35.286  1.00158.84           C  
ANISOU 1692  CA  GLU A 232    15252  16055  29045   1392  -5767   3354       C  
ATOM   1693  C   GLU A 232      42.929   1.502 -35.397  1.00155.12           C  
ANISOU 1693  C   GLU A 232    15052  15978  27907   1121  -5767   3221       C  
ATOM   1694  O   GLU A 232      43.390   1.039 -36.441  1.00154.55           O  
ANISOU 1694  O   GLU A 232    15452  16036  27234    966  -6128   3426       O  
ATOM   1695  CB  GLU A 232      43.849   3.783 -34.915  1.00155.89           C  
ANISOU 1695  CB  GLU A 232    15241  15593  28397   1409  -5320   3244       C  
ATOM   1696  CG  GLU A 232      43.621   5.287 -34.848  1.00159.81           C  
ANISOU 1696  CG  GLU A 232    15540  15651  29527   1664  -5328   3374       C  
ATOM   1697  CD  GLU A 232      44.701   6.028 -34.076  1.00157.01           C  
ANISOU 1697  CD  GLU A 232    15396  15191  29070   1682  -4773   3135       C  
ATOM   1698  OE1 GLU A 232      45.791   5.462 -33.894  1.00152.23           O  
ANISOU 1698  OE1 GLU A 232    15182  14852  27805   1482  -4487   2975       O  
ATOM   1699  OE2 GLU A 232      44.470   7.180 -33.650  1.00159.88           O  
ANISOU 1699  OE2 GLU A 232    15527  15188  30032   1900  -4636   3098       O  
ATOM   1700  N   MET A 233      42.693   0.764 -34.313  1.00152.96           N  
ANISOU 1700  N   MET A 233    14495  15879  27741   1067  -5351   2878       N  
ATOM   1701  CA  MET A 233      43.004  -0.665 -34.237  1.00149.54           C  
ANISOU 1701  CA  MET A 233    14288  15782  26749    820  -5294   2720       C  
ATOM   1702  C   MET A 233      41.951  -1.579 -34.874  1.00152.45           C  
ANISOU 1702  C   MET A 233    14451  16230  27243    707  -5832   2869       C  
ATOM   1703  O   MET A 233      42.227  -2.756 -35.111  1.00150.36           O  
ANISOU 1703  O   MET A 233    14463  16198  26467    491  -5922   2797       O  
ATOM   1704  CB  MET A 233      43.178  -1.075 -32.769  1.00146.38           C  
ANISOU 1704  CB  MET A 233    13689  15520  26408    792  -4633   2319       C  
ATOM   1705  CG  MET A 233      44.381  -0.451 -32.079  1.00142.91           C  
ANISOU 1705  CG  MET A 233    13533  15066  25697    835  -4112   2114       C  
ATOM   1706  SD  MET A 233      45.947  -1.147 -32.639  1.00138.17           S  
ANISOU 1706  SD  MET A 233    13659  14710  24129    627  -4092   2109       S  
ATOM   1707  CE  MET A 233      45.854  -2.796 -31.946  1.00135.11           C  
ANISOU 1707  CE  MET A 233    13251  14636  23446    423  -3905   1851       C  
ATOM   1708  N   LEU A 234      40.760  -1.047 -35.151  1.00157.60           N  
ANISOU 1708  N   LEU A 234    14611  16672  28597    852  -6204   3069       N  
ATOM   1709  CA  LEU A 234      39.621  -1.863 -35.602  1.00160.94           C  
ANISOU 1709  CA  LEU A 234    14708  17148  29292    744  -6710   3190       C  
ATOM   1710  C   LEU A 234      39.894  -2.756 -36.827  1.00160.65           C  
ANISOU 1710  C   LEU A 234    15195  17265  28577    515  -7283   3365       C  
ATOM   1711  O   LEU A 234      39.541  -3.936 -36.808  1.00160.19           O  
ANISOU 1711  O   LEU A 234    15094  17378  28391    311  -7410   3263       O  
ATOM   1712  CB  LEU A 234      38.386  -0.984 -35.857  1.00167.36           C  
ANISOU 1712  CB  LEU A 234    14922  17677  30988    967  -7096   3429       C  
ATOM   1713  CG  LEU A 234      37.751  -0.295 -34.642  1.00169.00           C  
ANISOU 1713  CG  LEU A 234    14465  17731  32016   1197  -6573   3223       C  
ATOM   1714  CD1 LEU A 234      36.603   0.600 -35.086  1.00175.80           C  
ANISOU 1714  CD1 LEU A 234    14770  18280  33743   1444  -7036   3498       C  
ATOM   1715  CD2 LEU A 234      37.271  -1.304 -33.607  1.00167.70           C  
ANISOU 1715  CD2 LEU A 234    13922  17784  32011   1053  -6150   2923       C  
ATOM   1716  N   PRO A 235      40.508  -2.204 -37.893  1.00161.16           N  
ANISOU 1716  N   PRO A 235    15769  17260  28203    540  -7620   3624       N  
ATOM   1717  CA  PRO A 235      40.817  -3.056 -39.052  1.00161.22           C  
ANISOU 1717  CA  PRO A 235    16333  17429  27494    324  -8115   3752       C  
ATOM   1718  C   PRO A 235      41.865  -4.139 -38.774  1.00155.51           C  
ANISOU 1718  C   PRO A 235    16078  16980  26029    129  -7719   3456       C  
ATOM   1719  O   PRO A 235      41.851  -5.184 -39.426  1.00155.79           O  
ANISOU 1719  O   PRO A 235    16416  17160  25616    -67  -8059   3442       O  
ATOM   1720  CB  PRO A 235      41.336  -2.062 -40.102  1.00163.39           C  
ANISOU 1720  CB  PRO A 235    17051  17565  27465    412  -8421   4091       C  
ATOM   1721  CG  PRO A 235      41.753  -0.860 -39.333  1.00162.08           C  
ANISOU 1721  CG  PRO A 235    16707  17212  27662    628  -7907   4048       C  
ATOM   1722  CD  PRO A 235      40.837  -0.790 -38.151  1.00162.71           C  
ANISOU 1722  CD  PRO A 235    16047  17207  28567    754  -7613   3836       C  
ATOM   1723  N   VAL A 236      42.757  -3.889 -37.817  1.00150.73           N  
ANISOU 1723  N   VAL A 236    15529  16425  25314    187  -7033   3216       N  
ATOM   1724  CA  VAL A 236      43.790  -4.857 -37.444  1.00145.50           C  
ANISOU 1724  CA  VAL A 236    15262  16002  24020     34  -6635   2937       C  
ATOM   1725  C   VAL A 236      43.196  -5.955 -36.563  1.00144.15           C  
ANISOU 1725  C   VAL A 236    14748  15943  24079    -88  -6468   2690       C  
ATOM   1726  O   VAL A 236      43.399  -7.140 -36.824  1.00142.82           O  
ANISOU 1726  O   VAL A 236    14858  15927  23479   -275  -6588   2584       O  
ATOM   1727  CB  VAL A 236      44.968  -4.182 -36.703  1.00141.46           C  
ANISOU 1727  CB  VAL A 236    14913  15499  23334    130  -6002   2779       C  
ATOM   1728  CG1 VAL A 236      46.041  -5.203 -36.344  1.00136.66           C  
ANISOU 1728  CG1 VAL A 236    14686  15130  22107    -12  -5639   2509       C  
ATOM   1729  CG2 VAL A 236      45.570  -3.072 -37.554  1.00142.91           C  
ANISOU 1729  CG2 VAL A 236    15424  15552  23323    225  -6139   3046       C  
ATOM   1730  N   LEU A 237      42.463  -5.551 -35.525  1.00144.77           N  
ANISOU 1730  N   LEU A 237    14234  15932  24839     16  -6176   2599       N  
ATOM   1731  CA  LEU A 237      41.857  -6.492 -34.575  1.00144.10           C  
ANISOU 1731  CA  LEU A 237    13781  15948  25021   -106  -5940   2389       C  
ATOM   1732  C   LEU A 237      40.862  -7.451 -35.237  1.00147.46           C  
ANISOU 1732  C   LEU A 237    14055  16391  25579   -288  -6518   2503       C  
ATOM   1733  O   LEU A 237      40.778  -8.620 -34.858  1.00146.05           O  
ANISOU 1733  O   LEU A 237    13890  16337  25263   -487  -6434   2346       O  
ATOM   1734  CB  LEU A 237      41.162  -5.734 -33.437  1.00145.51           C  
ANISOU 1734  CB  LEU A 237    13334  16018  25936     59  -5521   2293       C  
ATOM   1735  CG  LEU A 237      42.065  -4.958 -32.472  1.00142.19           C  
ANISOU 1735  CG  LEU A 237    13013  15587  25422    199  -4873   2088       C  
ATOM   1736  CD1 LEU A 237      41.251  -3.973 -31.646  1.00145.14           C  
ANISOU 1736  CD1 LEU A 237    12790  15788  26568    410  -4581   2032       C  
ATOM   1737  CD2 LEU A 237      42.839  -5.903 -31.564  1.00137.65           C  
ANISOU 1737  CD2 LEU A 237    12681  15232  24388     42  -4397   1807       C  
ATOM   1738  N   GLU A 238      40.111  -6.951 -36.217  1.00152.10           N  
ANISOU 1738  N   GLU A 238    14505  16836  26449   -228  -7129   2785       N  
ATOM   1739  CA  GLU A 238      39.162  -7.778 -36.968  1.00156.13           C  
ANISOU 1739  CA  GLU A 238    14890  17344  27089   -410  -7781   2914       C  
ATOM   1740  C   GLU A 238      39.867  -8.754 -37.914  1.00154.77           C  
ANISOU 1740  C   GLU A 238    15421  17299  26085   -613  -8112   2888       C  
ATOM   1741  O   GLU A 238      39.378  -9.862 -38.142  1.00156.46           O  
ANISOU 1741  O   GLU A 238    15628  17561  26257   -834  -8429   2834       O  
ATOM   1742  CB  GLU A 238      38.182  -6.899 -37.753  1.00162.03           C  
ANISOU 1742  CB  GLU A 238    15293  17890  28377   -274  -8388   3240       C  
ATOM   1743  CG  GLU A 238      37.160  -6.189 -36.877  1.00164.86           C  
ANISOU 1743  CG  GLU A 238    14828  18106  29706    -93  -8161   3250       C  
ATOM   1744  CD  GLU A 238      36.207  -5.312 -37.668  1.00171.10           C  
ANISOU 1744  CD  GLU A 238    15256  18670  31082     69  -8797   3587       C  
ATOM   1745  OE1 GLU A 238      36.633  -4.717 -38.681  1.00172.13           O  
ANISOU 1745  OE1 GLU A 238    15832  18717  30850    141  -9207   3827       O  
ATOM   1746  OE2 GLU A 238      35.027  -5.210 -37.271  1.00175.30           O  
ANISOU 1746  OE2 GLU A 238    15046  19105  32453    127  -8882   3627       O  
ATOM   1747  N   ALA A 239      41.005  -8.336 -38.467  1.00152.22           N  
ANISOU 1747  N   ALA A 239    15695  17017  25121   -542  -8026   2919       N  
ATOM   1748  CA  ALA A 239      41.818  -9.202 -39.325  1.00150.72           C  
ANISOU 1748  CA  ALA A 239    16208  16959  24098   -701  -8224   2853       C  
ATOM   1749  C   ALA A 239      42.465 -10.332 -38.522  1.00146.05           C  
ANISOU 1749  C   ALA A 239    15776  16514  23201   -832  -7752   2524       C  
ATOM   1750  O   ALA A 239      42.564 -11.464 -39.002  1.00146.31           O  
ANISOU 1750  O   ALA A 239    16143  16613  22834  -1017  -8003   2418       O  
ATOM   1751  CB  ALA A 239      42.883  -8.384 -40.041  1.00149.69           C  
ANISOU 1751  CB  ALA A 239    16617  16843  23414   -583  -8161   2979       C  
ATOM   1752  N   VAL A 240      42.909 -10.013 -37.306  1.00142.06           N  
ANISOU 1752  N   VAL A 240    15053  16042  22880   -732  -7089   2362       N  
ATOM   1753  CA  VAL A 240      43.477 -11.002 -36.385  1.00137.82           C  
ANISOU 1753  CA  VAL A 240    14612  15628  22126   -840  -6626   2079       C  
ATOM   1754  C   VAL A 240      42.422 -12.023 -35.952  1.00139.55           C  
ANISOU 1754  C   VAL A 240    14451  15829  22741  -1035  -6781   2019       C  
ATOM   1755  O   VAL A 240      42.707 -13.219 -35.864  1.00138.09           O  
ANISOU 1755  O   VAL A 240    14520  15706  22241  -1209  -6769   1860       O  
ATOM   1756  CB  VAL A 240      44.085 -10.319 -35.133  1.00134.13           C  
ANISOU 1756  CB  VAL A 240    13968  15191  21804   -694  -5925   1939       C  
ATOM   1757  CG1 VAL A 240      44.397 -11.333 -34.039  1.00130.96           C  
ANISOU 1757  CG1 VAL A 240    13555  14897  21305   -815  -5496   1689       C  
ATOM   1758  CG2 VAL A 240      45.344  -9.545 -35.501  1.00131.71           C  
ANISOU 1758  CG2 VAL A 240    14100  14914  21028   -558  -5726   1956       C  
ATOM   1759  N   ALA A 241      41.208 -11.542 -35.689  1.00142.87           N  
ANISOU 1759  N   ALA A 241    14249  16149  23884  -1004  -6921   2153       N  
ATOM   1760  CA  ALA A 241      40.109 -12.392 -35.224  1.00145.27           C  
ANISOU 1760  CA  ALA A 241    14086  16430  24677  -1198  -7033   2127       C  
ATOM   1761  C   ALA A 241      39.687 -13.458 -36.243  1.00148.11           C  
ANISOU 1761  C   ALA A 241    14676  16762  24836  -1436  -7703   2174       C  
ATOM   1762  O   ALA A 241      39.198 -14.521 -35.857  1.00148.88           O  
ANISOU 1762  O   ALA A 241    14612  16858  25096  -1661  -7731   2086       O  
ATOM   1763  CB  ALA A 241      38.913 -11.534 -34.839  1.00149.11           C  
ANISOU 1763  CB  ALA A 241    13825  16812  26019  -1083  -7050   2272       C  
ATOM   1764  N   LYS A 242      39.871 -13.173 -37.532  1.00149.93           N  
ANISOU 1764  N   LYS A 242    15302  16959  24704  -1400  -8241   2314       N  
ATOM   1765  CA  LYS A 242      39.505 -14.116 -38.597  1.00153.18           C  
ANISOU 1765  CA  LYS A 242    16008  17336  24854  -1621  -8926   2339       C  
ATOM   1766  C   LYS A 242      40.374 -15.372 -38.597  1.00150.09           C  
ANISOU 1766  C   LYS A 242    16184  17016  23827  -1780  -8777   2081       C  
ATOM   1767  O   LYS A 242      39.859 -16.485 -38.715  1.00152.14           O  
ANISOU 1767  O   LYS A 242    16438  17222  24147  -2023  -9083   2001       O  
ATOM   1768  CB  LYS A 242      39.579 -13.447 -39.975  1.00156.21           C  
ANISOU 1768  CB  LYS A 242    16759  17684  24906  -1537  -9506   2552       C  
ATOM   1769  CG  LYS A 242      38.348 -12.630 -40.334  1.00161.62           C  
ANISOU 1769  CG  LYS A 242    16890  18239  26275  -1472 -10015   2845       C  
ATOM   1770  CD  LYS A 242      38.379 -12.191 -41.790  1.00165.37           C  
ANISOU 1770  CD  LYS A 242    17817  18677  26338  -1447 -10701   3075       C  
ATOM   1771  CE  LYS A 242      37.005 -11.754 -42.273  1.00171.91           C  
ANISOU 1771  CE  LYS A 242    18110  19359  27847  -1455 -11406   3361       C  
ATOM   1772  NZ  LYS A 242      36.444 -10.637 -41.465  1.00172.43           N  
ANISOU 1772  NZ  LYS A 242    17448  19325  28741  -1217 -11099   3501       N  
ATOM   1773  N   ALA A 243      41.687 -15.188 -38.469  1.00145.44           N  
ANISOU 1773  N   ALA A 243    16065  16526  22667  -1643  -8319   1953       N  
ATOM   1774  CA  ALA A 243      42.630 -16.308 -38.462  1.00142.52           C  
ANISOU 1774  CA  ALA A 243    16233  16212  21704  -1740  -8139   1702       C  
ATOM   1775  C   ALA A 243      42.533 -17.157 -37.191  1.00140.21           C  
ANISOU 1775  C   ALA A 243    15669  15915  21690  -1861  -7717   1539       C  
ATOM   1776  O   ALA A 243      42.965 -18.311 -37.183  1.00139.35           O  
ANISOU 1776  O   ALA A 243    15906  15788  21251  -1996  -7711   1355       O  
ATOM   1777  CB  ALA A 243      44.053 -15.803 -38.649  1.00138.68           C  
ANISOU 1777  CB  ALA A 243    16246  15837  20608  -1547  -7752   1629       C  
ATOM   1778  N   GLY A 244      41.975 -16.587 -36.124  1.00139.61           N  
ANISOU 1778  N   GLY A 244    14994  15844  22204  -1809  -7358   1608       N  
ATOM   1779  CA  GLY A 244      41.767 -17.317 -34.876  1.00138.15           C  
ANISOU 1779  CA  GLY A 244    14524  15665  22299  -1942  -6946   1496       C  
ATOM   1780  C   GLY A 244      43.053 -17.465 -34.090  1.00132.95           C  
ANISOU 1780  C   GLY A 244    14200  15106  21208  -1841  -6349   1315       C  
ATOM   1781  O   GLY A 244      43.416 -18.567 -33.677  1.00131.58           O  
ANISOU 1781  O   GLY A 244    14242  14919  20831  -1979  -6224   1176       O  
ATOM   1782  N   LYS A 245      43.742 -16.344 -33.891  1.00130.35           N  
ANISOU 1782  N   LYS A 245    13909  14856  20762  -1604  -6011   1327       N  
ATOM   1783  CA  LYS A 245      45.007 -16.319 -33.162  1.00125.71           C  
ANISOU 1783  CA  LYS A 245    13604  14367  19790  -1493  -5472   1167       C  
ATOM   1784  C   LYS A 245      45.082 -15.079 -32.271  1.00124.11           C  
ANISOU 1784  C   LYS A 245    13066  14215  19875  -1314  -5006   1192       C  
ATOM   1785  O   LYS A 245      44.443 -14.068 -32.563  1.00126.27           O  
ANISOU 1785  O   LYS A 245    13031  14437  20508  -1209  -5140   1337       O  
ATOM   1786  CB  LYS A 245      46.182 -16.332 -34.142  1.00124.16           C  
ANISOU 1786  CB  LYS A 245    14015  14213  18946  -1393  -5587   1104       C  
ATOM   1787  CG  LYS A 245      46.357 -17.651 -34.876  1.00125.37           C  
ANISOU 1787  CG  LYS A 245    14594  14316  18724  -1545  -5933    995       C  
ATOM   1788  CD  LYS A 245      47.575 -17.630 -35.784  1.00124.20           C  
ANISOU 1788  CD  LYS A 245    15034  14230  17926  -1423  -5946    906       C  
ATOM   1789  CE  LYS A 245      47.918 -19.025 -36.283  1.00125.05           C  
ANISOU 1789  CE  LYS A 245    15585  14276  17651  -1542  -6158    722       C  
ATOM   1790  NZ  LYS A 245      49.174 -19.036 -37.080  1.00124.08           N  
ANISOU 1790  NZ  LYS A 245    16016  14228  16900  -1403  -6072    602       N  
ATOM   1791  N   PRO A 246      45.861 -15.153 -31.177  1.00120.71           N  
ANISOU 1791  N   PRO A 246    12704  13867  19292  -1274  -4481   1046       N  
ATOM   1792  CA  PRO A 246      46.016 -14.002 -30.285  1.00119.37           C  
ANISOU 1792  CA  PRO A 246    12275  13736  19342  -1113  -4028   1022       C  
ATOM   1793  C   PRO A 246      46.932 -12.918 -30.863  1.00117.77           C  
ANISOU 1793  C   PRO A 246    12322  13543  18882   -911  -3998   1045       C  
ATOM   1794  O   PRO A 246      47.505 -13.099 -31.940  1.00117.60           O  
ANISOU 1794  O   PRO A 246    12693  13525  18463   -898  -4286   1083       O  
ATOM   1795  CB  PRO A 246      46.618 -14.617 -29.018  1.00116.67           C  
ANISOU 1795  CB  PRO A 246    12020  13482  18824  -1176  -3562    857       C  
ATOM   1796  CG  PRO A 246      47.328 -15.838 -29.483  1.00115.38           C  
ANISOU 1796  CG  PRO A 246    12315  13326  18195  -1278  -3753    790       C  
ATOM   1797  CD  PRO A 246      46.594 -16.338 -30.692  1.00118.46           C  
ANISOU 1797  CD  PRO A 246    12741  13622  18644  -1383  -4315    895       C  
ATOM   1798  N   LEU A 247      47.060 -11.804 -30.142  1.00116.98           N  
ANISOU 1798  N   LEU A 247    12005  13438  19004   -765  -3637   1016       N  
ATOM   1799  CA  LEU A 247      47.813 -10.642 -30.618  1.00115.99           C  
ANISOU 1799  CA  LEU A 247    12047  13283  18741   -590  -3597   1064       C  
ATOM   1800  C   LEU A 247      48.694 -10.046 -29.520  1.00113.20           C  
ANISOU 1800  C   LEU A 247    11718  12979  18311   -501  -3075    896       C  
ATOM   1801  O   LEU A 247      48.332 -10.069 -28.344  1.00113.18           O  
ANISOU 1801  O   LEU A 247    11455  13002  18545   -522  -2741    777       O  
ATOM   1802  CB  LEU A 247      46.842  -9.576 -31.128  1.00119.42           C  
ANISOU 1802  CB  LEU A 247    12139  13571  19661   -481  -3838   1254       C  
ATOM   1803  CG  LEU A 247      47.430  -8.316 -31.767  1.00119.52           C  
ANISOU 1803  CG  LEU A 247    12309  13500  19604   -316  -3879   1372       C  
ATOM   1804  CD1 LEU A 247      48.244  -8.652 -33.008  1.00118.93           C  
ANISOU 1804  CD1 LEU A 247    12750  13479  18957   -356  -4174   1466       C  
ATOM   1805  CD2 LEU A 247      46.311  -7.345 -32.109  1.00123.61           C  
ANISOU 1805  CD2 LEU A 247    12423  13837  20703   -200  -4127   1566       C  
ATOM   1806  N   LEU A 248      49.851  -9.520 -29.917  1.00111.21           N  
ANISOU 1806  N   LEU A 248    11788  12748  17720   -416  -3008    887       N  
ATOM   1807  CA  LEU A 248      50.758  -8.828 -29.003  1.00108.86           C  
ANISOU 1807  CA  LEU A 248    11524  12477  17358   -337  -2581    738       C  
ATOM   1808  C   LEU A 248      51.016  -7.412 -29.513  1.00109.87           C  
ANISOU 1808  C   LEU A 248    11641  12479  17623   -197  -2599    849       C  
ATOM   1809  O   LEU A 248      51.511  -7.230 -30.627  1.00110.17           O  
ANISOU 1809  O   LEU A 248    11944  12504  17409   -181  -2829    995       O  
ATOM   1810  CB  LEU A 248      52.079  -9.593 -28.876  1.00105.67           C  
ANISOU 1810  CB  LEU A 248    11503  12210  16436   -387  -2450    611       C  
ATOM   1811  CG  LEU A 248      53.148  -9.010 -27.941  1.00103.36           C  
ANISOU 1811  CG  LEU A 248    11274  11962  16036   -334  -2064    450       C  
ATOM   1812  CD1 LEU A 248      52.625  -8.864 -26.520  1.00103.51           C  
ANISOU 1812  CD1 LEU A 248    11024  11985  16319   -351  -1751    302       C  
ATOM   1813  CD2 LEU A 248      54.397  -9.878 -27.961  1.00100.99           C  
ANISOU 1813  CD2 LEU A 248    11313  11789  15268   -374  -2011    354       C  
ATOM   1814  N   ILE A 249      50.677  -6.419 -28.695  1.00110.80           N  
ANISOU 1814  N   ILE A 249    11471  12493  18135   -102  -2343    778       N  
ATOM   1815  CA  ILE A 249      50.870  -5.015 -29.049  1.00112.09           C  
ANISOU 1815  CA  ILE A 249    11600  12483  18506     31  -2343    876       C  
ATOM   1816  C   ILE A 249      52.175  -4.507 -28.440  1.00109.58           C  
ANISOU 1816  C   ILE A 249    11484  12192  17956     44  -2007    714       C  
ATOM   1817  O   ILE A 249      52.295  -4.402 -27.218  1.00108.63           O  
ANISOU 1817  O   ILE A 249    11255  12100  17920     44  -1667    487       O  
ATOM   1818  CB  ILE A 249      49.706  -4.128 -28.542  1.00115.31           C  
ANISOU 1818  CB  ILE A 249    11556  12705  19548    155  -2271    873       C  
ATOM   1819  CG1 ILE A 249      48.344  -4.736 -28.902  1.00118.03           C  
ANISOU 1819  CG1 ILE A 249    11603  13042  20201    124  -2566   1000       C  
ATOM   1820  CG2 ILE A 249      49.826  -2.712 -29.095  1.00117.30           C  
ANISOU 1820  CG2 ILE A 249    11792  12723  20050    300  -2360   1022       C  
ATOM   1821  CD1 ILE A 249      48.136  -4.990 -30.380  1.00119.56           C  
ANISOU 1821  CD1 ILE A 249    11964  13210  20252     91  -3101   1277       C  
ATOM   1822  N   ILE A 250      53.153  -4.215 -29.296  1.00108.77           N  
ANISOU 1822  N   ILE A 250    11681  12092  17554     38  -2104    832       N  
ATOM   1823  CA  ILE A 250      54.392  -3.568 -28.868  1.00107.10           C  
ANISOU 1823  CA  ILE A 250    11618  11875  17198     42  -1831    720       C  
ATOM   1824  C   ILE A 250      54.409  -2.153 -29.442  1.00109.32           C  
ANISOU 1824  C   ILE A 250    11867  11920  17747    129  -1900    897       C  
ATOM   1825  O   ILE A 250      54.783  -1.943 -30.598  1.00110.09           O  
ANISOU 1825  O   ILE A 250    12176  11995  17655    113  -2105   1132       O  
ATOM   1826  CB  ILE A 250      55.648  -4.350 -29.313  1.00104.73           C  
ANISOU 1826  CB  ILE A 250    11661  11765  16365    -44  -1820    707       C  
ATOM   1827  CG1 ILE A 250      55.601  -5.785 -28.774  1.00102.90           C  
ANISOU 1827  CG1 ILE A 250    11475  11721  15901   -119  -1791    551       C  
ATOM   1828  CG2 ILE A 250      56.912  -3.651 -28.822  1.00103.51           C  
ANISOU 1828  CG2 ILE A 250    11595  11600  16132    -54  -1551    595       C  
ATOM   1829  CD1 ILE A 250      56.679  -6.696 -29.322  1.00101.27           C  
ANISOU 1829  CD1 ILE A 250    11584  11677  15216   -172  -1822    538       C  
ATOM   1830  N   ALA A 251      53.981  -1.196 -28.624  1.00110.70           N  
ANISOU 1830  N   ALA A 251    11793  11909  18359    219  -1720    783       N  
ATOM   1831  CA  ALA A 251      53.926   0.211 -29.011  1.00113.19           C  
ANISOU 1831  CA  ALA A 251    12050  11938  19017    316  -1772    930       C  
ATOM   1832  C   ALA A 251      54.746   1.045 -28.035  1.00112.47           C  
ANISOU 1832  C   ALA A 251    11968  11744  19019    315  -1435    695       C  
ATOM   1833  O   ALA A 251      55.312   0.511 -27.080  1.00110.21           O  
ANISOU 1833  O   ALA A 251    11731  11629  18512    243  -1191    431       O  
ATOM   1834  CB  ALA A 251      52.482   0.688 -29.037  1.00116.52           C  
ANISOU 1834  CB  ALA A 251    12127  12156  19987    458  -1923   1013       C  
ATOM   1835  N   GLU A 252      54.818   2.351 -28.282  1.00114.78           N  
ANISOU 1835  N   GLU A 252    12231  11743  19638    388  -1453    799       N  
ATOM   1836  CA  GLU A 252      55.465   3.272 -27.349  1.00115.03           C  
ANISOU 1836  CA  GLU A 252    12253  11613  19839    388  -1168    560       C  
ATOM   1837  C   GLU A 252      54.703   3.262 -26.025  1.00115.75           C  
ANISOU 1837  C   GLU A 252    12097  11682  20199    474   -917    220       C  
ATOM   1838  O   GLU A 252      55.304   3.188 -24.952  1.00114.41           O  
ANISOU 1838  O   GLU A 252    11988  11599  19883    409   -647    -85       O  
ATOM   1839  CB  GLU A 252      55.519   4.687 -27.931  1.00118.03           C  
ANISOU 1839  CB  GLU A 252    12635  11621  20587    456  -1271    762       C  
ATOM   1840  CG  GLU A 252      56.398   5.654 -27.147  1.00118.28           C  
ANISOU 1840  CG  GLU A 252    12721  11465  20755    411  -1023    540       C  
ATOM   1841  CD  GLU A 252      56.513   7.021 -27.799  1.00121.48           C  
ANISOU 1841  CD  GLU A 252    13159  11472  21525    452  -1143    777       C  
ATOM   1842  OE1 GLU A 252      56.438   7.110 -29.043  1.00122.60           O  
ANISOU 1842  OE1 GLU A 252    13406  11570  21603    441  -1410   1174       O  
ATOM   1843  OE2 GLU A 252      56.685   8.015 -27.063  1.00123.08           O  
ANISOU 1843  OE2 GLU A 252    13306  11391  22068    486   -976    567       O  
ATOM   1844  N   ASP A 253      53.377   3.332 -26.117  1.00118.27           N  
ANISOU 1844  N   ASP A 253    12137  11893  20906    615  -1009    282       N  
ATOM   1845  CA  ASP A 253      52.499   3.175 -24.959  1.00119.43           C  
ANISOU 1845  CA  ASP A 253    12016  12060  21301    696   -744    -11       C  
ATOM   1846  C   ASP A 253      51.076   2.870 -25.435  1.00121.97           C  
ANISOU 1846  C   ASP A 253    12016  12350  21974    809   -943    163       C  
ATOM   1847  O   ASP A 253      50.745   3.087 -26.603  1.00123.48           O  
ANISOU 1847  O   ASP A 253    12190  12423  22301    857  -1308    496       O  
ATOM   1848  CB  ASP A 253      52.511   4.448 -24.097  1.00121.85           C  
ANISOU 1848  CB  ASP A 253    12231  12066  21998    810   -475   -275       C  
ATOM   1849  CG  ASP A 253      52.148   4.185 -22.638  1.00122.12           C  
ANISOU 1849  CG  ASP A 253    12149  12212  22039    823    -75   -682       C  
ATOM   1850  OD1 ASP A 253      51.546   3.133 -22.330  1.00121.20           O  
ANISOU 1850  OD1 ASP A 253    11919  12350  21780    780    -11   -712       O  
ATOM   1851  OD2 ASP A 253      52.468   5.044 -21.789  1.00123.59           O  
ANISOU 1851  OD2 ASP A 253    12377  12220  22359    864    179   -975       O  
ATOM   1852  N   VAL A 254      50.252   2.345 -24.531  1.00122.88           N  
ANISOU 1852  N   VAL A 254    11882  12582  22224    834   -710    -50       N  
ATOM   1853  CA  VAL A 254      48.823   2.160 -24.781  1.00126.08           C  
ANISOU 1853  CA  VAL A 254    11887  12935  23082    946   -839     68       C  
ATOM   1854  C   VAL A 254      48.062   2.742 -23.590  1.00129.42           C  
ANISOU 1854  C   VAL A 254    11983  13230  23961   1094   -422   -249       C  
ATOM   1855  O   VAL A 254      48.096   2.182 -22.492  1.00128.46           O  
ANISOU 1855  O   VAL A 254    11871  13311  23624   1010    -55   -529       O  
ATOM   1856  CB  VAL A 254      48.459   0.672 -24.984  1.00124.27           C  
ANISOU 1856  CB  VAL A 254    11644  13019  22551    790   -975    162       C  
ATOM   1857  CG1 VAL A 254      46.995   0.524 -25.375  1.00127.87           C  
ANISOU 1857  CG1 VAL A 254    11657  13402  23523    885  -1178    323       C  
ATOM   1858  CG2 VAL A 254      49.350   0.042 -26.046  1.00121.18           C  
ANISOU 1858  CG2 VAL A 254    11637  12769  21635    646  -1313    397       C  
ATOM   1859  N   GLU A 255      47.383   3.868 -23.816  1.00133.86           N  
ANISOU 1859  N   GLU A 255    12269  13447  25142   1320   -475   -203       N  
ATOM   1860  CA  GLU A 255      46.796   4.661 -22.733  1.00137.74           C  
ANISOU 1860  CA  GLU A 255    12487  13749  26098   1501    -49   -544       C  
ATOM   1861  C   GLU A 255      45.284   4.814 -22.851  1.00142.81           C  
ANISOU 1861  C   GLU A 255    12571  14255  27434   1704    -81   -471       C  
ATOM   1862  O   GLU A 255      44.720   4.722 -23.943  1.00144.09           O  
ANISOU 1862  O   GLU A 255    12561  14342  27845   1752   -537   -112       O  
ATOM   1863  CB  GLU A 255      47.419   6.060 -22.715  1.00139.23           C  
ANISOU 1863  CB  GLU A 255    12832  13567  26501   1627    -12   -634       C  
ATOM   1864  CG  GLU A 255      48.925   6.084 -22.499  1.00135.46           C  
ANISOU 1864  CG  GLU A 255    12846  13183  25440   1433     49   -738       C  
ATOM   1865  CD  GLU A 255      49.517   7.477 -22.637  1.00137.31           C  
ANISOU 1865  CD  GLU A 255    13220  13014  25937   1526     19   -769       C  
ATOM   1866  OE1 GLU A 255      48.757   8.467 -22.569  1.00141.55           O  
ANISOU 1866  OE1 GLU A 255    13489  13185  27108   1764     65   -824       O  
ATOM   1867  OE2 GLU A 255      50.750   7.582 -22.812  1.00134.68           O  
ANISOU 1867  OE2 GLU A 255    13250  12715  25208   1359    -47   -736       O  
ATOM   1868  N   GLY A 256      44.644   5.049 -21.707  1.00146.25           N  
ANISOU 1868  N   GLY A 256    12728  14664  28174   1820    409   -823       N  
ATOM   1869  CA  GLY A 256      43.242   5.460 -21.643  1.00152.16           C  
ANISOU 1869  CA  GLY A 256    12887  15222  29704   2067    487   -831       C  
ATOM   1870  C   GLY A 256      42.239   4.518 -22.283  1.00153.54           C  
ANISOU 1870  C   GLY A 256    12688  15570  30078   2013    189   -534       C  
ATOM   1871  O   GLY A 256      42.009   3.413 -21.790  1.00152.27           O  
ANISOU 1871  O   GLY A 256    12478  15742  29633   1824    383   -602       O  
ATOM   1872  N   GLU A 257      41.647   4.965 -23.389  1.00156.72           N  
ANISOU 1872  N   GLU A 257    12841  15729  30974   2165   -311   -191       N  
ATOM   1873  CA  GLU A 257      40.537   4.258 -24.028  1.00159.39           C  
ANISOU 1873  CA  GLU A 257    12742  16161  31656   2149   -653     87       C  
ATOM   1874  C   GLU A 257      40.983   3.007 -24.787  1.00155.20           C  
ANISOU 1874  C   GLU A 257    12536  15944  30486   1844  -1055    351       C  
ATOM   1875  O   GLU A 257      40.268   2.006 -24.805  1.00155.83           O  
ANISOU 1875  O   GLU A 257    12354  16241  30613   1712  -1124    425       O  
ATOM   1876  CB  GLU A 257      39.782   5.210 -24.963  1.00164.48           C  
ANISOU 1876  CB  GLU A 257    13035  16417  33042   2423  -1112    375       C  
ATOM   1877  CG  GLU A 257      38.434   4.688 -25.452  1.00168.65           C  
ANISOU 1877  CG  GLU A 257    12967  16981  34128   2464  -1431    610       C  
ATOM   1878  CD  GLU A 257      38.492   4.044 -26.828  1.00167.27           C  
ANISOU 1878  CD  GLU A 257    12984  16899  33671   2292  -2177   1060       C  
ATOM   1879  OE1 GLU A 257      39.207   4.562 -27.713  1.00166.02           O  
ANISOU 1879  OE1 GLU A 257    13239  16582  33256   2303  -2573   1299       O  
ATOM   1880  OE2 GLU A 257      37.802   3.023 -27.029  1.00167.95           O  
ANISOU 1880  OE2 GLU A 257    12811  17207  33793   2136  -2364   1173       O  
ATOM   1881  N   ALA A 258      42.157   3.067 -25.414  1.00151.49           N  
ANISOU 1881  N   ALA A 258    12625  15488  29445   1731  -1306    483       N  
ATOM   1882  CA  ALA A 258      42.710   1.908 -26.119  1.00147.55           C  
ANISOU 1882  CA  ALA A 258    12491  15274  28295   1461  -1640    685       C  
ATOM   1883  C   ALA A 258      43.006   0.762 -25.152  1.00144.35           C  
ANISOU 1883  C   ALA A 258    12212  15218  27416   1238  -1241    434       C  
ATOM   1884  O   ALA A 258      42.670  -0.389 -25.428  1.00143.28           O  
ANISOU 1884  O   ALA A 258    12041  15301  27097   1055  -1430    552       O  
ATOM   1885  CB  ALA A 258      43.970   2.295 -26.879  1.00144.54           C  
ANISOU 1885  CB  ALA A 258    12667  14834  27417   1403  -1882    837       C  
ATOM   1886  N   LEU A 259      43.629   1.090 -24.021  1.00143.17           N  
ANISOU 1886  N   LEU A 259    12225  15100  27071   1246   -716     95       N  
ATOM   1887  CA  LEU A 259      43.956   0.102 -22.992  1.00140.71           C  
ANISOU 1887  CA  LEU A 259    12068  15100  26294   1044   -319   -141       C  
ATOM   1888  C   LEU A 259      42.699  -0.429 -22.304  1.00144.31           C  
ANISOU 1888  C   LEU A 259    12026  15659  27144   1034    -40   -230       C  
ATOM   1889  O   LEU A 259      42.561  -1.636 -22.108  1.00142.97           O  
ANISOU 1889  O   LEU A 259    11884  15747  26690    814    -19   -194       O  
ATOM   1890  CB  LEU A 259      44.903   0.710 -21.949  1.00139.19           C  
ANISOU 1890  CB  LEU A 259    12178  14892  25816   1064    134   -482       C  
ATOM   1891  CG  LEU A 259      45.447  -0.212 -20.850  1.00136.51           C  
ANISOU 1891  CG  LEU A 259    12096  14861  24909    854    512   -718       C  
ATOM   1892  CD1 LEU A 259      46.293  -1.335 -21.432  1.00132.00           C  
ANISOU 1892  CD1 LEU A 259    11913  14517  23723    626    198   -530       C  
ATOM   1893  CD2 LEU A 259      46.255   0.589 -19.841  1.00136.21           C  
ANISOU 1893  CD2 LEU A 259    12314  14758  24681    902    909  -1064       C  
ATOM   1894  N   ALA A 260      41.791   0.475 -21.943  1.00149.36           N  
ANISOU 1894  N   ALA A 260    12202  16085  28463   1272    184   -344       N  
ATOM   1895  CA  ALA A 260      40.557   0.104 -21.245  1.00153.65           C  
ANISOU 1895  CA  ALA A 260    12203  16713  29462   1286    527   -446       C  
ATOM   1896  C   ALA A 260      39.658  -0.809 -22.081  1.00155.11           C  
ANISOU 1896  C   ALA A 260    12051  16986  29896   1165     85   -121       C  
ATOM   1897  O   ALA A 260      39.081  -1.761 -21.555  1.00155.89           O  
ANISOU 1897  O   ALA A 260    11935  17303  29991    987    304   -150       O  
ATOM   1898  CB  ALA A 260      39.792   1.352 -20.824  1.00159.08           C  
ANISOU 1898  CB  ALA A 260    12440  17112  30890   1610    828   -632       C  
ATOM   1899  N   THR A 261      39.543  -0.517 -23.376  1.00155.83           N  
ANISOU 1899  N   THR A 261    12113  16901  30193   1244   -545    194       N  
ATOM   1900  CA  THR A 261      38.703  -1.309 -24.279  1.00157.73           C  
ANISOU 1900  CA  THR A 261    12063  17195  30672   1129  -1063    507       C  
ATOM   1901  C   THR A 261      39.303  -2.691 -24.550  1.00153.49           C  
ANISOU 1901  C   THR A 261    11953  16937  29428    798  -1265    600       C  
ATOM   1902  O   THR A 261      38.571  -3.678 -24.634  1.00154.98           O  
ANISOU 1902  O   THR A 261    11884  17259  29740    615  -1394    705       O  
ATOM   1903  CB  THR A 261      38.474  -0.586 -25.623  1.00159.83           C  
ANISOU 1903  CB  THR A 261    12256  17192  31277   1300  -1729    830       C  
ATOM   1904  OG1 THR A 261      38.027   0.753 -25.381  1.00164.09           O  
ANISOU 1904  OG1 THR A 261    12446  17423  32475   1631  -1557    745       O  
ATOM   1905  CG2 THR A 261      37.428  -1.315 -26.463  1.00162.84           C  
ANISOU 1905  CG2 THR A 261    12253  17607  32011   1198  -2271   1124       C  
ATOM   1906  N   LEU A 262      40.625  -2.755 -24.695  1.00148.82           N  
ANISOU 1906  N   LEU A 262    11992  16412  28139    722  -1298    561       N  
ATOM   1907  CA  LEU A 262      41.318  -4.033 -24.885  1.00144.81           C  
ANISOU 1907  CA  LEU A 262    11921  16145  26952    441  -1443    609       C  
ATOM   1908  C   LEU A 262      41.159  -4.945 -23.668  1.00144.52           C  
ANISOU 1908  C   LEU A 262    11823  16335  26751    255   -945    408       C  
ATOM   1909  O   LEU A 262      40.928  -6.143 -23.819  1.00143.94           O  
ANISOU 1909  O   LEU A 262    11773  16410  26505     23  -1108    510       O  
ATOM   1910  CB  LEU A 262      42.805  -3.812 -25.185  1.00140.21           C  
ANISOU 1910  CB  LEU A 262    11972  15581  25718    431  -1505    580       C  
ATOM   1911  CG  LEU A 262      43.145  -3.305 -26.591  1.00140.12           C  
ANISOU 1911  CG  LEU A 262    12175  15416  25646    511  -2065    849       C  
ATOM   1912  CD1 LEU A 262      44.573  -2.783 -26.645  1.00136.54           C  
ANISOU 1912  CD1 LEU A 262    12241  14951  24688    536  -1961    776       C  
ATOM   1913  CD2 LEU A 262      42.937  -4.396 -27.631  1.00139.75           C  
ANISOU 1913  CD2 LEU A 262    12255  15475  25366    328  -2595   1082       C  
ATOM   1914  N   VAL A 263      41.276  -4.372 -22.470  1.00145.47           N  
ANISOU 1914  N   VAL A 263    11887  16466  26916    348   -349    127       N  
ATOM   1915  CA  VAL A 263      41.095  -5.124 -21.221  1.00146.10           C  
ANISOU 1915  CA  VAL A 263    11925  16760  26823    176    177    -59       C  
ATOM   1916  C   VAL A 263      39.694  -5.744 -21.132  1.00150.84           C  
ANISOU 1916  C   VAL A 263    11941  17407  27961     79    211     51       C  
ATOM   1917  O   VAL A 263      39.548  -6.884 -20.692  1.00150.52           O  
ANISOU 1917  O   VAL A 263    11941  17557  27691   -179    336     77       O  
ATOM   1918  CB  VAL A 263      41.377  -4.239 -19.979  1.00146.96           C  
ANISOU 1918  CB  VAL A 263    12073  16853  26910    317    809   -401       C  
ATOM   1919  CG1 VAL A 263      40.865  -4.887 -18.696  1.00149.06           C  
ANISOU 1919  CG1 VAL A 263    12186  17326  27121    163   1388   -570       C  
ATOM   1920  CG2 VAL A 263      42.869  -3.961 -19.859  1.00142.34           C  
ANISOU 1920  CG2 VAL A 263    12107  16287  25688    312    805   -523       C  
ATOM   1921  N   VAL A 264      38.675  -4.998 -21.558  1.00155.60           N  
ANISOU 1921  N   VAL A 264    11991  17823  29305    279     84    132       N  
ATOM   1922  CA  VAL A 264      37.294  -5.491 -21.545  1.00160.58           C  
ANISOU 1922  CA  VAL A 264    11976  18478  30557    200     83    252       C  
ATOM   1923  C   VAL A 264      37.071  -6.572 -22.611  1.00160.06           C  
ANISOU 1923  C   VAL A 264    11945  18454  30413    -33   -572    555       C  
ATOM   1924  O   VAL A 264      36.403  -7.573 -22.349  1.00161.99           O  
ANISOU 1924  O   VAL A 264    11940  18826  30781   -274   -513    626       O  
ATOM   1925  CB  VAL A 264      36.278  -4.337 -21.728  1.00165.99           C  
ANISOU 1925  CB  VAL A 264    12019  18925  32123    515     95    254       C  
ATOM   1926  CG1 VAL A 264      34.860  -4.869 -21.901  1.00171.34           C  
ANISOU 1926  CG1 VAL A 264    11979  19618  33502    428    -19    423       C  
ATOM   1927  CG2 VAL A 264      36.334  -3.388 -20.538  1.00167.72           C  
ANISOU 1927  CG2 VAL A 264    12155  19102  32468    728    823    -98       C  
ATOM   1928  N   ASN A 265      37.629  -6.369 -23.804  1.00157.99           N  
ANISOU 1928  N   ASN A 265    12011  18080  29936     25  -1183    729       N  
ATOM   1929  CA  ASN A 265      37.479  -7.328 -24.907  1.00157.75           C  
ANISOU 1929  CA  ASN A 265    12090  18072  29776   -180  -1844    988       C  
ATOM   1930  C   ASN A 265      38.152  -8.677 -24.644  1.00154.25           C  
ANISOU 1930  C   ASN A 265    12114  17829  28665   -489  -1796    954       C  
ATOM   1931  O   ASN A 265      37.608  -9.724 -24.999  1.00155.62           O  
ANISOU 1931  O   ASN A 265    12173  18048  28908   -728  -2095   1093       O  
ATOM   1932  CB  ASN A 265      38.017  -6.737 -26.216  1.00156.29           C  
ANISOU 1932  CB  ASN A 265    12228  17734  29421    -40  -2453   1165       C  
ATOM   1933  CG  ASN A 265      37.137  -5.629 -26.766  1.00161.19           C  
ANISOU 1933  CG  ASN A 265    12345  18117  30781    223  -2721   1307       C  
ATOM   1934  OD1 ASN A 265      36.258  -5.112 -26.076  1.00165.33           O  
ANISOU 1934  OD1 ASN A 265    12286  18574  31956    363  -2367   1216       O  
ATOM   1935  ND2 ASN A 265      37.371  -5.258 -28.020  1.00161.23           N  
ANISOU 1935  ND2 ASN A 265    12581  17989  30689    299  -3345   1536       N  
ATOM   1936  N   THR A 266      39.331  -8.645 -24.028  1.00150.32           N  
ANISOU 1936  N   THR A 266    12134  17427  27552   -484  -1449    772       N  
ATOM   1937  CA  THR A 266      40.084  -9.864 -23.720  1.00147.05           C  
ANISOU 1937  CA  THR A 266    12190  17178  26502   -738  -1393    735       C  
ATOM   1938  C   THR A 266      39.484 -10.615 -22.532  1.00149.12           C  
ANISOU 1938  C   THR A 266    12203  17579  26876   -941   -902    659       C  
ATOM   1939  O   THR A 266      39.382 -11.843 -22.555  1.00149.01           O  
ANISOU 1939  O   THR A 266    12294  17637  26684  -1210  -1038    752       O  
ATOM   1940  CB  THR A 266      41.561  -9.553 -23.403  1.00142.26           C  
ANISOU 1940  CB  THR A 266    12181  16628  25242   -658  -1192    573       C  
ATOM   1941  OG1 THR A 266      41.639  -8.644 -22.297  1.00143.12           O  
ANISOU 1941  OG1 THR A 266    12172  16747  25458   -508   -614    352       O  
ATOM   1942  CG2 THR A 266      42.256  -8.941 -24.610  1.00140.22           C  
ANISOU 1942  CG2 THR A 266    12223  16252  24800   -507  -1654    674       C  
ATOM   1943  N   MET A 267      39.092  -9.866 -21.503  1.00151.47           N  
ANISOU 1943  N   MET A 267    12190  17900  27462   -815   -323    489       N  
ATOM   1944  CA  MET A 267      38.524 -10.435 -20.278  1.00153.95           C  
ANISOU 1944  CA  MET A 267    12275  18363  27856   -996    245    407       C  
ATOM   1945  C   MET A 267      37.197 -11.153 -20.540  1.00158.27           C  
ANISOU 1945  C   MET A 267    12250  18899  28984  -1189     87    602       C  
ATOM   1946  O   MET A 267      36.938 -12.211 -19.964  1.00159.15           O  
ANISOU 1946  O   MET A 267    12357  19130  28982  -1477    284    655       O  
ATOM   1947  CB  MET A 267      38.338  -9.331 -19.232  1.00156.45           C  
ANISOU 1947  CB  MET A 267    12371  18688  28384   -781    894    154       C  
ATOM   1948  CG  MET A 267      37.914  -9.811 -17.854  1.00159.26           C  
ANISOU 1948  CG  MET A 267    12597  19228  28685   -956   1579     34       C  
ATOM   1949  SD  MET A 267      38.160  -8.541 -16.594  1.00160.89           S  
ANISOU 1949  SD  MET A 267    12837  19461  28833   -705   2333   -344       S  
ATOM   1950  CE  MET A 267      37.064  -7.249 -17.177  1.00165.69           C  
ANISOU 1950  CE  MET A 267    12718  19828  30408   -356   2271   -364       C  
ATOM   1951  N   ARG A 268      36.363 -10.574 -21.403  1.00161.04           N  
ANISOU 1951  N   ARG A 268    12117  19095  29973  -1039   -286    725       N  
ATOM   1952  CA  ARG A 268      35.123 -11.225 -21.839  1.00165.26           C  
ANISOU 1952  CA  ARG A 268    12085  19596  31109  -1224   -574    933       C  
ATOM   1953  C   ARG A 268      35.415 -12.432 -22.732  1.00162.69           C  
ANISOU 1953  C   ARG A 268    12118  19260  30434  -1497  -1202   1118       C  
ATOM   1954  O   ARG A 268      34.665 -13.411 -22.725  1.00165.67           O  
ANISOU 1954  O   ARG A 268    12221  19660  31064  -1784  -1310   1252       O  
ATOM   1955  CB  ARG A 268      34.218 -10.236 -22.580  1.00169.45           C  
ANISOU 1955  CB  ARG A 268    12022  19946  32416   -968   -889   1026       C  
ATOM   1956  CG  ARG A 268      33.582  -9.192 -21.679  1.00173.56           C  
ANISOU 1956  CG  ARG A 268    12009  20445  33491   -718   -251    847       C  
ATOM   1957  CD  ARG A 268      32.724  -8.220 -22.472  1.00178.03           C  
ANISOU 1957  CD  ARG A 268    11990  20792  34860   -438   -626    961       C  
ATOM   1958  NE  ARG A 268      31.999  -7.295 -21.604  1.00182.89           N  
ANISOU 1958  NE  ARG A 268    12024  21366  36100   -190      4    775       N  
ATOM   1959  CZ  ARG A 268      31.171  -6.342 -22.031  1.00187.82           C  
ANISOU 1959  CZ  ARG A 268    12046  21784  37534    104   -167    829       C  
ATOM   1960  NH1 ARG A 268      30.945  -6.170 -23.331  1.00188.63           N  
ANISOU 1960  NH1 ARG A 268    12057  21709  37904    175   -990   1094       N  
ATOM   1961  NH2 ARG A 268      30.563  -5.554 -21.152  1.00192.43           N  
ANISOU 1961  NH2 ARG A 268    12125  22329  38660    337    483    614       N  
ATOM   1962  N   GLY A 269      36.498 -12.348 -23.504  1.00157.46           N  
ANISOU 1962  N   GLY A 269    12063  18552  29211  -1410  -1601   1117       N  
ATOM   1963  CA  GLY A 269      36.962 -13.460 -24.331  1.00154.66           C  
ANISOU 1963  CA  GLY A 269    12157  18185  28422  -1633  -2146   1233       C  
ATOM   1964  C   GLY A 269      36.467 -13.381 -25.762  1.00156.34           C  
ANISOU 1964  C   GLY A 269    12236  18250  28913  -1608  -2916   1420       C  
ATOM   1965  O   GLY A 269      35.979 -14.365 -26.310  1.00158.29           O  
ANISOU 1965  O   GLY A 269    12431  18460  29252  -1861  -3349   1549       O  
ATOM   1966  N   ILE A 270      36.601 -12.204 -26.367  1.00155.75           N  
ANISOU 1966  N   ILE A 270    12133  18079  28963  -1313  -3109   1440       N  
ATOM   1967  CA  ILE A 270      36.223 -11.996 -27.762  1.00157.34           C  
ANISOU 1967  CA  ILE A 270    12282  18142  29355  -1263  -3868   1638       C  
ATOM   1968  C   ILE A 270      37.456 -12.197 -28.642  1.00152.41           C  
ANISOU 1968  C   ILE A 270    12432  17521  27954  -1250  -4225   1635       C  
ATOM   1969  O   ILE A 270      37.432 -12.993 -29.583  1.00152.65           O  
ANISOU 1969  O   ILE A 270    12706  17520  27772  -1422  -4790   1736       O  
ATOM   1970  CB  ILE A 270      35.610 -10.591 -27.969  1.00160.60           C  
ANISOU 1970  CB  ILE A 270    12216  18420  30385   -947  -3908   1704       C  
ATOM   1971  CG1 ILE A 270      34.387 -10.420 -27.040  1.00165.53           C  
ANISOU 1971  CG1 ILE A 270    12034  19049  31808   -943  -3477   1674       C  
ATOM   1972  CG2 ILE A 270      35.276 -10.351 -29.442  1.00162.96           C  
ANISOU 1972  CG2 ILE A 270    12525  18574  30818   -897  -4745   1943       C  
ATOM   1973  CD1 ILE A 270      33.494  -9.234 -27.332  1.00170.37           C  
ANISOU 1973  CD1 ILE A 270    12028  19492  33212   -654  -3616   1769       C  
ATOM   1974  N   VAL A 271      38.528 -11.471 -28.325  1.00148.04           N  
ANISOU 1974  N   VAL A 271    12255  17003  26990  -1051  -3880   1506       N  
ATOM   1975  CA  VAL A 271      39.825 -11.637 -28.987  1.00143.21           C  
ANISOU 1975  CA  VAL A 271    12359  16421  25630  -1032  -4073   1475       C  
ATOM   1976  C   VAL A 271      40.938 -11.552 -27.939  1.00138.32           C  
ANISOU 1976  C   VAL A 271    12075  15919  24562   -982  -3458   1259       C  
ATOM   1977  O   VAL A 271      40.977 -10.607 -27.153  1.00138.25           O  
ANISOU 1977  O   VAL A 271    11867  15904  24757   -808  -3011   1156       O  
ATOM   1978  CB  VAL A 271      40.052 -10.565 -30.079  1.00143.68           C  
ANISOU 1978  CB  VAL A 271    12553  16362  25674   -810  -4469   1614       C  
ATOM   1979  CG1 VAL A 271      41.464 -10.648 -30.647  1.00139.25           C  
ANISOU 1979  CG1 VAL A 271    12709  15857  24343   -784  -4538   1568       C  
ATOM   1980  CG2 VAL A 271      39.029 -10.714 -31.197  1.00148.34           C  
ANISOU 1980  CG2 VAL A 271    12893  16844  26625   -874  -5171   1845       C  
ATOM   1981  N   LYS A 272      41.827 -12.545 -27.934  1.00134.49           N  
ANISOU 1981  N   LYS A 272    12092  15522  23483  -1131  -3460   1184       N  
ATOM   1982  CA  LYS A 272      42.978 -12.570 -27.020  1.00130.05           C  
ANISOU 1982  CA  LYS A 272    11887  15069  22454  -1097  -2969    998       C  
ATOM   1983  C   LYS A 272      44.045 -11.562 -27.458  1.00127.06           C  
ANISOU 1983  C   LYS A 272    11842  14671  21763   -876  -2962    961       C  
ATOM   1984  O   LYS A 272      44.505 -11.594 -28.600  1.00126.37           O  
ANISOU 1984  O   LYS A 272    12073  14546  21393   -849  -3370   1054       O  
ATOM   1985  CB  LYS A 272      43.586 -13.984 -26.938  1.00127.80           C  
ANISOU 1985  CB  LYS A 272    12016  14855  21687  -1309  -3025    949       C  
ATOM   1986  CG  LYS A 272      43.126 -14.856 -25.774  1.00128.72           C  
ANISOU 1986  CG  LYS A 272    11953  15037  21917  -1517  -2677    905       C  
ATOM   1987  CD  LYS A 272      41.680 -14.621 -25.357  1.00133.24           C  
ANISOU 1987  CD  LYS A 272    11871  15582  23171  -1579  -2558    984       C  
ATOM   1988  CE  LYS A 272      41.253 -15.580 -24.256  1.00134.51           C  
ANISOU 1988  CE  LYS A 272    11896  15816  23395  -1827  -2201    971       C  
ATOM   1989  NZ  LYS A 272      40.559 -16.784 -24.782  1.00136.89           N  
ANISOU 1989  NZ  LYS A 272    12114  16040  23856  -2103  -2605   1110       N  
ATOM   1990  N   VAL A 273      44.434 -10.679 -26.537  1.00125.51           N  
ANISOU 1990  N   VAL A 273    11583  14496  21609   -734  -2487    822       N  
ATOM   1991  CA  VAL A 273      45.378  -9.591 -26.817  1.00123.12           C  
ANISOU 1991  CA  VAL A 273    11524  14146  21108   -537  -2433    787       C  
ATOM   1992  C   VAL A 273      46.197  -9.274 -25.564  1.00120.17           C  
ANISOU 1992  C   VAL A 273    11284  13856  20518   -497  -1888    561       C  
ATOM   1993  O   VAL A 273      45.727  -9.465 -24.442  1.00121.00           O  
ANISOU 1993  O   VAL A 273    11165  14023  20786   -556  -1511    443       O  
ATOM   1994  CB  VAL A 273      44.660  -8.292 -27.268  1.00126.37           C  
ANISOU 1994  CB  VAL A 273    11580  14384  22048   -339  -2562    899       C  
ATOM   1995  CG1 VAL A 273      45.671  -7.222 -27.669  1.00124.60           C  
ANISOU 1995  CG1 VAL A 273    11651  14082  21606   -171  -2551    901       C  
ATOM   1996  CG2 VAL A 273      43.701  -8.557 -28.421  1.00129.67           C  
ANISOU 1996  CG2 VAL A 273    11807  14715  22745   -382  -3137   1137       C  
ATOM   1997  N   ALA A 274      47.422  -8.796 -25.768  1.00116.85           N  
ANISOU 1997  N   ALA A 274    11234  13443  19721   -411  -1854    506       N  
ATOM   1998  CA  ALA A 274      48.262  -8.299 -24.680  1.00114.67           C  
ANISOU 1998  CA  ALA A 274    11088  13219  19261   -360  -1410    293       C  
ATOM   1999  C   ALA A 274      49.032  -7.065 -25.144  1.00113.58           C  
ANISOU 1999  C   ALA A 274    11089  12968  19097   -197  -1436    297       C  
ATOM   2000  O   ALA A 274      49.488  -7.008 -26.287  1.00112.98           O  
ANISOU 2000  O   ALA A 274    11228  12855  18841   -175  -1765    452       O  
ATOM   2001  CB  ALA A 274      49.222  -9.381 -24.213  1.00111.75           C  
ANISOU 2001  CB  ALA A 274    11086  13008  18362   -499  -1317    201       C  
ATOM   2002  N   ALA A 275      49.174  -6.084 -24.253  1.00113.64           N  
ANISOU 2002  N   ALA A 275    10993  12914  19271    -95  -1080    125       N  
ATOM   2003  CA  ALA A 275      49.829  -4.818 -24.582  1.00113.09           C  
ANISOU 2003  CA  ALA A 275    11019  12692  19258     46  -1079    122       C  
ATOM   2004  C   ALA A 275      51.064  -4.585 -23.716  1.00110.30           C  
ANISOU 2004  C   ALA A 275    10937  12408  18560     20   -777    -98       C  
ATOM   2005  O   ALA A 275      51.013  -4.743 -22.494  1.00110.42           O  
ANISOU 2005  O   ALA A 275    10915  12507  18532    -21   -439   -314       O  
ATOM   2006  CB  ALA A 275      48.849  -3.667 -24.422  1.00116.80           C  
ANISOU 2006  CB  ALA A 275    11098  12948  20332    215   -988    111       C  
ATOM   2007  N   VAL A 276      52.168  -4.212 -24.361  1.00108.12           N  
ANISOU 2007  N   VAL A 276    10937  12104  18037     33   -908    -35       N  
ATOM   2008  CA  VAL A 276      53.425  -3.915 -23.672  1.00106.00           C  
ANISOU 2008  CA  VAL A 276    10905  11886  17484      2   -687   -221       C  
ATOM   2009  C   VAL A 276      54.116  -2.711 -24.311  1.00106.25           C  
ANISOU 2009  C   VAL A 276    11021  11738  17608     80   -759   -145       C  
ATOM   2010  O   VAL A 276      53.938  -2.445 -25.502  1.00107.01           O  
ANISOU 2010  O   VAL A 276    11127  11739  17791    124  -1033     99       O  
ATOM   2011  CB  VAL A 276      54.392  -5.120 -23.696  1.00103.05           C  
ANISOU 2011  CB  VAL A 276    10827  11728  16597   -123   -750   -227       C  
ATOM   2012  CG1 VAL A 276      53.805  -6.294 -22.929  1.00102.92           C  
ANISOU 2012  CG1 VAL A 276    10762  11861  16479   -222   -659   -298       C  
ATOM   2013  CG2 VAL A 276      54.726  -5.536 -25.124  1.00102.30           C  
ANISOU 2013  CG2 VAL A 276    10899  11652  16317   -131  -1081      3       C  
ATOM   2014  N   LYS A 277      54.903  -1.990 -23.517  1.00105.83           N  
ANISOU 2014  N   LYS A 277    11048  11633  17527     80   -528   -348       N  
ATOM   2015  CA  LYS A 277      55.698  -0.875 -24.031  1.00106.18           C  
ANISOU 2015  CA  LYS A 277    11189  11499  17653    114   -574   -283       C  
ATOM   2016  C   LYS A 277      56.879  -1.401 -24.843  1.00103.99           C  
ANISOU 2016  C   LYS A 277    11177  11363  16970     21   -725   -139       C  
ATOM   2017  O   LYS A 277      57.354  -2.516 -24.614  1.00101.95           O  
ANISOU 2017  O   LYS A 277    11050  11331  16355    -60   -718   -198       O  
ATOM   2018  CB  LYS A 277      56.221  -0.001 -22.888  1.00106.77           C  
ANISOU 2018  CB  LYS A 277    11277  11470  17820    113   -299   -573       C  
ATOM   2019  CG  LYS A 277      55.148   0.744 -22.113  1.00109.57           C  
ANISOU 2019  CG  LYS A 277    11387  11642  18603    233    -96   -754       C  
ATOM   2020  CD  LYS A 277      55.766   1.750 -21.155  1.00110.62           C  
ANISOU 2020  CD  LYS A 277    11593  11623  18812    232    134  -1047       C  
ATOM   2021  CE  LYS A 277      54.752   2.267 -20.149  1.00113.58           C  
ANISOU 2021  CE  LYS A 277    11765  11873  19514    345    421  -1316       C  
ATOM   2022  NZ  LYS A 277      55.278   3.427 -19.379  1.00115.47           N  
ANISOU 2022  NZ  LYS A 277    12093  11891  19888    364    607  -1608       N  
ATOM   2023  N   ALA A 278      57.346  -0.592 -25.791  1.00104.86           N  
ANISOU 2023  N   ALA A 278    11362  11329  17149     38   -845     54       N  
ATOM   2024  CA  ALA A 278      58.541  -0.918 -26.565  1.00103.37           C  
ANISOU 2024  CA  ALA A 278    11407  11264  16604    -46   -917    180       C  
ATOM   2025  C   ALA A 278      59.772  -0.737 -25.680  1.00102.43           C  
ANISOU 2025  C   ALA A 278    11361  11202  16355   -127   -711    -41       C  
ATOM   2026  O   ALA A 278      59.764   0.096 -24.772  1.00103.43           O  
ANISOU 2026  O   ALA A 278    11398  11182  16718   -118   -558   -232       O  
ATOM   2027  CB  ALA A 278      58.635  -0.030 -27.795  1.00105.23           C  
ANISOU 2027  CB  ALA A 278    11704  11323  16954    -24  -1073    473       C  
ATOM   2028  N   PRO A 279      60.836  -1.517 -25.936  1.00100.96           N  
ANISOU 2028  N   PRO A 279    11332  11219  15807   -202   -716    -29       N  
ATOM   2029  CA  PRO A 279      62.016  -1.471 -25.072  1.00100.18           C  
ANISOU 2029  CA  PRO A 279    11271  11194  15596   -283   -570   -233       C  
ATOM   2030  C   PRO A 279      62.832  -0.190 -25.250  1.00101.78           C  
ANISOU 2030  C   PRO A 279    11461  11213  15996   -337   -506   -197       C  
ATOM   2031  O   PRO A 279      62.947   0.318 -26.365  1.00102.81           O  
ANISOU 2031  O   PRO A 279    11632  11247  16181   -339   -574     54       O  
ATOM   2032  CB  PRO A 279      62.822  -2.692 -25.520  1.00 98.43           C  
ANISOU 2032  CB  PRO A 279    11185  11217  14996   -314   -622   -186       C  
ATOM   2033  CG  PRO A 279      62.449  -2.877 -26.949  1.00 98.99           C  
ANISOU 2033  CG  PRO A 279    11340  11287  14985   -276   -766     81       C  
ATOM   2034  CD  PRO A 279      61.012  -2.454 -27.062  1.00100.23           C  
ANISOU 2034  CD  PRO A 279    11388  11285  15409   -208   -867    160       C  
ATOM   2035  N   GLY A 280      63.383   0.319 -24.151  1.00102.33           N  
ANISOU 2035  N   GLY A 280    11493  11227  16159   -397   -389   -441       N  
ATOM   2036  CA  GLY A 280      64.196   1.535 -24.172  1.00104.32           C  
ANISOU 2036  CA  GLY A 280    11723  11279  16633   -481   -338   -443       C  
ATOM   2037  C   GLY A 280      63.375   2.798 -24.344  1.00107.02           C  
ANISOU 2037  C   GLY A 280    11994  11285  17381   -419   -337   -384       C  
ATOM   2038  O   GLY A 280      62.163   2.804 -24.114  1.00107.66           O  
ANISOU 2038  O   GLY A 280    12002  11290  17611   -301   -342   -427       O  
ATOM   2039  N   PHE A 281      64.048   3.872 -24.751  1.00109.08           N  
ANISOU 2039  N   PHE A 281    12259  11331  17854   -501   -329   -278       N  
ATOM   2040  CA  PHE A 281      63.393   5.147 -25.037  1.00111.95           C  
ANISOU 2040  CA  PHE A 281    12573  11321  18641   -443   -354   -178       C  
ATOM   2041  C   PHE A 281      64.201   5.949 -26.057  1.00113.89           C  
ANISOU 2041  C   PHE A 281    12874  11407  18989   -557   -389    120       C  
ATOM   2042  O   PHE A 281      65.363   5.639 -26.326  1.00113.11           O  
ANISOU 2042  O   PHE A 281    12819  11481  18676   -696   -342    178       O  
ATOM   2043  CB  PHE A 281      63.209   5.957 -23.749  1.00113.53           C  
ANISOU 2043  CB  PHE A 281    12714  11297  19125   -433   -243   -537       C  
ATOM   2044  CG  PHE A 281      64.484   6.551 -23.217  1.00114.45           C  
ANISOU 2044  CG  PHE A 281    12868  11335  19283   -612   -193   -697       C  
ATOM   2045  CD1 PHE A 281      65.364   5.783 -22.469  1.00112.71           C  
ANISOU 2045  CD1 PHE A 281    12681  11393  18750   -719   -165   -905       C  
ATOM   2046  CD2 PHE A 281      64.805   7.880 -23.469  1.00117.51           C  
ANISOU 2046  CD2 PHE A 281    13249  11351  20048   -683   -203   -626       C  
ATOM   2047  CE1 PHE A 281      66.540   6.327 -21.982  1.00113.92           C  
ANISOU 2047  CE1 PHE A 281    12838  11474  18972   -896   -163  -1048       C  
ATOM   2048  CE2 PHE A 281      65.981   8.429 -22.985  1.00118.69           C  
ANISOU 2048  CE2 PHE A 281    13412  11414  20270   -876   -180   -773       C  
ATOM   2049  CZ  PHE A 281      66.849   7.652 -22.241  1.00116.91           C  
ANISOU 2049  CZ  PHE A 281    13196  11486  19735   -984   -168   -989       C  
ATOM   2050  N   GLY A 282      63.574   6.977 -26.622  1.00116.84           N  
ANISOU 2050  N   GLY A 282    13236  11444  19712   -497   -465    322       N  
ATOM   2051  CA  GLY A 282      64.238   7.875 -27.562  1.00119.50           C  
ANISOU 2051  CA  GLY A 282    13645  11573  20185   -619   -493    641       C  
ATOM   2052  C   GLY A 282      64.573   7.234 -28.897  1.00119.11           C  
ANISOU 2052  C   GLY A 282    13725  11760  19769   -668   -548   1011       C  
ATOM   2053  O   GLY A 282      63.725   6.590 -29.516  1.00118.53           O  
ANISOU 2053  O   GLY A 282    13703  11812  19521   -547   -679   1163       O  
ATOM   2054  N   ASP A 283      65.818   7.412 -29.333  1.00119.92           N  
ANISOU 2054  N   ASP A 283    13880  11925  19760   -855   -440   1144       N  
ATOM   2055  CA  ASP A 283      66.274   6.909 -30.629  1.00120.22           C  
ANISOU 2055  CA  ASP A 283    14063  12180  19432   -918   -426   1485       C  
ATOM   2056  C   ASP A 283      66.511   5.404 -30.601  1.00117.25           C  
ANISOU 2056  C   ASP A 283    13713  12237  18599   -870   -383   1341       C  
ATOM   2057  O   ASP A 283      66.176   4.703 -31.559  1.00116.82           O  
ANISOU 2057  O   ASP A 283    13806  12362  18216   -813   -454   1541       O  
ATOM   2058  CB  ASP A 283      67.560   7.623 -31.061  1.00122.45           C  
ANISOU 2058  CB  ASP A 283    14357  12386  19783  -1144   -267   1667       C  
ATOM   2059  CG  ASP A 283      67.378   9.124 -31.214  1.00126.09           C  
ANISOU 2059  CG  ASP A 283    14825  12378  20703  -1216   -322   1862       C  
ATOM   2060  OD1 ASP A 283      66.223   9.589 -31.306  1.00127.13           O  
ANISOU 2060  OD1 ASP A 283    14989  12256  21057  -1065   -501   1944       O  
ATOM   2061  OD2 ASP A 283      68.399   9.842 -31.244  1.00128.12           O  
ANISOU 2061  OD2 ASP A 283    15042  12504  21134  -1425   -193   1938       O  
ATOM   2062  N   ARG A 284      67.090   4.910 -29.508  1.00115.71           N  
ANISOU 2062  N   ARG A 284    13395  12190  18379   -894   -289    996       N  
ATOM   2063  CA  ARG A 284      67.383   3.480 -29.375  1.00113.37           C  
ANISOU 2063  CA  ARG A 284    13115  12265  17693   -843   -258    849       C  
ATOM   2064  C   ARG A 284      66.116   2.614 -29.270  1.00111.47           C  
ANISOU 2064  C   ARG A 284    12924  12119  17309   -673   -407    780       C  
ATOM   2065  O   ARG A 284      66.162   1.419 -29.569  1.00109.88           O  
ANISOU 2065  O   ARG A 284    12799  12186  16763   -623   -425    761       O  
ATOM   2066  CB  ARG A 284      68.360   3.208 -28.213  1.00112.54           C  
ANISOU 2066  CB  ARG A 284    12869  12273  17616   -919   -164    529       C  
ATOM   2067  CG  ARG A 284      67.763   3.047 -26.824  1.00111.43           C  
ANISOU 2067  CG  ARG A 284    12662  12098  17576   -850   -225    187       C  
ATOM   2068  CD  ARG A 284      68.776   2.384 -25.906  1.00110.46           C  
ANISOU 2068  CD  ARG A 284    12463  12184  17323   -913   -186    -68       C  
ATOM   2069  NE  ARG A 284      68.376   2.468 -24.497  1.00110.31           N  
ANISOU 2069  NE  ARG A 284    12414  12104  17392   -896   -227   -394       N  
ATOM   2070  CZ  ARG A 284      68.249   1.427 -23.672  1.00108.66           C  
ANISOU 2070  CZ  ARG A 284    12230  12106  16947   -839   -264   -597       C  
ATOM   2071  NH1 ARG A 284      68.507   0.188 -24.084  1.00107.03           N  
ANISOU 2071  NH1 ARG A 284    12062  12163  16441   -783   -286   -523       N  
ATOM   2072  NH2 ARG A 284      67.870   1.628 -22.413  1.00108.95           N  
ANISOU 2072  NH2 ARG A 284    12277  12079  17040   -842   -273   -878       N  
ATOM   2073  N   ARG A 285      64.999   3.216 -28.857  1.00112.04           N  
ANISOU 2073  N   ARG A 285    12936  11958  17674   -586   -507    738       N  
ATOM   2074  CA  ARG A 285      63.699   2.534 -28.856  1.00110.95           C  
ANISOU 2074  CA  ARG A 285    12797  11876  17480   -440   -651    719       C  
ATOM   2075  C   ARG A 285      63.275   2.170 -30.277  1.00111.70           C  
ANISOU 2075  C   ARG A 285    13050  12039  17349   -406   -810   1051       C  
ATOM   2076  O   ARG A 285      62.764   1.075 -30.522  1.00110.44           O  
ANISOU 2076  O   ARG A 285    12950  12077  16933   -344   -914   1036       O  
ATOM   2077  CB  ARG A 285      62.617   3.417 -28.219  1.00112.48           C  
ANISOU 2077  CB  ARG A 285    12852  11774  18108   -344   -695    630       C  
ATOM   2078  CG  ARG A 285      61.287   2.708 -27.981  1.00111.75           C  
ANISOU 2078  CG  ARG A 285    12679  11750  18029   -207   -801    562       C  
ATOM   2079  CD  ARG A 285      60.092   3.653 -28.027  1.00114.39           C  
ANISOU 2079  CD  ARG A 285    12875  11768  18818    -81   -899    641       C  
ATOM   2080  NE  ARG A 285      60.031   4.545 -26.865  1.00115.44           N  
ANISOU 2080  NE  ARG A 285    12878  11675  19310    -53   -732    359       N  
ATOM   2081  CZ  ARG A 285      60.147   5.875 -26.894  1.00118.10           C  
ANISOU 2081  CZ  ARG A 285    13188  11660  20024    -47   -717    405       C  
ATOM   2082  NH1 ARG A 285      60.335   6.535 -28.035  1.00120.17           N  
ANISOU 2082  NH1 ARG A 285    13540  11746  20370    -77   -860    766       N  
ATOM   2083  NH2 ARG A 285      60.069   6.559 -25.757  1.00119.15           N  
ANISOU 2083  NH2 ARG A 285    13227  11600  20443    -18   -556     83       N  
ATOM   2084  N   LYS A 286      63.493   3.099 -31.203  1.00114.14           N  
ANISOU 2084  N   LYS A 286    13450  12173  17745   -463   -840   1353       N  
ATOM   2085  CA  LYS A 286      63.118   2.913 -32.604  1.00115.65           C  
ANISOU 2085  CA  LYS A 286    13842  12408  17691   -450  -1011   1698       C  
ATOM   2086  C   LYS A 286      64.048   1.915 -33.292  1.00114.58           C  
ANISOU 2086  C   LYS A 286    13889  12596  17048   -519   -899   1729       C  
ATOM   2087  O   LYS A 286      63.645   1.218 -34.224  1.00114.79           O  
ANISOU 2087  O   LYS A 286    14106  12763  16743   -484  -1044   1875       O  
ATOM   2088  CB  LYS A 286      63.133   4.259 -33.335  1.00119.42           C  
ANISOU 2088  CB  LYS A 286    14388  12583  18401   -505  -1066   2036       C  
ATOM   2089  CG  LYS A 286      62.192   5.286 -32.721  1.00121.01           C  
ANISOU 2089  CG  LYS A 286    14408  12416  19151   -405  -1181   2004       C  
ATOM   2090  CD  LYS A 286      62.295   6.648 -33.387  1.00124.90           C  
ANISOU 2090  CD  LYS A 286    14976  12562  19917   -464  -1242   2344       C  
ATOM   2091  CE  LYS A 286      61.529   7.693 -32.590  1.00126.40           C  
ANISOU 2091  CE  LYS A 286    14960  12352  20712   -349  -1302   2229       C  
ATOM   2092  NZ  LYS A 286      61.574   9.037 -33.223  1.00130.49           N  
ANISOU 2092  NZ  LYS A 286    15556  12472  21550   -394  -1394   2574       N  
ATOM   2093  N   ALA A 287      65.291   1.854 -32.820  1.00113.67           N  
ANISOU 2093  N   ALA A 287    13707  12589  16892   -611   -650   1574       N  
ATOM   2094  CA  ALA A 287      66.260   0.865 -33.285  1.00112.91           C  
ANISOU 2094  CA  ALA A 287    13718  12798  16384   -647   -497   1537       C  
ATOM   2095  C   ALA A 287      65.885  -0.543 -32.814  1.00109.99           C  
ANISOU 2095  C   ALA A 287    13349  12642  15798   -538   -575   1283       C  
ATOM   2096  O   ALA A 287      65.903  -1.490 -33.601  1.00110.00           O  
ANISOU 2096  O   ALA A 287    13536  12835  15424   -501   -607   1326       O  
ATOM   2097  CB  ALA A 287      67.654   1.234 -32.795  1.00113.12           C  
ANISOU 2097  CB  ALA A 287    13597  12854  16526   -769   -236   1435       C  
ATOM   2098  N   MET A 288      65.544  -0.670 -31.531  1.00107.82           N  
ANISOU 2098  N   MET A 288    12890  12323  15751   -495   -599   1019       N  
ATOM   2099  CA  MET A 288      65.179  -1.965 -30.940  1.00105.13           C  
ANISOU 2099  CA  MET A 288    12543  12158  15244   -415   -666    793       C  
ATOM   2100  C   MET A 288      63.823  -2.488 -31.420  1.00104.91           C  
ANISOU 2100  C   MET A 288    12604  12116  15140   -334   -907    881       C  
ATOM   2101  O   MET A 288      63.593  -3.697 -31.411  1.00103.47           O  
ANISOU 2101  O   MET A 288    12494  12090  14727   -290   -982    776       O  
ATOM   2102  CB  MET A 288      65.190  -1.888 -29.408  1.00103.60           C  
ANISOU 2102  CB  MET A 288    12158  11922  15283   -416   -610    510       C  
ATOM   2103  CG  MET A 288      66.584  -1.799 -28.807  1.00103.29           C  
ANISOU 2103  CG  MET A 288    12029  11959  15254   -495   -438    364       C  
ATOM   2104  SD  MET A 288      66.581  -1.770 -27.003  1.00101.89           S  
ANISOU 2104  SD  MET A 288    11700  11752  15259   -511   -420     28       S  
ATOM   2105  CE  MET A 288      66.201  -3.485 -26.638  1.00 99.60           C  
ANISOU 2105  CE  MET A 288    11489  11691  14661   -423   -508   -100       C  
ATOM   2106  N   LEU A 289      62.926  -1.587 -31.820  1.00106.54           N  
ANISOU 2106  N   LEU A 289    12789  12115  15574   -316  -1051   1074       N  
ATOM   2107  CA  LEU A 289      61.654  -1.991 -32.433  1.00107.12           C  
ANISOU 2107  CA  LEU A 289    12925  12165  15609   -251  -1328   1203       C  
ATOM   2108  C   LEU A 289      61.877  -2.683 -33.777  1.00108.21           C  
ANISOU 2108  C   LEU A 289    13355  12459  15298   -271  -1433   1374       C  
ATOM   2109  O   LEU A 289      61.132  -3.592 -34.141  1.00108.04           O  
ANISOU 2109  O   LEU A 289    13424  12517  15106   -237  -1646   1366       O  
ATOM   2110  CB  LEU A 289      60.714  -0.792 -32.614  1.00109.41           C  
ANISOU 2110  CB  LEU A 289    13106  12176  16287   -211  -1481   1398       C  
ATOM   2111  CG  LEU A 289      59.668  -0.593 -31.513  1.00108.93           C  
ANISOU 2111  CG  LEU A 289    12769  11979  16639   -130  -1509   1222       C  
ATOM   2112  CD1 LEU A 289      59.089   0.813 -31.560  1.00111.71           C  
ANISOU 2112  CD1 LEU A 289    12987  12009  17446    -74  -1575   1373       C  
ATOM   2113  CD2 LEU A 289      58.561  -1.631 -31.632  1.00108.54           C  
ANISOU 2113  CD2 LEU A 289    12684  12029  16524    -82  -1728   1203       C  
ATOM   2114  N   GLN A 290      62.902  -2.244 -34.505  1.00109.71           N  
ANISOU 2114  N   GLN A 290    13697  12689  15297   -338  -1274   1521       N  
ATOM   2115  CA  GLN A 290      63.257  -2.842 -35.792  1.00111.35           C  
ANISOU 2115  CA  GLN A 290    14219  13063  15025   -362  -1301   1662       C  
ATOM   2116  C   GLN A 290      63.970  -4.190 -35.615  1.00109.59           C  
ANISOU 2116  C   GLN A 290    14066  13081  14492   -332  -1159   1403       C  
ATOM   2117  O   GLN A 290      63.888  -5.053 -36.490  1.00110.50           O  
ANISOU 2117  O   GLN A 290    14439  13326  14217   -313  -1250   1416       O  
ATOM   2118  CB  GLN A 290      64.113  -1.859 -36.609  1.00114.04           C  
ANISOU 2118  CB  GLN A 290    14687  13363  15276   -457  -1124   1924       C  
ATOM   2119  CG  GLN A 290      64.559  -2.337 -37.985  1.00116.41           C  
ANISOU 2119  CG  GLN A 290    15348  13845  15036   -495  -1083   2083       C  
ATOM   2120  CD  GLN A 290      63.378  -2.482 -38.938  1.00118.47           C  
ANISOU 2120  CD  GLN A 290    15856  14059  15095   -472  -1472   2292       C  
ATOM   2121  OE1 GLN A 290      62.438  -3.224 -38.663  1.00116.87           O  
ANISOU 2121  OE1 GLN A 290    15611  13859  14932   -401  -1736   2157       O  
ATOM   2122  NE2 GLN A 290      63.404  -1.743 -40.049  1.00122.26           N  
ANISOU 2122  NE2 GLN A 290    16590  14487  15375   -548  -1528   2642       N  
ATOM   2123  N   ASP A 291      64.668  -4.366 -34.492  1.00107.48           N  
ANISOU 2123  N   ASP A 291    13584  12854  14397   -325   -958   1165       N  
ATOM   2124  CA  ASP A 291      65.250  -5.667 -34.138  1.00105.81           C  
ANISOU 2124  CA  ASP A 291    13397  12828  13977   -272   -869    915       C  
ATOM   2125  C   ASP A 291      64.161  -6.722 -33.976  1.00104.67           C  
ANISOU 2125  C   ASP A 291    13313  12693  13763   -216  -1130    811       C  
ATOM   2126  O   ASP A 291      64.310  -7.851 -34.442  1.00104.61           O  
ANISOU 2126  O   ASP A 291    13492  12804  13448   -174  -1168    717       O  
ATOM   2127  CB  ASP A 291      66.064  -5.581 -32.839  1.00103.84           C  
ANISOU 2127  CB  ASP A 291    12891  12592  13969   -280   -684    704       C  
ATOM   2128  CG  ASP A 291      67.366  -4.823 -33.006  1.00104.99           C  
ANISOU 2128  CG  ASP A 291    12959  12764  14168   -351   -417    764       C  
ATOM   2129  OD1 ASP A 291      67.527  -4.107 -34.018  1.00107.37           O  
ANISOU 2129  OD1 ASP A 291    13380  13032  14382   -411   -351   1004       O  
ATOM   2130  OD2 ASP A 291      68.232  -4.940 -32.113  1.00103.67           O  
ANISOU 2130  OD2 ASP A 291    12607  12647  14136   -359   -284    587       O  
ATOM   2131  N   ILE A 292      63.073  -6.342 -33.308  1.00104.16           N  
ANISOU 2131  N   ILE A 292    13078  12489  14008   -217  -1293    819       N  
ATOM   2132  CA  ILE A 292      61.931  -7.232 -33.096  1.00103.77           C  
ANISOU 2132  CA  ILE A 292    13026  12428  13971   -194  -1535    749       C  
ATOM   2133  C   ILE A 292      61.236  -7.529 -34.426  1.00106.44           C  
ANISOU 2133  C   ILE A 292    13608  12767  14065   -199  -1807    923       C  
ATOM   2134  O   ILE A 292      60.824  -8.661 -34.675  1.00106.42           O  
ANISOU 2134  O   ILE A 292    13738  12823  13872   -194  -1976    836       O  
ATOM   2135  CB  ILE A 292      60.918  -6.631 -32.090  1.00103.08           C  
ANISOU 2135  CB  ILE A 292    12659  12194  14312   -193  -1594    726       C  
ATOM   2136  CG1 ILE A 292      61.564  -6.489 -30.706  1.00101.11           C  
ANISOU 2136  CG1 ILE A 292    12226  11961  14228   -200  -1352    513       C  
ATOM   2137  CG2 ILE A 292      59.672  -7.503 -31.982  1.00103.04           C  
ANISOU 2137  CG2 ILE A 292    12616  12177  14355   -193  -1837    695       C  
ATOM   2138  CD1 ILE A 292      60.793  -5.613 -29.740  1.00101.22           C  
ANISOU 2138  CD1 ILE A 292    11992  11823  14642   -196  -1318    470       C  
ATOM   2139  N   ALA A 293      61.115  -6.511 -35.275  1.00109.17           N  
ANISOU 2139  N   ALA A 293    14033  13033  14412   -222  -1871   1176       N  
ATOM   2140  CA  ALA A 293      60.477  -6.661 -36.585  1.00112.23           C  
ANISOU 2140  CA  ALA A 293    14689  13419  14533   -240  -2167   1375       C  
ATOM   2141  C   ALA A 293      61.234  -7.630 -37.494  1.00113.32           C  
ANISOU 2141  C   ALA A 293    15182  13737  14135   -243  -2103   1300       C  
ATOM   2142  O   ALA A 293      60.618  -8.417 -38.212  1.00114.88           O  
ANISOU 2142  O   ALA A 293    15606  13965  14075   -253  -2378   1298       O  
ATOM   2143  CB  ALA A 293      60.334  -5.304 -37.260  1.00114.97           C  
ANISOU 2143  CB  ALA A 293    15069  13632  14979   -266  -2231   1691       C  
ATOM   2144  N   THR A 294      62.563  -7.564 -37.462  1.00113.02           N  
ANISOU 2144  N   THR A 294    15182  13809  13949   -235  -1741   1226       N  
ATOM   2145  CA  THR A 294      63.400  -8.478 -38.237  1.00114.33           C  
ANISOU 2145  CA  THR A 294    15646  14149  13645   -209  -1597   1111       C  
ATOM   2146  C   THR A 294      63.371  -9.885 -37.638  1.00112.51           C  
ANISOU 2146  C   THR A 294    15400  13966  13381   -144  -1638    810       C  
ATOM   2147  O   THR A 294      63.359 -10.877 -38.369  1.00114.03           O  
ANISOU 2147  O   THR A 294    15884  14226  13214   -117  -1729    706       O  
ATOM   2148  CB  THR A 294      64.862  -7.991 -38.297  1.00114.80           C  
ANISOU 2148  CB  THR A 294    15670  14310  13639   -214  -1166   1115       C  
ATOM   2149  OG1 THR A 294      64.893  -6.591 -38.597  1.00116.47           O  
ANISOU 2149  OG1 THR A 294    15835  14428  13991   -296  -1115   1404       O  
ATOM   2150  CG2 THR A 294      65.639  -8.751 -39.363  1.00117.26           C  
ANISOU 2150  CG2 THR A 294    16318  14797  13439   -180   -990   1044       C  
ATOM   2151  N   LEU A 295      63.367  -9.958 -36.308  1.00109.75           N  
ANISOU 2151  N   LEU A 295    14737  13568  13394   -125  -1574    673       N  
ATOM   2152  CA  LEU A 295      63.328 -11.230 -35.585  1.00108.06           C  
ANISOU 2152  CA  LEU A 295    14490  13371  13196    -78  -1618    425       C  
ATOM   2153  C   LEU A 295      62.010 -11.961 -35.832  1.00108.48           C  
ANISOU 2153  C   LEU A 295    14648  13345  13224   -115  -1993    426       C  
ATOM   2154  O   LEU A 295      62.004 -13.141 -36.183  1.00108.89           O  
ANISOU 2154  O   LEU A 295    14913  13417  13040    -90  -2096    278       O  
ATOM   2155  CB  LEU A 295      63.531 -10.983 -34.080  1.00105.49           C  
ANISOU 2155  CB  LEU A 295    13827  13009  13243    -76  -1485    325       C  
ATOM   2156  CG  LEU A 295      63.696 -12.151 -33.090  1.00103.75           C  
ANISOU 2156  CG  LEU A 295    13545  12803  13073    -36  -1484    103       C  
ATOM   2157  CD1 LEU A 295      62.366 -12.772 -32.684  1.00103.35           C  
ANISOU 2157  CD1 LEU A 295    13464  12659  13145    -89  -1756     90       C  
ATOM   2158  CD2 LEU A 295      64.647 -13.211 -33.633  1.00104.71           C  
ANISOU 2158  CD2 LEU A 295    13877  13010  12896     55  -1387    -46       C  
ATOM   2159  N   THR A 296      60.901 -11.249 -35.645  1.00108.51           N  
ANISOU 2159  N   THR A 296    14482  13241  13504   -173  -2199    586       N  
ATOM   2160  CA  THR A 296      59.564 -11.826 -35.798  1.00109.35           C  
ANISOU 2160  CA  THR A 296    14598  13264  13686   -228  -2571    610       C  
ATOM   2161  C   THR A 296      59.112 -11.903 -37.259  1.00112.48           C  
ANISOU 2161  C   THR A 296    15319  13661  13754   -262  -2867    747       C  
ATOM   2162  O   THR A 296      58.191 -12.653 -37.584  1.00113.78           O  
ANISOU 2162  O   THR A 296    15571  13774  13886   -317  -3207    725       O  
ATOM   2163  CB  THR A 296      58.514 -11.022 -35.005  1.00108.85           C  
ANISOU 2163  CB  THR A 296    14174  13081  14102   -261  -2664    721       C  
ATOM   2164  OG1 THR A 296      58.481  -9.669 -35.478  1.00110.18           O  
ANISOU 2164  OG1 THR A 296    14298  13194  14370   -249  -2657    944       O  
ATOM   2165  CG2 THR A 296      58.837 -11.035 -33.513  1.00106.14           C  
ANISOU 2165  CG2 THR A 296    13557  12742  14029   -245  -2395    563       C  
ATOM   2166  N   GLY A 297      59.751 -11.125 -38.131  1.00113.94           N  
ANISOU 2166  N   GLY A 297    15693  13905  13693   -248  -2750    897       N  
ATOM   2167  CA  GLY A 297      59.409 -11.112 -39.550  1.00117.38           C  
ANISOU 2167  CA  GLY A 297    16496  14361  13741   -290  -3018   1049       C  
ATOM   2168  C   GLY A 297      58.155 -10.302 -39.820  1.00118.98           C  
ANISOU 2168  C   GLY A 297    16576  14432  14200   -343  -3401   1319       C  
ATOM   2169  O   GLY A 297      57.196 -10.803 -40.408  1.00121.14           O  
ANISOU 2169  O   GLY A 297    16978  14660  14388   -399  -3823   1359       O  
ATOM   2170  N   GLY A 298      58.172  -9.045 -39.382  1.00118.19           N  
ANISOU 2170  N   GLY A 298    16213  14250  14443   -324  -3271   1497       N  
ATOM   2171  CA  GLY A 298      57.056  -8.120 -39.582  1.00120.09           C  
ANISOU 2171  CA  GLY A 298    16288  14332  15008   -339  -3602   1768       C  
ATOM   2172  C   GLY A 298      57.540  -6.774 -40.087  1.00121.72           C  
ANISOU 2172  C   GLY A 298    16565  14484  15198   -334  -3483   2046       C  
ATOM   2173  O   GLY A 298      58.600  -6.684 -40.710  1.00122.61           O  
ANISOU 2173  O   GLY A 298    16969  14714  14901   -355  -3236   2078       O  
ATOM   2174  N   THR A 299      56.762  -5.727 -39.818  1.00122.48           N  
ANISOU 2174  N   THR A 299    16385  14388  15762   -305  -3645   2251       N  
ATOM   2175  CA  THR A 299      57.103  -4.369 -40.246  1.00124.39           C  
ANISOU 2175  CA  THR A 299    16674  14514  16074   -305  -3574   2548       C  
ATOM   2176  C   THR A 299      56.682  -3.341 -39.196  1.00123.31           C  
ANISOU 2176  C   THR A 299    16091  14158  16604   -233  -3489   2569       C  
ATOM   2177  O   THR A 299      55.610  -3.454 -38.598  1.00122.95           O  
ANISOU 2177  O   THR A 299    15731  14009  16975   -180  -3687   2505       O  
ATOM   2178  CB  THR A 299      56.428  -4.010 -41.586  1.00128.96           C  
ANISOU 2178  CB  THR A 299    17546  15030  16422   -343  -4032   2901       C  
ATOM   2179  OG1 THR A 299      56.618  -5.075 -42.526  1.00130.31           O  
ANISOU 2179  OG1 THR A 299    18147  15397  15966   -409  -4166   2831       O  
ATOM   2180  CG2 THR A 299      57.010  -2.722 -42.159  1.00131.40           C  
ANISOU 2180  CG2 THR A 299    18007  15238  16680   -370  -3914   3233       C  
ATOM   2181  N   VAL A 300      57.532  -2.338 -38.986  1.00123.15           N  
ANISOU 2181  N   VAL A 300    16042  14059  16689   -239  -3180   2649       N  
ATOM   2182  CA  VAL A 300      57.260  -1.274 -38.022  1.00122.57           C  
ANISOU 2182  CA  VAL A 300    15597  13750  17224   -172  -3068   2643       C  
ATOM   2183  C   VAL A 300      56.336  -0.235 -38.657  1.00126.43           C  
ANISOU 2183  C   VAL A 300    16051  13977  18009   -124  -3432   3002       C  
ATOM   2184  O   VAL A 300      56.528   0.154 -39.812  1.00129.57           O  
ANISOU 2184  O   VAL A 300    16770  14356  18102   -181  -3598   3323       O  
ATOM   2185  CB  VAL A 300      58.563  -0.594 -37.538  1.00121.33           C  
ANISOU 2185  CB  VAL A 300    15426  13579  17092   -217  -2626   2577       C  
ATOM   2186  CG1 VAL A 300      58.260   0.508 -36.528  1.00121.16           C  
ANISOU 2186  CG1 VAL A 300    15057  13287  17690   -150  -2527   2530       C  
ATOM   2187  CG2 VAL A 300      59.507  -1.619 -36.923  1.00117.83           C  
ANISOU 2187  CG2 VAL A 300    14998  13387  16384   -249  -2307   2242       C  
ATOM   2188  N   ILE A 301      55.340   0.208 -37.892  1.00126.42           N  
ANISOU 2188  N   ILE A 301    15659  13770  18603    -14  -3544   2952       N  
ATOM   2189  CA  ILE A 301      54.365   1.194 -38.355  1.00130.28           C  
ANISOU 2189  CA  ILE A 301    16029  13970  19498     72  -3907   3270       C  
ATOM   2190  C   ILE A 301      54.569   2.504 -37.592  1.00130.55           C  
ANISOU 2190  C   ILE A 301    15822  13713  20065    149  -3665   3265       C  
ATOM   2191  O   ILE A 301      54.032   2.687 -36.498  1.00129.37           O  
ANISOU 2191  O   ILE A 301    15293  13447  20413    255  -3537   3027       O  
ATOM   2192  CB  ILE A 301      52.919   0.682 -38.164  1.00131.18           C  
ANISOU 2192  CB  ILE A 301    15839  14047  19955    159  -4264   3225       C  
ATOM   2193  CG1 ILE A 301      52.732  -0.663 -38.878  1.00130.94           C  
ANISOU 2193  CG1 ILE A 301    16060  14281  19408     60  -4521   3195       C  
ATOM   2194  CG2 ILE A 301      51.911   1.696 -38.693  1.00135.88           C  
ANISOU 2194  CG2 ILE A 301    16283  14333  21011    271  -4680   3573       C  
ATOM   2195  CD1 ILE A 301      51.509  -1.432 -38.428  1.00130.92           C  
ANISOU 2195  CD1 ILE A 301    15719  14296  19727     96  -4761   3052       C  
ATOM   2196  N   SER A 302      55.355   3.405 -38.180  1.00132.42           N  
ANISOU 2196  N   SER A 302    16300  13828  20186     84  -3588   3521       N  
ATOM   2197  CA  SER A 302      55.679   4.695 -37.571  1.00133.21           C  
ANISOU 2197  CA  SER A 302    16234  13616  20764    127  -3373   3534       C  
ATOM   2198  C   SER A 302      54.935   5.841 -38.256  1.00138.30           C  
ANISOU 2198  C   SER A 302    16868  13890  21788    215  -3738   3945       C  
ATOM   2199  O   SER A 302      54.680   5.792 -39.461  1.00141.33           O  
ANISOU 2199  O   SER A 302    17532  14296  21871    172  -4096   4314       O  
ATOM   2200  CB  SER A 302      57.187   4.944 -37.650  1.00131.98           C  
ANISOU 2200  CB  SER A 302    16319  13550  20275    -34  -2996   3530       C  
ATOM   2201  OG  SER A 302      57.638   4.921 -38.994  1.00134.43           O  
ANISOU 2201  OG  SER A 302    17039  13961  20077   -156  -3125   3893       O  
ATOM   2202  N   GLU A 303      54.596   6.870 -37.481  1.00139.56           N  
ANISOU 2202  N   GLU A 303    16724  13696  22603    343  -3657   3876       N  
ATOM   2203  CA  GLU A 303      53.966   8.080 -38.021  1.00144.68           C  
ANISOU 2203  CA  GLU A 303    17338  13923  23710    451  -3980   4258       C  
ATOM   2204  C   GLU A 303      54.949   8.929 -38.834  1.00147.17           C  
ANISOU 2204  C   GLU A 303    18027  14097  23793    296  -3933   4627       C  
ATOM   2205  O   GLU A 303      54.535   9.671 -39.725  1.00151.80           O  
ANISOU 2205  O   GLU A 303    18755  14421  24500    326  -4293   5077       O  
ATOM   2206  CB  GLU A 303      53.364   8.938 -36.898  1.00145.51           C  
ANISOU 2206  CB  GLU A 303    17011  13664  24610    650  -3857   4026       C  
ATOM   2207  CG  GLU A 303      52.099   8.372 -36.269  1.00145.14           C  
ANISOU 2207  CG  GLU A 303    16546  13660  24937    835  -3974   3784       C  
ATOM   2208  CD  GLU A 303      51.401   9.372 -35.366  1.00147.46           C  
ANISOU 2208  CD  GLU A 303    16434  13546  26047   1062  -3880   3618       C  
ATOM   2209  OE1 GLU A 303      52.094  10.078 -34.603  1.00146.73           O  
ANISOU 2209  OE1 GLU A 303    16336  13275  26138   1049  -3520   3400       O  
ATOM   2210  OE2 GLU A 303      50.157   9.451 -35.414  1.00150.37           O  
ANISOU 2210  OE2 GLU A 303    16478  13764  26892   1257  -4169   3690       O  
ATOM   2211  N   GLU A 304      56.240   8.820 -38.521  1.00144.45           N  
ANISOU 2211  N   GLU A 304    17828  13919  23135    124  -3499   4455       N  
ATOM   2212  CA  GLU A 304      57.277   9.632 -39.168  1.00146.80           C  
ANISOU 2212  CA  GLU A 304    18432  14092  23253    -55  -3366   4776       C  
ATOM   2213  C   GLU A 304      57.394   9.359 -40.667  1.00149.79           C  
ANISOU 2213  C   GLU A 304    19253  14638  23022   -179  -3620   5236       C  
ATOM   2214  O   GLU A 304      57.422  10.293 -41.470  1.00154.50           O  
ANISOU 2214  O   GLU A 304    20066  14965  23670   -234  -3804   5698       O  
ATOM   2215  CB  GLU A 304      58.637   9.401 -38.501  1.00143.17           C  
ANISOU 2215  CB  GLU A 304    17982  13833  22580   -220  -2852   4463       C  
ATOM   2216  CG  GLU A 304      58.725   9.922 -37.075  1.00141.23           C  
ANISOU 2216  CG  GLU A 304    17389  13370  22899   -145  -2595   4055       C  
ATOM   2217  CD  GLU A 304      60.133   9.862 -36.510  1.00138.63           C  
ANISOU 2217  CD  GLU A 304    17085  13192  22393   -334  -2159   3815       C  
ATOM   2218  OE1 GLU A 304      60.958   9.077 -37.024  1.00137.00           O  
ANISOU 2218  OE1 GLU A 304    17082  13351  21620   -481  -2008   3848       O  
ATOM   2219  OE2 GLU A 304      60.413  10.597 -35.541  1.00138.44           O  
ANISOU 2219  OE2 GLU A 304    16870  12915  22814   -332  -1975   3577       O  
ATOM   2220  N   ILE A 305      57.465   8.082 -41.033  1.00147.51           N  
ANISOU 2220  N   ILE A 305    19122  14781  22144   -229  -3628   5107       N  
ATOM   2221  CA  ILE A 305      57.569   7.681 -42.439  1.00150.46           C  
ANISOU 2221  CA  ILE A 305    19958  15359  21848   -348  -3852   5475       C  
ATOM   2222  C   ILE A 305      56.243   7.916 -43.169  1.00154.79           C  
ANISOU 2222  C   ILE A 305    20548  15715  22549   -225  -4477   5823       C  
ATOM   2223  O   ILE A 305      56.235   8.254 -44.354  1.00159.35           O  
ANISOU 2223  O   ILE A 305    21518  16252  22773   -316  -4748   6289       O  
ATOM   2224  CB  ILE A 305      57.995   6.200 -42.578  1.00147.02           C  
ANISOU 2224  CB  ILE A 305    19682  15413  20765   -416  -3688   5180       C  
ATOM   2225  CG1 ILE A 305      59.391   5.989 -41.977  1.00143.55           C  
ANISOU 2225  CG1 ILE A 305    19211  15164  20166   -537  -3100   4891       C  
ATOM   2226  CG2 ILE A 305      57.991   5.771 -44.042  1.00150.61           C  
ANISOU 2226  CG2 ILE A 305    20647  16070  20507   -524  -3943   5522       C  
ATOM   2227  CD1 ILE A 305      59.747   4.539 -41.724  1.00139.46           C  
ANISOU 2227  CD1 ILE A 305    18712  15057  19218   -542  -2912   4496       C  
ATOM   2228  N   GLY A 306      55.132   7.741 -42.455  1.00153.78           N  
ANISOU 2228  N   GLY A 306    20009  15471  22949    -25  -4704   5605       N  
ATOM   2229  CA  GLY A 306      53.796   7.952 -43.012  1.00158.01           C  
ANISOU 2229  CA  GLY A 306    20468  15806  23759    116  -5320   5899       C  
ATOM   2230  C   GLY A 306      53.037   6.651 -43.185  1.00156.73           C  
ANISOU 2230  C   GLY A 306    20267  15953  23327    144  -5604   5717       C  
ATOM   2231  O   GLY A 306      52.566   6.337 -44.279  1.00160.14           O  
ANISOU 2231  O   GLY A 306    20996  16468  23379     97  -6072   6020       O  
ATOM   2232  N   MET A 307      52.923   5.897 -42.094  1.00152.14           N  
ANISOU 2232  N   MET A 307    19337  15531  22936    204  -5331   5227       N  
ATOM   2233  CA  MET A 307      52.201   4.628 -42.079  1.00150.65           C  
ANISOU 2233  CA  MET A 307    19054  15608  22578    217  -5554   5011       C  
ATOM   2234  C   MET A 307      51.192   4.643 -40.935  1.00149.22           C  
ANISOU 2234  C   MET A 307    18270  15273  23150    403  -5557   4734       C  
ATOM   2235  O   MET A 307      51.536   4.996 -39.806  1.00146.39           O  
ANISOU 2235  O   MET A 307    17639  14829  23154    463  -5117   4441       O  
ATOM   2236  CB  MET A 307      53.180   3.465 -41.905  1.00146.38           C  
ANISOU 2236  CB  MET A 307    18737  15468  21411     72  -5160   4674       C  
ATOM   2237  CG  MET A 307      54.079   3.226 -43.109  1.00148.21           C  
ANISOU 2237  CG  MET A 307    19559  15909  20842   -102  -5147   4903       C  
ATOM   2238  SD  MET A 307      55.285   1.910 -42.842  1.00143.55           S  
ANISOU 2238  SD  MET A 307    19176  15750  19616   -226  -4640   4477       S  
ATOM   2239  CE  MET A 307      56.583   2.795 -41.984  1.00140.94           C  
ANISOU 2239  CE  MET A 307    18708  15324  19516   -260  -4010   4365       C  
ATOM   2240  N   GLU A 308      49.953   4.260 -41.235  1.00151.46           N  
ANISOU 2240  N   GLU A 308    18352  15531  23663    482  -6050   4825       N  
ATOM   2241  CA  GLU A 308      48.857   4.322 -40.267  1.00151.28           C  
ANISOU 2241  CA  GLU A 308    17722  15353  24403    663  -6078   4616       C  
ATOM   2242  C   GLU A 308      48.415   2.930 -39.820  1.00148.30           C  
ANISOU 2242  C   GLU A 308    17171  15278  23896    603  -6057   4284       C  
ATOM   2243  O   GLU A 308      48.555   1.957 -40.563  1.00147.87           O  
ANISOU 2243  O   GLU A 308    17451  15484  23249    453  -6273   4316       O  
ATOM   2244  CB  GLU A 308      47.670   5.070 -40.875  1.00157.17           C  
ANISOU 2244  CB  GLU A 308    18254  15779  25685    819  -6674   5000       C  
ATOM   2245  CG  GLU A 308      47.979   6.511 -41.255  1.00160.65           C  
ANISOU 2245  CG  GLU A 308    18827  15845  26366    899  -6731   5356       C  
ATOM   2246  CD  GLU A 308      46.781   7.246 -41.831  1.00166.88           C  
ANISOU 2246  CD  GLU A 308    19381  16287  27736   1081  -7357   5750       C  
ATOM   2247  OE1 GLU A 308      45.841   6.583 -42.319  1.00169.04           O  
ANISOU 2247  OE1 GLU A 308    19537  16666  28023   1086  -7858   5847       O  
ATOM   2248  OE2 GLU A 308      46.782   8.494 -41.798  1.00169.86           O  
ANISOU 2248  OE2 GLU A 308    19686  16266  28585   1217  -7372   5968       O  
ATOM   2249  N   LEU A 309      47.879   2.849 -38.602  1.00146.56           N  
ANISOU 2249  N   LEU A 309    16445  15010  24230    715  -5785   3963       N  
ATOM   2250  CA  LEU A 309      47.359   1.591 -38.054  1.00144.27           C  
ANISOU 2250  CA  LEU A 309    15930  14966  23918    654  -5741   3666       C  
ATOM   2251  C   LEU A 309      46.067   1.149 -38.742  1.00148.25           C  
ANISOU 2251  C   LEU A 309    16236  15448  24643    665  -6365   3870       C  
ATOM   2252  O   LEU A 309      45.739  -0.039 -38.740  1.00147.04           O  
ANISOU 2252  O   LEU A 309    16065  15520  24282    542  -6475   3721       O  
ATOM   2253  CB  LEU A 309      47.115   1.710 -36.542  1.00142.03           C  
ANISOU 2253  CB  LEU A 309    15169  14633  24162    762  -5248   3292       C  
ATOM   2254  CG  LEU A 309      48.325   1.931 -35.628  1.00137.72           C  
ANISOU 2254  CG  LEU A 309    14769  14149  23410    728  -4632   3002       C  
ATOM   2255  CD1 LEU A 309      47.879   2.098 -34.182  1.00136.69           C  
ANISOU 2255  CD1 LEU A 309    14173  13949  23811    842  -4216   2653       C  
ATOM   2256  CD2 LEU A 309      49.325   0.786 -35.737  1.00133.52           C  
ANISOU 2256  CD2 LEU A 309    14634  13964  22132    529  -4457   2844       C  
ATOM   2257  N   GLU A 310      45.335   2.102 -39.318  1.00153.28           N  
ANISOU 2257  N   GLU A 310    16715  15794  25731    807  -6794   4215       N  
ATOM   2258  CA  GLU A 310      44.117   1.791 -40.068  1.00157.97           C  
ANISOU 2258  CA  GLU A 310    17116  16342  26563    818  -7474   4459       C  
ATOM   2259  C   GLU A 310      44.427   0.993 -41.337  1.00158.70           C  
ANISOU 2259  C   GLU A 310    17789  16655  25852    607  -7915   4647       C  
ATOM   2260  O   GLU A 310      43.654   0.118 -41.728  1.00160.36           O  
ANISOU 2260  O   GLU A 310    17918  16980  26032    516  -8349   4656       O  
ATOM   2261  CB  GLU A 310      43.349   3.068 -40.438  1.00163.80           C  
ANISOU 2261  CB  GLU A 310    17579  16688  27967   1037  -7865   4820       C  
ATOM   2262  CG  GLU A 310      42.624   3.742 -39.279  1.00164.78           C  
ANISOU 2262  CG  GLU A 310    17015  16564  29028   1281  -7565   4628       C  
ATOM   2263  CD  GLU A 310      43.465   4.792 -38.576  1.00162.96           C  
ANISOU 2263  CD  GLU A 310    16845  16134  28936   1395  -7009   4504       C  
ATOM   2264  OE1 GLU A 310      44.654   4.523 -38.300  1.00158.34           O  
ANISOU 2264  OE1 GLU A 310    16652  15743  27764   1248  -6560   4308       O  
ATOM   2265  OE2 GLU A 310      42.933   5.887 -38.295  1.00166.53           O  
ANISOU 2265  OE2 GLU A 310    16940  16218  30115   1636  -7033   4594       O  
ATOM   2266  N   LYS A 311      45.561   1.297 -41.967  1.00157.70           N  
ANISOU 2266  N   LYS A 311    18249  16588  25082    522  -7785   4784       N  
ATOM   2267  CA  LYS A 311      45.956   0.663 -43.227  1.00159.09           C  
ANISOU 2267  CA  LYS A 311    19047  16968  24431    333  -8143   4963       C  
ATOM   2268  C   LYS A 311      46.840  -0.579 -43.048  1.00154.20           C  
ANISOU 2268  C   LYS A 311    18757  16697  23134    158  -7763   4603       C  
ATOM   2269  O   LYS A 311      47.349  -1.120 -44.031  1.00155.08           O  
ANISOU 2269  O   LYS A 311    19430  16992  22500     10  -7937   4684       O  
ATOM   2270  CB  LYS A 311      46.682   1.681 -44.111  1.00161.73           C  
ANISOU 2270  CB  LYS A 311    19856  17177  24415    327  -8206   5348       C  
ATOM   2271  CG  LYS A 311      45.887   2.952 -44.372  1.00167.00           C  
ANISOU 2271  CG  LYS A 311    20262  17458  25732    506  -8616   5750       C  
ATOM   2272  CD  LYS A 311      46.467   3.760 -45.523  1.00170.81           C  
ANISOU 2272  CD  LYS A 311    21316  17838  25746    444  -8841   6218       C  
ATOM   2273  CE  LYS A 311      46.087   3.172 -46.873  1.00175.23           C  
ANISOU 2273  CE  LYS A 311    22336  18548  25694    298  -9517   6502       C  
ATOM   2274  NZ  LYS A 311      46.722   3.910 -47.998  1.00179.19           N  
ANISOU 2274  NZ  LYS A 311    23461  18986  25634    209  -9681   6965       N  
ATOM   2275  N   ALA A 312      47.019  -1.031 -41.808  1.00149.46           N  
ANISOU 2275  N   ALA A 312    17826  16179  22782    181  -7249   4207       N  
ATOM   2276  CA  ALA A 312      47.845  -2.206 -41.524  1.00144.96           C  
ANISOU 2276  CA  ALA A 312    17520  15902  21653     40  -6888   3864       C  
ATOM   2277  C   ALA A 312      47.098  -3.500 -41.846  1.00145.89           C  
ANISOU 2277  C   ALA A 312    17642  16163  21625    -82  -7287   3755       C  
ATOM   2278  O   ALA A 312      45.877  -3.575 -41.693  1.00148.44           O  
ANISOU 2278  O   ALA A 312    17530  16374  22495    -48  -7651   3811       O  
ATOM   2279  CB  ALA A 312      48.286  -2.199 -40.068  1.00140.13           C  
ANISOU 2279  CB  ALA A 312    16575  15311  21354    102  -6244   3514       C  
ATOM   2280  N   THR A 313      47.845  -4.511 -42.290  1.00144.15           N  
ANISOU 2280  N   THR A 313    17899  16174  20695   -226  -7210   3591       N  
ATOM   2281  CA  THR A 313      47.286  -5.820 -42.642  1.00145.14           C  
ANISOU 2281  CA  THR A 313    18119  16421  20604   -368  -7573   3451       C  
ATOM   2282  C   THR A 313      48.070  -6.941 -41.964  1.00140.46           C  
ANISOU 2282  C   THR A 313    17647  16021  19700   -444  -7103   3054       C  
ATOM   2283  O   THR A 313      49.115  -6.696 -41.360  1.00136.92           O  
ANISOU 2283  O   THR A 313    17259  15635  19127   -390  -6537   2911       O  
ATOM   2284  CB  THR A 313      47.305  -6.047 -44.166  1.00149.47           C  
ANISOU 2284  CB  THR A 313    19253  17033  20505   -477  -8108   3670       C  
ATOM   2285  OG1 THR A 313      48.622  -5.800 -44.676  1.00148.29           O  
ANISOU 2285  OG1 THR A 313    19646  17006  19689   -491  -7755   3692       O  
ATOM   2286  CG2 THR A 313      46.313  -5.126 -44.856  1.00154.99           C  
ANISOU 2286  CG2 THR A 313    19808  17530  21549   -420  -8720   4084       C  
ATOM   2287  N   LEU A 314      47.563  -8.168 -42.074  1.00141.00           N  
ANISOU 2287  N   LEU A 314    17747  16160  19665   -573  -7369   2886       N  
ATOM   2288  CA  LEU A 314      48.181  -9.339 -41.435  1.00137.09           C  
ANISOU 2288  CA  LEU A 314    17354  15805  18927   -646  -6997   2523       C  
ATOM   2289  C   LEU A 314      49.624  -9.603 -41.877  1.00135.11           C  
ANISOU 2289  C   LEU A 314    17672  15714  17949   -649  -6651   2399       C  
ATOM   2290  O   LEU A 314      50.418 -10.147 -41.106  1.00131.16           O  
ANISOU 2290  O   LEU A 314    17178  15304  17351   -636  -6180   2132       O  
ATOM   2291  CB  LEU A 314      47.335 -10.595 -41.683  1.00139.11           C  
ANISOU 2291  CB  LEU A 314    17606  16064  19182   -808  -7438   2405       C  
ATOM   2292  CG  LEU A 314      45.982 -10.658 -40.967  1.00140.47           C  
ANISOU 2292  CG  LEU A 314    17129  16113  20129   -837  -7649   2440       C  
ATOM   2293  CD1 LEU A 314      45.092 -11.727 -41.585  1.00144.04           C  
ANISOU 2293  CD1 LEU A 314    17640  16541  20547  -1028  -8246   2412       C  
ATOM   2294  CD2 LEU A 314      46.162 -10.908 -39.476  1.00136.09           C  
ANISOU 2294  CD2 LEU A 314    16189  15582  19934   -807  -7064   2206       C  
ATOM   2295  N   GLU A 315      49.957  -9.225 -43.109  1.00138.26           N  
ANISOU 2295  N   GLU A 315    18538  16148  17844   -665  -6881   2600       N  
ATOM   2296  CA  GLU A 315      51.314  -9.395 -43.629  1.00137.25           C  
ANISOU 2296  CA  GLU A 315    18937  16180  17029   -664  -6525   2505       C  
ATOM   2297  C   GLU A 315      52.330  -8.504 -42.908  1.00133.68           C  
ANISOU 2297  C   GLU A 315    18339  15742  16709   -556  -5917   2510       C  
ATOM   2298  O   GLU A 315      53.479  -8.903 -42.711  1.00131.08           O  
ANISOU 2298  O   GLU A 315    18210  15548  16044   -542  -5466   2301       O  
ATOM   2299  CB  GLU A 315      51.346  -9.104 -45.130  1.00142.36           C  
ANISOU 2299  CB  GLU A 315    20122  16865  17101   -722  -6907   2757       C  
ATOM   2300  CG  GLU A 315      52.672  -9.439 -45.797  1.00142.42           C  
ANISOU 2300  CG  GLU A 315    20707  17062  16343   -739  -6544   2635       C  
ATOM   2301  CD  GLU A 315      52.658  -9.202 -47.295  1.00148.08           C  
ANISOU 2301  CD  GLU A 315    22006  17835  16422   -816  -6911   2881       C  
ATOM   2302  OE1 GLU A 315      51.609  -8.784 -47.830  1.00152.08           O  
ANISOU 2302  OE1 GLU A 315    22479  18225  17080   -859  -7509   3162       O  
ATOM   2303  OE2 GLU A 315      53.702  -9.433 -47.938  1.00148.99           O  
ANISOU 2303  OE2 GLU A 315    22613  18116  15879   -833  -6599   2796       O  
ATOM   2304  N   ASP A 316      51.904  -7.301 -42.526  1.00133.90           N  
ANISOU 2304  N   ASP A 316    18011  15614  17251   -476  -5926   2740       N  
ATOM   2305  CA  ASP A 316      52.769  -6.359 -41.806  1.00130.97           C  
ANISOU 2305  CA  ASP A 316    17476  15211  17075   -389  -5402   2745       C  
ATOM   2306  C   ASP A 316      53.076  -6.845 -40.386  1.00125.99           C  
ANISOU 2306  C   ASP A 316    16504  14620  16745   -353  -4965   2409       C  
ATOM   2307  O   ASP A 316      54.156  -6.578 -39.855  1.00123.19           O  
ANISOU 2307  O   ASP A 316    16164  14326  16315   -320  -4490   2293       O  
ATOM   2308  CB  ASP A 316      52.122  -4.968 -41.745  1.00133.12           C  
ANISOU 2308  CB  ASP A 316    17452  15253  17871   -304  -5566   3057       C  
ATOM   2309  CG  ASP A 316      51.885  -4.365 -43.122  1.00138.12           C  
ANISOU 2309  CG  ASP A 316    18444  15827  18206   -338  -6003   3447       C  
ATOM   2310  OD1 ASP A 316      52.695  -4.617 -44.040  1.00139.35           O  
ANISOU 2310  OD1 ASP A 316    19124  16137  17685   -418  -5945   3495       O  
ATOM   2311  OD2 ASP A 316      50.887  -3.631 -43.283  1.00141.08           O  
ANISOU 2311  OD2 ASP A 316    18577  15998  19026   -279  -6401   3711       O  
ATOM   2312  N   LEU A 317      52.121  -7.548 -39.781  1.00125.16           N  
ANISOU 2312  N   LEU A 317    16092  14481  16981   -375  -5143   2271       N  
ATOM   2313  CA  LEU A 317      52.283  -8.098 -38.432  1.00121.01           C  
ANISOU 2313  CA  LEU A 317    15269  13994  16711   -363  -4771   1978       C  
ATOM   2314  C   LEU A 317      53.337  -9.203 -38.399  1.00118.42           C  
ANISOU 2314  C   LEU A 317    15269  13841  15884   -409  -4517   1720       C  
ATOM   2315  O   LEU A 317      53.349 -10.085 -39.260  1.00120.09           O  
ANISOU 2315  O   LEU A 317    15828  14122  15677   -478  -4762   1679       O  
ATOM   2316  CB  LEU A 317      50.949  -8.648 -37.907  1.00121.73           C  
ANISOU 2316  CB  LEU A 317    14977  14012  17263   -407  -5034   1929       C  
ATOM   2317  CG  LEU A 317      49.970  -7.667 -37.249  1.00122.84           C  
ANISOU 2317  CG  LEU A 317    14590  13982  18099   -320  -5058   2050       C  
ATOM   2318  CD1 LEU A 317      49.732  -6.409 -38.066  1.00126.19           C  
ANISOU 2318  CD1 LEU A 317    15039  14261  18646   -235  -5311   2371       C  
ATOM   2319  CD2 LEU A 317      48.643  -8.355 -36.974  1.00124.55           C  
ANISOU 2319  CD2 LEU A 317    14453  14152  18716   -391  -5357   2025       C  
ATOM   2320  N   GLY A 318      54.220  -9.143 -37.403  1.00114.65           N  
ANISOU 2320  N   GLY A 318    14680  13418  15464   -363  -4043   1539       N  
ATOM   2321  CA  GLY A 318      55.197 -10.203 -37.166  1.00112.07           C  
ANISOU 2321  CA  GLY A 318    14574  13230  14777   -378  -3792   1285       C  
ATOM   2322  C   GLY A 318      54.532 -11.398 -36.514  1.00110.90           C  
ANISOU 2322  C   GLY A 318    14290  13071  14775   -443  -3904   1103       C  
ATOM   2323  O   GLY A 318      53.359 -11.334 -36.137  1.00111.68           O  
ANISOU 2323  O   GLY A 318    14075  13074  15282   -483  -4111   1167       O  
ATOM   2324  N   GLN A 319      55.277 -12.490 -36.375  1.00109.23           N  
ANISOU 2324  N   GLN A 319    14296  12944  14260   -453  -3761    885       N  
ATOM   2325  CA  GLN A 319      54.728 -13.714 -35.800  1.00108.59           C  
ANISOU 2325  CA  GLN A 319    14140  12829  14288   -533  -3871    727       C  
ATOM   2326  C   GLN A 319      55.803 -14.574 -35.131  1.00105.81           C  
ANISOU 2326  C   GLN A 319    13908  12544  13748   -495  -3556    495       C  
ATOM   2327  O   GLN A 319      56.974 -14.543 -35.516  1.00105.27           O  
ANISOU 2327  O   GLN A 319    14081  12563  13352   -412  -3345    425       O  
ATOM   2328  CB  GLN A 319      53.999 -14.515 -36.885  1.00111.88           C  
ANISOU 2328  CB  GLN A 319    14806  13199  14504   -628  -4340    748       C  
ATOM   2329  CG  GLN A 319      53.185 -15.690 -36.363  1.00112.23           C  
ANISOU 2329  CG  GLN A 319    14728  13160  14753   -751  -4531    635       C  
ATOM   2330  CD  GLN A 319      52.243 -16.256 -37.410  1.00116.04           C  
ANISOU 2330  CD  GLN A 319    15377  13564  15147   -873  -5071    687       C  
ATOM   2331  OE1 GLN A 319      51.166 -15.711 -37.649  1.00118.23           O  
ANISOU 2331  OE1 GLN A 319    15411  13779  15731   -928  -5382    876       O  
ATOM   2332  NE2 GLN A 319      52.642 -17.360 -38.036  1.00117.20           N  
ANISOU 2332  NE2 GLN A 319    15937  13701  14892   -911  -5203    509       N  
ATOM   2333  N   ALA A 320      55.383 -15.333 -34.122  1.00104.35           N  
ANISOU 2333  N   ALA A 320    13538  12313  13794   -559  -3527    392       N  
ATOM   2334  CA  ALA A 320      56.253 -16.262 -33.401  1.00102.21           C  
ANISOU 2334  CA  ALA A 320    13369  12071  13394   -531  -3301    198       C  
ATOM   2335  C   ALA A 320      55.432 -17.471 -32.953  1.00102.61           C  
ANISOU 2335  C   ALA A 320    13378  12019  13588   -661  -3497    136       C  
ATOM   2336  O   ALA A 320      54.230 -17.537 -33.221  1.00104.60           O  
ANISOU 2336  O   ALA A 320    13498  12194  14049   -776  -3790    236       O  
ATOM   2337  CB  ALA A 320      56.885 -15.569 -32.205  1.00 99.59           C  
ANISOU 2337  CB  ALA A 320    12802  11800  13235   -470  -2924    173       C  
ATOM   2338  N   LYS A 321      56.079 -18.426 -32.287  1.00100.94           N  
ANISOU 2338  N   LYS A 321    13269  11793  13290   -648  -3354    -10       N  
ATOM   2339  CA  LYS A 321      55.389 -19.622 -31.799  1.00101.54           C  
ANISOU 2339  CA  LYS A 321    13330  11746  13504   -788  -3518    -51       C  
ATOM   2340  C   LYS A 321      54.792 -19.434 -30.407  1.00100.27           C  
ANISOU 2340  C   LYS A 321    12814  11588  13696   -881  -3338     20       C  
ATOM   2341  O   LYS A 321      53.742 -20.006 -30.104  1.00101.80           O  
ANISOU 2341  O   LYS A 321    12864  11690  14125  -1045  -3496     76       O  
ATOM   2342  CB  LYS A 321      56.326 -20.832 -31.797  1.00101.35           C  
ANISOU 2342  CB  LYS A 321    13619  11661  13226   -728  -3487   -229       C  
ATOM   2343  CG  LYS A 321      56.702 -21.320 -33.187  1.00103.38           C  
ANISOU 2343  CG  LYS A 321    14263  11881  13134   -664  -3686   -345       C  
ATOM   2344  CD  LYS A 321      57.261 -22.733 -33.152  1.00104.05           C  
ANISOU 2344  CD  LYS A 321    14629  11829  13076   -631  -3730   -535       C  
ATOM   2345  CE  LYS A 321      57.571 -23.238 -34.551  1.00106.65           C  
ANISOU 2345  CE  LYS A 321    15369  12112  13039   -565  -3911   -692       C  
ATOM   2346  NZ  LYS A 321      58.107 -24.627 -34.536  1.00107.86           N  
ANISOU 2346  NZ  LYS A 321    15801  12090  13089   -508  -3953   -907       N  
ATOM   2347  N   ARG A 322      55.454 -18.646 -29.562  1.00 97.98           N  
ANISOU 2347  N   ARG A 322    12389  11402  13435   -790  -3004     11       N  
ATOM   2348  CA  ARG A 322      54.990 -18.436 -28.190  1.00 97.20           C  
ANISOU 2348  CA  ARG A 322    12007  11326  13598   -869  -2786     49       C  
ATOM   2349  C   ARG A 322      55.593 -17.170 -27.579  1.00 95.32           C  
ANISOU 2349  C   ARG A 322    11622  11198  13394   -760  -2477     35       C  
ATOM   2350  O   ARG A 322      56.690 -16.754 -27.957  1.00 94.17           O  
ANISOU 2350  O   ARG A 322    11625  11113  13043   -630  -2389    -19       O  
ATOM   2351  CB  ARG A 322      55.340 -19.659 -27.338  1.00 96.92           C  
ANISOU 2351  CB  ARG A 322    12105  11241  13479   -936  -2734    -13       C  
ATOM   2352  CG  ARG A 322      54.733 -19.668 -25.943  1.00 97.08           C  
ANISOU 2352  CG  ARG A 322    11892  11282  13711  -1064  -2528     42       C  
ATOM   2353  CD  ARG A 322      54.613 -21.086 -25.406  1.00 98.13           C  
ANISOU 2353  CD  ARG A 322    12168  11305  13811  -1200  -2609     55       C  
ATOM   2354  NE  ARG A 322      54.514 -21.129 -23.949  1.00 98.14           N  
ANISOU 2354  NE  ARG A 322    12061  11361  13866  -1293  -2342     98       N  
ATOM   2355  CZ  ARG A 322      55.545 -20.997 -23.113  1.00 96.81           C  
ANISOU 2355  CZ  ARG A 322    12006  11273  13505  -1206  -2148     41       C  
ATOM   2356  NH1 ARG A 322      56.780 -20.798 -23.568  1.00 95.22           N  
ANISOU 2356  NH1 ARG A 322    11975  11105  13095  -1018  -2169    -60       N  
ATOM   2357  NH2 ARG A 322      55.340 -21.057 -21.804  1.00 97.39           N  
ANISOU 2357  NH2 ARG A 322    12015  11400  13588  -1316  -1929     90       N  
ATOM   2358  N   VAL A 323      54.859 -16.558 -26.650  1.00 95.42           N  
ANISOU 2358  N   VAL A 323    11340  11230  13684   -819  -2304     76       N  
ATOM   2359  CA  VAL A 323      55.340 -15.386 -25.910  1.00 94.25           C  
ANISOU 2359  CA  VAL A 323    11059  11157  13593   -735  -2008     30       C  
ATOM   2360  C   VAL A 323      54.937 -15.467 -24.436  1.00 94.39           C  
ANISOU 2360  C   VAL A 323    10918  11211  13736   -827  -1756     -8       C  
ATOM   2361  O   VAL A 323      53.885 -16.013 -24.104  1.00 96.21           O  
ANISOU 2361  O   VAL A 323    11004  11404  14146   -959  -1783     52       O  
ATOM   2362  CB  VAL A 323      54.812 -14.058 -26.504  1.00 95.14           C  
ANISOU 2362  CB  VAL A 323    10970  11239  13938   -665  -2029    109       C  
ATOM   2363  CG1 VAL A 323      55.331 -13.855 -27.920  1.00 95.26           C  
ANISOU 2363  CG1 VAL A 323    11191  11240  13761   -582  -2240    168       C  
ATOM   2364  CG2 VAL A 323      53.291 -14.007 -26.482  1.00 97.43           C  
ANISOU 2364  CG2 VAL A 323    10963  11460  14594   -752  -2131    207       C  
ATOM   2365  N   VAL A 324      55.782 -14.919 -23.565  1.00 93.00           N  
ANISOU 2365  N   VAL A 324    10774  11109  13453   -772  -1512   -107       N  
ATOM   2366  CA  VAL A 324      55.524 -14.890 -22.125  1.00 93.43           C  
ANISOU 2366  CA  VAL A 324    10738  11218  13541   -855  -1249   -164       C  
ATOM   2367  C   VAL A 324      55.745 -13.466 -21.611  1.00 93.33           C  
ANISOU 2367  C   VAL A 324    10591  11236  13631   -773  -1009   -264       C  
ATOM   2368  O   VAL A 324      56.709 -12.807 -22.003  1.00 92.03           O  
ANISOU 2368  O   VAL A 324    10512  11078  13378   -667  -1024   -312       O  
ATOM   2369  CB  VAL A 324      56.446 -15.866 -21.363  1.00 92.59           C  
ANISOU 2369  CB  VAL A 324    10886  11160  13132   -896  -1232   -207       C  
ATOM   2370  CG1 VAL A 324      56.118 -15.869 -19.876  1.00 93.67           C  
ANISOU 2370  CG1 VAL A 324    10980  11365  13242  -1007   -972   -243       C  
ATOM   2371  CG2 VAL A 324      56.330 -17.273 -21.935  1.00 92.92           C  
ANISOU 2371  CG2 VAL A 324    11091  11122  13089   -958  -1486   -126       C  
ATOM   2372  N   ILE A 325      54.849 -12.997 -20.741  1.00 95.01           N  
ANISOU 2372  N   ILE A 325    10593  11459  14046   -826   -774   -303       N  
ATOM   2373  CA  ILE A 325      54.907 -11.626 -20.222  1.00 95.55           C  
ANISOU 2373  CA  ILE A 325    10531  11517  14254   -744   -536   -430       C  
ATOM   2374  C   ILE A 325      54.720 -11.595 -18.701  1.00 96.92           C  
ANISOU 2374  C   ILE A 325    10705  11774  14344   -828   -213   -562       C  
ATOM   2375  O   ILE A 325      53.643 -11.910 -18.197  1.00 98.90           O  
ANISOU 2375  O   ILE A 325    10792  12042  14742   -920    -57   -533       O  
ATOM   2376  CB  ILE A 325      53.839 -10.721 -20.879  1.00 97.25           C  
ANISOU 2376  CB  ILE A 325    10438  11620  14890   -669   -551   -371       C  
ATOM   2377  CG1 ILE A 325      53.885 -10.844 -22.409  1.00 96.69           C  
ANISOU 2377  CG1 ILE A 325    10405  11478  14855   -613   -903   -210       C  
ATOM   2378  CG2 ILE A 325      54.040  -9.268 -20.460  1.00 97.89           C  
ANISOU 2378  CG2 ILE A 325    10422  11640  15132   -560   -335   -513       C  
ATOM   2379  CD1 ILE A 325      52.730 -10.177 -23.126  1.00 98.90           C  
ANISOU 2379  CD1 ILE A 325    10389  11639  15547   -556  -1016    -97       C  
ATOM   2380  N   ASN A 326      55.773 -11.202 -17.984  1.00 96.27           N  
ANISOU 2380  N   ASN A 326    10808  11747  14020   -809   -113   -706       N  
ATOM   2381  CA  ASN A 326      55.727 -11.041 -16.529  1.00 97.92           C  
ANISOU 2381  CA  ASN A 326    11086  12043  14075   -887    179   -858       C  
ATOM   2382  C   ASN A 326      55.285  -9.627 -16.139  1.00 99.63           C  
ANISOU 2382  C   ASN A 326    11120  12194  14539   -806    444  -1037       C  
ATOM   2383  O   ASN A 326      54.954  -8.810 -17.002  1.00 99.61           O  
ANISOU 2383  O   ASN A 326    10918  12063  14866   -689    382  -1010       O  
ATOM   2384  CB  ASN A 326      57.106 -11.328 -15.919  1.00 96.83           C  
ANISOU 2384  CB  ASN A 326    11252  11988  13550   -913     99   -932       C  
ATOM   2385  CG  ASN A 326      57.589 -12.741 -16.187  1.00 95.79           C  
ANISOU 2385  CG  ASN A 326    11307  11893  13194   -968   -146   -775       C  
ATOM   2386  OD1 ASN A 326      58.672 -12.942 -16.736  1.00 94.18           O  
ANISOU 2386  OD1 ASN A 326    11222  11680  12879   -897   -363   -756       O  
ATOM   2387  ND2 ASN A 326      56.791 -13.728 -15.791  1.00 97.19           N  
ANISOU 2387  ND2 ASN A 326    11501  12097  13327  -1097    -99   -663       N  
ATOM   2388  N   LYS A 327      55.279  -9.352 -14.835  1.00101.45           N  
ANISOU 2388  N   LYS A 327    11446  12501  14599   -867    731  -1221       N  
ATOM   2389  CA  LYS A 327      55.021  -8.008 -14.305  1.00103.38           C  
ANISOU 2389  CA  LYS A 327    11583  12668  15025   -785   1004  -1456       C  
ATOM   2390  C   LYS A 327      55.983  -6.961 -14.876  1.00101.68           C  
ANISOU 2390  C   LYS A 327    11404  12325  14902   -671    843  -1537       C  
ATOM   2391  O   LYS A 327      55.612  -5.797 -15.027  1.00102.92           O  
ANISOU 2391  O   LYS A 327    11390  12329  15385   -560    963  -1651       O  
ATOM   2392  CB  LYS A 327      55.111  -8.021 -12.771  1.00105.80           C  
ANISOU 2392  CB  LYS A 327    12101  13103  14995   -892   1304  -1662       C  
ATOM   2393  CG  LYS A 327      54.799  -6.693 -12.092  1.00108.69           C  
ANISOU 2393  CG  LYS A 327    12398  13385  15514   -813   1628  -1961       C  
ATOM   2394  CD  LYS A 327      54.815  -6.826 -10.574  1.00111.60           C  
ANISOU 2394  CD  LYS A 327    13024  13907  15472   -939   1936  -2166       C  
ATOM   2395  CE  LYS A 327      54.753  -5.472  -9.885  1.00114.52           C  
ANISOU 2395  CE  LYS A 327    13408  14175  15927   -856   2224  -2524       C  
ATOM   2396  NZ  LYS A 327      53.438  -4.797 -10.063  1.00117.20           N  
ANISOU 2396  NZ  LYS A 327    13376  14391  16763   -723   2549  -2603       N  
ATOM   2397  N   ASP A 328      57.211  -7.375 -15.189  1.00 99.00           N  
ANISOU 2397  N   ASP A 328    11271  12035  14308   -697    580  -1472       N  
ATOM   2398  CA  ASP A 328      58.224  -6.463 -15.723  1.00 97.67           C  
ANISOU 2398  CA  ASP A 328    11131  11761  14217   -624    438  -1524       C  
ATOM   2399  C   ASP A 328      59.186  -7.145 -16.713  1.00 94.63           C  
ANISOU 2399  C   ASP A 328    10832  11415  13705   -616    128  -1335       C  
ATOM   2400  O   ASP A 328      60.383  -6.853 -16.727  1.00 93.80           O  
ANISOU 2400  O   ASP A 328    10834  11315  13489   -619     20  -1388       O  
ATOM   2401  CB  ASP A 328      58.987  -5.800 -14.556  1.00 99.10           C  
ANISOU 2401  CB  ASP A 328    11490  11959  14202   -677    556  -1791       C  
ATOM   2402  CG  ASP A 328      59.447  -6.799 -13.489  1.00 99.38           C  
ANISOU 2402  CG  ASP A 328    11784  12188  13785   -808    543  -1827       C  
ATOM   2403  OD1 ASP A 328      59.255  -8.017 -13.675  1.00 98.33           O  
ANISOU 2403  OD1 ASP A 328    11693  12157  13509   -854    443  -1635       O  
ATOM   2404  OD2 ASP A 328      59.999  -6.362 -12.451  1.00100.93           O  
ANISOU 2404  OD2 ASP A 328    12161  12420  13765   -872    612  -2045       O  
ATOM   2405  N   THR A 329      58.651  -8.038 -17.548  1.00 93.24           N  
ANISOU 2405  N   THR A 329    10599  11260  13565   -606     -5  -1129       N  
ATOM   2406  CA  THR A 329      59.445  -8.745 -18.562  1.00 90.84           C  
ANISOU 2406  CA  THR A 329    10389  10986  13139   -581   -266   -972       C  
ATOM   2407  C   THR A 329      58.565  -9.241 -19.713  1.00 90.19           C  
ANISOU 2407  C   THR A 329    10201  10856  13209   -548   -405   -778       C  
ATOM   2408  O   THR A 329      57.429  -9.654 -19.491  1.00 91.31           O  
ANISOU 2408  O   THR A 329    10235  10998  13459   -592   -345   -735       O  
ATOM   2409  CB  THR A 329      60.165  -9.974 -17.962  1.00 90.17           C  
ANISOU 2409  CB  THR A 329    10515  11033  12711   -652   -359   -966       C  
ATOM   2410  OG1 THR A 329      60.859  -9.603 -16.764  1.00 91.15           O  
ANISOU 2410  OG1 THR A 329    10754  11216  12663   -705   -267  -1140       O  
ATOM   2411  CG2 THR A 329      61.160 -10.564 -18.952  1.00 88.51           C  
ANISOU 2411  CG2 THR A 329    10390  10838  12400   -592   -586   -860       C  
ATOM   2412  N   THR A 330      59.098  -9.198 -20.934  1.00 88.66           N  
ANISOU 2412  N   THR A 330    10041  10626  13017   -482   -588   -662       N  
ATOM   2413  CA  THR A 330      58.442  -9.789 -22.107  1.00 88.22           C  
ANISOU 2413  CA  THR A 330     9962  10538  13019   -463   -784   -486       C  
ATOM   2414  C   THR A 330      59.441 -10.664 -22.859  1.00 86.76           C  
ANISOU 2414  C   THR A 330     9982  10414  12568   -441   -957   -430       C  
ATOM   2415  O   THR A 330      60.571 -10.246 -23.108  1.00 86.18           O  
ANISOU 2415  O   THR A 330     9977  10361  12405   -395   -942   -461       O  
ATOM   2416  CB  THR A 330      57.894  -8.712 -23.063  1.00 88.97           C  
ANISOU 2416  CB  THR A 330     9906  10503  13394   -387   -838   -384       C  
ATOM   2417  OG1 THR A 330      56.862  -7.970 -22.405  1.00 90.61           O  
ANISOU 2417  OG1 THR A 330     9889  10629  13908   -377   -676   -445       O  
ATOM   2418  CG2 THR A 330      57.314  -9.339 -24.330  1.00 89.14           C  
ANISOU 2418  CG2 THR A 330     9951  10501  13414   -379  -1098   -202       C  
ATOM   2419  N   THR A 331      59.009 -11.870 -23.224  1.00 86.56           N  
ANISOU 2419  N   THR A 331    10040  10404  12443   -477  -1111   -356       N  
ATOM   2420  CA  THR A 331      59.862 -12.838 -23.907  1.00 85.62           C  
ANISOU 2420  CA  THR A 331    10128  10321  12082   -440  -1262   -335       C  
ATOM   2421  C   THR A 331      59.198 -13.298 -25.203  1.00 86.25           C  
ANISOU 2421  C   THR A 331    10261  10344  12166   -432  -1479   -218       C  
ATOM   2422  O   THR A 331      58.014 -13.631 -25.211  1.00 87.20           O  
ANISOU 2422  O   THR A 331    10289  10413  12428   -506  -1570   -155       O  
ATOM   2423  CB  THR A 331      60.126 -14.063 -23.007  1.00 85.35           C  
ANISOU 2423  CB  THR A 331    10219  10329  11881   -496  -1278   -386       C  
ATOM   2424  OG1 THR A 331      60.682 -13.629 -21.758  1.00 85.09           O  
ANISOU 2424  OG1 THR A 331    10165  10356  11808   -519  -1114   -488       O  
ATOM   2425  CG2 THR A 331      61.092 -15.039 -23.671  1.00 84.95           C  
ANISOU 2425  CG2 THR A 331    10369  10284  11622   -421  -1420   -393       C  
ATOM   2426  N   ILE A 332      59.968 -13.308 -26.292  1.00 86.12           N  
ANISOU 2426  N   ILE A 332    10391  10341  11989   -354  -1558   -194       N  
ATOM   2427  CA  ILE A 332      59.492 -13.778 -27.596  1.00 87.22           C  
ANISOU 2427  CA  ILE A 332    10657  10438  12042   -347  -1782   -105       C  
ATOM   2428  C   ILE A 332      60.255 -15.045 -27.974  1.00 87.32           C  
ANISOU 2428  C   ILE A 332    10918  10471  11786   -306  -1863   -184       C  
ATOM   2429  O   ILE A 332      61.482 -15.027 -28.084  1.00 86.92           O  
ANISOU 2429  O   ILE A 332    10952  10483  11589   -217  -1745   -253       O  
ATOM   2430  CB  ILE A 332      59.681 -12.710 -28.693  1.00 87.84           C  
ANISOU 2430  CB  ILE A 332    10753  10510  12113   -290  -1797     -2       C  
ATOM   2431  CG1 ILE A 332      58.895 -11.444 -28.340  1.00 88.28           C  
ANISOU 2431  CG1 ILE A 332    10558  10496  12487   -307  -1739     76       C  
ATOM   2432  CG2 ILE A 332      59.223 -13.246 -30.046  1.00 89.43           C  
ANISOU 2432  CG2 ILE A 332    11145  10682  12149   -293  -2056     82       C  
ATOM   2433  CD1 ILE A 332      59.244 -10.239 -29.187  1.00 89.08           C  
ANISOU 2433  CD1 ILE A 332    10669  10562  12615   -255  -1719    195       C  
ATOM   2434  N   ILE A 333      59.518 -16.134 -28.188  1.00 88.41           N  
ANISOU 2434  N   ILE A 333    11154  10540  11897   -370  -2064   -178       N  
ATOM   2435  CA  ILE A 333      60.110 -17.457 -28.380  1.00 88.89           C  
ANISOU 2435  CA  ILE A 333    11450  10567  11755   -332  -2152   -275       C  
ATOM   2436  C   ILE A 333      59.864 -17.971 -29.798  1.00 90.87           C  
ANISOU 2436  C   ILE A 333    11931  10765  11830   -315  -2373   -278       C  
ATOM   2437  O   ILE A 333      58.717 -18.058 -30.242  1.00 92.15           O  
ANISOU 2437  O   ILE A 333    12072  10859  12080   -416  -2592   -198       O  
ATOM   2438  CB  ILE A 333      59.525 -18.471 -27.374  1.00 88.98           C  
ANISOU 2438  CB  ILE A 333    11441  10501  11864   -442  -2217   -281       C  
ATOM   2439  CG1 ILE A 333      59.605 -17.921 -25.945  1.00 87.86           C  
ANISOU 2439  CG1 ILE A 333    11106  10425  11850   -484  -2001   -274       C  
ATOM   2440  CG2 ILE A 333      60.268 -19.798 -27.455  1.00 89.42           C  
ANISOU 2440  CG2 ILE A 333    11741  10484  11749   -380  -2302   -380       C  
ATOM   2441  CD1 ILE A 333      58.648 -18.588 -24.983  1.00 88.59           C  
ANISOU 2441  CD1 ILE A 333    11130  10462  12068   -641  -2023   -221       C  
ATOM   2442  N   ASP A 334      60.951 -18.313 -30.492  1.00 91.64           N  
ANISOU 2442  N   ASP A 334    12242  10896  11679   -187  -2315   -379       N  
ATOM   2443  CA  ASP A 334      60.899 -18.911 -31.831  1.00 94.02           C  
ANISOU 2443  CA  ASP A 334    12836  11155  11731   -155  -2489   -434       C  
ATOM   2444  C   ASP A 334      60.178 -18.007 -32.838  1.00 95.56           C  
ANISOU 2444  C   ASP A 334    13046  11380  11880   -209  -2619   -295       C  
ATOM   2445  O   ASP A 334      59.016 -18.233 -33.186  1.00 96.75           O  
ANISOU 2445  O   ASP A 334    13208  11448  12101   -323  -2904   -226       O  
ATOM   2446  CB  ASP A 334      60.258 -20.307 -31.772  1.00 95.25           C  
ANISOU 2446  CB  ASP A 334    13143  11151  11894   -231  -2741   -509       C  
ATOM   2447  CG  ASP A 334      60.658 -21.194 -32.946  1.00 97.59           C  
ANISOU 2447  CG  ASP A 334    13805  11384  11888   -149  -2861   -665       C  
ATOM   2448  OD1 ASP A 334      60.908 -20.671 -34.051  1.00 98.92           O  
ANISOU 2448  OD1 ASP A 334    14128  11637  11817    -94  -2840   -665       O  
ATOM   2449  OD2 ASP A 334      60.719 -22.427 -32.761  1.00 98.52           O  
ANISOU 2449  OD2 ASP A 334    14077  11355  11998   -141  -2972   -790       O  
ATOM   2450  N   GLY A 335      60.891 -16.985 -33.303  1.00 95.95           N  
ANISOU 2450  N   GLY A 335    13089  11540  11828   -135  -2427   -237       N  
ATOM   2451  CA  GLY A 335      60.348 -16.031 -34.264  1.00 97.86           C  
ANISOU 2451  CA  GLY A 335    13369  11803  12010   -175  -2542    -67       C  
ATOM   2452  C   GLY A 335      60.305 -16.586 -35.676  1.00101.14           C  
ANISOU 2452  C   GLY A 335    14164  12218  12045   -167  -2731   -103       C  
ATOM   2453  O   GLY A 335      61.165 -17.379 -36.066  1.00102.05           O  
ANISOU 2453  O   GLY A 335    14520  12362  11892    -76  -2621   -278       O  
ATOM   2454  N   VAL A 336      59.306 -16.154 -36.442  1.00103.56           N  
ANISOU 2454  N   VAL A 336    14528  12489  12330   -253  -3024     55       N  
ATOM   2455  CA  VAL A 336      59.104 -16.622 -37.817  1.00107.24           C  
ANISOU 2455  CA  VAL A 336    15393  12954  12399   -274  -3273     33       C  
ATOM   2456  C   VAL A 336      60.106 -15.991 -38.793  1.00109.17           C  
ANISOU 2456  C   VAL A 336    15889  13333  12257   -195  -3039     78       C  
ATOM   2457  O   VAL A 336      60.360 -16.546 -39.864  1.00112.05           O  
ANISOU 2457  O   VAL A 336    16652  13734  12187   -176  -3106    -18       O  
ATOM   2458  CB  VAL A 336      57.651 -16.352 -38.288  1.00109.30           C  
ANISOU 2458  CB  VAL A 336    15612  13127  12788   -406  -3727    214       C  
ATOM   2459  CG1 VAL A 336      57.460 -16.699 -39.761  1.00113.28           C  
ANISOU 2459  CG1 VAL A 336    16569  13641  12827   -443  -4025    209       C  
ATOM   2460  CG2 VAL A 336      56.667 -17.145 -37.438  1.00108.55           C  
ANISOU 2460  CG2 VAL A 336    15286  12903  13053   -508  -3941    156       C  
ATOM   2461  N   GLY A 337      60.682 -14.849 -38.416  1.00108.11           N  
ANISOU 2461  N   GLY A 337    15533  13267  12274   -160  -2750    216       N  
ATOM   2462  CA  GLY A 337      61.611 -14.113 -39.277  1.00110.21           C  
ANISOU 2462  CA  GLY A 337    15986  13657  12230   -118  -2495    310       C  
ATOM   2463  C   GLY A 337      62.704 -14.966 -39.899  1.00112.16           C  
ANISOU 2463  C   GLY A 337    16543  14005  12064    -19  -2251     87       C  
ATOM   2464  O   GLY A 337      63.200 -15.906 -39.277  1.00110.76           O  
ANISOU 2464  O   GLY A 337    16310  13809  11964     63  -2131   -149       O  
ATOM   2465  N   GLU A 338      63.080 -14.623 -41.128  1.00115.95           N  
ANISOU 2465  N   GLU A 338    17357  14590  12109    -24  -2168    171       N  
ATOM   2466  CA  GLU A 338      64.044 -15.408 -41.900  1.00118.84           C  
ANISOU 2466  CA  GLU A 338    18061  15061  12029     74  -1913    -52       C  
ATOM   2467  C   GLU A 338      65.456 -15.311 -41.329  1.00117.77           C  
ANISOU 2467  C   GLU A 338    17690  15023  12032    195  -1405   -161       C  
ATOM   2468  O   GLU A 338      65.818 -14.314 -40.702  1.00115.92           O  
ANISOU 2468  O   GLU A 338    17125  14814  12104    166  -1220      3       O  
ATOM   2469  CB  GLU A 338      64.053 -14.953 -43.364  1.00123.33           C  
ANISOU 2469  CB  GLU A 338    19065  15737  12058     17  -1924     94       C  
ATOM   2470  CG  GLU A 338      62.754 -15.218 -44.116  1.00125.83           C  
ANISOU 2470  CG  GLU A 338    19692  15969  12149    -94  -2474    167       C  
ATOM   2471  CD  GLU A 338      62.460 -16.696 -44.309  1.00127.07           C  
ANISOU 2471  CD  GLU A 338    20116  16044  12120    -59  -2694   -165       C  
ATOM   2472  OE1 GLU A 338      63.400 -17.518 -44.251  1.00127.38           O  
ANISOU 2472  OE1 GLU A 338    20246  16118  12033     76  -2372   -456       O  
ATOM   2473  OE2 GLU A 338      61.279 -17.040 -44.525  1.00128.08           O  
ANISOU 2473  OE2 GLU A 338    20351  16053  12259   -167  -3204   -135       O  
ATOM   2474  N   GLU A 339      66.245 -16.358 -41.554  1.00119.53           N  
ANISOU 2474  N   GLU A 339    18079  15283  12054    332  -1200   -451       N  
ATOM   2475  CA  GLU A 339      67.633 -16.404 -41.094  1.00119.30           C  
ANISOU 2475  CA  GLU A 339    17814  15345  12167    469   -737   -576       C  
ATOM   2476  C   GLU A 339      68.528 -15.408 -41.833  1.00122.04           C  
ANISOU 2476  C   GLU A 339    18187  15873  12308    447   -329   -413       C  
ATOM   2477  O   GLU A 339      69.480 -14.883 -41.255  1.00120.97           O  
ANISOU 2477  O   GLU A 339    17707  15805  12451    479     -2   -377       O  
ATOM   2478  CB  GLU A 339      68.194 -17.824 -41.231  1.00120.88           C  
ANISOU 2478  CB  GLU A 339    18191  15509  12227    648   -638   -934       C  
ATOM   2479  CG  GLU A 339      67.721 -18.786 -40.152  1.00118.11           C  
ANISOU 2479  CG  GLU A 339    17686  14969  12219    687   -921  -1085       C  
ATOM   2480  CD  GLU A 339      68.387 -18.570 -38.805  1.00114.88           C  
ANISOU 2480  CD  GLU A 339    16805  14555  12287    743   -764  -1066       C  
ATOM   2481  OE1 GLU A 339      69.190 -17.623 -38.657  1.00114.60           O  
ANISOU 2481  OE1 GLU A 339    16525  14652  12366    741   -459   -943       O  
ATOM   2482  OE2 GLU A 339      68.103 -19.360 -37.884  1.00112.93           O  
ANISOU 2482  OE2 GLU A 339    16448  14163  12296    773   -963  -1169       O  
ATOM   2483  N   ALA A 340      68.216 -15.149 -43.102  1.00126.07           N  
ANISOU 2483  N   ALA A 340    19111  16458  12331    373   -364   -302       N  
ATOM   2484  CA  ALA A 340      68.963 -14.181 -43.905  1.00129.33           C  
ANISOU 2484  CA  ALA A 340    19608  17039  12491    315     16    -97       C  
ATOM   2485  C   ALA A 340      68.775 -12.755 -43.387  1.00127.54           C  
ANISOU 2485  C   ALA A 340    19058  16775  12624    170    -14    255       C  
ATOM   2486  O   ALA A 340      69.736 -11.990 -43.300  1.00128.04           O  
ANISOU 2486  O   ALA A 340    18902  16930  12816    145    377    372       O  
ATOM   2487  CB  ALA A 340      68.541 -14.269 -45.363  1.00134.06           C  
ANISOU 2487  CB  ALA A 340    20787  17715  12432    250    -79    -40       C  
ATOM   2488  N   ALA A 341      67.535 -12.410 -43.045  1.00125.88           N  
ANISOU 2488  N   ALA A 341    18806  16417  12606     76   -478    414       N  
ATOM   2489  CA  ALA A 341      67.207 -11.080 -42.527  1.00124.41           C  
ANISOU 2489  CA  ALA A 341    18327  16145  12795    -40   -552    722       C  
ATOM   2490  C   ALA A 341      67.790 -10.843 -41.133  1.00120.89           C  
ANISOU 2490  C   ALA A 341    17376  15654  12903     -1   -373    632       C  
ATOM   2491  O   ALA A 341      68.318  -9.765 -40.855  1.00120.69           O  
ANISOU 2491  O   ALA A 341    17115  15626  13113    -72   -161    811       O  
ATOM   2492  CB  ALA A 341      65.698 -10.880 -42.505  1.00123.63           C  
ANISOU 2492  CB  ALA A 341    18285  15891  12797   -118  -1090    875       C  
ATOM   2493  N   ILE A 342      67.691 -11.850 -40.265  1.00118.63           N  
ANISOU 2493  N   ILE A 342    16945  15318  12810     98   -479    363       N  
ATOM   2494  CA  ILE A 342      68.199 -11.749 -38.893  1.00115.57           C  
ANISOU 2494  CA  ILE A 342    16123  14890  12895    134   -364    263       C  
ATOM   2495  C   ILE A 342      69.724 -11.633 -38.883  1.00117.00           C  
ANISOU 2495  C   ILE A 342    16142  15205  13107    194     92    189       C  
ATOM   2496  O   ILE A 342      70.273 -10.721 -38.264  1.00116.19           O  
ANISOU 2496  O   ILE A 342    15724  15096  13324    130    252    292       O  
ATOM   2497  CB  ILE A 342      67.744 -12.944 -38.022  1.00113.08           C  
ANISOU 2497  CB  ILE A 342    15745  14490  12730    219   -594     20       C  
ATOM   2498  CG1 ILE A 342      66.229 -12.883 -37.797  1.00111.85           C  
ANISOU 2498  CG1 ILE A 342    15619  14195  12682    130  -1019    120       C  
ATOM   2499  CG2 ILE A 342      68.458 -12.937 -36.674  1.00110.33           C  
ANISOU 2499  CG2 ILE A 342    15010  14130  12780    264   -455    -89       C  
ATOM   2500  CD1 ILE A 342      65.618 -14.177 -37.302  1.00110.66           C  
ANISOU 2500  CD1 ILE A 342    15518  13958  12570    175  -1269    -83       C  
ATOM   2501  N   GLN A 343      70.398 -12.558 -39.563  1.00119.73           N  
ANISOU 2501  N   GLN A 343    16687  15659  13144    316    300      0       N  
ATOM   2502  CA  GLN A 343      71.860 -12.516 -39.688  1.00121.96           C  
ANISOU 2502  CA  GLN A 343    16795  16083  13459    389    768    -77       C  
ATOM   2503  C   GLN A 343      72.349 -11.236 -40.377  1.00124.75           C  
ANISOU 2503  C   GLN A 343    17135  16529  13732    244   1060    205       C  
ATOM   2504  O   GLN A 343      73.428 -10.732 -40.059  1.00125.40           O  
ANISOU 2504  O   GLN A 343    16897  16682  14067    225   1388    232       O  
ATOM   2505  CB  GLN A 343      72.386 -13.752 -40.437  1.00124.88           C  
ANISOU 2505  CB  GLN A 343    17424  16540  13484    568    956   -349       C  
ATOM   2506  CG  GLN A 343      73.764 -14.241 -39.995  1.00125.71           C  
ANISOU 2506  CG  GLN A 343    17212  16723  13829    732   1315   -557       C  
ATOM   2507  CD  GLN A 343      73.930 -14.353 -38.479  1.00121.93           C  
ANISOU 2507  CD  GLN A 343    16308  16139  13878    766   1136   -623       C  
ATOM   2508  OE1 GLN A 343      73.019 -14.772 -37.762  1.00118.83           O  
ANISOU 2508  OE1 GLN A 343    15949  15605  13595    756    750   -662       O  
ATOM   2509  NE2 GLN A 343      75.105 -13.971 -37.989  1.00122.50           N  
ANISOU 2509  NE2 GLN A 343    15981  16288  14274    791   1418   -626       N  
ATOM   2510  N   GLY A 344      71.555 -10.717 -41.312  1.00126.80           N  
ANISOU 2510  N   GLY A 344    17741  16778  13659    129    917    431       N  
ATOM   2511  CA  GLY A 344      71.852  -9.444 -41.965  1.00129.75           C  
ANISOU 2511  CA  GLY A 344    18148  17197  13953    -35   1132    761       C  
ATOM   2512  C   GLY A 344      71.772  -8.268 -41.007  1.00127.48           C  
ANISOU 2512  C   GLY A 344    17479  16768  14188   -159   1047    951       C  
ATOM   2513  O   GLY A 344      72.625  -7.382 -41.035  1.00129.17           O  
ANISOU 2513  O   GLY A 344    17495  17017  14567   -264   1358   1110       O  
ATOM   2514  N   ARG A 345      70.743  -8.264 -40.161  1.00124.20           N  
ANISOU 2514  N   ARG A 345    16962  16185  14041   -155    638    925       N  
ATOM   2515  CA  ARG A 345      70.567  -7.230 -39.137  1.00122.00           C  
ANISOU 2515  CA  ARG A 345    16340  15749  14265   -249    538   1039       C  
ATOM   2516  C   ARG A 345      71.691  -7.272 -38.098  1.00120.55           C  
ANISOU 2516  C   ARG A 345    15748  15604  14451   -219    774    858       C  
ATOM   2517  O   ARG A 345      72.124  -6.227 -37.610  1.00120.49           O  
ANISOU 2517  O   ARG A 345    15480  15521  14778   -336    877    978       O  
ATOM   2518  CB  ARG A 345      69.201  -7.392 -38.453  1.00119.10           C  
ANISOU 2518  CB  ARG A 345    15957  15219  14075   -225     92   1001       C  
ATOM   2519  CG  ARG A 345      68.865  -6.353 -37.390  1.00117.06           C  
ANISOU 2519  CG  ARG A 345    15384  14782  14310   -301    -14   1079       C  
ATOM   2520  CD  ARG A 345      68.648  -4.968 -37.981  1.00119.47           C  
ANISOU 2520  CD  ARG A 345    15744  14966  14681   -434    -13   1419       C  
ATOM   2521  NE  ARG A 345      68.195  -4.012 -36.971  1.00117.80           N  
ANISOU 2521  NE  ARG A 345    15260  14543  14955   -483   -140   1456       N  
ATOM   2522  CZ  ARG A 345      67.940  -2.724 -37.201  1.00119.55           C  
ANISOU 2522  CZ  ARG A 345    15466  14583  15373   -584   -176   1725       C  
ATOM   2523  NH1 ARG A 345      68.089  -2.208 -38.418  1.00123.05           N  
ANISOU 2523  NH1 ARG A 345    16161  15038  15554   -667   -107   2026       N  
ATOM   2524  NH2 ARG A 345      67.535  -1.943 -36.204  1.00118.10           N  
ANISOU 2524  NH2 ARG A 345    15035  14191  15643   -603   -278   1692       N  
ATOM   2525  N   VAL A 346      72.152  -8.476 -37.761  1.00119.74           N  
ANISOU 2525  N   VAL A 346    15595  15595  14304    -67    827    573       N  
ATOM   2526  CA  VAL A 346      73.285  -8.645 -36.847  1.00119.04           C  
ANISOU 2526  CA  VAL A 346    15127  15556  14547    -19   1016    403       C  
ATOM   2527  C   VAL A 346      74.563  -8.074 -37.465  1.00122.64           C  
ANISOU 2527  C   VAL A 346    15445  16140  15012    -85   1458    508       C  
ATOM   2528  O   VAL A 346      75.357  -7.440 -36.773  1.00122.75           O  
ANISOU 2528  O   VAL A 346    15096  16137  15406   -164   1580    523       O  
ATOM   2529  CB  VAL A 346      73.494 -10.130 -36.457  1.00118.00           C  
ANISOU 2529  CB  VAL A 346    14999  15475  14360    179    956     98       C  
ATOM   2530  CG1 VAL A 346      74.813 -10.330 -35.718  1.00118.35           C  
ANISOU 2530  CG1 VAL A 346    14657  15587  14721    247   1163    -49       C  
ATOM   2531  CG2 VAL A 346      72.339 -10.618 -35.593  1.00114.56           C  
ANISOU 2531  CG2 VAL A 346    14612  14902  14012    204    545     11       C  
ATOM   2532  N   ALA A 347      74.750  -8.295 -38.765  1.00126.00           N  
ANISOU 2532  N   ALA A 347    16166  16693  15012    -67   1697    578       N  
ATOM   2533  CA  ALA A 347      75.911  -7.766 -39.485  1.00129.92           C  
ANISOU 2533  CA  ALA A 347    16562  17332  15466   -145   2176    704       C  
ATOM   2534  C   ALA A 347      75.928  -6.234 -39.518  1.00130.86           C  
ANISOU 2534  C   ALA A 347    16573  17351  15797   -390   2225   1039       C  
ATOM   2535  O   ALA A 347      76.995  -5.625 -39.437  1.00133.03           O  
ANISOU 2535  O   ALA A 347    16541  17675  16329   -496   2546   1118       O  
ATOM   2536  CB  ALA A 347      75.954  -8.324 -40.900  1.00133.69           C  
ANISOU 2536  CB  ALA A 347    17462  17970  15363    -83   2418    708       C  
ATOM   2537  N   GLN A 348      74.750  -5.621 -39.638  1.00129.64           N  
ANISOU 2537  N   GLN A 348    16652  17036  15569   -479   1897   1237       N  
ATOM   2538  CA  GLN A 348      74.626  -4.160 -39.635  1.00130.60           C  
ANISOU 2538  CA  GLN A 348    16698  16997  15924   -693   1883   1557       C  
ATOM   2539  C   GLN A 348      75.048  -3.559 -38.299  1.00128.43           C  
ANISOU 2539  C   GLN A 348    15968  16585  16242   -761   1821   1471       C  
ATOM   2540  O   GLN A 348      75.863  -2.637 -38.258  1.00130.46           O  
ANISOU 2540  O   GLN A 348    15996  16805  16766   -929   2053   1622       O  
ATOM   2541  CB  GLN A 348      73.186  -3.733 -39.933  1.00129.70           C  
ANISOU 2541  CB  GLN A 348    16895  16710  15673   -725   1483   1753       C  
ATOM   2542  CG  GLN A 348      72.728  -3.996 -41.358  1.00132.93           C  
ANISOU 2542  CG  GLN A 348    17797  17222  15488   -724   1490   1927       C  
ATOM   2543  CD  GLN A 348      71.239  -3.759 -41.541  1.00131.96           C  
ANISOU 2543  CD  GLN A 348    17930  16927  15281   -724   1006   2080       C  
ATOM   2544  OE1 GLN A 348      70.630  -2.970 -40.817  1.00129.91           O  
ANISOU 2544  OE1 GLN A 348    17483  16444  15432   -771    759   2172       O  
ATOM   2545  NE2 GLN A 348      70.644  -4.443 -42.513  1.00133.75           N  
ANISOU 2545  NE2 GLN A 348    18579  17250  14989   -667    864   2094       N  
ATOM   2546  N   ILE A 349      74.490  -4.091 -37.214  1.00124.69           N  
ANISOU 2546  N   ILE A 349    15382  16035  15957   -646   1506   1228       N  
ATOM   2547  CA  ILE A 349      74.742  -3.569 -35.867  1.00122.74           C  
ANISOU 2547  CA  ILE A 349    14770  15655  16210   -706   1389   1114       C  
ATOM   2548  C   ILE A 349      76.181  -3.870 -35.434  1.00124.06           C  
ANISOU 2548  C   ILE A 349    14579  15960  16598   -701   1651    956       C  
ATOM   2549  O   ILE A 349      76.800  -3.073 -34.727  1.00124.65           O  
ANISOU 2549  O   ILE A 349    14343  15944  17073   -839   1680    966       O  
ATOM   2550  CB  ILE A 349      73.742  -4.138 -34.827  1.00118.63           C  
ANISOU 2550  CB  ILE A 349    14260  15042  15770   -588   1011    900       C  
ATOM   2551  CG1 ILE A 349      72.296  -3.812 -35.229  1.00117.91           C  
ANISOU 2551  CG1 ILE A 349    14453  14808  15540   -591    744   1059       C  
ATOM   2552  CG2 ILE A 349      74.010  -3.555 -33.443  1.00116.98           C  
ANISOU 2552  CG2 ILE A 349    13729  14704  16012   -662    904    772       C  
ATOM   2553  CD1 ILE A 349      71.248  -4.628 -34.501  1.00114.59           C  
ANISOU 2553  CD1 ILE A 349    14085  14349  15104   -465    429    864       C  
ATOM   2554  N   ARG A 350      76.707  -5.013 -35.868  1.00125.05           N  
ANISOU 2554  N   ARG A 350    14741  16287  16484   -539   1825    803       N  
ATOM   2555  CA  ARG A 350      78.086  -5.402 -35.565  1.00126.69           C  
ANISOU 2555  CA  ARG A 350    14583  16635  16918   -495   2081    655       C  
ATOM   2556  C   ARG A 350      79.108  -4.497 -36.260  1.00131.03           C  
ANISOU 2556  C   ARG A 350    14950  17247  17587   -680   2493    875       C  
ATOM   2557  O   ARG A 350      80.225  -4.325 -35.768  1.00132.64           O  
ANISOU 2557  O   ARG A 350    14734  17497  18164   -735   2649    812       O  
ATOM   2558  CB  ARG A 350      78.317  -6.863 -35.956  1.00127.00           C  
ANISOU 2558  CB  ARG A 350    14733  16842  16676   -247   2179    434       C  
ATOM   2559  CG  ARG A 350      79.591  -7.475 -35.397  1.00128.15           C  
ANISOU 2559  CG  ARG A 350    14467  17096  17126   -134   2333    229       C  
ATOM   2560  CD  ARG A 350      79.466  -8.987 -35.318  1.00127.12           C  
ANISOU 2560  CD  ARG A 350    14463  17022  16811    143   2232    -36       C  
ATOM   2561  NE  ARG A 350      78.600  -9.409 -34.218  1.00122.92           N  
ANISOU 2561  NE  ARG A 350    13999  16351  16353    194   1770   -156       N  
ATOM   2562  CZ  ARG A 350      78.285 -10.674 -33.954  1.00121.56           C  
ANISOU 2562  CZ  ARG A 350    13963  16166  16056    400   1587   -359       C  
ATOM   2563  NH1 ARG A 350      78.756 -11.658 -34.711  1.00124.03           N  
ANISOU 2563  NH1 ARG A 350    14369  16578  16177    596   1808   -496       N  
ATOM   2564  NH2 ARG A 350      77.488 -10.956 -32.929  1.00118.05           N  
ANISOU 2564  NH2 ARG A 350    13574  15598  15681    405   1196   -428       N  
ATOM   2565  N   GLN A 351      78.724  -3.930 -37.403  1.00133.37           N  
ANISOU 2565  N   GLN A 351    15560  17543  17570   -788   2655   1148       N  
ATOM   2566  CA  GLN A 351      79.551  -2.946 -38.101  1.00137.82           C  
ANISOU 2566  CA  GLN A 351    16004  18138  18223  -1010   3044   1423       C  
ATOM   2567  C   GLN A 351      79.484  -1.583 -37.408  1.00137.28           C  
ANISOU 2567  C   GLN A 351    15734  17818  18608  -1251   2877   1593       C  
ATOM   2568  O   GLN A 351      80.470  -0.845 -37.391  1.00140.27           O  
ANISOU 2568  O   GLN A 351    15798  18186  19310  -1445   3132   1716       O  
ATOM   2569  CB  GLN A 351      79.109  -2.805 -39.559  1.00141.01           C  
ANISOU 2569  CB  GLN A 351    16875  18616  18084  -1054   3243   1685       C  
ATOM   2570  CG  GLN A 351      80.156  -2.159 -40.458  1.00146.70           C  
ANISOU 2570  CG  GLN A 351    17501  19457  18779  -1247   3775   1941       C  
ATOM   2571  CD  GLN A 351      79.579  -1.613 -41.753  1.00150.00           C  
ANISOU 2571  CD  GLN A 351    18417  19875  18700  -1375   3884   2301       C  
ATOM   2572  OE1 GLN A 351      78.437  -1.154 -41.796  1.00148.30           O  
ANISOU 2572  OE1 GLN A 351    18504  19468  18376  -1410   3500   2460       O  
ATOM   2573  NE2 GLN A 351      80.376  -1.648 -42.817  1.00155.21           N  
ANISOU 2573  NE2 GLN A 351    19161  20750  19059  -1445   4413   2440       N  
ATOM   2574  N   GLN A 352      78.319  -1.250 -36.854  1.00133.80           N  
ANISOU 2574  N   GLN A 352    15468  17162  18208  -1241   2459   1592       N  
ATOM   2575  CA  GLN A 352      78.141  -0.007 -36.096  1.00133.23           C  
ANISOU 2575  CA  GLN A 352    15234  16811  18574  -1433   2266   1690       C  
ATOM   2576  C   GLN A 352      78.968   0.024 -34.807  1.00132.31           C  
ANISOU 2576  C   GLN A 352    14668  16668  18937  -1471   2190   1441       C  
ATOM   2577  O   GLN A 352      79.334   1.101 -34.334  1.00133.59           O  
ANISOU 2577  O   GLN A 352    14617  16638  19501  -1684   2166   1521       O  
ATOM   2578  CB  GLN A 352      76.661   0.221 -35.769  1.00130.01           C  
ANISOU 2578  CB  GLN A 352    15098  16192  18105  -1367   1859   1698       C  
ATOM   2579  CG  GLN A 352      75.806   0.563 -36.980  1.00131.62           C  
ANISOU 2579  CG  GLN A 352    15717  16345  17946  -1389   1847   2015       C  
ATOM   2580  CD  GLN A 352      74.325   0.667 -36.655  1.00128.73           C  
ANISOU 2580  CD  GLN A 352    15560  15786  17565  -1291   1430   2005       C  
ATOM   2581  OE1 GLN A 352      73.838   0.052 -35.705  1.00125.05           O  
ANISOU 2581  OE1 GLN A 352    15009  15314  17188  -1153   1196   1721       O  
ATOM   2582  NE2 GLN A 352      73.599   1.447 -37.449  1.00130.75           N  
ANISOU 2582  NE2 GLN A 352    16081  15880  17718  -1366   1337   2331       N  
ATOM   2583  N   ILE A 353      79.249  -1.150 -34.240  1.00130.40           N  
ANISOU 2583  N   ILE A 353    14298  16595  18650  -1272   2121   1143       N  
ATOM   2584  CA  ILE A 353      80.145  -1.268 -33.081  1.00130.14           C  
ANISOU 2584  CA  ILE A 353    13844  16575  19028  -1293   2031    915       C  
ATOM   2585  C   ILE A 353      81.559  -0.799 -33.441  1.00134.50           C  
ANISOU 2585  C   ILE A 353    14017  17212  19873  -1466   2389   1030       C  
ATOM   2586  O   ILE A 353      82.246  -0.186 -32.620  1.00135.66           O  
ANISOU 2586  O   ILE A 353    13812  17259  20470  -1629   2299    973       O  
ATOM   2587  CB  ILE A 353      80.185  -2.721 -32.538  1.00127.82           C  
ANISOU 2587  CB  ILE A 353    13520  16446  18599  -1026   1889    619       C  
ATOM   2588  CG1 ILE A 353      78.854  -3.064 -31.858  1.00123.57           C  
ANISOU 2588  CG1 ILE A 353    13265  15791  17893   -912   1503    492       C  
ATOM   2589  CG2 ILE A 353      81.333  -2.912 -31.549  1.00128.79           C  
ANISOU 2589  CG2 ILE A 353    13186  16620  19127  -1041   1830    430       C  
ATOM   2590  CD1 ILE A 353      78.659  -4.536 -31.556  1.00121.40           C  
ANISOU 2590  CD1 ILE A 353    13073  15650  17400   -658   1370    265       C  
ATOM   2591  N   GLU A 354      81.976  -1.086 -34.672  1.00137.23           N  
ANISOU 2591  N   GLU A 354    14441  17742  19957  -1440   2797   1185       N  
ATOM   2592  CA  GLU A 354      83.292  -0.686 -35.173  1.00141.90           C  
ANISOU 2592  CA  GLU A 354    14673  18446  20797  -1606   3224   1322       C  
ATOM   2593  C   GLU A 354      83.345   0.815 -35.469  1.00144.49           C  
ANISOU 2593  C   GLU A 354    14989  18562  21346  -1943   3319   1647       C  
ATOM   2594  O   GLU A 354      84.374   1.459 -35.257  1.00147.70           O  
ANISOU 2594  O   GLU A 354    14984  18938  22197  -2163   3481   1717       O  
ATOM   2595  CB  GLU A 354      83.643  -1.481 -36.435  1.00144.59           C  
ANISOU 2595  CB  GLU A 354    15155  19057  20725  -1465   3678   1374       C  
ATOM   2596  CG  GLU A 354      83.686  -2.991 -36.230  1.00142.56           C  
ANISOU 2596  CG  GLU A 354    14905  18979  20283  -1124   3619   1049       C  
ATOM   2597  CD  GLU A 354      85.028  -3.517 -35.738  1.00144.74           C  
ANISOU 2597  CD  GLU A 354    14621  19396  20976  -1046   3778    858       C  
ATOM   2598  OE1 GLU A 354      86.058  -2.825 -35.881  1.00148.77           O  
ANISOU 2598  OE1 GLU A 354    14732  19943  21851  -1250   4074    994       O  
ATOM   2599  OE2 GLU A 354      85.052  -4.645 -35.205  1.00142.64           O  
ANISOU 2599  OE2 GLU A 354    14301  19194  20698   -778   3592    580       O  
ATOM   2600  N   GLU A 355      82.231   1.360 -35.956  1.00143.26           N  
ANISOU 2600  N   GLU A 355    15276  18243  20913  -1985   3195   1853       N  
ATOM   2601  CA  GLU A 355      82.117   2.789 -36.258  1.00145.65           C  
ANISOU 2601  CA  GLU A 355    15637  18285  21414  -2283   3231   2186       C  
ATOM   2602  C   GLU A 355      81.812   3.643 -35.022  1.00143.54           C  
ANISOU 2602  C   GLU A 355    15226  17695  21618  -2404   2827   2073       C  
ATOM   2603  O   GLU A 355      81.929   4.869 -35.074  1.00145.89           O  
ANISOU 2603  O   GLU A 355    15479  17733  22218  -2669   2843   2300       O  
ATOM   2604  CB  GLU A 355      81.025   3.015 -37.308  1.00145.74           C  
ANISOU 2604  CB  GLU A 355    16190  18236  20949  -2256   3223   2467       C  
ATOM   2605  CG  GLU A 355      81.291   2.326 -38.639  1.00148.60           C  
ANISOU 2605  CG  GLU A 355    16782  18898  20779  -2179   3634   2604       C  
ATOM   2606  CD  GLU A 355      80.105   2.379 -39.586  1.00148.40           C  
ANISOU 2606  CD  GLU A 355    17332  18827  20225  -2122   3514   2835       C  
ATOM   2607  OE1 GLU A 355      79.131   3.107 -39.299  1.00146.62           O  
ANISOU 2607  OE1 GLU A 355    17284  18314  20111  -2166   3149   2954       O  
ATOM   2608  OE2 GLU A 355      80.149   1.688 -40.625  1.00150.30           O  
ANISOU 2608  OE2 GLU A 355    17848  19315  19944  -2026   3778   2889       O  
ATOM   2609  N   ALA A 356      81.420   3.000 -33.922  1.00139.43           N  
ANISOU 2609  N   ALA A 356    14656  17176  21144  -2216   2476   1724       N  
ATOM   2610  CA  ALA A 356      81.060   3.702 -32.687  1.00137.65           C  
ANISOU 2610  CA  ALA A 356    14347  16667  21287  -2302   2097   1558       C  
ATOM   2611  C   ALA A 356      82.236   4.485 -32.105  1.00140.87           C  
ANISOU 2611  C   ALA A 356    14316  16965  22240  -2574   2138   1537       C  
ATOM   2612  O   ALA A 356      83.308   3.925 -31.867  1.00142.21           O  
ANISOU 2612  O   ALA A 356    14119  17343  22568  -2571   2253   1408       O  
ATOM   2613  CB  ALA A 356      80.532   2.716 -31.654  1.00133.19           C  
ANISOU 2613  CB  ALA A 356    13817  16185  20602  -2054   1771   1194       C  
ATOM   2614  N   THR A 357      82.019   5.778 -31.875  1.00142.36           N  
ANISOU 2614  N   THR A 357    14535  16807  22747  -2807   2022   1660       N  
ATOM   2615  CA  THR A 357      83.033   6.652 -31.286  1.00145.66           C  
ANISOU 2615  CA  THR A 357    14569  17055  23719  -3106   2002   1636       C  
ATOM   2616  C   THR A 357      82.983   6.616 -29.758  1.00143.37           C  
ANISOU 2616  C   THR A 357    14150  16654  23668  -3079   1580   1236       C  
ATOM   2617  O   THR A 357      84.024   6.589 -29.101  1.00145.26           O  
ANISOU 2617  O   THR A 357    13999  16947  24243  -3208   1513   1080       O  
ATOM   2618  CB  THR A 357      82.855   8.109 -31.757  1.00148.98           C  
ANISOU 2618  CB  THR A 357    15103  17102  24397  -3392   2065   1956       C  
ATOM   2619  OG1 THR A 357      81.536   8.565 -31.431  1.00146.33           O  
ANISOU 2619  OG1 THR A 357    15136  16481  23980  -3286   1771   1910       O  
ATOM   2620  CG2 THR A 357      83.068   8.216 -33.260  1.00152.23           C  
ANISOU 2620  CG2 THR A 357    15636  17631  24570  -3474   2501   2391       C  
ATOM   2621  N   SER A 358      81.771   6.614 -29.204  1.00139.71           N  
ANISOU 2621  N   SER A 358    14015  16043  23025  -2917   1298   1076       N  
ATOM   2622  CA  SER A 358      81.567   6.631 -27.753  1.00137.76           C  
ANISOU 2622  CA  SER A 358    13735  15682  22925  -2891    919    696       C  
ATOM   2623  C   SER A 358      81.523   5.219 -27.164  1.00134.39           C  
ANISOU 2623  C   SER A 358    13293  15575  22195  -2625    785    431       C  
ATOM   2624  O   SER A 358      81.208   4.254 -27.862  1.00132.33           O  
ANISOU 2624  O   SER A 358    13162  15555  21561  -2406    937    514       O  
ATOM   2625  CB  SER A 358      80.269   7.372 -27.418  1.00136.13           C  
ANISOU 2625  CB  SER A 358    13872  15146  22702  -2848    727    648       C  
ATOM   2626  OG  SER A 358      80.036   7.406 -26.021  1.00134.67           O  
ANISOU 2626  OG  SER A 358    13698  14861  22610  -2825    406    264       O  
ATOM   2627  N   ASP A 359      81.839   5.115 -25.874  1.00134.23           N  
ANISOU 2627  N   ASP A 359    13137  15535  22329  -2655    481    114       N  
ATOM   2628  CA  ASP A 359      81.776   3.841 -25.149  1.00131.47           C  
ANISOU 2628  CA  ASP A 359    12798  15440  21714  -2423    295   -131       C  
ATOM   2629  C   ASP A 359      80.335   3.442 -24.860  1.00127.66           C  
ANISOU 2629  C   ASP A 359    12718  14926  20858  -2204    173   -236       C  
ATOM   2630  O   ASP A 359      79.948   2.298 -25.089  1.00124.94           O  
ANISOU 2630  O   ASP A 359    12493  14807  20171  -1969    203   -247       O  
ATOM   2631  CB  ASP A 359      82.554   3.920 -23.829  1.00132.87           C  
ANISOU 2631  CB  ASP A 359    12741  15595  22148  -2550    -31   -413       C  
ATOM   2632  CG  ASP A 359      84.058   3.968 -24.032  1.00136.68           C  
ANISOU 2632  CG  ASP A 359    12742  16184  23006  -2721     47   -336       C  
ATOM   2633  OD1 ASP A 359      84.536   3.623 -25.134  1.00137.62           O  
ANISOU 2633  OD1 ASP A 359    12700  16473  23115  -2678    391   -101       O  
ATOM   2634  OD2 ASP A 359      84.767   4.341 -23.075  1.00138.92           O  
ANISOU 2634  OD2 ASP A 359    12802  16387  23593  -2900   -235   -521       O  
ATOM   2635  N   TYR A 360      79.549   4.388 -24.350  1.00127.89           N  
ANISOU 2635  N   TYR A 360    12939  14663  20989  -2284     43   -323       N  
ATOM   2636  CA  TYR A 360      78.130   4.159 -24.073  1.00124.90           C  
ANISOU 2636  CA  TYR A 360    12899  14227  20330  -2092    -40   -417       C  
ATOM   2637  C   TYR A 360      77.382   3.707 -25.329  1.00123.61           C  
ANISOU 2637  C   TYR A 360    12917  14157  19890  -1924    164   -147       C  
ATOM   2638  O   TYR A 360      76.537   2.812 -25.263  1.00120.89           O  
ANISOU 2638  O   TYR A 360    12758  13947  19225  -1714    112   -209       O  
ATOM   2639  CB  TYR A 360      77.485   5.426 -23.502  1.00126.01           C  
ANISOU 2639  CB  TYR A 360    13174  13996  20708  -2208   -146   -529       C  
ATOM   2640  CG  TYR A 360      75.994   5.309 -23.263  1.00123.31           C  
ANISOU 2640  CG  TYR A 360    13127  13573  20152  -2012   -190   -614       C  
ATOM   2641  CD1 TYR A 360      75.499   4.738 -22.094  1.00121.38           C  
ANISOU 2641  CD1 TYR A 360    12997  13412  19708  -1906   -358   -924       C  
ATOM   2642  CD2 TYR A 360      75.079   5.772 -24.206  1.00123.05           C  
ANISOU 2642  CD2 TYR A 360    13248  13380  20124  -1940    -67   -370       C  
ATOM   2643  CE1 TYR A 360      74.135   4.628 -21.872  1.00119.38           C  
ANISOU 2643  CE1 TYR A 360    12969  13095  19294  -1737   -358   -997       C  
ATOM   2644  CE2 TYR A 360      73.715   5.666 -23.994  1.00120.96           C  
ANISOU 2644  CE2 TYR A 360    13192  13040  19724  -1757   -115   -443       C  
ATOM   2645  CZ  TYR A 360      73.247   5.095 -22.826  1.00119.14           C  
ANISOU 2645  CZ  TYR A 360    13037  12904  19326  -1658   -239   -762       C  
ATOM   2646  OH  TYR A 360      71.892   4.993 -22.612  1.00117.40           O  
ANISOU 2646  OH  TYR A 360    12982  12617  19006  -1488   -247   -831       O  
ATOM   2647  N   ASP A 361      77.694   4.331 -26.464  1.00126.26           N  
ANISOU 2647  N   ASP A 361    13213  14417  20343  -2037    384    158       N  
ATOM   2648  CA  ASP A 361      77.124   3.929 -27.751  1.00125.75           C  
ANISOU 2648  CA  ASP A 361    13339  14457  19980  -1907    569    434       C  
ATOM   2649  C   ASP A 361      77.551   2.509 -28.117  1.00124.46           C  
ANISOU 2649  C   ASP A 361    13133  14657  19499  -1738    667    406       C  
ATOM   2650  O   ASP A 361      76.747   1.731 -28.627  1.00122.28           O  
ANISOU 2650  O   ASP A 361    13083  14499  18876  -1548    673    452       O  
ATOM   2651  CB  ASP A 361      77.540   4.901 -28.862  1.00129.41           C  
ANISOU 2651  CB  ASP A 361    13778  14781  20610  -2098    798    787       C  
ATOM   2652  CG  ASP A 361      76.916   6.280 -28.705  1.00131.07           C  
ANISOU 2652  CG  ASP A 361    14098  14580  21120  -2226    696    866       C  
ATOM   2653  OD1 ASP A 361      76.404   6.593 -27.609  1.00130.08           O  
ANISOU 2653  OD1 ASP A 361    14001  14277  21145  -2200    474    593       O  
ATOM   2654  OD2 ASP A 361      76.945   7.057 -29.682  1.00133.81           O  
ANISOU 2654  OD2 ASP A 361    14516  14773  21552  -2352    847   1203       O  
ATOM   2655  N   ARG A 362      78.813   2.179 -27.845  1.00126.26           N  
ANISOU 2655  N   ARG A 362    13056  15039  19876  -1806    725    322       N  
ATOM   2656  CA  ARG A 362      79.340   0.835 -28.093  1.00125.64           C  
ANISOU 2656  CA  ARG A 362    12891  15273  19570  -1627    812    261       C  
ATOM   2657  C   ARG A 362      78.675  -0.220 -27.201  1.00121.98           C  
ANISOU 2657  C   ARG A 362    12570  14900  18875  -1418    552     10       C  
ATOM   2658  O   ARG A 362      78.304  -1.291 -27.680  1.00120.12           O  
ANISOU 2658  O   ARG A 362    12487  14832  18320  -1217    598     15       O  
ATOM   2659  CB  ARG A 362      80.861   0.806 -27.891  1.00128.81           C  
ANISOU 2659  CB  ARG A 362    12871  15788  20282  -1744    903    221       C  
ATOM   2660  CG  ARG A 362      81.526  -0.481 -28.360  1.00129.25           C  
ANISOU 2660  CG  ARG A 362    12796  16142  20170  -1548   1067    192       C  
ATOM   2661  CD  ARG A 362      83.041  -0.445 -28.210  1.00133.02           C  
ANISOU 2661  CD  ARG A 362    12790  16722  21027  -1657   1173    170       C  
ATOM   2662  NE  ARG A 362      83.671   0.526 -29.109  1.00136.98           N  
ANISOU 2662  NE  ARG A 362    13123  17173  21749  -1890   1510    428       N  
ATOM   2663  CZ  ARG A 362      84.091   1.746 -28.765  1.00139.69           C  
ANISOU 2663  CZ  ARG A 362    13274  17307  22492  -2185   1459    494       C  
ATOM   2664  NH1 ARG A 362      83.967   2.199 -27.520  1.00138.90           N  
ANISOU 2664  NH1 ARG A 362    13137  17027  22610  -2284   1075    287       N  
ATOM   2665  NH2 ARG A 362      84.647   2.528 -29.685  1.00143.63           N  
ANISOU 2665  NH2 ARG A 362    13638  17767  23164  -2398   1802    768       N  
ATOM   2666  N   GLU A 363      78.526   0.088 -25.914  1.00121.18           N  
ANISOU 2666  N   GLU A 363    12440  14679  18921  -1479    283   -207       N  
ATOM   2667  CA  GLU A 363      77.950  -0.860 -24.952  1.00118.26           C  
ANISOU 2667  CA  GLU A 363    12208  14393  18331  -1317     45   -431       C  
ATOM   2668  C   GLU A 363      76.502  -1.225 -25.276  1.00115.04           C  
ANISOU 2668  C   GLU A 363    12131  13957  17618  -1167     37   -387       C  
ATOM   2669  O   GLU A 363      76.108  -2.383 -25.138  1.00112.83           O  
ANISOU 2669  O   GLU A 363    11971  13822  17077   -994    -37   -459       O  
ATOM   2670  CB  GLU A 363      78.031  -0.313 -23.522  1.00119.02           C  
ANISOU 2670  CB  GLU A 363    12259  14359  18603  -1443   -218   -669       C  
ATOM   2671  CG  GLU A 363      79.449  -0.206 -22.974  1.00122.08           C  
ANISOU 2671  CG  GLU A 363    12309  14801  19273  -1578   -322   -759       C  
ATOM   2672  CD  GLU A 363      79.499   0.050 -21.476  1.00122.70           C  
ANISOU 2672  CD  GLU A 363    12410  14797  19412  -1674   -648  -1030       C  
ATOM   2673  OE1 GLU A 363      78.434   0.271 -20.859  1.00121.28           O  
ANISOU 2673  OE1 GLU A 363    12508  14503  19067  -1649   -737  -1157       O  
ATOM   2674  OE2 GLU A 363      80.615   0.033 -20.912  1.00125.11           O  
ANISOU 2674  OE2 GLU A 363    12450  15155  19928  -1779   -815  -1120       O  
ATOM   2675  N   LYS A 364      75.715  -0.239 -25.700  1.00114.90           N  
ANISOU 2675  N   LYS A 364    12247  13737  17670  -1235     94   -261       N  
ATOM   2676  CA  LYS A 364      74.305  -0.464 -26.018  1.00112.53           C  
ANISOU 2676  CA  LYS A 364    12213  13388  17152  -1104     59   -206       C  
ATOM   2677  C   LYS A 364      74.111  -1.229 -27.328  1.00111.97           C  
ANISOU 2677  C   LYS A 364    12272  13471  16799   -982    194     -6       C  
ATOM   2678  O   LYS A 364      73.157  -1.998 -27.461  1.00110.10           O  
ANISOU 2678  O   LYS A 364    12223  13290  16318   -840    111    -20       O  
ATOM   2679  CB  LYS A 364      73.544   0.863 -26.055  1.00113.38           C  
ANISOU 2679  CB  LYS A 364    12397  13204  17477  -1197     50   -129       C  
ATOM   2680  CG  LYS A 364      73.495   1.573 -24.715  1.00113.84           C  
ANISOU 2680  CG  LYS A 364    12401  13087  17766  -1290    -86   -384       C  
ATOM   2681  CD  LYS A 364      72.473   0.930 -23.793  1.00111.59           C  
ANISOU 2681  CD  LYS A 364    12258  12844  17294  -1158   -216   -594       C  
ATOM   2682  CE  LYS A 364      72.312   1.723 -22.509  1.00112.62           C  
ANISOU 2682  CE  LYS A 364    12392  12790  17606  -1247   -313   -861       C  
ATOM   2683  NZ  LYS A 364      71.554   0.986 -21.461  1.00110.91           N  
ANISOU 2683  NZ  LYS A 364    12303  12672  17166  -1148   -403  -1085       N  
ATOM   2684  N   LEU A 365      75.013  -1.024 -28.286  1.00113.94           N  
ANISOU 2684  N   LEU A 365    12426  13788  17075  -1050    407    171       N  
ATOM   2685  CA  LEU A 365      75.006  -1.799 -29.529  1.00114.07           C  
ANISOU 2685  CA  LEU A 365    12584  13977  16777   -938    566    323       C  
ATOM   2686  C   LEU A 365      75.338  -3.271 -29.273  1.00112.63           C  
ANISOU 2686  C   LEU A 365    12385  14014  16395   -763    530    140       C  
ATOM   2687  O   LEU A 365      74.815  -4.157 -29.949  1.00111.55           O  
ANISOU 2687  O   LEU A 365    12458  13975  15948   -621    539    166       O  
ATOM   2688  CB  LEU A 365      75.992  -1.207 -30.541  1.00117.49           C  
ANISOU 2688  CB  LEU A 365    12911  14448  17282  -1067    859    544       C  
ATOM   2689  CG  LEU A 365      75.617   0.161 -31.119  1.00119.45           C  
ANISOU 2689  CG  LEU A 365    13247  14468  17669  -1235    915    808       C  
ATOM   2690  CD1 LEU A 365      76.832   0.843 -31.731  1.00123.27           C  
ANISOU 2690  CD1 LEU A 365    13536  14968  18331  -1425   1205    995       C  
ATOM   2691  CD2 LEU A 365      74.503   0.035 -32.145  1.00119.06           C  
ANISOU 2691  CD2 LEU A 365    13540  14401  17295  -1145    884   1009       C  
ATOM   2692  N   GLN A 366      76.207  -3.524 -28.296  1.00112.95           N  
ANISOU 2692  N   GLN A 366    12181  14107  16625   -776    459    -41       N  
ATOM   2693  CA  GLN A 366      76.557  -4.891 -27.906  1.00112.02           C  
ANISOU 2693  CA  GLN A 366    12031  14154  16376   -604    377   -209       C  
ATOM   2694  C   GLN A 366      75.391  -5.624 -27.231  1.00108.80           C  
ANISOU 2694  C   GLN A 366    11853  13714  15769   -495    133   -327       C  
ATOM   2695  O   GLN A 366      75.267  -6.845 -27.349  1.00107.88           O  
ANISOU 2695  O   GLN A 366    11842  13700  15447   -334     85   -393       O  
ATOM   2696  CB  GLN A 366      77.788  -4.891 -26.997  1.00113.66           C  
ANISOU 2696  CB  GLN A 366    11906  14408  16869   -657    310   -345       C  
ATOM   2697  CG  GLN A 366      79.079  -4.618 -27.742  1.00117.19           C  
ANISOU 2697  CG  GLN A 366    12068  14949  17509   -716    585   -245       C  
ATOM   2698  CD  GLN A 366      80.325  -4.929 -26.932  1.00119.08           C  
ANISOU 2698  CD  GLN A 366    11940  15267  18037   -718    486   -384       C  
ATOM   2699  OE1 GLN A 366      80.304  -4.936 -25.699  1.00118.43           O  
ANISOU 2699  OE1 GLN A 366    11811  15128  18055   -754    181   -535       O  
ATOM   2700  NE2 GLN A 366      81.427  -5.177 -27.630  1.00122.04           N  
ANISOU 2700  NE2 GLN A 366    12045  15776  18546   -681    746   -330       N  
ATOM   2701  N   GLU A 367      74.547  -4.877 -26.521  1.00107.40           N  
ANISOU 2701  N   GLU A 367    11746  13384  15676   -587     -3   -359       N  
ATOM   2702  CA  GLU A 367      73.338  -5.435 -25.911  1.00104.70           C  
ANISOU 2702  CA  GLU A 367    11603  13008  15171   -511   -183   -447       C  
ATOM   2703  C   GLU A 367      72.302  -5.840 -26.959  1.00103.18           C  
ANISOU 2703  C   GLU A 367    11639  12815  14748   -422   -155   -312       C  
ATOM   2704  O   GLU A 367      71.619  -6.852 -26.794  1.00101.70           O  
ANISOU 2704  O   GLU A 367    11594  12671  14374   -321   -272   -371       O  
ATOM   2705  CB  GLU A 367      72.714  -4.439 -24.927  1.00104.80           C  
ANISOU 2705  CB  GLU A 367    11612  12854  15352   -625   -280   -532       C  
ATOM   2706  CG  GLU A 367      73.532  -4.223 -23.661  1.00105.94           C  
ANISOU 2706  CG  GLU A 367    11604  13000  15648   -715   -393   -720       C  
ATOM   2707  CD  GLU A 367      73.005  -3.089 -22.798  1.00106.72           C  
ANISOU 2707  CD  GLU A 367    11723  12912  15911   -837   -447   -831       C  
ATOM   2708  OE1 GLU A 367      71.826  -2.708 -22.950  1.00106.14           O  
ANISOU 2708  OE1 GLU A 367    11782  12722  15825   -811   -416   -794       O  
ATOM   2709  OE2 GLU A 367      73.775  -2.577 -21.959  1.00108.48           O  
ANISOU 2709  OE2 GLU A 367    11825  13099  16293   -956   -529   -970       O  
ATOM   2710  N   ARG A 368      72.188  -5.054 -28.029  1.00103.77           N  
ANISOU 2710  N   ARG A 368    11759  12831  14837   -475    -22   -118       N  
ATOM   2711  CA  ARG A 368      71.211  -5.329 -29.087  1.00103.10           C  
ANISOU 2711  CA  ARG A 368    11908  12739  14525   -410    -40     29       C  
ATOM   2712  C   ARG A 368      71.557  -6.578 -29.900  1.00102.87           C  
ANISOU 2712  C   ARG A 368    12007  12879  14200   -284     17     16       C  
ATOM   2713  O   ARG A 368      70.663  -7.343 -30.266  1.00102.02           O  
ANISOU 2713  O   ARG A 368    12101  12781  13878   -203   -107     17       O  
ATOM   2714  CB  ARG A 368      71.052  -4.122 -30.021  1.00105.11           C  
ANISOU 2714  CB  ARG A 368    12206  12876  14853   -509     58    270       C  
ATOM   2715  CG  ARG A 368      70.428  -2.910 -29.351  1.00105.14           C  
ANISOU 2715  CG  ARG A 368    12135  12654  15156   -601    -25    284       C  
ATOM   2716  CD  ARG A 368      69.636  -2.035 -30.317  1.00106.70           C  
ANISOU 2716  CD  ARG A 368    12467  12695  15379   -633    -47    546       C  
ATOM   2717  NE  ARG A 368      70.479  -1.395 -31.337  1.00109.47           N  
ANISOU 2717  NE  ARG A 368    12834  13050  15710   -734    143    774       N  
ATOM   2718  CZ  ARG A 368      70.360  -1.512 -32.665  1.00111.14           C  
ANISOU 2718  CZ  ARG A 368    13254  13325  15647   -725    200   1008       C  
ATOM   2719  NH1 ARG A 368      69.422  -2.259 -33.250  1.00110.38           N  
ANISOU 2719  NH1 ARG A 368    13380  13290  15269   -617     44   1048       N  
ATOM   2720  NH2 ARG A 368      71.214  -0.850 -33.431  1.00114.01           N  
ANISOU 2720  NH2 ARG A 368    13614  13693  16011   -845    418   1213       N  
ATOM   2721  N   VAL A 369      72.843  -6.777 -30.185  1.00103.84           N  
ANISOU 2721  N   VAL A 369    11998  13120  14335   -268    208     -8       N  
ATOM   2722  CA  VAL A 369      73.296  -7.981 -30.897  1.00104.23           C  
ANISOU 2722  CA  VAL A 369    12149  13317  14134   -121    303    -68       C  
ATOM   2723  C   VAL A 369      73.233  -9.226 -30.011  1.00101.94           C  
ANISOU 2723  C   VAL A 369    11856  13054  13820      6    119   -273       C  
ATOM   2724  O   VAL A 369      72.925 -10.317 -30.493  1.00101.68           O  
ANISOU 2724  O   VAL A 369    12019  13059  13554    132     75   -332       O  
ATOM   2725  CB  VAL A 369      74.723  -7.834 -31.491  1.00107.26           C  
ANISOU 2725  CB  VAL A 369    12353  13825  14576   -124    611    -40       C  
ATOM   2726  CG1 VAL A 369      74.762  -6.702 -32.504  1.00109.56           C  
ANISOU 2726  CG1 VAL A 369    12702  14092  14833   -264    816    204       C  
ATOM   2727  CG2 VAL A 369      75.779  -7.623 -30.409  1.00107.58           C  
ANISOU 2727  CG2 VAL A 369    12034  13877  14962   -165    607   -155       C  
ATOM   2728  N   ALA A 370      73.526  -9.061 -28.723  1.00100.46           N  
ANISOU 2728  N   ALA A 370    11475  12833  13863    -37      0   -378       N  
ATOM   2729  CA  ALA A 370      73.472 -10.167 -27.767  1.00 98.82           C  
ANISOU 2729  CA  ALA A 370    11280  12636  13631     59   -197   -534       C  
ATOM   2730  C   ALA A 370      72.049 -10.703 -27.621  1.00 96.54           C  
ANISOU 2730  C   ALA A 370    11235  12272  13170     73   -381   -533       C  
ATOM   2731  O   ALA A 370      71.841 -11.915 -27.567  1.00 96.03           O  
ANISOU 2731  O   ALA A 370    11301  12217  12969    182   -490   -606       O  
ATOM   2732  CB  ALA A 370      74.014  -9.726 -26.415  1.00 98.69           C  
ANISOU 2732  CB  ALA A 370    11046  12598  13851    -23   -310   -624       C  
ATOM   2733  N   LYS A 371      71.079  -9.794 -27.553  1.00 95.45           N  
ANISOU 2733  N   LYS A 371    11141  12045  13080    -37   -417   -448       N  
ATOM   2734  CA  LYS A 371      69.660 -10.163 -27.507  1.00 93.86           C  
ANISOU 2734  CA  LYS A 371    11115  11772  12773    -39   -572   -424       C  
ATOM   2735  C   LYS A 371      69.224 -10.878 -28.788  1.00 94.21           C  
ANISOU 2735  C   LYS A 371    11379  11838  12578     37   -587   -356       C  
ATOM   2736  O   LYS A 371      68.533 -11.898 -28.734  1.00 93.59           O  
ANISOU 2736  O   LYS A 371    11445  11737  12376     83   -738   -403       O  
ATOM   2737  CB  LYS A 371      68.780  -8.921 -27.290  1.00 93.47           C  
ANISOU 2737  CB  LYS A 371    11019  11609  12884   -149   -581   -343       C  
ATOM   2738  CG  LYS A 371      68.736  -8.411 -25.858  1.00 92.76           C  
ANISOU 2738  CG  LYS A 371    10799  11470  12975   -225   -615   -462       C  
ATOM   2739  CD  LYS A 371      68.079  -7.039 -25.789  1.00 93.22           C  
ANISOU 2739  CD  LYS A 371    10793  11387  13236   -309   -573   -403       C  
ATOM   2740  CE  LYS A 371      67.651  -6.674 -24.375  1.00 92.83           C  
ANISOU 2740  CE  LYS A 371    10682  11277  13310   -369   -604   -557       C  
ATOM   2741  NZ  LYS A 371      68.777  -6.690 -23.399  1.00 93.23           N  
ANISOU 2741  NZ  LYS A 371    10649  11388  13383   -415   -610   -706       N  
ATOM   2742  N   LEU A 372      69.645 -10.341 -29.932  1.00 95.51           N  
ANISOU 2742  N   LEU A 372    11584  12040  12663     34   -432   -245       N  
ATOM   2743  CA  LEU A 372      69.189 -10.819 -31.238  1.00 96.36           C  
ANISOU 2743  CA  LEU A 372    11949  12171  12493     83   -451   -173       C  
ATOM   2744  C   LEU A 372      69.898 -12.104 -31.671  1.00 97.10           C  
ANISOU 2744  C   LEU A 372    12157  12348  12387    224   -391   -314       C  
ATOM   2745  O   LEU A 372      69.247 -13.096 -31.997  1.00 96.98           O  
ANISOU 2745  O   LEU A 372    12355  12300  12191    281   -547   -374       O  
ATOM   2746  CB  LEU A 372      69.393  -9.724 -32.291  1.00 98.23           C  
ANISOU 2746  CB  LEU A 372    12226  12419  12676     13   -294     19       C  
ATOM   2747  CG  LEU A 372      68.716  -9.900 -33.653  1.00 99.82           C  
ANISOU 2747  CG  LEU A 372    12733  12630  12563     21   -361    146       C  
ATOM   2748  CD1 LEU A 372      67.201  -9.935 -33.523  1.00 98.72           C  
ANISOU 2748  CD1 LEU A 372    12678  12372  12457    -15   -669    206       C  
ATOM   2749  CD2 LEU A 372      69.137  -8.773 -34.583  1.00102.22           C  
ANISOU 2749  CD2 LEU A 372    13075  12954  12809    -62   -172    364       C  
ATOM   2750  N   ALA A 373      71.229 -12.077 -31.669  1.00 98.07           N  
ANISOU 2750  N   ALA A 373    12120  12561  12577    281   -168   -374       N  
ATOM   2751  CA  ALA A 373      72.036 -13.219 -32.115  1.00 99.32           C  
ANISOU 2751  CA  ALA A 373    12347  12791  12600    447    -60   -523       C  
ATOM   2752  C   ALA A 373      72.143 -14.336 -31.069  1.00 97.78           C  
ANISOU 2752  C   ALA A 373    12095  12540  12516    549   -242   -687       C  
ATOM   2753  O   ALA A 373      72.448 -15.475 -31.414  1.00 98.90           O  
ANISOU 2753  O   ALA A 373    12359  12673  12544    703   -239   -820       O  
ATOM   2754  CB  ALA A 373      73.426 -12.750 -32.520  1.00101.67           C  
ANISOU 2754  CB  ALA A 373    12441  13208  12981    476    268   -516       C  
ATOM   2755  N   GLY A 374      71.897 -14.010 -29.802  1.00 95.52           N  
ANISOU 2755  N   GLY A 374    11649  12202  12441    464   -396   -676       N  
ATOM   2756  CA  GLY A 374      72.006 -14.982 -28.709  1.00 94.37           C  
ANISOU 2756  CA  GLY A 374    11468  12004  12384    533   -583   -787       C  
ATOM   2757  C   GLY A 374      70.929 -16.054 -28.712  1.00 93.28           C  
ANISOU 2757  C   GLY A 374    11589  11761  12093    554   -798   -817       C  
ATOM   2758  O   GLY A 374      71.210 -17.225 -28.439  1.00 93.84           O  
ANISOU 2758  O   GLY A 374    11726  11772  12155    674   -900   -917       O  
ATOM   2759  N   GLY A 375      69.695 -15.653 -29.006  1.00 78.13           N  
ANISOU 2759  N   GLY A 375    11673   8934   9077  -1022   -804  -1418       N  
ATOM   2760  CA  GLY A 375      68.573 -16.585 -29.087  1.00 76.72           C  
ANISOU 2760  CA  GLY A 375    11333   8701   9116   -736   -855  -1465       C  
ATOM   2761  C   GLY A 375      67.989 -16.946 -27.732  1.00 74.28           C  
ANISOU 2761  C   GLY A 375    10720   8374   9125   -364   -879  -1455       C  
ATOM   2762  O   GLY A 375      68.325 -16.333 -26.715  1.00 73.61           O  
ANISOU 2762  O   GLY A 375    10591   8277   9098   -288   -898  -1402       O  
ATOM   2763  N   VAL A 376      67.116 -17.952 -27.727  1.00 73.21           N  
ANISOU 2763  N   VAL A 376    10391   8253   9170   -172   -880  -1505       N  
ATOM   2764  CA  VAL A 376      66.419 -18.397 -26.516  1.00 71.37           C  
ANISOU 2764  CA  VAL A 376     9875   8043   9196    117   -907  -1498       C  
ATOM   2765  C   VAL A 376      66.466 -19.921 -26.388  1.00 70.47           C  
ANISOU 2765  C   VAL A 376     9491   8028   9253    166   -728  -1576       C  
ATOM   2766  O   VAL A 376      66.143 -20.632 -27.341  1.00 71.13           O  
ANISOU 2766  O   VAL A 376     9628   8106   9291     94   -718  -1629       O  
ATOM   2767  CB  VAL A 376      64.941 -17.950 -26.537  1.00 71.73           C  
ANISOU 2767  CB  VAL A 376     9991   8006   9256    304  -1193  -1472       C  
ATOM   2768  CG1 VAL A 376      64.179 -18.530 -25.351  1.00 70.41           C  
ANISOU 2768  CG1 VAL A 376     9488   7951   9313    540  -1188  -1492       C  
ATOM   2769  CG2 VAL A 376      64.845 -16.432 -26.544  1.00 72.93           C  
ANISOU 2769  CG2 VAL A 376    10450   8005   9253    326  -1443  -1414       C  
ATOM   2770  N   ALA A 377      66.860 -20.410 -25.211  1.00 69.15           N  
ANISOU 2770  N   ALA A 377     9078   7924   9269    280   -617  -1579       N  
ATOM   2771  CA  ALA A 377      66.823 -21.843 -24.910  1.00 68.60           C  
ANISOU 2771  CA  ALA A 377     8809   7892   9363    343   -522  -1637       C  
ATOM   2772  C   ALA A 377      65.403 -22.245 -24.533  1.00 68.38           C  
ANISOU 2772  C   ALA A 377     8694   7866   9419    443   -669  -1594       C  
ATOM   2773  O   ALA A 377      64.725 -21.522 -23.800  1.00 68.10           O  
ANISOU 2773  O   ALA A 377     8602   7867   9406    548   -783  -1540       O  
ATOM   2774  CB  ALA A 377      67.782 -22.182 -23.777  1.00 67.67           C  
ANISOU 2774  CB  ALA A 377     8502   7818   9388    410   -396  -1648       C  
ATOM   2775  N   VAL A 378      64.962 -23.397 -25.030  1.00 68.95           N  
ANISOU 2775  N   VAL A 378     8753   7926   9519    402   -669  -1635       N  
ATOM   2776  CA  VAL A 378      63.607 -23.886 -24.780  1.00 69.29           C  
ANISOU 2776  CA  VAL A 378     8703   8021   9602    425   -802  -1601       C  
ATOM   2777  C   VAL A 378      63.654 -25.296 -24.199  1.00 69.36           C  
ANISOU 2777  C   VAL A 378     8614   8016   9724    387   -759  -1605       C  
ATOM   2778  O   VAL A 378      63.831 -26.275 -24.929  1.00 70.27           O  
ANISOU 2778  O   VAL A 378     8831   8042   9824    318   -741  -1662       O  
ATOM   2779  CB  VAL A 378      62.758 -23.879 -26.070  1.00 70.53           C  
ANISOU 2779  CB  VAL A 378     9007   8156   9633    354   -921  -1622       C  
ATOM   2780  CG1 VAL A 378      61.345 -24.381 -25.796  1.00 71.09           C  
ANISOU 2780  CG1 VAL A 378     8936   8343   9728    354  -1058  -1600       C  
ATOM   2781  CG2 VAL A 378      62.709 -22.479 -26.662  1.00 71.08           C  
ANISOU 2781  CG2 VAL A 378     9250   8187   9569    380  -1026  -1608       C  
ATOM   2782  N   ILE A 379      63.492 -25.387 -22.881  1.00 68.81           N  
ANISOU 2782  N   ILE A 379     8380   8016   9746    424   -766  -1548       N  
ATOM   2783  CA  ILE A 379      63.429 -26.673 -22.196  1.00 69.26           C  
ANISOU 2783  CA  ILE A 379     8396   8038   9880    346   -783  -1523       C  
ATOM   2784  C   ILE A 379      62.000 -27.200 -22.281  1.00 70.44           C  
ANISOU 2784  C   ILE A 379     8498   8303   9961    211   -907  -1486       C  
ATOM   2785  O   ILE A 379      61.064 -26.525 -21.854  1.00 70.64           O  
ANISOU 2785  O   ILE A 379     8361   8534   9944    225   -963  -1466       O  
ATOM   2786  CB  ILE A 379      63.833 -26.554 -20.710  1.00 68.47           C  
ANISOU 2786  CB  ILE A 379     8163   7979   9871    384   -750  -1464       C  
ATOM   2787  CG1 ILE A 379      65.248 -25.978 -20.576  1.00 67.67           C  
ANISOU 2787  CG1 ILE A 379     8079   7802   9830    503   -634  -1501       C  
ATOM   2788  CG2 ILE A 379      63.765 -27.916 -20.027  1.00 69.28           C  
ANISOU 2788  CG2 ILE A 379     8298   8004  10021    262   -817  -1421       C  
ATOM   2789  CD1 ILE A 379      65.593 -25.511 -19.178  1.00 66.75           C  
ANISOU 2789  CD1 ILE A 379     7836   7741   9784    551   -609  -1436       C  
ATOM   2790  N   LYS A 380      61.838 -28.398 -22.838  1.00 71.70           N  
ANISOU 2790  N   LYS A 380     8794   8351  10096     83   -961  -1498       N  
ATOM   2791  CA  LYS A 380      60.538 -29.064 -22.885  1.00 73.20           C  
ANISOU 2791  CA  LYS A 380     8952   8660  10198   -112  -1086  -1453       C  
ATOM   2792  C   LYS A 380      60.536 -30.241 -21.916  1.00 74.10           C  
ANISOU 2792  C   LYS A 380     9112   8714  10328   -290  -1149  -1380       C  
ATOM   2793  O   LYS A 380      61.212 -31.244 -22.143  1.00 74.79           O  
ANISOU 2793  O   LYS A 380     9422   8543  10450   -311  -1191  -1400       O  
ATOM   2794  CB  LYS A 380      60.210 -29.517 -24.310  1.00 74.35           C  
ANISOU 2794  CB  LYS A 380     9276   8710  10262   -178  -1143  -1502       C  
ATOM   2795  CG  LYS A 380      59.526 -28.442 -25.141  1.00 74.54           C  
ANISOU 2795  CG  LYS A 380     9241   8870  10208   -108  -1178  -1533       C  
ATOM   2796  CD  LYS A 380      59.335 -28.861 -26.592  1.00 75.66           C  
ANISOU 2796  CD  LYS A 380     9593   8896  10259   -184  -1230  -1578       C  
ATOM   2797  CE  LYS A 380      60.417 -28.292 -27.496  1.00 75.21           C  
ANISOU 2797  CE  LYS A 380     9704   8683  10186    -71  -1125  -1654       C  
ATOM   2798  NZ  LYS A 380      60.186 -28.655 -28.922  1.00 76.53           N  
ANISOU 2798  NZ  LYS A 380    10080   8760  10236   -168  -1172  -1706       N  
ATOM   2799  N   VAL A 381      59.767 -30.105 -20.838  1.00 74.63           N  
ANISOU 2799  N   VAL A 381     8982   9025  10349   -421  -1177  -1312       N  
ATOM   2800  CA  VAL A 381      59.773 -31.072 -19.744  1.00 75.80           C  
ANISOU 2800  CA  VAL A 381     9189   9135  10474   -643  -1248  -1219       C  
ATOM   2801  C   VAL A 381      58.890 -32.271 -20.084  1.00 78.22           C  
ANISOU 2801  C   VAL A 381     9645   9435  10637   -971  -1402  -1164       C  
ATOM   2802  O   VAL A 381      57.682 -32.125 -20.263  1.00 79.47           O  
ANISOU 2802  O   VAL A 381     9630   9900  10665  -1143  -1433  -1161       O  
ATOM   2803  CB  VAL A 381      59.276 -30.432 -18.428  1.00 75.68           C  
ANISOU 2803  CB  VAL A 381     8897   9438  10419   -708  -1201  -1177       C  
ATOM   2804  CG1 VAL A 381      59.309 -31.441 -17.287  1.00 77.09           C  
ANISOU 2804  CG1 VAL A 381     9182   9571  10537  -1000  -1288  -1064       C  
ATOM   2805  CG2 VAL A 381      60.118 -29.213 -18.076  1.00 73.65           C  
ANISOU 2805  CG2 VAL A 381     8526   9169  10287   -399  -1072  -1224       C  
ATOM   2806  N   GLY A 382      59.501 -33.452 -20.157  1.00 79.45           N  
ANISOU 2806  N   GLY A 382    10130   9247  10811  -1053  -1521  -1135       N  
ATOM   2807  CA  GLY A 382      58.786 -34.690 -20.468  1.00 82.06           C  
ANISOU 2807  CA  GLY A 382    10699   9489  10988  -1389  -1709  -1071       C  
ATOM   2808  C   GLY A 382      58.468 -35.513 -19.232  1.00 84.08           C  
ANISOU 2808  C   GLY A 382    11064   9759  11123  -1755  -1853   -929       C  
ATOM   2809  O   GLY A 382      59.143 -35.399 -18.207  1.00 83.45           O  
ANISOU 2809  O   GLY A 382    10982   9608  11117  -1693  -1839   -890       O  
ATOM   2810  N   ALA A 383      57.432 -36.343 -19.337  1.00 86.69           N  
ANISOU 2810  N   ALA A 383    11507  10187  11241  -2177  -2004   -844       N  
ATOM   2811  CA  ALA A 383      57.048 -37.265 -18.265  1.00 89.27           C  
ANISOU 2811  CA  ALA A 383    12019  10519  11381  -2642  -2182   -688       C  
ATOM   2812  C   ALA A 383      56.139 -38.369 -18.807  1.00 92.39           C  
ANISOU 2812  C   ALA A 383    12682  10879  11542  -3088  -2393   -609       C  
ATOM   2813  O   ALA A 383      55.708 -38.317 -19.959  1.00 92.28           O  
ANISOU 2813  O   ALA A 383    12639  10901  11518  -3024  -2376   -680       O  
ATOM   2814  CB  ALA A 383      56.357 -36.514 -17.136  1.00 89.26           C  
ANISOU 2814  CB  ALA A 383    11605  11035  11272  -2833  -2043   -649       C  
ATOM   2815  N   ALA A 384      55.849 -39.362 -17.970  1.00 95.45           N  
ANISOU 2815  N   ALA A 384    13358  11190  11718  -3573  -2609   -451       N  
ATOM   2816  CA  ALA A 384      55.014 -40.497 -18.370  1.00 99.02           C  
ANISOU 2816  CA  ALA A 384    14138  11581  11904  -4083  -2852   -346       C  
ATOM   2817  C   ALA A 384      53.553 -40.088 -18.552  1.00100.25           C  
ANISOU 2817  C   ALA A 384    13860  12388  11840  -4437  -2734   -346       C  
ATOM   2818  O   ALA A 384      52.953 -40.359 -19.594  1.00101.22           O  
ANISOU 2818  O   ALA A 384    14027  12542  11889  -4525  -2790   -375       O  
ATOM   2819  CB  ALA A 384      55.124 -41.619 -17.348  1.00102.17           C  
ANISOU 2819  CB  ALA A 384    15007  11713  12100  -4555  -3148   -161       C  
ATOM   2820  N   THR A 385      52.995 -39.441 -17.532  1.00100.60           N  
ANISOU 2820  N   THR A 385    13476  12970  11777  -4627  -2579   -334       N  
ATOM   2821  CA  THR A 385      51.614 -38.958 -17.563  1.00102.24           C  
ANISOU 2821  CA  THR A 385    13174  13894  11775  -4915  -2458   -389       C  
ATOM   2822  C   THR A 385      51.581 -37.430 -17.556  1.00 99.66           C  
ANISOU 2822  C   THR A 385    12263  13952  11652  -4400  -2177   -579       C  
ATOM   2823  O   THR A 385      52.611 -36.781 -17.363  1.00 96.80           O  
ANISOU 2823  O   THR A 385    11907  13322  11550  -3921  -2071   -629       O  
ATOM   2824  CB  THR A 385      50.813 -39.488 -16.357  1.00105.79           C  
ANISOU 2824  CB  THR A 385    13565  14770  11858  -5628  -2521   -262       C  
ATOM   2825  OG1 THR A 385      51.440 -39.070 -15.139  1.00104.55           O  
ANISOU 2825  OG1 THR A 385    13335  14624  11764  -5536  -2426   -241       O  
ATOM   2826  CG2 THR A 385      50.738 -41.008 -16.390  1.00109.22           C  
ANISOU 2826  CG2 THR A 385    14643  14815  12039  -6212  -2855    -55       C  
ATOM   2827  N   GLU A 386      50.395 -36.863 -17.768  1.00101.23           N  
ANISOU 2827  N   GLU A 386    11969  14776  11718  -4499  -2086   -695       N  
ATOM   2828  CA  GLU A 386      50.224 -35.409 -17.796  1.00 99.50           C  
ANISOU 2828  CA  GLU A 386    11220  14924  11661  -4004  -1884   -898       C  
ATOM   2829  C   GLU A 386      50.358 -34.783 -16.406  1.00 99.61           C  
ANISOU 2829  C   GLU A 386    10945  15248  11654  -3988  -1737   -937       C  
ATOM   2830  O   GLU A 386      50.866 -33.670 -16.274  1.00 97.19           O  
ANISOU 2830  O   GLU A 386    10437  14924  11566  -3474  -1602  -1057       O  
ATOM   2831  CB  GLU A 386      48.866 -35.038 -18.397  1.00101.62           C  
ANISOU 2831  CB  GLU A 386    11040  15786  11782  -4093  -1882  -1043       C  
ATOM   2832  CG  GLU A 386      48.714 -33.555 -18.710  1.00 99.86           C  
ANISOU 2832  CG  GLU A 386    10375  15815  11751  -3495  -1760  -1271       C  
ATOM   2833  CD  GLU A 386      47.388 -33.220 -19.368  1.00102.31           C  
ANISOU 2833  CD  GLU A 386    10260  16681  11930  -3529  -1813  -1436       C  
ATOM   2834  OE1 GLU A 386      46.374 -33.877 -19.050  1.00105.80           O  
ANISOU 2834  OE1 GLU A 386    10500  17620  12077  -4072  -1858  -1428       O  
ATOM   2835  OE2 GLU A 386      47.357 -32.292 -20.203  1.00101.01           O  
ANISOU 2835  OE2 GLU A 386     9968  16468  11942  -3031  -1829  -1578       O  
ATOM   2836  N   VAL A 387      49.903 -35.497 -15.378  1.00102.87           N  
ANISOU 2836  N   VAL A 387    11366  15940  11778  -4582  -1777   -833       N  
ATOM   2837  CA  VAL A 387      49.978 -35.004 -13.999  1.00103.35           C  
ANISOU 2837  CA  VAL A 387    11173  16329  11767  -4651  -1641   -866       C  
ATOM   2838  C   VAL A 387      51.438 -34.880 -13.550  1.00100.29           C  
ANISOU 2838  C   VAL A 387    11140  15327  11638  -4310  -1632   -770       C  
ATOM   2839  O   VAL A 387      51.806 -33.912 -12.883  1.00 98.57           O  
ANISOU 2839  O   VAL A 387    10670  15240  11543  -3983  -1477   -868       O  
ATOM   2840  CB  VAL A 387      49.203 -35.919 -13.019  1.00107.78           C  
ANISOU 2840  CB  VAL A 387    11736  17309  11905  -5467  -1704   -750       C  
ATOM   2841  CG1 VAL A 387      49.365 -35.438 -11.580  1.00108.14           C  
ANISOU 2841  CG1 VAL A 387    11560  17664  11862  -5555  -1559   -780       C  
ATOM   2842  CG2 VAL A 387      47.727 -35.979 -13.395  1.00111.41           C  
ANISOU 2842  CG2 VAL A 387    11753  18493  12082  -5829  -1690   -876       C  
ATOM   2843  N   GLU A 388      52.256 -35.862 -13.925  1.00 99.98           N  
ANISOU 2843  N   GLU A 388    11681  14632  11674  -4375  -1817   -600       N  
ATOM   2844  CA  GLU A 388      53.686 -35.855 -13.609  1.00 97.55           C  
ANISOU 2844  CA  GLU A 388    11713  13733  11617  -4033  -1844   -532       C  
ATOM   2845  C   GLU A 388      54.441 -34.792 -14.408  1.00 94.07           C  
ANISOU 2845  C   GLU A 388    11141  13081  11518  -3327  -1704   -678       C  
ATOM   2846  O   GLU A 388      55.413 -34.218 -13.916  1.00 92.09           O  
ANISOU 2846  O   GLU A 388    10901  12630  11460  -2992  -1621   -693       O  
ATOM   2847  CB  GLU A 388      54.302 -37.232 -13.878  1.00 98.73           C  
ANISOU 2847  CB  GLU A 388    12511  13257  11745  -4250  -2123   -362       C  
ATOM   2848  CG  GLU A 388      53.773 -38.340 -12.979  1.00102.73           C  
ANISOU 2848  CG  GLU A 388    13297  13839  11896  -4988  -2326   -173       C  
ATOM   2849  CD  GLU A 388      54.250 -39.716 -13.405  1.00104.49           C  
ANISOU 2849  CD  GLU A 388    14214  13408  12079  -5183  -2668    -26       C  
ATOM   2850  OE1 GLU A 388      53.412 -40.638 -13.490  1.00108.07           O  
ANISOU 2850  OE1 GLU A 388    14890  13954  12218  -5782  -2856     90       O  
ATOM   2851  OE2 GLU A 388      55.463 -39.875 -13.659  1.00102.60           O  
ANISOU 2851  OE2 GLU A 388    14297  12576  12109  -4735  -2764    -44       O  
ATOM   2852  N   MET A 389      53.994 -34.542 -15.636  1.00 93.89           N  
ANISOU 2852  N   MET A 389    11017  13108  11546  -3142  -1691   -776       N  
ATOM   2853  CA  MET A 389      54.613 -33.540 -16.507  1.00 91.03           C  
ANISOU 2853  CA  MET A 389    10569  12565  11452  -2551  -1581   -905       C  
ATOM   2854  C   MET A 389      54.393 -32.122 -15.982  1.00 89.99           C  
ANISOU 2854  C   MET A 389     9985  12827  11380  -2251  -1407  -1044       C  
ATOM   2855  O   MET A 389      55.307 -31.298 -16.011  1.00 87.48           O  
ANISOU 2855  O   MET A 389     9679  12288  11269  -1832  -1319  -1092       O  
ATOM   2856  CB  MET A 389      54.056 -33.664 -17.929  1.00 91.54           C  
ANISOU 2856  CB  MET A 389    10662  12612  11505  -2502  -1642   -964       C  
ATOM   2857  CG  MET A 389      54.801 -32.849 -18.979  1.00 88.86           C  
ANISOU 2857  CG  MET A 389    10367  11994  11398  -1981  -1569  -1065       C  
ATOM   2858  SD  MET A 389      54.053 -31.252 -19.373  1.00 88.32           S  
ANISOU 2858  SD  MET A 389     9836  12352  11367  -1632  -1472  -1245       S  
ATOM   2859  CE  MET A 389      52.415 -31.731 -19.929  1.00 91.64           C  
ANISOU 2859  CE  MET A 389    10047  13218  11551  -1984  -1590  -1283       C  
ATOM   2860  N   LYS A 390      53.181 -31.845 -15.507  1.00 92.53           N  
ANISOU 2860  N   LYS A 390     9908  13745  11501  -2472  -1371  -1127       N  
ATOM   2861  CA  LYS A 390      52.845 -30.535 -14.943  1.00 92.54           C  
ANISOU 2861  CA  LYS A 390     9468  14161  11529  -2178  -1239  -1303       C  
ATOM   2862  C   LYS A 390      53.557 -30.296 -13.613  1.00 91.76           C  
ANISOU 2862  C   LYS A 390     9380  14026  11456  -2178  -1148  -1254       C  
ATOM   2863  O   LYS A 390      54.033 -29.190 -13.351  1.00 90.00           O  
ANISOU 2863  O   LYS A 390     9027  13784  11382  -1768  -1056  -1351       O  
ATOM   2864  CB  LYS A 390      51.331 -30.405 -14.740  1.00 96.12           C  
ANISOU 2864  CB  LYS A 390     9452  15333  11737  -2421  -1233  -1451       C  
ATOM   2865  CG  LYS A 390      50.516 -30.425 -16.025  1.00 97.27           C  
ANISOU 2865  CG  LYS A 390     9505  15595  11859  -2366  -1331  -1536       C  
ATOM   2866  CD  LYS A 390      50.650 -29.126 -16.801  1.00 95.59           C  
ANISOU 2866  CD  LYS A 390     9171  15295  11854  -1750  -1334  -1704       C  
ATOM   2867  CE  LYS A 390      49.784 -29.141 -18.049  1.00 97.08           C  
ANISOU 2867  CE  LYS A 390     9271  15611  12001  -1710  -1462  -1788       C  
ATOM   2868  NZ  LYS A 390      49.854 -27.851 -18.789  1.00 95.95           N  
ANISOU 2868  NZ  LYS A 390     9057  15372  12027  -1138  -1518  -1947       N  
ATOM   2869  N   GLU A 391      53.617 -31.333 -12.780  1.00 93.43           N  
ANISOU 2869  N   GLU A 391     9781  14213  11504  -2661  -1200  -1095       N  
ATOM   2870  CA  GLU A 391      54.267 -31.245 -11.471  1.00 93.14           C  
ANISOU 2870  CA  GLU A 391     9796  14130  11461  -2734  -1144  -1024       C  
ATOM   2871  C   GLU A 391      55.776 -31.050 -11.626  1.00 89.77           C  
ANISOU 2871  C   GLU A 391     9699  13083  11327  -2339  -1153   -951       C  
ATOM   2872  O   GLU A 391      56.379 -30.251 -10.905  1.00 88.46           O  
ANISOU 2872  O   GLU A 391     9439  12908  11262  -2097  -1055   -985       O  
ATOM   2873  CB  GLU A 391      53.966 -32.498 -10.634  1.00 96.32           C  
ANISOU 2873  CB  GLU A 391    10410  14601  11586  -3401  -1254   -849       C  
ATOM   2874  CG  GLU A 391      54.112 -32.315  -9.125  1.00 97.38           C  
ANISOU 2874  CG  GLU A 391    10452  14958  11588  -3618  -1180   -815       C  
ATOM   2875  CD  GLU A 391      55.550 -32.384  -8.635  1.00 95.10           C  
ANISOU 2875  CD  GLU A 391    10535  14085  11513  -3405  -1234   -683       C  
ATOM   2876  OE1 GLU A 391      56.290 -33.298  -9.060  1.00 94.69           O  
ANISOU 2876  OE1 GLU A 391    10948  13472  11558  -3436  -1418   -535       O  
ATOM   2877  OE2 GLU A 391      55.938 -31.529  -7.810  1.00 93.94           O  
ANISOU 2877  OE2 GLU A 391    10209  14052  11429  -3196  -1106   -743       O  
ATOM   2878  N   LYS A 392      56.377 -31.777 -12.567  1.00 88.74           N  
ANISOU 2878  N   LYS A 392     9935  12468  11315  -2278  -1272   -870       N  
ATOM   2879  CA  LYS A 392      57.809 -31.652 -12.847  1.00 86.11           C  
ANISOU 2879  CA  LYS A 392     9869  11605  11242  -1903  -1278   -843       C  
ATOM   2880  C   LYS A 392      58.140 -30.286 -13.447  1.00 83.31           C  
ANISOU 2880  C   LYS A 392     9304  11280  11069  -1402  -1135   -986       C  
ATOM   2881  O   LYS A 392      59.125 -29.658 -13.061  1.00 81.63           O  
ANISOU 2881  O   LYS A 392     9114  10892  11007  -1134  -1065   -992       O  
ATOM   2882  CB  LYS A 392      58.280 -32.766 -13.789  1.00 86.68           C  
ANISOU 2882  CB  LYS A 392    10347  11215  11369  -1941  -1442   -779       C  
ATOM   2883  CG  LYS A 392      59.792 -32.845 -13.950  1.00 85.10           C  
ANISOU 2883  CG  LYS A 392    10407  10521  11405  -1600  -1468   -780       C  
ATOM   2884  CD  LYS A 392      60.207 -34.012 -14.832  1.00 86.37           C  
ANISOU 2884  CD  LYS A 392    10960  10256  11598  -1618  -1650   -765       C  
ATOM   2885  CE  LYS A 392      61.718 -34.070 -14.996  1.00 85.15           C  
ANISOU 2885  CE  LYS A 392    10992   9691  11671  -1242  -1670   -826       C  
ATOM   2886  NZ  LYS A 392      62.140 -35.123 -15.960  1.00 86.52           N  
ANISOU 2886  NZ  LYS A 392    11513   9479  11882  -1176  -1840   -879       N  
ATOM   2887  N   LYS A 393      57.314 -29.835 -14.388  1.00 83.21           N  
ANISOU 2887  N   LYS A 393     9112  11480  11022  -1302  -1119  -1094       N  
ATOM   2888  CA  LYS A 393      57.495 -28.529 -15.026  1.00 81.27           C  
ANISOU 2888  CA  LYS A 393     8725  11247  10905   -868  -1041  -1223       C  
ATOM   2889  C   LYS A 393      57.527 -27.390 -14.008  1.00 80.37           C  
ANISOU 2889  C   LYS A 393     8361  11371  10802   -684   -945  -1299       C  
ATOM   2890  O   LYS A 393      58.313 -26.452 -14.146  1.00 78.40           O  
ANISOU 2890  O   LYS A 393     8157  10939  10690   -353   -896  -1336       O  
ATOM   2891  CB  LYS A 393      56.380 -28.283 -16.044  1.00 82.72           C  
ANISOU 2891  CB  LYS A 393     8748  11673  11008   -839  -1092  -1329       C  
ATOM   2892  CG  LYS A 393      56.491 -26.971 -16.802  1.00 81.66           C  
ANISOU 2892  CG  LYS A 393     8546  11505  10975   -417  -1080  -1453       C  
ATOM   2893  CD  LYS A 393      55.397 -26.863 -17.852  1.00 83.44           C  
ANISOU 2893  CD  LYS A 393     8656  11927  11119   -402  -1180  -1547       C  
ATOM   2894  CE  LYS A 393      55.492 -25.566 -18.638  1.00 82.86           C  
ANISOU 2894  CE  LYS A 393     8591  11768  11123     -1  -1229  -1658       C  
ATOM   2895  NZ  LYS A 393      55.099 -24.380 -17.827  1.00 83.61           N  
ANISOU 2895  NZ  LYS A 393     8413  12148  11206    250  -1234  -1798       N  
ATOM   2896  N   ALA A 394      56.670 -27.479 -12.993  1.00 81.98           N  
ANISOU 2896  N   ALA A 394     8311  11999  10836   -927   -922  -1329       N  
ATOM   2897  CA  ALA A 394      56.637 -26.492 -11.916  1.00 81.75           C  
ANISOU 2897  CA  ALA A 394     8040  12231  10787   -779   -833  -1423       C  
ATOM   2898  C   ALA A 394      57.956 -26.463 -11.146  1.00 79.67           C  
ANISOU 2898  C   ALA A 394     7999  11624  10648   -724   -789  -1301       C  
ATOM   2899  O   ALA A 394      58.481 -25.389 -10.847  1.00 78.37           O  
ANISOU 2899  O   ALA A 394     7787  11409  10578   -417   -732  -1363       O  
ATOM   2900  CB  ALA A 394      55.482 -26.783 -10.969  1.00 84.72           C  
ANISOU 2900  CB  ALA A 394     8099  13176  10915  -1127   -803  -1490       C  
ATOM   2901  N   ARG A 395      58.485 -27.645 -10.831  1.00 79.66           N  
ANISOU 2901  N   ARG A 395     8258  11371  10636  -1021   -846  -1133       N  
ATOM   2902  CA  ARG A 395      59.760 -27.762 -10.118  1.00 77.99           C  
ANISOU 2902  CA  ARG A 395     8265  10820  10546   -972   -845  -1021       C  
ATOM   2903  C   ARG A 395      60.945 -27.266 -10.954  1.00 75.35           C  
ANISOU 2903  C   ARG A 395     8094  10093  10439   -589   -826  -1036       C  
ATOM   2904  O   ARG A 395      61.926 -26.774 -10.400  1.00 74.24           O  
ANISOU 2904  O   ARG A 395     8004   9797  10407   -430   -784  -1010       O  
ATOM   2905  CB  ARG A 395      60.003 -29.207  -9.660  1.00 79.34           C  
ANISOU 2905  CB  ARG A 395     8723  10777  10643  -1358   -981   -853       C  
ATOM   2906  CG  ARG A 395      59.068 -29.667  -8.550  1.00 81.99           C  
ANISOU 2906  CG  ARG A 395     8945  11495  10710  -1828   -996   -804       C  
ATOM   2907  CD  ARG A 395      59.507 -30.982  -7.920  1.00 83.48           C  
ANISOU 2907  CD  ARG A 395     9513  11386  10817  -2213  -1180   -610       C  
ATOM   2908  NE  ARG A 395      59.274 -32.135  -8.794  1.00 84.77           N  
ANISOU 2908  NE  ARG A 395     9955  11316  10936  -2411  -1353   -541       N  
ATOM   2909  CZ  ARG A 395      60.173 -32.682  -9.618  1.00 83.71           C  
ANISOU 2909  CZ  ARG A 395    10136  10676  10992  -2184  -1477   -518       C  
ATOM   2910  NH1 ARG A 395      61.410 -32.200  -9.716  1.00 81.46           N  
ANISOU 2910  NH1 ARG A 395     9904  10088  10956  -1763  -1438   -558       N  
ATOM   2911  NH2 ARG A 395      59.827 -33.731 -10.357  1.00 85.24           N  
ANISOU 2911  NH2 ARG A 395    10588  10690  11108  -2389  -1644   -471       N  
ATOM   2912  N   VAL A 396      60.851 -27.396 -12.277  1.00 74.60           N  
ANISOU 2912  N   VAL A 396     8078   9872  10394   -478   -855  -1080       N  
ATOM   2913  CA  VAL A 396      61.888 -26.894 -13.184  1.00 72.51           C  
ANISOU 2913  CA  VAL A 396     7945   9311  10291   -171   -820  -1116       C  
ATOM   2914  C   VAL A 396      61.910 -25.362 -13.216  1.00 71.38           C  
ANISOU 2914  C   VAL A 396     7655   9294  10173    107   -743  -1208       C  
ATOM   2915  O   VAL A 396      62.981 -24.756 -13.162  1.00 70.20           O  
ANISOU 2915  O   VAL A 396     7587   8961  10122    283   -694  -1200       O  
ATOM   2916  CB  VAL A 396      61.709 -27.446 -14.617  1.00 72.67           C  
ANISOU 2916  CB  VAL A 396     8102   9190  10318   -165   -872  -1149       C  
ATOM   2917  CG1 VAL A 396      62.630 -26.733 -15.601  1.00 71.21           C  
ANISOU 2917  CG1 VAL A 396     8009   8805  10241    110   -811  -1213       C  
ATOM   2918  CG2 VAL A 396      61.979 -28.942 -14.644  1.00 73.74           C  
ANISOU 2918  CG2 VAL A 396     8475   9088  10451   -380   -984  -1070       C  
ATOM   2919  N   GLU A 397      60.733 -24.747 -13.308  1.00 72.31           N  
ANISOU 2919  N   GLU A 397     7564   9723  10185    146   -759  -1306       N  
ATOM   2920  CA  GLU A 397      60.624 -23.285 -13.331  1.00 71.99           C  
ANISOU 2920  CA  GLU A 397     7428   9775  10148    438   -754  -1414       C  
ATOM   2921  C   GLU A 397      61.141 -22.658 -12.039  1.00 71.26           C  
ANISOU 2921  C   GLU A 397     7277   9725  10070    498   -694  -1403       C  
ATOM   2922  O   GLU A 397      61.893 -21.682 -12.080  1.00 70.28           O  
ANISOU 2922  O   GLU A 397     7254   9440  10007    708   -685  -1413       O  
ATOM   2923  CB  GLU A 397      59.172 -22.855 -13.558  1.00 74.03           C  
ANISOU 2923  CB  GLU A 397     7443  10395  10288    499   -825  -1563       C  
ATOM   2924  CG  GLU A 397      58.661 -23.122 -14.964  1.00 74.73           C  
ANISOU 2924  CG  GLU A 397     7603  10428  10363    510   -910  -1592       C  
ATOM   2925  CD  GLU A 397      57.218 -22.692 -15.166  1.00 77.24           C  
ANISOU 2925  CD  GLU A 397     7647  11132  10568    596  -1008  -1760       C  
ATOM   2926  OE1 GLU A 397      56.856 -22.365 -16.315  1.00 77.88           O  
ANISOU 2926  OE1 GLU A 397     7799  11143  10647    735  -1119  -1817       O  
ATOM   2927  OE2 GLU A 397      56.440 -22.680 -14.188  1.00 79.02           O  
ANISOU 2927  OE2 GLU A 397     7575  11755  10692    522   -983  -1852       O  
ATOM   2928  N   ASP A 398      60.731 -23.219 -10.901  1.00 71.98           N  
ANISOU 2928  N   ASP A 398     7228  10040  10080    274   -663  -1375       N  
ATOM   2929  CA  ASP A 398      61.174 -22.738  -9.588  1.00 71.48           C  
ANISOU 2929  CA  ASP A 398     7113  10036  10008    285   -607  -1359       C  
ATOM   2930  C   ASP A 398      62.675 -22.927  -9.398  1.00 69.25           C  
ANISOU 2930  C   ASP A 398     7068   9375   9868    299   -585  -1222       C  
ATOM   2931  O   ASP A 398      63.349 -22.046  -8.864  1.00 68.32           O  
ANISOU 2931  O   ASP A 398     6976   9188   9791    451   -553  -1225       O  
ATOM   2932  CB  ASP A 398      60.423 -23.454  -8.456  1.00 73.48           C  
ANISOU 2932  CB  ASP A 398     7195  10619  10103    -43   -581  -1345       C  
ATOM   2933  CG  ASP A 398      58.954 -23.066  -8.380  1.00 76.09           C  
ANISOU 2933  CG  ASP A 398     7191  11454  10264    -39   -576  -1537       C  
ATOM   2934  OD1 ASP A 398      58.504 -22.212  -9.174  1.00 76.47           O  
ANISOU 2934  OD1 ASP A 398     7154  11561  10339    267   -625  -1686       O  
ATOM   2935  OD2 ASP A 398      58.243 -23.622  -7.518  1.00 78.47           O  
ANISOU 2935  OD2 ASP A 398     7312  12114  10388   -357   -539  -1551       O  
ATOM   2936  N   ALA A 399      63.187 -24.078  -9.831  1.00 68.54           N  
ANISOU 2936  N   ALA A 399     7147   9052   9842    150   -620  -1121       N  
ATOM   2937  CA  ALA A 399      64.620 -24.362  -9.763  1.00 66.95           C  
ANISOU 2937  CA  ALA A 399     7133   8522   9782    201   -622  -1036       C  
ATOM   2938  C   ALA A 399      65.415 -23.449 -10.692  1.00 65.37           C  
ANISOU 2938  C   ALA A 399     7000   8168   9669    455   -577  -1091       C  
ATOM   2939  O   ALA A 399      66.536 -23.058 -10.373  1.00 64.48           O  
ANISOU 2939  O   ALA A 399     6947   7917   9634    539   -545  -1061       O  
ATOM   2940  CB  ALA A 399      64.892 -25.821 -10.097  1.00 67.68           C  
ANISOU 2940  CB  ALA A 399     7396   8404   9913     36   -713   -967       C  
ATOM   2941  N   LEU A 400      64.830 -23.112 -11.839  1.00 65.31           N  
ANISOU 2941  N   LEU A 400     6992   8198   9623    542   -587  -1167       N  
ATOM   2942  CA  LEU A 400      65.455 -22.188 -12.784  1.00 64.43           C  
ANISOU 2942  CA  LEU A 400     6983   7960   9535    716   -565  -1211       C  
ATOM   2943  C   LEU A 400      65.552 -20.771 -12.214  1.00 63.96           C  
ANISOU 2943  C   LEU A 400     6906   7959   9435    860   -565  -1237       C  
ATOM   2944  O   LEU A 400      66.533 -20.072 -12.466  1.00 63.32           O  
ANISOU 2944  O   LEU A 400     6948   7738   9372    924   -541  -1220       O  
ATOM   2945  CB  LEU A 400      64.684 -22.171 -14.109  1.00 65.03           C  
ANISOU 2945  CB  LEU A 400     7097   8057   9553    747   -612  -1278       C  
ATOM   2946  CG  LEU A 400      65.253 -21.312 -15.244  1.00 64.67           C  
ANISOU 2946  CG  LEU A 400     7214   7874   9484    854   -613  -1312       C  
ATOM   2947  CD1 LEU A 400      66.630 -21.800 -15.669  1.00 64.13           C  
ANISOU 2947  CD1 LEU A 400     7247   7635   9483    803   -525  -1293       C  
ATOM   2948  CD2 LEU A 400      64.295 -21.312 -16.425  1.00 65.55           C  
ANISOU 2948  CD2 LEU A 400     7365   8019   9519    869   -694  -1371       C  
ATOM   2949  N   HIS A 401      64.547 -20.353 -11.445  1.00 64.65           N  
ANISOU 2949  N   HIS A 401     6845   8270   9447    899   -600  -1292       N  
ATOM   2950  CA  HIS A 401      64.559 -19.020 -10.838  1.00 64.68           C  
ANISOU 2950  CA  HIS A 401     6852   8319   9402   1071   -632  -1346       C  
ATOM   2951  C   HIS A 401      65.630 -18.953  -9.752  1.00 63.41           C  
ANISOU 2951  C   HIS A 401     6725   8071   9293   1009   -566  -1254       C  
ATOM   2952  O   HIS A 401      66.387 -17.982  -9.672  1.00 62.76           O  
ANISOU 2952  O   HIS A 401     6774   7862   9207   1101   -579  -1239       O  
ATOM   2953  CB  HIS A 401      63.196 -18.681 -10.226  1.00 66.54           C  
ANISOU 2953  CB  HIS A 401     6869   8874   9536   1153   -682  -1482       C  
ATOM   2954  CG  HIS A 401      62.144 -18.302 -11.225  1.00 68.10           C  
ANISOU 2954  CG  HIS A 401     7029   9172   9675   1308   -798  -1614       C  
ATOM   2955  ND1 HIS A 401      62.026 -18.900 -12.464  1.00 68.08           N  
ANISOU 2955  ND1 HIS A 401     7107   9066   9693   1239   -822  -1582       N  
ATOM   2956  CD2 HIS A 401      61.138 -17.397 -11.149  1.00 69.97           C  
ANISOU 2956  CD2 HIS A 401     7149   9608   9826   1548   -919  -1797       C  
ATOM   2957  CE1 HIS A 401      61.004 -18.369 -13.113  1.00 69.60           C  
ANISOU 2957  CE1 HIS A 401     7245   9380   9818   1410   -956  -1718       C  
ATOM   2958  NE2 HIS A 401      60.448 -17.455 -12.337  1.00 70.93           N  
ANISOU 2958  NE2 HIS A 401     7287   9735   9927   1617  -1028  -1860       N  
ATOM   2959  N   ALA A 402      65.682 -19.993  -8.921  1.00 63.17           N  
ANISOU 2959  N   ALA A 402     6606   8102   9295    827   -520  -1185       N  
ATOM   2960  CA  ALA A 402      66.651 -20.082  -7.830  1.00 62.37           C  
ANISOU 2960  CA  ALA A 402     6536   7916   9243    752   -485  -1091       C  
ATOM   2961  C   ALA A 402      68.083 -20.221  -8.342  1.00 61.24           C  
ANISOU 2961  C   ALA A 402     6531   7523   9214    766   -465  -1025       C  
ATOM   2962  O   ALA A 402      69.009 -19.658  -7.758  1.00 60.94           O  
ANISOU 2962  O   ALA A 402     6539   7413   9202    790   -448   -982       O  
ATOM   2963  CB  ALA A 402      66.310 -21.249  -6.914  1.00 63.08           C  
ANISOU 2963  CB  ALA A 402     6552   8102   9313    521   -490  -1024       C  
ATOM   2964  N   THR A 403      68.257 -20.968  -9.431  1.00 61.01           N  
ANISOU 2964  N   THR A 403     6549   7393   9236    748   -466  -1037       N  
ATOM   2965  CA  THR A 403      69.574 -21.167 -10.032  1.00 60.47           C  
ANISOU 2965  CA  THR A 403     6558   7162   9255    771   -433  -1032       C  
ATOM   2966  C   THR A 403      70.122 -19.863 -10.620  1.00 60.26           C  
ANISOU 2966  C   THR A 403     6613   7116   9165    844   -398  -1060       C  
ATOM   2967  O   THR A 403      71.304 -19.564 -10.449  1.00 60.10           O  
ANISOU 2967  O   THR A 403     6611   7048   9174    828   -359  -1039       O  
ATOM   2968  CB  THR A 403      69.535 -22.254 -11.125  1.00 60.83           C  
ANISOU 2968  CB  THR A 403     6637   7130   9344    749   -444  -1078       C  
ATOM   2969  OG1 THR A 403      69.085 -23.489 -10.556  1.00 61.32           O  
ANISOU 2969  OG1 THR A 403     6693   7165   9439    642   -519  -1034       O  
ATOM   2970  CG2 THR A 403      70.911 -22.470 -11.731  1.00 60.89           C  
ANISOU 2970  CG2 THR A 403     6672   7039   9425    797   -398  -1130       C  
ATOM   2971  N   ARG A 404      69.267 -19.101 -11.307  1.00 60.78           N  
ANISOU 2971  N   ARG A 404     6742   7221   9130    906   -437  -1108       N  
ATOM   2972  CA  ARG A 404      69.658 -17.785 -11.839  1.00 61.37           C  
ANISOU 2972  CA  ARG A 404     6979   7237   9100    941   -464  -1117       C  
ATOM   2973  C   ARG A 404      70.186 -16.882 -10.726  1.00 60.68           C  
ANISOU 2973  C   ARG A 404     6928   7139   8987    954   -480  -1069       C  
ATOM   2974  O   ARG A 404      71.273 -16.321 -10.840  1.00 60.67           O  
ANISOU 2974  O   ARG A 404     7025   7076   8948    877   -454  -1031       O  
ATOM   2975  CB  ARG A 404      68.505 -17.082 -12.575  1.00 63.05           C  
ANISOU 2975  CB  ARG A 404     7289   7460   9204   1043   -577  -1182       C  
ATOM   2976  CG  ARG A 404      68.930 -15.717 -13.290  1.00 64.73           C  
ANISOU 2976  CG  ARG A 404     7779   7543   9272   1042   -669  -1177       C  
ATOM   2977  CD  ARG A 404      68.147 -15.193 -14.463  1.00 66.61           C  
ANISOU 2977  CD  ARG A 404     8196   7716   9396   1100   -810  -1230       C  
ATOM   2978  NE  ARG A 404      68.562 -13.953 -15.198  1.00 68.41           N  
ANISOU 2978  NE  ARG A 404     8770   7776   9446   1039   -945  -1204       N  
ATOM   2979  CZ  ARG A 404      69.290 -13.953 -16.324  1.00 69.50           C  
ANISOU 2979  CZ  ARG A 404     9069   7856   9481    828   -901  -1170       C  
ATOM   2980  NH1 ARG A 404      69.642 -15.089 -16.929  1.00 69.41           N  
ANISOU 2980  NH1 ARG A 404     8896   7935   9541    719   -731  -1191       N  
ATOM   2981  NH2 ARG A 404      69.633 -12.796 -16.889  1.00 70.99           N  
ANISOU 2981  NH2 ARG A 404     9610   7894   9466    712  -1048  -1128       N  
ATOM   2982  N   ALA A 405      69.410 -16.766  -9.649  1.00 60.14           N  
ANISOU 2982  N   ALA A 405     6771   7161   8918   1027   -517  -1079       N  
ATOM   2983  CA  ALA A 405      69.779 -15.945  -8.493  1.00 59.66           C  
ANISOU 2983  CA  ALA A 405     6746   7097   8822   1050   -539  -1046       C  
ATOM   2984  C   ALA A 405      71.078 -16.408  -7.829  1.00 58.83           C  
ANISOU 2984  C   ALA A 405     6598   6946   8806    923   -464   -952       C  
ATOM   2985  O   ALA A 405      71.851 -15.588  -7.326  1.00 58.94           O  
ANISOU 2985  O   ALA A 405     6706   6909   8778    894   -477   -906       O  
ATOM   2986  CB  ALA A 405      68.649 -15.944  -7.476  1.00 60.06           C  
ANISOU 2986  CB  ALA A 405     6660   7317   8843   1132   -567  -1109       C  
ATOM   2987  N   ALA A 406      71.303 -17.720  -7.818  1.00 58.32           N  
ANISOU 2987  N   ALA A 406     6409   6891   8858    854   -415   -931       N  
ATOM   2988  CA  ALA A 406      72.535 -18.293  -7.277  1.00 58.03           C  
ANISOU 2988  CA  ALA A 406     6321   6802   8923    782   -388   -872       C  
ATOM   2989  C   ALA A 406      73.742 -17.937  -8.143  1.00 58.15           C  
ANISOU 2989  C   ALA A 406     6373   6788   8931    748   -339   -895       C  
ATOM   2990  O   ALA A 406      74.812 -17.624  -7.622  1.00 58.46           O  
ANISOU 2990  O   ALA A 406     6395   6833   8985    695   -327   -859       O  
ATOM   2991  CB  ALA A 406      72.408 -19.802  -7.148  1.00 58.21           C  
ANISOU 2991  CB  ALA A 406     6260   6798   9057    747   -411   -866       C  
ATOM   2992  N   VAL A 407      73.563 -17.984  -9.461  1.00 58.13           N  
ANISOU 2992  N   VAL A 407     6413   6788   8885    751   -310   -962       N  
ATOM   2993  CA  VAL A 407      74.626 -17.632 -10.404  1.00 58.60           C  
ANISOU 2993  CA  VAL A 407     6500   6882   8882    663   -244  -1006       C  
ATOM   2994  C   VAL A 407      75.018 -16.154 -10.300  1.00 58.71           C  
ANISOU 2994  C   VAL A 407     6684   6890   8733    562   -270   -950       C  
ATOM   2995  O   VAL A 407      76.186 -15.808 -10.480  1.00 59.41           O  
ANISOU 2995  O   VAL A 407     6758   7053   8761    422   -216   -952       O  
ATOM   2996  CB  VAL A 407      74.222 -17.989 -11.856  1.00 59.17           C  
ANISOU 2996  CB  VAL A 407     6613   6962   8907    658   -212  -1090       C  
ATOM   2997  CG1 VAL A 407      75.152 -17.344 -12.878  1.00 60.37           C  
ANISOU 2997  CG1 VAL A 407     6834   7192   8911    502   -141  -1135       C  
ATOM   2998  CG2 VAL A 407      74.218 -19.498 -12.037  1.00 59.41           C  
ANISOU 2998  CG2 VAL A 407     6500   6984   9086    732   -194  -1160       C  
ATOM   2999  N   GLU A 408      74.047 -15.292 -10.006  1.00 58.21           N  
ANISOU 2999  N   GLU A 408     6783   6750   8583    630   -370   -917       N  
ATOM   3000  CA  GLU A 408      74.299 -13.854  -9.910  1.00 58.65           C  
ANISOU 3000  CA  GLU A 408     7083   6734   8465    554   -457   -867       C  
ATOM   3001  C   GLU A 408      75.092 -13.473  -8.661  1.00 58.27           C  
ANISOU 3001  C   GLU A 408     7011   6696   8433    499   -457   -795       C  
ATOM   3002  O   GLU A 408      76.096 -12.767  -8.760  1.00 59.05           O  
ANISOU 3002  O   GLU A 408     7217   6804   8415    316   -456   -748       O  
ATOM   3003  CB  GLU A 408      72.982 -13.070  -9.942  1.00 59.00           C  
ANISOU 3003  CB  GLU A 408     7315   6680   8423    717   -612   -898       C  
ATOM   3004  CG  GLU A 408      72.250 -13.158 -11.272  1.00 59.61           C  
ANISOU 3004  CG  GLU A 408     7483   6724   8442    750   -660   -959       C  
ATOM   3005  CD  GLU A 408      70.993 -12.318 -11.332  1.00 60.56           C  
ANISOU 3005  CD  GLU A 408     7782   6754   8475    951   -859  -1020       C  
ATOM   3006  OE1 GLU A 408      70.711 -11.581 -10.357  1.00 60.90           O  
ANISOU 3006  OE1 GLU A 408     7891   6760   8486   1078   -959  -1034       O  
ATOM   3007  OE2 GLU A 408      70.284 -12.404 -12.365  1.00 61.35           O  
ANISOU 3007  OE2 GLU A 408     7949   6825   8533   1001   -927  -1073       O  
ATOM   3008  N   GLU A 409      74.640 -13.935  -7.494  1.00 57.25           N  
ANISOU 3008  N   GLU A 409     6750   6580   8420    618   -463   -783       N  
ATOM   3009  CA  GLU A 409      75.211 -13.496  -6.213  1.00 57.04           C  
ANISOU 3009  CA  GLU A 409     6733   6545   8392    576   -487   -712       C  
ATOM   3010  C   GLU A 409      75.609 -14.632  -5.262  1.00 56.52           C  
ANISOU 3010  C   GLU A 409     6438   6539   8497    576   -434   -681       C  
ATOM   3011  O   GLU A 409      75.853 -14.390  -4.077  1.00 56.19           O  
ANISOU 3011  O   GLU A 409     6400   6488   8459    554   -466   -621       O  
ATOM   3012  CB  GLU A 409      74.226 -12.559  -5.506  1.00 57.08           C  
ANISOU 3012  CB  GLU A 409     6898   6488   8300    708   -599   -731       C  
ATOM   3013  CG  GLU A 409      73.833 -11.341  -6.331  1.00 57.86           C  
ANISOU 3013  CG  GLU A 409     7298   6464   8220    745   -734   -766       C  
ATOM   3014  CD  GLU A 409      72.863 -10.424  -5.613  1.00 58.35           C  
ANISOU 3014  CD  GLU A 409     7509   6465   8193    950   -882   -839       C  
ATOM   3015  OE1 GLU A 409      72.870 -10.391  -4.364  1.00 57.95           O  
ANISOU 3015  OE1 GLU A 409     7384   6466   8169    985   -866   -833       O  
ATOM   3016  OE2 GLU A 409      72.094  -9.728  -6.305  1.00 59.33           O  
ANISOU 3016  OE2 GLU A 409     7834   6495   8214   1090  -1032   -921       O  
ATOM   3017  N   GLY A 410      75.698 -15.857  -5.776  1.00 47.85           N  
ANISOU 3017  N   GLY A 410     3941   6027   8213    244    536   -944       N  
ATOM   3018  CA  GLY A 410      76.099 -17.007  -4.962  1.00 47.55           C  
ANISOU 3018  CA  GLY A 410     3822   5826   8418    231    401  -1094       C  
ATOM   3019  C   GLY A 410      74.991 -17.521  -4.062  1.00 46.02           C  
ANISOU 3019  C   GLY A 410     3702   5544   8238    214    191  -1094       C  
ATOM   3020  O   GLY A 410      73.835 -17.111  -4.190  1.00 45.46           O  
ANISOU 3020  O   GLY A 410     3737   5554   7980    217    151  -1014       O  
ATOM   3021  N   VAL A 411      75.356 -18.412  -3.139  1.00 45.73           N  
ANISOU 3021  N   VAL A 411     3603   5337   8433    198     63  -1173       N  
ATOM   3022  CA  VAL A 411      74.403 -19.015  -2.199  1.00 44.68           C  
ANISOU 3022  CA  VAL A 411     3528   5102   8345    182   -119  -1161       C  
ATOM   3023  C   VAL A 411      74.893 -18.913  -0.755  1.00 43.97           C  
ANISOU 3023  C   VAL A 411     3427   4820   8456    143   -234  -1073       C  
ATOM   3024  O   VAL A 411      76.098 -18.908  -0.499  1.00 45.01           O  
ANISOU 3024  O   VAL A 411     3467   4866   8768    137   -215  -1099       O  
ATOM   3025  CB  VAL A 411      74.122 -20.500  -2.531  1.00 45.28           C  
ANISOU 3025  CB  VAL A 411     3547   5160   8494    216   -192  -1355       C  
ATOM   3026  CG1 VAL A 411      73.502 -20.627  -3.915  1.00 46.40           C  
ANISOU 3026  CG1 VAL A 411     3714   5503   8412    265   -113  -1465       C  
ATOM   3027  CG2 VAL A 411      75.387 -21.344  -2.433  1.00 46.23           C  
ANISOU 3027  CG2 VAL A 411     3529   5170   8864    228   -189  -1490       C  
ATOM   3028  N   VAL A 412      73.946 -18.838   0.177  1.00 42.82           N  
ANISOU 3028  N   VAL A 412     3376   4614   8277    121   -352   -974       N  
ATOM   3029  CA  VAL A 412      74.243 -18.799   1.610  1.00 42.13           C  
ANISOU 3029  CA  VAL A 412     3309   4366   8331     97   -478   -889       C  
ATOM   3030  C   VAL A 412      73.458 -19.895   2.319  1.00 41.80           C  
ANISOU 3030  C   VAL A 412     3299   4236   8346    100   -610   -900       C  
ATOM   3031  O   VAL A 412      72.582 -20.521   1.722  1.00 41.88           O  
ANISOU 3031  O   VAL A 412     3314   4302   8294    114   -605   -964       O  
ATOM   3032  CB  VAL A 412      73.910 -17.427   2.243  1.00 41.29           C  
ANISOU 3032  CB  VAL A 412     3297   4266   8123     68   -474   -729       C  
ATOM   3033  CG1 VAL A 412      74.885 -16.368   1.754  1.00 42.07           C  
ANISOU 3033  CG1 VAL A 412     3338   4398   8246     58   -356   -703       C  
ATOM   3034  CG2 VAL A 412      72.475 -17.007   1.950  1.00 40.62           C  
ANISOU 3034  CG2 VAL A 412     3316   4284   7833     66   -450   -659       C  
ATOM   3035  N   ALA A 413      73.773 -20.117   3.591  1.00 41.69           N  
ANISOU 3035  N   ALA A 413     3303   4081   8454     92   -731   -832       N  
ATOM   3036  CA  ALA A 413      73.114 -21.157   4.377  1.00 41.70           C  
ANISOU 3036  CA  ALA A 413     3334   3981   8527     96   -846   -805       C  
ATOM   3037  C   ALA A 413      71.628 -20.853   4.567  1.00 40.89           C  
ANISOU 3037  C   ALA A 413     3342   3934   8258     82   -835   -711       C  
ATOM   3038  O   ALA A 413      71.253 -19.725   4.885  1.00 40.13           O  
ANISOU 3038  O   ALA A 413     3333   3891   8021     66   -804   -608       O  
ATOM   3039  CB  ALA A 413      73.800 -21.314   5.723  1.00 41.91           C  
ANISOU 3039  CB  ALA A 413     3378   3866   8678    100   -974   -726       C  
ATOM   3040  N   GLY A 414      70.792 -21.870   4.372  1.00 41.33           N  
ANISOU 3040  N   GLY A 414     3376   3963   8361     88   -863   -755       N  
ATOM   3041  CA  GLY A 414      69.339 -21.708   4.386  1.00 40.87           C  
ANISOU 3041  CA  GLY A 414     3389   3950   8186     76   -847   -690       C  
ATOM   3042  C   GLY A 414      68.740 -21.856   5.770  1.00 40.59           C  
ANISOU 3042  C   GLY A 414     3438   3813   8172     63   -909   -537       C  
ATOM   3043  O   GLY A 414      69.455 -21.841   6.770  1.00 40.73           O  
ANISOU 3043  O   GLY A 414     3487   3747   8239     68   -971   -463       O  
ATOM   3044  N   GLY A 415      67.416 -21.990   5.824  1.00 40.50           N  
ANISOU 3044  N   GLY A 415     3460   3809   8117     52   -892   -489       N  
ATOM   3045  CA  GLY A 415      66.701 -22.157   7.090  1.00 40.62           C  
ANISOU 3045  CA  GLY A 415     3554   3737   8140     43   -918   -334       C  
ATOM   3046  C   GLY A 415      66.832 -20.972   8.030  1.00 40.13           C  
ANISOU 3046  C   GLY A 415     3614   3707   7924     40   -905   -211       C  
ATOM   3047  O   GLY A 415      66.745 -21.126   9.246  1.00 39.98           O  
ANISOU 3047  O   GLY A 415     3671   3617   7901     47   -941    -91       O  
ATOM   3048  N   GLY A 416      67.051 -19.790   7.462  1.00 40.26           N  
ANISOU 3048  N   GLY A 416     3649   3832   7815     36   -853   -241       N  
ATOM   3049  CA  GLY A 416      67.200 -18.562   8.238  1.00 40.36           C  
ANISOU 3049  CA  GLY A 416     3759   3871   7704     34   -843   -154       C  
ATOM   3050  C   GLY A 416      68.455 -18.450   9.093  1.00 41.08           C  
ANISOU 3050  C   GLY A 416     3871   3898   7839     49   -926   -140       C  
ATOM   3051  O   GLY A 416      68.525 -17.573   9.959  1.00 41.46           O  
ANISOU 3051  O   GLY A 416     4007   3950   7796     55   -944    -77       O  
ATOM   3052  N   VAL A 417      69.455 -19.300   8.846  1.00 41.67           N  
ANISOU 3052  N   VAL A 417     3858   3913   8061     60   -984   -214       N  
ATOM   3053  CA  VAL A 417      70.677 -19.286   9.658  1.00 42.36           C  
ANISOU 3053  CA  VAL A 417     3948   3925   8220     79  -1088   -207       C  
ATOM   3054  C   VAL A 417      71.676 -18.244   9.152  1.00 42.40           C  
ANISOU 3054  C   VAL A 417     3902   3972   8234     72  -1063   -277       C  
ATOM   3055  O   VAL A 417      72.495 -17.742   9.922  1.00 43.08           O  
ANISOU 3055  O   VAL A 417     4009   4013   8346     84  -1145   -265       O  
ATOM   3056  CB  VAL A 417      71.388 -20.659   9.734  1.00 43.39           C  
ANISOU 3056  CB  VAL A 417     3993   3947   8546     98  -1175   -248       C  
ATOM   3057  CG1 VAL A 417      70.401 -21.780  10.037  1.00 43.74           C  
ANISOU 3057  CG1 VAL A 417     4055   3932   8632    100  -1182   -180       C  
ATOM   3058  CG2 VAL A 417      72.172 -20.943   8.461  1.00 43.82           C  
ANISOU 3058  CG2 VAL A 417     3903   4019   8725     94  -1131   -400       C  
ATOM   3059  N   ALA A 418      71.628 -17.941   7.857  1.00 42.01           N  
ANISOU 3059  N   ALA A 418     3782   4006   8172     56   -953   -349       N  
ATOM   3060  CA  ALA A 418      72.501 -16.920   7.284  1.00 42.13           C  
ANISOU 3060  CA  ALA A 418     3742   4061   8204     46   -895   -390       C  
ATOM   3061  C   ALA A 418      72.247 -15.560   7.929  1.00 41.40           C  
ANISOU 3061  C   ALA A 418     3735   3984   8008     36   -892   -311       C  
ATOM   3062  O   ALA A 418      73.187 -14.809   8.186  1.00 42.07           O  
ANISOU 3062  O   ALA A 418     3786   4031   8166     33   -919   -327       O  
ATOM   3063  CB  ALA A 418      72.313 -16.836   5.774  1.00 42.36           C  
ANISOU 3063  CB  ALA A 418     3704   4200   8190     39   -762   -452       C  
ATOM   3064  N   LEU A 419      70.979 -15.252   8.189  1.00 40.33           N  
ANISOU 3064  N   LEU A 419     3696   3895   7730     31   -861   -238       N  
ATOM   3065  CA  LEU A 419      70.610 -13.981   8.809  1.00 39.90           C  
ANISOU 3065  CA  LEU A 419     3722   3853   7584     27   -853   -177       C  
ATOM   3066  C   LEU A 419      71.066 -13.894  10.266  1.00 39.88           C  
ANISOU 3066  C   LEU A 419     3789   3771   7590     49   -981   -160       C  
ATOM   3067  O   LEU A 419      71.593 -12.864  10.688  1.00 40.28           O  
ANISOU 3067  O   LEU A 419     3847   3799   7658     50  -1013   -175       O  
ATOM   3068  CB  LEU A 419      69.097 -13.749   8.709  1.00 39.42           C  
ANISOU 3068  CB  LEU A 419     3735   3856   7387     21   -783   -112       C  
ATOM   3069  CG  LEU A 419      68.561 -13.492   7.295  1.00 39.17           C  
ANISOU 3069  CG  LEU A 419     3651   3919   7311      8   -674   -123       C  
ATOM   3070  CD1 LEU A 419      67.050 -13.644   7.253  1.00 38.91           C  
ANISOU 3070  CD1 LEU A 419     3670   3926   7186      8   -641    -74       C  
ATOM   3071  CD2 LEU A 419      68.966 -12.114   6.794  1.00 39.16           C  
ANISOU 3071  CD2 LEU A 419     3625   3951   7303     -2   -608   -102       C  
ATOM   3072  N   ILE A 420      70.863 -14.968  11.026  1.00 39.63           N  
ANISOU 3072  N   ILE A 420     3808   3696   7552     71  -1059   -128       N  
ATOM   3073  CA  ILE A 420      71.271 -14.995  12.435  1.00 40.15           C  
ANISOU 3073  CA  ILE A 420     3959   3703   7590    106  -1192   -100       C  
ATOM   3074  C   ILE A 420      72.797 -15.074  12.589  1.00 40.51           C  
ANISOU 3074  C   ILE A 420     3922   3674   7792    120  -1313   -175       C  
ATOM   3075  O   ILE A 420      73.353 -14.540  13.552  1.00 40.89           O  
ANISOU 3075  O   ILE A 420     4019   3687   7827    148  -1429   -189       O  
ATOM   3076  CB  ILE A 420      70.577 -16.140  13.216  1.00 40.81           C  
ANISOU 3076  CB  ILE A 420     4126   3762   7617    129  -1228    -10       C  
ATOM   3077  CG1 ILE A 420      70.730 -15.941  14.726  1.00 41.89           C  
ANISOU 3077  CG1 ILE A 420     4394   3879   7644    176  -1343     42       C  
ATOM   3078  CG2 ILE A 420      71.132 -17.500  12.827  1.00 41.44           C  
ANISOU 3078  CG2 ILE A 420     4113   3775   7857    133  -1277    -31       C  
ATOM   3079  CD1 ILE A 420      69.726 -16.729  15.540  1.00 42.40           C  
ANISOU 3079  CD1 ILE A 420     4568   3944   7595    198  -1321    170       C  
ATOM   3080  N   ARG A 421      73.462 -15.735  11.642  1.00 40.17           N  
ANISOU 3080  N   ARG A 421     3749   3607   7904    106  -1288   -235       N  
ATOM   3081  CA  ARG A 421      74.927 -15.796  11.611  1.00 40.84           C  
ANISOU 3081  CA  ARG A 421     3721   3614   8179    116  -1378   -317       C  
ATOM   3082  C   ARG A 421      75.513 -14.403  11.408  1.00 40.66           C  
ANISOU 3082  C   ARG A 421     3650   3595   8200     97  -1348   -364       C  
ATOM   3083  O   ARG A 421      76.427 -13.990  12.122  1.00 41.63           O  
ANISOU 3083  O   ARG A 421     3751   3646   8418    116  -1477   -408       O  
ATOM   3084  CB  ARG A 421      75.401 -16.732  10.490  1.00 40.91           C  
ANISOU 3084  CB  ARG A 421     3592   3610   8341    104  -1315   -385       C  
ATOM   3085  CG  ARG A 421      76.909 -16.788  10.274  1.00 41.89           C  
ANISOU 3085  CG  ARG A 421     3570   3653   8692    110  -1372   -479       C  
ATOM   3086  CD  ARG A 421      77.663 -17.327  11.481  1.00 42.98           C  
ANISOU 3086  CD  ARG A 421     3722   3679   8929    153  -1583   -475       C  
ATOM   3087  NE  ARG A 421      77.227 -18.680  11.837  1.00 43.38           N  
ANISOU 3087  NE  ARG A 421     3813   3692   8978    178  -1646   -421       N  
ATOM   3088  CZ  ARG A 421      76.676 -19.044  12.997  1.00 43.73           C  
ANISOU 3088  CZ  ARG A 421     3997   3719   8900    211  -1755   -314       C  
ATOM   3089  NH1 ARG A 421      76.482 -18.169  13.982  1.00 43.96           N  
ANISOU 3089  NH1 ARG A 421     4151   3777   8772    230  -1826   -266       N  
ATOM   3090  NH2 ARG A 421      76.325 -20.312  13.180  1.00 44.08           N  
ANISOU 3090  NH2 ARG A 421     4050   3711   8986    229  -1790   -254       N  
ATOM   3091  N   VAL A 422      74.983 -13.697  10.415  1.00 39.64           N  
ANISOU 3091  N   VAL A 422     3498   3544   8019     63  -1185   -353       N  
ATOM   3092  CA  VAL A 422      75.375 -12.323  10.134  1.00 39.61           C  
ANISOU 3092  CA  VAL A 422     3445   3537   8065     40  -1128   -369       C  
ATOM   3093  C   VAL A 422      75.082 -11.410  11.327  1.00 39.80           C  
ANISOU 3093  C   VAL A 422     3574   3536   8010     57  -1225   -355       C  
ATOM   3094  O   VAL A 422      75.911 -10.576  11.693  1.00 40.66           O  
ANISOU 3094  O   VAL A 422     3630   3577   8243     58  -1293   -410       O  
ATOM   3095  CB  VAL A 422      74.663 -11.805   8.865  1.00 38.99           C  
ANISOU 3095  CB  VAL A 422     3346   3558   7909      9   -936   -326       C  
ATOM   3096  CG1 VAL A 422      74.696 -10.287   8.785  1.00 39.43           C  
ANISOU 3096  CG1 VAL A 422     3387   3605   7987    -10   -879   -299       C  
ATOM   3097  CG2 VAL A 422      75.299 -12.414   7.625  1.00 39.34           C  
ANISOU 3097  CG2 VAL A 422     3265   3630   8052      0   -836   -373       C  
ATOM   3098  N   ALA A 423      73.906 -11.572  11.927  1.00 39.37           N  
ANISOU 3098  N   ALA A 423     3661   3534   7762     73  -1227   -292       N  
ATOM   3099  CA  ALA A 423      73.491 -10.745  13.062  1.00 39.74           C  
ANISOU 3099  CA  ALA A 423     3821   3576   7699     97  -1298   -289       C  
ATOM   3100  C   ALA A 423      74.420 -10.886  14.270  1.00 41.20           C  
ANISOU 3100  C   ALA A 423     4035   3689   7929    143  -1502   -349       C  
ATOM   3101  O   ALA A 423      74.669  -9.908  14.979  1.00 41.83           O  
ANISOU 3101  O   ALA A 423     4142   3739   8009    161  -1583   -408       O  
ATOM   3102  CB  ALA A 423      72.060 -11.075  13.460  1.00 39.14           C  
ANISOU 3102  CB  ALA A 423     3882   3571   7416    109  -1242   -206       C  
ATOM   3103  N   SER A 424      74.929 -12.096  14.502  1.00 41.97           N  
ANISOU 3103  N   SER A 424     4122   3753   8071    166  -1597   -342       N  
ATOM   3104  CA  SER A 424      75.840 -12.351  15.622  1.00 43.64           C  
ANISOU 3104  CA  SER A 424     4359   3897   8323    219  -1814   -388       C  
ATOM   3105  C   SER A 424      77.202 -11.675  15.433  1.00 44.87           C  
ANISOU 3105  C   SER A 424     4364   3961   8721    210  -1900   -505       C  
ATOM   3106  O   SER A 424      77.863 -11.314  16.409  1.00 46.26           O  
ANISOU 3106  O   SER A 424     4563   4085   8927    254  -2088   -575       O  
ATOM   3107  CB  SER A 424      76.034 -13.855  15.826  1.00 43.90           C  
ANISOU 3107  CB  SER A 424     4401   3902   8375    246  -1890   -332       C  
ATOM   3108  OG  SER A 424      76.669 -14.447  14.708  1.00 43.50           O  
ANISOU 3108  OG  SER A 424     4186   3808   8530    212  -1826   -369       O  
ATOM   3109  N   LYS A 425      77.614 -11.507  14.178  1.00 44.78           N  
ANISOU 3109  N   LYS A 425     4196   3931   8884    158  -1761   -527       N  
ATOM   3110  CA  LYS A 425      78.886 -10.855  13.860  1.00 45.93           C  
ANISOU 3110  CA  LYS A 425     4172   3981   9296    140  -1799   -623       C  
ATOM   3111  C   LYS A 425      78.865  -9.329  14.044  1.00 45.99           C  
ANISOU 3111  C   LYS A 425     4168   3964   9341    124  -1786   -667       C  
ATOM   3112  O   LYS A 425      79.923  -8.709  14.125  1.00 46.98           O  
ANISOU 3112  O   LYS A 425     4163   3986   9701    119  -1865   -758       O  
ATOM   3113  CB  LYS A 425      79.320 -11.202  12.429  1.00 46.02           C  
ANISOU 3113  CB  LYS A 425     4024   3992   9468     95  -1624   -620       C  
ATOM   3114  CG  LYS A 425      79.811 -12.634  12.261  1.00 46.79           C  
ANISOU 3114  CG  LYS A 425     4067   4062   9647    114  -1674   -632       C  
ATOM   3115  CD  LYS A 425      80.575 -12.820  10.956  1.00 47.57           C  
ANISOU 3115  CD  LYS A 425     3979   4142   9952     80  -1522   -675       C  
ATOM   3116  CE  LYS A 425      81.505 -14.027  10.998  1.00 48.86           C  
ANISOU 3116  CE  LYS A 425     4038   4223  10302    107  -1622   -737       C  
ATOM   3117  NZ  LYS A 425      80.783 -15.315  10.801  1.00 48.53           N  
ANISOU 3117  NZ  LYS A 425     4065   4233  10139    122  -1598   -694       N  
ATOM   3118  N   LEU A 426      77.673  -8.732  14.110  1.00 44.95           N  
ANISOU 3118  N   LEU A 426     4156   3912   9009    117  -1689   -610       N  
ATOM   3119  CA  LEU A 426      77.530  -7.275  14.216  1.00 45.03           C  
ANISOU 3119  CA  LEU A 426     4149   3891   9067    101  -1660   -648       C  
ATOM   3120  C   LEU A 426      77.137  -6.805  15.622  1.00 45.57           C  
ANISOU 3120  C   LEU A 426     4364   3966   8984    156  -1820   -711       C  
ATOM   3121  O   LEU A 426      76.438  -5.800  15.774  1.00 45.43           O  
ANISOU 3121  O   LEU A 426     4394   3963   8902    151  -1762   -719       O  
ATOM   3122  CB  LEU A 426      76.494  -6.784  13.199  1.00 43.89           C  
ANISOU 3122  CB  LEU A 426     4015   3824   8836     57  -1431   -547       C  
ATOM   3123  CG  LEU A 426      76.756  -7.128  11.730  1.00 43.51           C  
ANISOU 3123  CG  LEU A 426     3843   3801   8886     12  -1253   -484       C  
ATOM   3124  CD1 LEU A 426      75.530  -6.820  10.886  1.00 42.42           C  
ANISOU 3124  CD1 LEU A 426     3760   3765   8591    -11  -1068   -377       C  
ATOM   3125  CD2 LEU A 426      77.968  -6.376  11.203  1.00 44.67           C  
ANISOU 3125  CD2 LEU A 426     3803   3842   9326    -18  -1222   -529       C  
ATOM   3126  N   ALA A 427      77.594  -7.521  16.647  1.00 46.45           N  
ANISOU 3126  N   ALA A 427     4546   4065   9035    215  -2022   -757       N  
ATOM   3127  CA  ALA A 427      77.283  -7.169  18.034  1.00 47.39           C  
ANISOU 3127  CA  ALA A 427     4822   4212   8971    283  -2184   -823       C  
ATOM   3128  C   ALA A 427      77.942  -5.855  18.456  1.00 48.73           C  
ANISOU 3128  C   ALA A 427     4913   4287   9313    291  -2300   -980       C  
ATOM   3129  O   ALA A 427      77.403  -5.127  19.288  1.00 49.24           O  
ANISOU 3129  O   ALA A 427     5089   4382   9235    331  -2354  -1049       O  
ATOM   3130  CB  ALA A 427      77.703  -8.294  18.969  1.00 48.38           C  
ANISOU 3130  CB  ALA A 427     5040   4350   8991    351  -2382   -816       C  
ATOM   3131  N   ASP A 428      79.108  -5.563  17.882  1.00 49.61           N  
ANISOU 3131  N   ASP A 428     4823   4278   9750    256  -2333  -1046       N  
ATOM   3132  CA  ASP A 428      79.869  -4.355  18.215  1.00 51.08           C  
ANISOU 3132  CA  ASP A 428     4891   4339  10176    257  -2452  -1203       C  
ATOM   3133  C   ASP A 428      79.478  -3.136  17.378  1.00 50.47           C  
ANISOU 3133  C   ASP A 428     4714   4216  10243    192  -2252  -1179       C  
ATOM   3134  O   ASP A 428      80.022  -2.051  17.581  1.00 51.58           O  
ANISOU 3134  O   ASP A 428     4743   4237  10617    185  -2326  -1301       O  
ATOM   3135  CB  ASP A 428      81.369  -4.616  18.043  1.00 52.36           C  
ANISOU 3135  CB  ASP A 428     4858   4368  10665    250  -2587  -1284       C  
ATOM   3136  CG  ASP A 428      81.869  -5.753  18.911  1.00 53.21           C  
ANISOU 3136  CG  ASP A 428     5046   4497  10671    322  -2818  -1311       C  
ATOM   3137  OD1 ASP A 428      81.444  -5.851  20.081  1.00 53.95           O  
ANISOU 3137  OD1 ASP A 428     5329   4664  10505    399  -2982  -1352       O  
ATOM   3138  OD2 ASP A 428      82.698  -6.548  18.422  1.00 53.40           O  
ANISOU 3138  OD2 ASP A 428     4944   4465  10878    307  -2834  -1288       O  
ATOM   3139  N   LEU A 429      78.545  -3.309  16.442  1.00 48.80           N  
ANISOU 3139  N   LEU A 429     4537   4092   9909    147  -2011  -1023       N  
ATOM   3140  CA  LEU A 429      78.132  -2.218  15.561  1.00 48.26           C  
ANISOU 3140  CA  LEU A 429     4381   3988   9965     89  -1816   -965       C  
ATOM   3141  C   LEU A 429      77.360  -1.156  16.337  1.00 48.85           C  
ANISOU 3141  C   LEU A 429     4546   4058   9954    118  -1856  -1042       C  
ATOM   3142  O   LEU A 429      76.394  -1.470  17.037  1.00 48.67           O  
ANISOU 3142  O   LEU A 429     4709   4146   9636    163  -1876  -1035       O  
ATOM   3143  CB  LEU A 429      77.274  -2.752  14.410  1.00 46.34           C  
ANISOU 3143  CB  LEU A 429     4170   3858   9577     49  -1579   -785       C  
ATOM   3144  CG  LEU A 429      76.875  -1.752  13.320  1.00 45.77           C  
ANISOU 3144  CG  LEU A 429     4006   3764   9619     -5  -1369   -686       C  
ATOM   3145  CD1 LEU A 429      78.090  -1.226  12.574  1.00 46.64           C  
ANISOU 3145  CD1 LEU A 429     3898   3745  10077    -51  -1317   -691       C  
ATOM   3146  CD2 LEU A 429      75.902  -2.399  12.349  1.00 44.31           C  
ANISOU 3146  CD2 LEU A 429     3890   3717   9228    -25  -1181   -529       C  
ATOM   3147  N   ARG A 430      77.793   0.096  16.201  1.00 50.02           N  
ANISOU 3147  N   ARG A 430     4553   4071  10381     92  -1856  -1116       N  
ATOM   3148  CA  ARG A 430      77.183   1.228  16.895  1.00 50.97           C  
ANISOU 3148  CA  ARG A 430     4723   4154  10488    119  -1899  -1218       C  
ATOM   3149  C   ARG A 430      76.847   2.349  15.918  1.00 51.04           C  
ANISOU 3149  C   ARG A 430     4605   4079  10707     57  -1703  -1126       C  
ATOM   3150  O   ARG A 430      77.243   2.313  14.753  1.00 50.68           O  
ANISOU 3150  O   ARG A 430     4427   4001  10828     -2  -1550   -991       O  
ATOM   3151  CB  ARG A 430      78.129   1.760  17.971  1.00 53.16           C  
ANISOU 3151  CB  ARG A 430     4945   4311  10939    165  -2160  -1451       C  
ATOM   3152  CG  ARG A 430      78.412   0.785  19.103  1.00 53.90           C  
ANISOU 3152  CG  ARG A 430     5187   4491  10799    245  -2387  -1548       C  
ATOM   3153  CD  ARG A 430      77.226   0.655  20.042  1.00 53.74           C  
ANISOU 3153  CD  ARG A 430     5409   4618  10390    313  -2404  -1569       C  
ATOM   3154  NE  ARG A 430      77.489  -0.301  21.116  1.00 54.65           N  
ANISOU 3154  NE  ARG A 430     5679   4824  10261    395  -2609  -1629       N  
ATOM   3155  CZ  ARG A 430      77.443  -1.626  20.988  1.00 53.76           C  
ANISOU 3155  CZ  ARG A 430     5647   4807   9973    401  -2589  -1489       C  
ATOM   3156  NH1 ARG A 430      77.149  -2.196  19.822  1.00 51.97           N  
ANISOU 3156  NH1 ARG A 430     5362   4604   9778    331  -2378  -1305       N  
ATOM   3157  NH2 ARG A 430      77.699  -2.395  22.040  1.00 55.03           N  
ANISOU 3157  NH2 ARG A 430     5947   5036   9923    484  -2789  -1536       N  
ATOM   3158  N   GLY A 431      76.104   3.338  16.408  1.00 51.95           N  
ANISOU 3158  N   GLY A 431     4764   4165  10808     78  -1706  -1197       N  
ATOM   3159  CA  GLY A 431      75.716   4.504  15.617  1.00 52.43           C  
ANISOU 3159  CA  GLY A 431     4709   4129  11082     30  -1543  -1111       C  
ATOM   3160  C   GLY A 431      76.206   5.796  16.242  1.00 54.83           C  
ANISOU 3160  C   GLY A 431     4893   4246  11694     40  -1669  -1299       C  
ATOM   3161  O   GLY A 431      77.052   5.784  17.139  1.00 56.43           O  
ANISOU 3161  O   GLY A 431     5070   4383  11985     78  -1888  -1500       O  
ATOM   3162  N   GLN A 432      75.655   6.912  15.774  1.00 55.44           N  
ANISOU 3162  N   GLN A 432     4891   4231  11941     12  -1543  -1240       N  
ATOM   3163  CA  GLN A 432      76.064   8.240  16.228  1.00 57.87           C  
ANISOU 3163  CA  GLN A 432     5054   4332  12601     14  -1639  -1408       C  
ATOM   3164  C   GLN A 432      75.478   8.615  17.595  1.00 58.82           C  
ANISOU 3164  C   GLN A 432     5309   4477  12562     95  -1806  -1652       C  
ATOM   3165  O   GLN A 432      76.043   9.454  18.300  1.00 61.03           O  
ANISOU 3165  O   GLN A 432     5491   4602  13093    119  -1972  -1878       O  
ATOM   3166  CB  GLN A 432      75.671   9.298  15.195  1.00 58.43           C  
ANISOU 3166  CB  GLN A 432     4985   4282  12932    -43  -1437  -1234       C  
ATOM   3167  CG  GLN A 432      76.256   9.083  13.807  1.00 58.43           C  
ANISOU 3167  CG  GLN A 432     4849   4258  13092   -116  -1250   -986       C  
ATOM   3168  CD  GLN A 432      75.698  10.054  12.777  1.00 59.14           C  
ANISOU 3168  CD  GLN A 432     4840   4264  13363   -160  -1041   -773       C  
ATOM   3169  OE1 GLN A 432      74.507  10.382  12.790  1.00 58.68           O  
ANISOU 3169  OE1 GLN A 432     4883   4264  13148   -137   -980   -722       O  
ATOM   3170  NE2 GLN A 432      76.557  10.515  11.870  1.00 60.44           N  
ANISOU 3170  NE2 GLN A 432     4805   4291  13867   -220   -925   -635       N  
ATOM   3171  N   ASN A 433      74.351   8.004  17.960  1.00 57.45           N  
ANISOU 3171  N   ASN A 433     5350   4493  11983    139  -1757  -1615       N  
ATOM   3172  CA  ASN A 433      73.737   8.225  19.273  1.00 58.40           C  
ANISOU 3172  CA  ASN A 433     5624   4674  11888    225  -1886  -1834       C  
ATOM   3173  C   ASN A 433      72.983   6.987  19.764  1.00 56.90           C  
ANISOU 3173  C   ASN A 433     5677   4720  11221    275  -1868  -1776       C  
ATOM   3174  O   ASN A 433      72.869   5.996  19.042  1.00 55.17           O  
ANISOU 3174  O   ASN A 433     5496   4604  10861    238  -1759  -1571       O  
ATOM   3175  CB  ASN A 433      72.817   9.450  19.235  1.00 59.19           C  
ANISOU 3175  CB  ASN A 433     5682   4685  12121    228  -1787  -1867       C  
ATOM   3176  CG  ASN A 433      71.704   9.318  18.211  1.00 57.53           C  
ANISOU 3176  CG  ASN A 433     5501   4550  11805    185  -1539  -1599       C  
ATOM   3177  OD1 ASN A 433      70.799   8.499  18.365  1.00 56.74           O  
ANISOU 3177  OD1 ASN A 433     5575   4632  11350    212  -1467  -1521       O  
ATOM   3178  ND2 ASN A 433      71.755  10.138  17.167  1.00 57.67           N  
ANISOU 3178  ND2 ASN A 433     5344   4424  12142    122  -1411  -1452       N  
ATOM   3179  N   GLU A 434      72.472   7.050  20.992  1.00 57.90           N  
ANISOU 3179  N   GLU A 434     5963   4929  11106    361  -1971  -1959       N  
ATOM   3180  CA  GLU A 434      71.848   5.889  21.631  1.00 57.23           C  
ANISOU 3180  CA  GLU A 434     6108   5056  10578    417  -1967  -1913       C  
ATOM   3181  C   GLU A 434      70.568   5.413  20.935  1.00 54.91           C  
ANISOU 3181  C   GLU A 434     5890   4876  10097    384  -1722  -1681       C  
ATOM   3182  O   GLU A 434      70.287   4.216  20.920  1.00 53.60           O  
ANISOU 3182  O   GLU A 434     5845   4851   9668    390  -1680  -1549       O  
ATOM   3183  CB  GLU A 434      71.575   6.175  23.115  1.00 59.45           C  
ANISOU 3183  CB  GLU A 434     6545   5405  10637    525  -2113  -2162       C  
ATOM   3184  CG  GLU A 434      70.976   5.009  23.899  1.00 59.44           C  
ANISOU 3184  CG  GLU A 434     6789   5621  10173    592  -2106  -2107       C  
ATOM   3185  CD  GLU A 434      71.762   3.713  23.753  1.00 58.91           C  
ANISOU 3185  CD  GLU A 434     6756   5617  10009    581  -2192  -1983       C  
ATOM   3186  OE1 GLU A 434      73.012   3.758  23.808  1.00 59.85           O  
ANISOU 3186  OE1 GLU A 434     6771   5639  10327    578  -2384  -2081       O  
ATOM   3187  OE2 GLU A 434      71.126   2.647  23.588  1.00 57.48           O  
ANISOU 3187  OE2 GLU A 434     6694   5569   9577    575  -2071  -1792       O  
ATOM   3188  N   ASP A 435      69.795   6.334  20.365  1.00 54.63           N  
ANISOU 3188  N   ASP A 435     5773   4767  10215    353  -1574  -1632       N  
ATOM   3189  CA  ASP A 435      68.592   5.953  19.620  1.00 52.97           C  
ANISOU 3189  CA  ASP A 435     5608   4648   9868    322  -1360  -1417       C  
ATOM   3190  C   ASP A 435      68.943   5.136  18.378  1.00 51.02           C  
ANISOU 3190  C   ASP A 435     5295   4427   9661    249  -1275  -1188       C  
ATOM   3191  O   ASP A 435      68.242   4.179  18.045  1.00 49.84           O  
ANISOU 3191  O   ASP A 435     5237   4407   9291    242  -1172  -1038       O  
ATOM   3192  CB  ASP A 435      67.766   7.183  19.229  1.00 53.62           C  
ANISOU 3192  CB  ASP A 435     5598   4627  10147    307  -1241  -1412       C  
ATOM   3193  CG  ASP A 435      67.071   7.830  20.418  1.00 55.57           C  
ANISOU 3193  CG  ASP A 435     5935   4885  10293    386  -1273  -1627       C  
ATOM   3194  OD1 ASP A 435      66.873   7.155  21.452  1.00 56.46           O  
ANISOU 3194  OD1 ASP A 435     6222   5135  10092    453  -1330  -1722       O  
ATOM   3195  OD2 ASP A 435      66.706   9.020  20.312  1.00 56.82           O  
ANISOU 3195  OD2 ASP A 435     5989   4912  10686    385  -1234  -1698       O  
ATOM   3196  N   GLN A 436      70.027   5.510  17.702  1.00 51.01           N  
ANISOU 3196  N   GLN A 436     5129   4300   9950    199  -1313  -1169       N  
ATOM   3197  CA  GLN A 436      70.524   4.738  16.562  1.00 49.69           C  
ANISOU 3197  CA  GLN A 436     4895   4162   9821    139  -1236   -980       C  
ATOM   3198  C   GLN A 436      71.050   3.371  17.000  1.00 49.11           C  
ANISOU 3198  C   GLN A 436     4923   4197   9536    162  -1336   -992       C  
ATOM   3199  O   GLN A 436      70.856   2.379  16.300  1.00 47.64           O  
ANISOU 3199  O   GLN A 436     4767   4107   9226    136  -1246   -838       O  
ATOM   3200  CB  GLN A 436      71.617   5.507  15.820  1.00 50.60           C  
ANISOU 3200  CB  GLN A 436     4803   4111  10312     86  -1239   -964       C  
ATOM   3201  CG  GLN A 436      71.105   6.707  15.046  1.00 51.09           C  
ANISOU 3201  CG  GLN A 436     4748   4064  10599     51  -1103   -867       C  
ATOM   3202  CD  GLN A 436      72.223   7.485  14.373  1.00 52.39           C  
ANISOU 3202  CD  GLN A 436     4699   4049  11156     -1  -1093   -836       C  
ATOM   3203  OE1 GLN A 436      73.407   7.229  14.602  1.00 53.50           O  
ANISOU 3203  OE1 GLN A 436     4767   4130  11428     -9  -1205   -926       O  
ATOM   3204  NE2 GLN A 436      71.853   8.438  13.536  1.00 52.72           N  
ANISOU 3204  NE2 GLN A 436     4633   3996  11402    -36   -957   -698       N  
ATOM   3205  N   ASN A 437      71.707   3.325  18.157  1.00 50.37           N  
ANISOU 3205  N   ASN A 437     5134   4340   9663    216  -1530  -1181       N  
ATOM   3206  CA  ASN A 437      72.172   2.059  18.730  1.00 50.25           C  
ANISOU 3206  CA  ASN A 437     5228   4423   9441    252  -1648  -1192       C  
ATOM   3207  C   ASN A 437      71.019   1.091  18.983  1.00 49.27           C  
ANISOU 3207  C   ASN A 437     5286   4464   8971    279  -1553  -1082       C  
ATOM   3208  O   ASN A 437      71.150  -0.108  18.743  1.00 48.46           O  
ANISOU 3208  O   ASN A 437     5227   4437   8748    271  -1545   -974       O  
ATOM   3209  CB  ASN A 437      72.943   2.292  20.036  1.00 52.13           C  
ANISOU 3209  CB  ASN A 437     5509   4624   9671    323  -1893  -1421       C  
ATOM   3210  CG  ASN A 437      74.269   2.997  19.822  1.00 53.11           C  
ANISOU 3210  CG  ASN A 437     5436   4573  10170    295  -2018  -1536       C  
ATOM   3211  OD1 ASN A 437      74.771   3.079  18.701  1.00 52.38           O  
ANISOU 3211  OD1 ASN A 437     5179   4398  10322    221  -1918  -1421       O  
ATOM   3212  ND2 ASN A 437      74.847   3.506  20.902  1.00 55.01           N  
ANISOU 3212  ND2 ASN A 437     5685   4755  10458    357  -2238  -1769       N  
ATOM   3213  N   VAL A 438      69.898   1.618  19.472  1.00 49.53           N  
ANISOU 3213  N   VAL A 438     5409   4539   8869    312  -1478  -1115       N  
ATOM   3214  CA  VAL A 438      68.692   0.815  19.675  1.00 48.65           C  
ANISOU 3214  CA  VAL A 438     5446   4568   8470    333  -1358  -1004       C  
ATOM   3215  C   VAL A 438      68.146   0.343  18.329  1.00 46.77           C  
ANISOU 3215  C   VAL A 438     5139   4353   8276    264  -1185   -800       C  
ATOM   3216  O   VAL A 438      67.741  -0.810  18.192  1.00 45.86           O  
ANISOU 3216  O   VAL A 438     5098   4332   7995    261  -1133   -684       O  
ATOM   3217  CB  VAL A 438      67.604   1.595  20.450  1.00 49.48           C  
ANISOU 3217  CB  VAL A 438     5639   4700   8460    383  -1295  -1096       C  
ATOM   3218  CG1 VAL A 438      66.278   0.845  20.437  1.00 48.63           C  
ANISOU 3218  CG1 VAL A 438     5642   4713   8122    389  -1129   -955       C  
ATOM   3219  CG2 VAL A 438      68.055   1.839  21.884  1.00 51.59           C  
ANISOU 3219  CG2 VAL A 438     6016   4988   8596    471  -1470  -1306       C  
ATOM   3220  N   GLY A 439      68.141   1.238  17.345  1.00 46.56           N  
ANISOU 3220  N   GLY A 439     4971   4239   8480    213  -1103   -756       N  
ATOM   3221  CA  GLY A 439      67.724   0.898  15.988  1.00 45.50           C  
ANISOU 3221  CA  GLY A 439     4767   4133   8387    156   -957   -572       C  
ATOM   3222  C   GLY A 439      68.526  -0.245  15.388  1.00 45.19           C  
ANISOU 3222  C   GLY A 439     4699   4131   8337    128   -981   -496       C  
ATOM   3223  O   GLY A 439      67.968  -1.108  14.704  1.00 44.50           O  
ANISOU 3223  O   GLY A 439     4633   4126   8146    108   -890   -373       O  
ATOM   3224  N   ILE A 440      69.832  -0.254  15.648  1.00 46.17           N  
ANISOU 3224  N   ILE A 440     4764   4187   8589    129  -1112   -585       N  
ATOM   3225  CA  ILE A 440      70.708  -1.337  15.195  1.00 45.95           C  
ANISOU 3225  CA  ILE A 440     4699   4181   8579    109  -1149   -539       C  
ATOM   3226  C   ILE A 440      70.309  -2.660  15.849  1.00 45.76           C  
ANISOU 3226  C   ILE A 440     4818   4259   8306    146  -1191   -515       C  
ATOM   3227  O   ILE A 440      70.142  -3.667  15.163  1.00 44.91           O  
ANISOU 3227  O   ILE A 440     4707   4210   8143    123  -1125   -412       O  
ATOM   3228  CB  ILE A 440      72.196  -1.028  15.485  1.00 47.24           C  
ANISOU 3228  CB  ILE A 440     4758   4232   8957    109  -1297   -658       C  
ATOM   3229  CG1 ILE A 440      72.683   0.106  14.578  1.00 47.72           C  
ANISOU 3229  CG1 ILE A 440     4644   4178   9309     59  -1218   -636       C  
ATOM   3230  CG2 ILE A 440      73.068  -2.261  15.273  1.00 46.97           C  
ANISOU 3230  CG2 ILE A 440     4700   4220   8926    104  -1359   -634       C  
ATOM   3231  CD1 ILE A 440      73.952   0.782  15.055  1.00 49.30           C  
ANISOU 3231  CD1 ILE A 440     4725   4233   9771     62  -1365   -783       C  
ATOM   3232  N   LYS A 441      70.142  -2.647  17.170  1.00 46.86           N  
ANISOU 3232  N   LYS A 441     5084   4422   8299    206  -1298   -608       N  
ATOM   3233  CA  LYS A 441      69.791  -3.860  17.915  1.00 46.96           C  
ANISOU 3233  CA  LYS A 441     5240   4524   8076    248  -1337   -565       C  
ATOM   3234  C   LYS A 441      68.404  -4.386  17.543  1.00 45.74           C  
ANISOU 3234  C   LYS A 441     5148   4454   7776    234  -1166   -433       C  
ATOM   3235  O   LYS A 441      68.182  -5.596  17.536  1.00 45.60           O  
ANISOU 3235  O   LYS A 441     5182   4489   7655    236  -1151   -343       O  
ATOM   3236  CB  LYS A 441      69.877  -3.620  19.428  1.00 48.69           C  
ANISOU 3236  CB  LYS A 441     5594   4764   8140    327  -1477   -688       C  
ATOM   3237  CG  LYS A 441      71.270  -3.270  19.942  1.00 50.17           C  
ANISOU 3237  CG  LYS A 441     5729   4872   8462    354  -1690   -836       C  
ATOM   3238  CD  LYS A 441      72.256  -4.418  19.791  1.00 50.24           C  
ANISOU 3238  CD  LYS A 441     5703   4867   8518    351  -1799   -792       C  
ATOM   3239  CE  LYS A 441      73.669  -3.982  20.141  1.00 51.80           C  
ANISOU 3239  CE  LYS A 441     5805   4962   8912    370  -2009   -944       C  
ATOM   3240  NZ  LYS A 441      74.670  -5.009  19.744  1.00 51.98           N  
ANISOU 3240  NZ  LYS A 441     5747   4949   9055    355  -2089   -898       N  
ATOM   3241  N   VAL A 442      67.477  -3.478  17.241  1.00 45.21           N  
ANISOU 3241  N   VAL A 442     5063   4385   7727    220  -1047   -423       N  
ATOM   3242  CA  VAL A 442      66.153  -3.858  16.743  1.00 44.28           C  
ANISOU 3242  CA  VAL A 442     4970   4330   7522    202   -889   -306       C  
ATOM   3243  C   VAL A 442      66.276  -4.668  15.449  1.00 43.37           C  
ANISOU 3243  C   VAL A 442     4767   4231   7481    150   -833   -199       C  
ATOM   3244  O   VAL A 442      65.588  -5.676  15.275  1.00 43.01           O  
ANISOU 3244  O   VAL A 442     4757   4240   7342    146   -775   -115       O  
ATOM   3245  CB  VAL A 442      65.254  -2.616  16.518  1.00 43.98           C  
ANISOU 3245  CB  VAL A 442     4899   4268   7544    196   -787   -320       C  
ATOM   3246  CG1 VAL A 442      64.053  -2.943  15.638  1.00 42.82           C  
ANISOU 3246  CG1 VAL A 442     4725   4166   7376    166   -642   -194       C  
ATOM   3247  CG2 VAL A 442      64.786  -2.056  17.853  1.00 45.15           C  
ANISOU 3247  CG2 VAL A 442     5157   4428   7569    256   -807   -426       C  
ATOM   3248  N   ALA A 443      67.149  -4.218  14.550  1.00 43.27           N  
ANISOU 3248  N   ALA A 443     4631   4167   7641    115   -846   -209       N  
ATOM   3249  CA  ALA A 443      67.364  -4.894  13.271  1.00 42.60           C  
ANISOU 3249  CA  ALA A 443     4461   4108   7615     74   -788   -128       C  
ATOM   3250  C   ALA A 443      68.061  -6.240  13.450  1.00 42.95           C  
ANISOU 3250  C   ALA A 443     4521   4167   7629     81   -866   -133       C  
ATOM   3251  O   ALA A 443      67.682  -7.224  12.816  1.00 42.51           O  
ANISOU 3251  O   ALA A 443     4456   4159   7536     67   -815    -71       O  
ATOM   3252  CB  ALA A 443      68.167  -4.007  12.332  1.00 42.68           C  
ANISOU 3252  CB  ALA A 443     4339   4063   7811     41   -761   -129       C  
ATOM   3253  N   LEU A 444      69.071  -6.280  14.316  1.00 44.32           N  
ANISOU 3253  N   LEU A 444     4712   4291   7835    107  -1003   -214       N  
ATOM   3254  CA  LEU A 444      69.830  -7.509  14.569  1.00 44.93           C  
ANISOU 3254  CA  LEU A 444     4796   4362   7910    121  -1100   -218       C  
ATOM   3255  C   LEU A 444      68.988  -8.571  15.276  1.00 45.70           C  
ANISOU 3255  C   LEU A 444     5018   4514   7832    151  -1099   -152       C  
ATOM   3256  O   LEU A 444      69.166  -9.768  15.039  1.00 45.58           O  
ANISOU 3256  O   LEU A 444     4988   4502   7827    147  -1115   -108       O  
ATOM   3257  CB  LEU A 444      71.079  -7.211  15.402  1.00 45.74           C  
ANISOU 3257  CB  LEU A 444     4886   4394   8096    151  -1271   -324       C  
ATOM   3258  CG  LEU A 444      72.125  -6.282  14.780  1.00 45.82           C  
ANISOU 3258  CG  LEU A 444     4748   4322   8340    119  -1285   -392       C  
ATOM   3259  CD1 LEU A 444      73.177  -5.919  15.815  1.00 47.25           C  
ANISOU 3259  CD1 LEU A 444     4926   4426   8601    158  -1479   -518       C  
ATOM   3260  CD2 LEU A 444      72.772  -6.907  13.555  1.00 45.23           C  
ANISOU 3260  CD2 LEU A 444     4543   4239   8401     78  -1218   -352       C  
ATOM   3261  N   ARG A 445      68.078  -8.128  16.140  1.00 46.94           N  
ANISOU 3261  N   ARG A 445     5288   4705   7843    181  -1069   -145       N  
ATOM   3262  CA  ARG A 445      67.163  -9.036  16.830  1.00 47.84           C  
ANISOU 3262  CA  ARG A 445     5516   4866   7792    209  -1031    -61       C  
ATOM   3263  C   ARG A 445      66.105  -9.563  15.859  1.00 45.97           C  
ANISOU 3263  C   ARG A 445     5230   4659   7575    168   -886     27       C  
ATOM   3264  O   ARG A 445      65.664 -10.707  15.971  1.00 45.62           O  
ANISOU 3264  O   ARG A 445     5215   4625   7493    170   -863    105       O  
ATOM   3265  CB  ARG A 445      66.483  -8.328  18.005  1.00 50.23           C  
ANISOU 3265  CB  ARG A 445     5947   5204   7932    257  -1016    -89       C  
ATOM   3266  CG  ARG A 445      66.160  -9.226  19.182  1.00 52.83           C  
ANISOU 3266  CG  ARG A 445     6423   5576   8074    311  -1041    -21       C  
ATOM   3267  CD  ARG A 445      65.255  -8.510  20.189  1.00 55.22           C  
ANISOU 3267  CD  ARG A 445     6849   5933   8197    359   -970    -44       C  
ATOM   3268  NE  ARG A 445      65.236  -7.035  20.200  1.00 56.45           N  
ANISOU 3268  NE  ARG A 445     6977   6074   8396    363   -967   -174       N  
ATOM   3269  CZ  ARG A 445      66.027  -6.208  20.878  1.00 58.31           C  
ANISOU 3269  CZ  ARG A 445     7243   6293   8619    405  -1101   -315       C  
ATOM   3270  NH1 ARG A 445      66.994  -6.663  21.662  1.00 59.67           N  
ANISOU 3270  NH1 ARG A 445     7483   6470   8716    454  -1273   -354       N  
ATOM   3271  NH2 ARG A 445      65.837  -4.894  20.750  1.00 58.77           N  
ANISOU 3271  NH2 ARG A 445     7251   6318   8759    399  -1071   -424       N  
ATOM   3272  N   ALA A 446      65.707  -8.715  14.913  1.00 44.61           N  
ANISOU 3272  N   ALA A 446     4980   4494   7476    134   -800     16       N  
ATOM   3273  CA  ALA A 446      64.716  -9.076  13.898  1.00 43.24           C  
ANISOU 3273  CA  ALA A 446     4751   4354   7324    101   -686     83       C  
ATOM   3274  C   ALA A 446      65.223 -10.143  12.926  1.00 42.30           C  
ANISOU 3274  C   ALA A 446     4548   4236   7288     76   -704     94       C  
ATOM   3275  O   ALA A 446      64.429 -10.908  12.380  1.00 41.92           O  
ANISOU 3275  O   ALA A 446     4475   4210   7242     62   -646    138       O  
ATOM   3276  CB  ALA A 446      64.276  -7.837  13.131  1.00 42.76           C  
ANISOU 3276  CB  ALA A 446     4630   4300   7316     82   -612     75       C  
ATOM   3277  N   MET A 447      66.537 -10.192  12.712  1.00 41.89           N  
ANISOU 3277  N   MET A 447     4442   4152   7321     73   -785     40       N  
ATOM   3278  CA  MET A 447      67.138 -11.169  11.799  1.00 41.32           C  
ANISOU 3278  CA  MET A 447     4282   4079   7338     55   -797     27       C  
ATOM   3279  C   MET A 447      67.067 -12.608  12.325  1.00 40.91           C  
ANISOU 3279  C   MET A 447     4264   4001   7279     70   -848     58       C  
ATOM   3280  O   MET A 447      67.300 -13.557  11.572  1.00 40.60           O  
ANISOU 3280  O   MET A 447     4149   3956   7319     58   -848     42       O  
ATOM   3281  CB  MET A 447      68.593 -10.791  11.499  1.00 42.00           C  
ANISOU 3281  CB  MET A 447     4288   4125   7543     49   -857    -39       C  
ATOM   3282  CG  MET A 447      68.740  -9.533  10.656  1.00 42.17           C  
ANISOU 3282  CG  MET A 447     4241   4162   7617     25   -781    -47       C  
ATOM   3283  SD  MET A 447      70.444  -8.951  10.546  1.00 43.36           S  
ANISOU 3283  SD  MET A 447     4288   4239   7945     17   -842   -119       S  
ATOM   3284  CE  MET A 447      70.190  -7.249  10.054  1.00 43.44           C  
ANISOU 3284  CE  MET A 447     4260   4244   8001     -3   -748    -89       C  
ATOM   3285  N   GLU A 448      66.754 -12.765  13.610  1.00 40.68           N  
ANISOU 3285  N   GLU A 448     4345   3955   7154    102   -888    102       N  
ATOM   3286  CA  GLU A 448      66.552 -14.084  14.206  1.00 40.73           C  
ANISOU 3286  CA  GLU A 448     4393   3929   7151    119   -921    170       C  
ATOM   3287  C   GLU A 448      65.146 -14.634  13.943  1.00 40.54           C  
ANISOU 3287  C   GLU A 448     4370   3923   7111    102   -807    242       C  
ATOM   3288  O   GLU A 448      64.912 -15.832  14.098  1.00 41.30           O  
ANISOU 3288  O   GLU A 448     4458   3976   7258    104   -813    299       O  
ATOM   3289  CB  GLU A 448      66.785 -14.027  15.719  1.00 41.40           C  
ANISOU 3289  CB  GLU A 448     4610   4003   7115    169  -1002    208       C  
ATOM   3290  CG  GLU A 448      68.146 -13.486  16.136  1.00 41.61           C  
ANISOU 3290  CG  GLU A 448     4637   4004   7169    194  -1146    124       C  
ATOM   3291  CD  GLU A 448      68.364 -13.526  17.639  1.00 42.59           C  
ANISOU 3291  CD  GLU A 448     4904   4130   7148    258  -1252    153       C  
ATOM   3292  OE1 GLU A 448      67.902 -14.487  18.291  1.00 43.13           O  
ANISOU 3292  OE1 GLU A 448     5050   4196   7137    284  -1246    265       O  
ATOM   3293  OE2 GLU A 448      69.009 -12.599  18.168  1.00 42.89           O  
ANISOU 3293  OE2 GLU A 448     4973   4171   7152    285  -1345     66       O  
ATOM   3294  N   ALA A 449      64.219 -13.761  13.544  1.00 39.85           N  
ANISOU 3294  N   ALA A 449     4278   3881   6979     87   -709    240       N  
ATOM   3295  CA  ALA A 449      62.797 -14.113  13.444  1.00 39.38           C  
ANISOU 3295  CA  ALA A 449     4217   3831   6914     75   -605    303       C  
ATOM   3296  C   ALA A 449      62.475 -15.250  12.467  1.00 39.18           C  
ANISOU 3296  C   ALA A 449     4087   3783   7016     50   -595    296       C  
ATOM   3297  O   ALA A 449      61.669 -16.121  12.794  1.00 39.66           O  
ANISOU 3297  O   ALA A 449     4147   3803   7119     47   -554    363       O  
ATOM   3298  CB  ALA A 449      61.973 -12.878  13.106  1.00 38.82           C  
ANISOU 3298  CB  ALA A 449     4142   3806   6801     67   -522    289       C  
ATOM   3299  N   PRO A 450      63.087 -15.246  11.267  1.00 38.87           N  
ANISOU 3299  N   PRO A 450     3954   3768   7044     34   -627    210       N  
ATOM   3300  CA  PRO A 450      62.821 -16.333  10.317  1.00 38.92           C  
ANISOU 3300  CA  PRO A 450     3862   3761   7165     19   -630    170       C  
ATOM   3301  C   PRO A 450      63.192 -17.714  10.856  1.00 39.73           C  
ANISOU 3301  C   PRO A 450     3951   3773   7368     26   -686    196       C  
ATOM   3302  O   PRO A 450      62.411 -18.653  10.712  1.00 40.04           O  
ANISOU 3302  O   PRO A 450     3942   3765   7507     16   -664    216       O  
ATOM   3303  CB  PRO A 450      63.693 -15.973   9.108  1.00 38.71           C  
ANISOU 3303  CB  PRO A 450     3762   3792   7153     13   -651     70       C  
ATOM   3304  CG  PRO A 450      63.894 -14.501   9.212  1.00 38.40           C  
ANISOU 3304  CG  PRO A 450     3768   3799   7020     15   -623     85       C  
ATOM   3305  CD  PRO A 450      63.976 -14.226  10.684  1.00 38.68           C  
ANISOU 3305  CD  PRO A 450     3906   3788   7001     31   -646    146       C  
ATOM   3306  N   LEU A 451      64.368 -17.834  11.470  1.00 40.12           N  
ANISOU 3306  N   LEU A 451     4036   3790   7418     44   -766    198       N  
ATOM   3307  CA  LEU A 451      64.794 -19.100  12.071  1.00 40.97           C  
ANISOU 3307  CA  LEU A 451     4137   3802   7627     58   -833    243       C  
ATOM   3308  C   LEU A 451      63.886 -19.466  13.238  1.00 41.41           C  
ANISOU 3308  C   LEU A 451     4283   3816   7635     70   -788    390       C  
ATOM   3309  O   LEU A 451      63.379 -20.583  13.306  1.00 41.86           O  
ANISOU 3309  O   LEU A 451     4295   3794   7815     63   -772    447       O  
ATOM   3310  CB  LEU A 451      66.249 -19.022  12.545  1.00 41.43           C  
ANISOU 3310  CB  LEU A 451     4215   3833   7691     83   -945    218       C  
ATOM   3311  CG  LEU A 451      66.878 -20.330  13.056  1.00 42.40           C  
ANISOU 3311  CG  LEU A 451     4316   3849   7945    104  -1039    260       C  
ATOM   3312  CD1 LEU A 451      68.369 -20.352  12.770  1.00 42.74           C  
ANISOU 3312  CD1 LEU A 451     4292   3866   8079    117  -1144    162       C  
ATOM   3313  CD2 LEU A 451      66.641 -20.548  14.543  1.00 43.43           C  
ANISOU 3313  CD2 LEU A 451     4579   3944   7978    139  -1069    416       C  
ATOM   3314  N   ARG A 452      63.697 -18.520  14.155  1.00 41.32           N  
ANISOU 3314  N   ARG A 452     4393   3853   7453     91   -761    448       N  
ATOM   3315  CA  ARG A 452      62.848 -18.729  15.329  1.00 42.13           C  
ANISOU 3315  CA  ARG A 452     4599   3939   7469    111   -692    590       C  
ATOM   3316  C   ARG A 452      61.445 -19.199  14.946  1.00 42.25           C  
ANISOU 3316  C   ARG A 452     4548   3925   7577     80   -569    638       C  
ATOM   3317  O   ARG A 452      60.864 -20.044  15.630  1.00 43.46           O  
ANISOU 3317  O   ARG A 452     4722   4013   7776     86   -516    766       O  
ATOM   3318  CB  ARG A 452      62.764 -17.449  16.167  1.00 42.10           C  
ANISOU 3318  CB  ARG A 452     4723   4013   7258    140   -666    597       C  
ATOM   3319  CG  ARG A 452      64.026 -17.151  16.958  1.00 42.62           C  
ANISOU 3319  CG  ARG A 452     4875   4088   7228    183   -800    576       C  
ATOM   3320  CD  ARG A 452      63.994 -15.757  17.565  1.00 42.55           C  
ANISOU 3320  CD  ARG A 452     4964   4154   7046    209   -789    527       C  
ATOM   3321  NE  ARG A 452      65.050 -15.573  18.558  1.00 43.59           N  
ANISOU 3321  NE  ARG A 452     5194   4292   7073    263   -929    513       N  
ATOM   3322  CZ  ARG A 452      65.012 -16.040  19.807  1.00 45.34           C  
ANISOU 3322  CZ  ARG A 452     5550   4523   7152    320   -959    619       C  
ATOM   3323  NH1 ARG A 452      63.966 -16.732  20.250  1.00 46.14           N  
ANISOU 3323  NH1 ARG A 452     5701   4620   7209    324   -832    764       N  
ATOM   3324  NH2 ARG A 452      66.033 -15.818  20.625  1.00 46.54           N  
ANISOU 3324  NH2 ARG A 452     5786   4687   7207    375  -1117    584       N  
ATOM   3325  N   GLN A 453      60.913 -18.657  13.852  1.00 41.20           N  
ANISOU 3325  N   GLN A 453     4331   3838   7485     50   -529    541       N  
ATOM   3326  CA  GLN A 453      59.607 -19.070  13.343  1.00 41.29           C  
ANISOU 3326  CA  GLN A 453     4255   3818   7613     23   -441    556       C  
ATOM   3327  C   GLN A 453      59.648 -20.502  12.811  1.00 42.04           C  
ANISOU 3327  C   GLN A 453     4233   3815   7923      6   -486    539       C  
ATOM   3328  O   GLN A 453      58.750 -21.293  13.094  1.00 43.02           O  
ANISOU 3328  O   GLN A 453     4313   3856   8175     -6   -421    621       O  
ATOM   3329  CB  GLN A 453      59.124 -18.114  12.244  1.00 40.21           C  
ANISOU 3329  CB  GLN A 453     4060   3761   7458      6   -419    451       C  
ATOM   3330  CG  GLN A 453      57.771 -18.477  11.644  1.00 40.25           C  
ANISOU 3330  CG  GLN A 453     3962   3736   7594    -16   -357    445       C  
ATOM   3331  CD  GLN A 453      56.651 -18.484  12.674  1.00 40.88           C  
ANISOU 3331  CD  GLN A 453     4082   3770   7677    -15   -232    574       C  
ATOM   3332  OE1 GLN A 453      56.626 -17.670  13.600  1.00 40.88           O  
ANISOU 3332  OE1 GLN A 453     4197   3812   7523      6   -171    635       O  
ATOM   3333  NE2 GLN A 453      55.713 -19.405  12.511  1.00 41.67           N  
ANISOU 3333  NE2 GLN A 453     4081   3784   7967    -36   -187    605       N  
ATOM   3334  N   ILE A 454      60.683 -20.828  12.038  1.00 41.87           N  
ANISOU 3334  N   ILE A 454     4150   3795   7960      6   -588    426       N  
ATOM   3335  CA  ILE A 454      60.854 -22.185  11.505  1.00 42.64           C  
ANISOU 3335  CA  ILE A 454     4128   3795   8277     -3   -643    378       C  
ATOM   3336  C   ILE A 454      60.931 -23.206  12.643  1.00 44.16           C  
ANISOU 3336  C   ILE A 454     4354   3864   8559      8   -646    533       C  
ATOM   3337  O   ILE A 454      60.288 -24.253  12.588  1.00 45.11           O  
ANISOU 3337  O   ILE A 454     4384   3872   8881     -7   -622    572       O  
ATOM   3338  CB  ILE A 454      62.111 -22.297  10.609  1.00 41.94           C  
ANISOU 3338  CB  ILE A 454     3979   3735   8220      4   -741    227       C  
ATOM   3339  CG1 ILE A 454      61.889 -21.550   9.290  1.00 41.06           C  
ANISOU 3339  CG1 ILE A 454     3814   3739   8047     -4   -725     85       C  
ATOM   3340  CG2 ILE A 454      62.445 -23.755  10.315  1.00 42.74           C  
ANISOU 3340  CG2 ILE A 454     3966   3714   8556      3   -805    180       C  
ATOM   3341  CD1 ILE A 454      63.160 -21.245   8.529  1.00 40.66           C  
ANISOU 3341  CD1 ILE A 454     3737   3753   7958      6   -778    -34       C  
ATOM   3342  N   VAL A 455      61.711 -22.880  13.670  1.00 44.77           N  
ANISOU 3342  N   VAL A 455     4558   3959   8492     40   -680    624       N  
ATOM   3343  CA  VAL A 455      61.874 -23.745  14.837  1.00 46.45           C  
ANISOU 3343  CA  VAL A 455     4831   4074   8741     65   -693    798       C  
ATOM   3344  C   VAL A 455      60.561 -23.882  15.611  1.00 47.67           C  
ANISOU 3344  C   VAL A 455     5032   4199   8880     59   -547    965       C  
ATOM   3345  O   VAL A 455      60.259 -24.954  16.135  1.00 49.23           O  
ANISOU 3345  O   VAL A 455     5205   4276   9221     60   -518   1107       O  
ATOM   3346  CB  VAL A 455      62.992 -23.220  15.771  1.00 46.82           C  
ANISOU 3346  CB  VAL A 455     5018   4171   8599    112   -782    843       C  
ATOM   3347  CG1 VAL A 455      63.049 -24.012  17.069  1.00 48.69           C  
ANISOU 3347  CG1 VAL A 455     5349   4331   8819    150   -793   1051       C  
ATOM   3348  CG2 VAL A 455      64.343 -23.286  15.073  1.00 46.34           C  
ANISOU 3348  CG2 VAL A 455     4885   4104   8615    116   -920    695       C  
ATOM   3349  N   LEU A 456      59.787 -22.801  15.684  1.00 47.49           N  
ANISOU 3349  N   LEU A 456     5065   4274   8702     53   -448    954       N  
ATOM   3350  CA  LEU A 456      58.486 -22.828  16.359  1.00 48.92           C  
ANISOU 3350  CA  LEU A 456     5276   4434   8877     47   -286   1096       C  
ATOM   3351  C   LEU A 456      57.501 -23.768  15.656  1.00 49.86           C  
ANISOU 3351  C   LEU A 456     5222   4435   9287      3   -230   1090       C  
ATOM   3352  O   LEU A 456      56.760 -24.496  16.316  1.00 51.44           O  
ANISOU 3352  O   LEU A 456     5407   4537   9600     -2   -124   1253       O  
ATOM   3353  CB  LEU A 456      57.895 -21.416  16.464  1.00 48.17           C  
ANISOU 3353  CB  LEU A 456     5255   4462   8585     52   -200   1052       C  
ATOM   3354  CG  LEU A 456      56.527 -21.313  17.155  1.00 49.07           C  
ANISOU 3354  CG  LEU A 456     5391   4562   8691     50    -12   1182       C  
ATOM   3355  CD1 LEU A 456      56.703 -21.225  18.665  1.00 50.48           C  
ANISOU 3355  CD1 LEU A 456     5751   4776   8652    102     52   1349       C  
ATOM   3356  CD2 LEU A 456      55.722 -20.131  16.635  1.00 48.16           C  
ANISOU 3356  CD2 LEU A 456     5247   4525   8524     35     55   1078       C  
ATOM   3357  N   ASN A 457      57.504 -23.760  14.325  1.00 49.41           N  
ANISOU 3357  N   ASN A 457     5033   4386   9354    -24   -302    902       N  
ATOM   3358  CA  ASN A 457      56.636 -24.651  13.546  1.00 50.36           C  
ANISOU 3358  CA  ASN A 457     4974   4396   9762    -61   -287    850       C  
ATOM   3359  C   ASN A 457      57.010 -26.124  13.698  1.00 52.17           C  
ANISOU 3359  C   ASN A 457     5119   4461  10239    -65   -338    908       C  
ATOM   3360  O   ASN A 457      56.152 -26.999  13.587  1.00 53.30           O  
ANISOU 3360  O   ASN A 457     5134   4469  10647    -92   -287    947       O  
ATOM   3361  CB  ASN A 457      56.644 -24.255  12.068  1.00 49.26           C  
ANISOU 3361  CB  ASN A 457     4734   4330   9651    -74   -372    620       C  
ATOM   3362  CG  ASN A 457      56.098 -22.858  11.844  1.00 48.19           C  
ANISOU 3362  CG  ASN A 457     4655   4330   9323    -72   -318    581       C  
ATOM   3363  OD1 ASN A 457      55.913 -22.098  12.794  1.00 48.54           O  
ANISOU 3363  OD1 ASN A 457     4822   4421   9196    -57   -229    696       O  
ATOM   3364  ND2 ASN A 457      55.834 -22.511  10.596  1.00 47.45           N  
ANISOU 3364  ND2 ASN A 457     4474   4299   9255    -79   -375    418       N  
ATOM   3365  N   CYS A 458      58.292 -26.390  13.947  1.00 52.73           N  
ANISOU 3365  N   CYS A 458     5249   4531  10254    -37   -444    912       N  
ATOM   3366  CA  CYS A 458      58.762 -27.743  14.246  1.00 54.47           C  
ANISOU 3366  CA  CYS A 458     5404   4587  10704    -33   -500    993       C  
ATOM   3367  C   CYS A 458      58.262 -28.233  15.606  1.00 56.59           C  
ANISOU 3367  C   CYS A 458     5751   4765  10984    -21   -387   1275       C  
ATOM   3368  O   CYS A 458      58.163 -29.438  15.831  1.00 58.36           O  
ANISOU 3368  O   CYS A 458     5886   4816  11469    -28   -386   1382       O  
ATOM   3369  CB  CYS A 458      60.292 -27.806  14.221  1.00 54.07           C  
ANISOU 3369  CB  CYS A 458     5398   4561  10584      0   -646    929       C  
ATOM   3370  SG  CYS A 458      61.050 -27.350  12.645  1.00 52.77           S  
ANISOU 3370  SG  CYS A 458     5139   4498  10413     -7   -756    618       S  
ATOM   3371  N   GLY A 459      57.957 -27.299  16.506  1.00 56.94           N  
ANISOU 3371  N   GLY A 459     5962   4925  10747      1   -286   1396       N  
ATOM   3372  CA  GLY A 459      57.494 -27.627  17.852  1.00 59.36           C  
ANISOU 3372  CA  GLY A 459     6374   5185  10993     24   -157   1671       C  
ATOM   3373  C   GLY A 459      58.603 -27.587  18.889  1.00 60.77           C  
ANISOU 3373  C   GLY A 459     6731   5412  10947     87   -240   1799       C  
ATOM   3374  O   GLY A 459      58.413 -28.038  20.019  1.00 62.82           O  
ANISOU 3374  O   GLY A 459     7089   5630  11148    120   -158   2045       O  
ATOM   3375  N   GLU A 460      59.762 -27.052  18.504  1.00 60.48           N  
ANISOU 3375  N   GLU A 460     6731   5460  10785    108   -403   1636       N  
ATOM   3376  CA  GLU A 460      60.905 -26.906  19.405  1.00 61.72           C  
ANISOU 3376  CA  GLU A 460     7045   5669  10735    171   -520   1715       C  
ATOM   3377  C   GLU A 460      60.987 -25.471  19.923  1.00 60.91           C  
ANISOU 3377  C   GLU A 460     7112   5753  10277    204   -499   1669       C  
ATOM   3378  O   GLU A 460      60.357 -24.568  19.370  1.00 59.22           O  
ANISOU 3378  O   GLU A 460     6873   5621  10006    173   -419   1543       O  
ATOM   3379  CB  GLU A 460      62.202 -27.269  18.678  1.00 61.62           C  
ANISOU 3379  CB  GLU A 460     6943   5611  10859    174   -717   1557       C  
ATOM   3380  CG  GLU A 460      62.219 -28.664  18.071  1.00 62.90           C  
ANISOU 3380  CG  GLU A 460     6920   5583  11394    145   -756   1556       C  
ATOM   3381  CD  GLU A 460      62.120 -29.759  19.115  1.00 65.94           C  
ANISOU 3381  CD  GLU A 460     7341   5828  11882    175   -735   1833       C  
ATOM   3382  OE1 GLU A 460      62.904 -29.724  20.089  1.00 67.41           O  
ANISOU 3382  OE1 GLU A 460     7673   6045  11893    238   -822   1967       O  
ATOM   3383  OE2 GLU A 460      61.263 -30.657  18.958  1.00 67.59           O  
ANISOU 3383  OE2 GLU A 460     7429   5891  12358    139   -638   1921       O  
ATOM   3384  N   GLU A 461      61.764 -25.272  20.986  1.00 62.14           N  
ANISOU 3384  N   GLU A 461     7436   5967  10208    272   -583   1765       N  
ATOM   3385  CA  GLU A 461      61.917 -23.952  21.607  1.00 62.02           C  
ANISOU 3385  CA  GLU A 461     7586   6118   9860    314   -583   1711       C  
ATOM   3386  C   GLU A 461      62.851 -23.071  20.775  1.00 59.81           C  
ANISOU 3386  C   GLU A 461     7256   5900   9568    301   -725   1463       C  
ATOM   3387  O   GLU A 461      64.022 -23.414  20.603  1.00 59.85           O  
ANISOU 3387  O   GLU A 461     7227   5862   9650    317   -898   1407       O  
ATOM   3388  CB  GLU A 461      62.449 -24.087  23.037  1.00 64.50           C  
ANISOU 3388  CB  GLU A 461     8097   6476   9931    402   -646   1886       C  
ATOM   3389  CG  GLU A 461      61.431 -24.668  24.008  1.00 67.02           C  
ANISOU 3389  CG  GLU A 461     8507   6777  10180    427   -459   2152       C  
ATOM   3390  CD  GLU A 461      62.025 -25.026  25.359  1.00 69.87           C  
ANISOU 3390  CD  GLU A 461     9062   7175  10309    523   -537   2354       C  
ATOM   3391  OE1 GLU A 461      63.059 -25.728  25.395  1.00 70.88           O  
ANISOU 3391  OE1 GLU A 461     9170   7224  10537    550   -729   2388       O  
ATOM   3392  OE2 GLU A 461      61.447 -24.620  26.390  1.00 71.52           O  
ANISOU 3392  OE2 GLU A 461     9445   7495  10234    577   -407   2481       O  
ATOM   3393  N   PRO A 462      62.339 -21.938  20.249  1.00 57.92           N  
ANISOU 3393  N   PRO A 462     7003   5752   9251    271   -647   1323       N  
ATOM   3394  CA  PRO A 462      63.150 -21.071  19.385  1.00 56.15           C  
ANISOU 3394  CA  PRO A 462     6718   5579   9035    253   -754   1110       C  
ATOM   3395  C   PRO A 462      64.387 -20.494  20.072  1.00 56.47           C  
ANISOU 3395  C   PRO A 462     6867   5673   8914    310   -917   1062       C  
ATOM   3396  O   PRO A 462      65.455 -20.424  19.459  1.00 56.05           O  
ANISOU 3396  O   PRO A 462     6734   5597   8965    301  -1051    936       O  
ATOM   3397  CB  PRO A 462      62.184 -19.941  19.001  1.00 55.09           C  
ANISOU 3397  CB  PRO A 462     6582   5530   8820    224   -620   1030       C  
ATOM   3398  CG  PRO A 462      60.823 -20.487  19.239  1.00 55.95           C  
ANISOU 3398  CG  PRO A 462     6677   5599   8981    207   -446   1166       C  
ATOM   3399  CD  PRO A 462      60.967 -21.419  20.401  1.00 57.97           C  
ANISOU 3399  CD  PRO A 462     7033   5807   9184    253   -449   1366       C  
ATOM   3400  N   SER A 463      64.234 -20.074  21.325  1.00 57.46           N  
ANISOU 3400  N   SER A 463     7167   5871   8792    370   -904   1151       N  
ATOM   3401  CA  SER A 463      65.344 -19.526  22.106  1.00 58.08           C  
ANISOU 3401  CA  SER A 463     7359   6003   8703    436  -1078   1098       C  
ATOM   3402  C   SER A 463      66.525 -20.490  22.179  1.00 58.41           C  
ANISOU 3402  C   SER A 463     7361   5955   8874    462  -1267   1133       C  
ATOM   3403  O   SER A 463      67.670 -20.079  22.016  1.00 58.05           O  
ANISOU 3403  O   SER A 463     7283   5907   8863    476  -1435   1000       O  
ATOM   3404  CB  SER A 463      64.884 -19.187  23.520  1.00 60.19           C  
ANISOU 3404  CB  SER A 463     7834   6366   8668    511  -1029   1210       C  
ATOM   3405  OG  SER A 463      63.625 -18.539  23.507  1.00 60.26           O  
ANISOU 3405  OG  SER A 463     7866   6437   8593    488   -821   1210       O  
ATOM   3406  N   VAL A 464      66.238 -21.770  22.407  1.00 58.84           N  
ANISOU 3406  N   VAL A 464     7403   5921   9030    467  -1238   1312       N  
ATOM   3407  CA  VAL A 464      67.289 -22.773  22.596  1.00 59.23           C  
ANISOU 3407  CA  VAL A 464     7419   5870   9214    500  -1418   1373       C  
ATOM   3408  C   VAL A 464      68.067 -23.003  21.302  1.00 57.21           C  
ANISOU 3408  C   VAL A 464     6959   5529   9247    445  -1498   1199       C  
ATOM   3409  O   VAL A 464      69.295 -23.082  21.319  1.00 57.57           O  
ANISOU 3409  O   VAL A 464     6969   5536   9366    474  -1683   1126       O  
ATOM   3410  CB  VAL A 464      66.718 -24.118  23.101  1.00 60.93           C  
ANISOU 3410  CB  VAL A 464     7652   5988   9509    514  -1350   1624       C  
ATOM   3411  CG1 VAL A 464      67.825 -25.158  23.233  1.00 62.15           C  
ANISOU 3411  CG1 VAL A 464     7753   6019   9840    550  -1546   1685       C  
ATOM   3412  CG2 VAL A 464      66.009 -23.929  24.436  1.00 62.90           C  
ANISOU 3412  CG2 VAL A 464     8115   6333   9452    579  -1254   1818       C  
ATOM   3413  N   VAL A 465      67.348 -23.102  20.187  1.00 55.27           N  
ANISOU 3413  N   VAL A 465     6580   5259   9161    372  -1359   1127       N  
ATOM   3414  CA  VAL A 465      67.967 -23.346  18.884  1.00 53.80           C  
ANISOU 3414  CA  VAL A 465     6206   5012   9223    324  -1405    957       C  
ATOM   3415  C   VAL A 465      68.725 -22.108  18.406  1.00 52.58           C  
ANISOU 3415  C   VAL A 465     6031   4940   9005    316  -1461    766       C  
ATOM   3416  O   VAL A 465      69.860 -22.212  17.947  1.00 52.45           O  
ANISOU 3416  O   VAL A 465     5918   4879   9130    318  -1580    655       O  
ATOM   3417  CB  VAL A 465      66.924 -23.766  17.825  1.00 52.65           C  
ANISOU 3417  CB  VAL A 465     5933   4833   9237    258  -1251    922       C  
ATOM   3418  CG1 VAL A 465      67.576 -23.943  16.460  1.00 51.65           C  
ANISOU 3418  CG1 VAL A 465     5630   4674   9320    220  -1292    728       C  
ATOM   3419  CG2 VAL A 465      66.233 -25.057  18.240  1.00 53.98           C  
ANISOU 3419  CG2 VAL A 465     6086   4885   9537    259  -1198   1105       C  
ATOM   3420  N   ALA A 466      68.090 -20.944  18.513  1.00 51.89           N  
ANISOU 3420  N   ALA A 466     6022   4961   8729    306  -1367    731       N  
ATOM   3421  CA  ALA A 466      68.714 -19.680  18.122  1.00 51.00           C  
ANISOU 3421  CA  ALA A 466     5892   4917   8569    297  -1406    570       C  
ATOM   3422  C   ALA A 466      70.010 -19.431  18.895  1.00 52.22           C  
ANISOU 3422  C   ALA A 466     6094   5057   8687    354  -1602    533       C  
ATOM   3423  O   ALA A 466      70.990 -18.931  18.338  1.00 51.53           O  
ANISOU 3423  O   ALA A 466     5913   4956   8710    341  -1680    393       O  
ATOM   3424  CB  ALA A 466      67.744 -18.526  18.336  1.00 50.43           C  
ANISOU 3424  CB  ALA A 466     5908   4945   8306    289  -1281    563       C  
ATOM   3425  N   ASN A 467      70.003 -19.785  20.177  1.00 54.13           N  
ANISOU 3425  N   ASN A 467     6482   5304   8781    419  -1681    663       N  
ATOM   3426  CA  ASN A 467      71.175 -19.633  21.035  1.00 55.77           C  
ANISOU 3426  CA  ASN A 467     6750   5500   8937    487  -1898    637       C  
ATOM   3427  C   ASN A 467      72.314 -20.568  20.616  1.00 55.90           C  
ANISOU 3427  C   ASN A 467     6629   5397   9213    490  -2043    610       C  
ATOM   3428  O   ASN A 467      73.481 -20.177  20.633  1.00 56.27           O  
ANISOU 3428  O   ASN A 467     6620   5416   9341    511  -2204    492       O  
ATOM   3429  CB  ASN A 467      70.791 -19.895  22.496  1.00 58.03           C  
ANISOU 3429  CB  ASN A 467     7241   5836   8969    568  -1940    805       C  
ATOM   3430  CG  ASN A 467      71.773 -19.291  23.478  1.00 60.07           C  
ANISOU 3430  CG  ASN A 467     7603   6135   9083    649  -2160    740       C  
ATOM   3431  OD1 ASN A 467      72.055 -18.093  23.427  1.00 60.04           O  
ANISOU 3431  OD1 ASN A 467     7599   6185   9026    646  -2192    576       O  
ATOM   3432  ND2 ASN A 467      72.284 -20.111  24.394  1.00 62.34           N  
ANISOU 3432  ND2 ASN A 467     7977   6392   9316    726  -2321    869       N  
ATOM   3433  N   THR A 468      71.964 -21.795  20.232  1.00 55.72           N  
ANISOU 3433  N   THR A 468     6535   5289   9345    468  -1986    710       N  
ATOM   3434  CA  THR A 468      72.947 -22.790  19.796  1.00 55.99           C  
ANISOU 3434  CA  THR A 468     6423   5194   9653    471  -2107    681       C  
ATOM   3435  C   THR A 468      73.577 -22.428  18.449  1.00 54.50           C  
ANISOU 3435  C   THR A 468     6046   4987   9671    414  -2074    475       C  
ATOM   3436  O   THR A 468      74.775 -22.630  18.251  1.00 55.16           O  
ANISOU 3436  O   THR A 468     6023   4998   9938    430  -2210    385       O  
ATOM   3437  CB  THR A 468      72.315 -24.195  19.696  1.00 56.46           C  
ANISOU 3437  CB  THR A 468     6443   5155   9853    461  -2040    831       C  
ATOM   3438  OG1 THR A 468      71.663 -24.519  20.931  1.00 57.74           O  
ANISOU 3438  OG1 THR A 468     6782   5338   9817    513  -2035   1052       O  
ATOM   3439  CG2 THR A 468      73.372 -25.253  19.400  1.00 57.39           C  
ANISOU 3439  CG2 THR A 468     6416   5125  10264    477  -2184    805       C  
ATOM   3440  N   VAL A 469      72.770 -21.903  17.529  1.00 52.88           N  
ANISOU 3440  N   VAL A 469     5802   4851   9439    352  -1892    407       N  
ATOM   3441  CA  VAL A 469      73.266 -21.502  16.210  1.00 51.71           C  
ANISOU 3441  CA  VAL A 469     5493   4710   9442    303  -1832    230       C  
ATOM   3442  C   VAL A 469      74.222 -20.315  16.333  1.00 51.97           C  
ANISOU 3442  C   VAL A 469     5520   4778   9449    313  -1914    118       C  
ATOM   3443  O   VAL A 469      75.271 -20.292  15.689  1.00 51.99           O  
ANISOU 3443  O   VAL A 469     5380   4731   9641    303  -1959      0       O  
ATOM   3444  CB  VAL A 469      72.110 -21.157  15.239  1.00 50.00           C  
ANISOU 3444  CB  VAL A 469     5254   4572   9170    245  -1631    200       C  
ATOM   3445  CG1 VAL A 469      72.642 -20.554  13.945  1.00 49.02           C  
ANISOU 3445  CG1 VAL A 469     4996   4485   9143    206  -1566     36       C  
ATOM   3446  CG2 VAL A 469      71.291 -22.400  14.928  1.00 50.08           C  
ANISOU 3446  CG2 VAL A 469     5221   4523   9282    230  -1564    269       C  
ATOM   3447  N   LYS A 470      73.857 -19.336  17.160  1.00 52.46           N  
ANISOU 3447  N   LYS A 470     5722   4915   9293    334  -1927    150       N  
ATOM   3448  CA  LYS A 470      74.714 -18.172  17.408  1.00 52.84           C  
ANISOU 3448  CA  LYS A 470     5765   4980   9331    348  -2022     39       C  
ATOM   3449  C   LYS A 470      76.067 -18.561  18.010  1.00 54.47           C  
ANISOU 3449  C   LYS A 470     5927   5094   9674    400  -2250      3       C  
ATOM   3450  O   LYS A 470      77.086 -17.938  17.705  1.00 55.10           O  
ANISOU 3450  O   LYS A 470     5896   5138   9901    393  -2319   -126       O  
ATOM   3451  CB  LYS A 470      74.007 -17.153  18.312  1.00 53.21           C  
ANISOU 3451  CB  LYS A 470     5979   5117   9118    372  -2008     69       C  
ATOM   3452  CG  LYS A 470      73.046 -16.238  17.568  1.00 52.08           C  
ANISOU 3452  CG  LYS A 470     5831   5052   8903    317  -1811     39       C  
ATOM   3453  CD  LYS A 470      72.531 -15.102  18.445  1.00 52.60           C  
ANISOU 3453  CD  LYS A 470     6037   5191   8757    345  -1810     30       C  
ATOM   3454  CE  LYS A 470      71.239 -15.474  19.152  1.00 52.99           C  
ANISOU 3454  CE  LYS A 470     6238   5302   8592    368  -1716    167       C  
ATOM   3455  NZ  LYS A 470      70.800 -14.411  20.097  1.00 53.76           N  
ANISOU 3455  NZ  LYS A 470     6477   5474   8475    408  -1719    141       N  
ATOM   3456  N   GLY A 471      76.072 -19.589  18.857  1.00 55.64           N  
ANISOU 3456  N   GLY A 471     6152   5198   9789    455  -2365    126       N  
ATOM   3457  CA  GLY A 471      77.304 -20.094  19.463  1.00 57.30           C  
ANISOU 3457  CA  GLY A 471     6323   5314  10135    514  -2603    113       C  
ATOM   3458  C   GLY A 471      78.312 -20.627  18.458  1.00 57.11           C  
ANISOU 3458  C   GLY A 471     6074   5179  10445    484  -2621      3       C  
ATOM   3459  O   GLY A 471      79.521 -20.499  18.661  1.00 58.68           O  
ANISOU 3459  O   GLY A 471     6183   5304  10806    515  -2795    -85       O  
ATOM   3460  N   GLY A 472      77.817 -21.222  17.375  1.00 55.68           N  
ANISOU 3460  N   GLY A 472     5796   4988  10372    429  -2444     -2       N  
ATOM   3461  CA  GLY A 472      78.674 -21.762  16.321  1.00 55.58           C  
ANISOU 3461  CA  GLY A 472     5570   4886  10659    402  -2424   -121       C  
ATOM   3462  C   GLY A 472      79.212 -20.704  15.373  1.00 54.77           C  
ANISOU 3462  C   GLY A 472     5346   4822  10640    355  -2323   -280       C  
ATOM   3463  O   GLY A 472      78.999 -19.506  15.575  1.00 54.38           O  
ANISOU 3463  O   GLY A 472     5368   4849  10442    342  -2293   -300       O  
ATOM   3464  N   ASP A 473      79.909 -21.158  14.332  1.00 55.05           N  
ANISOU 3464  N   ASP A 473     5193   4800  10923    331  -2262   -390       N  
ATOM   3465  CA  ASP A 473      80.536 -20.272  13.346  1.00 55.01           C  
ANISOU 3465  CA  ASP A 473     5051   4820  11027    289  -2145   -526       C  
ATOM   3466  C   ASP A 473      80.238 -20.723  11.919  1.00 53.74           C  
ANISOU 3466  C   ASP A 473     4782   4701  10935    247  -1935   -595       C  
ATOM   3467  O   ASP A 473      79.880 -21.877  11.685  1.00 53.66           O  
ANISOU 3467  O   ASP A 473     4751   4657  10980    256  -1923   -580       O  
ATOM   3468  CB  ASP A 473      82.056 -20.244  13.550  1.00 57.17           C  
ANISOU 3468  CB  ASP A 473     5173   4974  11574    316  -2299   -624       C  
ATOM   3469  CG  ASP A 473      82.461 -19.647  14.887  1.00 58.77           C  
ANISOU 3469  CG  ASP A 473     5471   5145  11714    363  -2527   -593       C  
ATOM   3470  OD1 ASP A 473      82.040 -18.508  15.189  1.00 58.49           O  
ANISOU 3470  OD1 ASP A 473     5534   5187  11499    349  -2499   -586       O  
ATOM   3471  OD2 ASP A 473      83.212 -20.316  15.632  1.00 60.98           O  
ANISOU 3471  OD2 ASP A 473     5723   5319  12128    420  -2744   -583       O  
ATOM   3472  N   GLY A 474      80.397 -19.802  10.973  1.00 52.96           N  
ANISOU 3472  N   GLY A 474     4612   4674  10835    206  -1774   -670       N  
ATOM   3473  CA  GLY A 474      80.283 -20.111   9.549  1.00 52.67           C  
ANISOU 3473  CA  GLY A 474     4469   4696  10846    177  -1576   -753       C  
ATOM   3474  C   GLY A 474      78.890 -20.544   9.130  1.00 51.70           C  
ANISOU 3474  C   GLY A 474     4445   4666  10529    163  -1471   -702       C  
ATOM   3475  O   GLY A 474      77.899 -19.922   9.513  1.00 50.98           O  
ANISOU 3475  O   GLY A 474     4497   4650  10220    150  -1448   -608       O  
ATOM   3476  N   ASN A 475      78.818 -21.617   8.345  1.00 52.20           N  
ANISOU 3476  N   ASN A 475     4420   4717  10693    169  -1414   -779       N  
ATOM   3477  CA  ASN A 475      77.540 -22.148   7.858  1.00 51.53           C  
ANISOU 3477  CA  ASN A 475     4398   4704  10474    158  -1329   -761       C  
ATOM   3478  C   ASN A 475      76.931 -23.222   8.775  1.00 51.38           C  
ANISOU 3478  C   ASN A 475     4446   4589  10485    179  -1456   -667       C  
ATOM   3479  O   ASN A 475      76.074 -23.997   8.347  1.00 50.99           O  
ANISOU 3479  O   ASN A 475     4394   4549  10430    174  -1408   -679       O  
ATOM   3480  CB  ASN A 475      77.706 -22.690   6.429  1.00 52.31           C  
ANISOU 3480  CB  ASN A 475     4367   4854  10654    157  -1193   -917       C  
ATOM   3481  CG  ASN A 475      77.950 -21.587   5.408  1.00 52.41           C  
ANISOU 3481  CG  ASN A 475     4349   4999  10563    136  -1023   -968       C  
ATOM   3482  OD1 ASN A 475      77.146 -20.663   5.269  1.00 50.87           O  
ANISOU 3482  OD1 ASN A 475     4259   4913  10155    114   -949   -891       O  
ATOM   3483  ND2 ASN A 475      79.063 -21.685   4.680  1.00 53.94           N  
ANISOU 3483  ND2 ASN A 475     4395   5180  10920    145   -950  -1091       N  
ATOM   3484  N   TYR A 476      77.376 -23.265  10.031  1.00 51.59           N  
ANISOU 3484  N   TYR A 476     4528   4524  10548    206  -1619   -570       N  
ATOM   3485  CA  TYR A 476      76.778 -24.141  11.039  1.00 51.81           C  
ANISOU 3485  CA  TYR A 476     4645   4470  10568    230  -1729   -433       C  
ATOM   3486  C   TYR A 476      75.384 -23.635  11.387  1.00 50.62           C  
ANISOU 3486  C   TYR A 476     4656   4416  10160    210  -1653   -313       C  
ATOM   3487  O   TYR A 476      75.191 -22.439  11.611  1.00 50.21           O  
ANISOU 3487  O   TYR A 476     4694   4456   9925    198  -1618   -286       O  
ATOM   3488  CB  TYR A 476      77.652 -24.177  12.296  1.00 52.99           C  
ANISOU 3488  CB  TYR A 476     4832   4522  10777    276  -1930   -354       C  
ATOM   3489  CG  TYR A 476      77.071 -24.964  13.452  1.00 53.68           C  
ANISOU 3489  CG  TYR A 476     5039   4540  10817    310  -2040   -175       C  
ATOM   3490  CD1 TYR A 476      77.160 -26.352  13.492  1.00 54.74           C  
ANISOU 3490  CD1 TYR A 476     5093   4539  11164    332  -2102   -144       C  
ATOM   3491  CD2 TYR A 476      76.448 -24.316  14.517  1.00 53.61           C  
ANISOU 3491  CD2 TYR A 476     5218   4597  10553    325  -2074    -32       C  
ATOM   3492  CE1 TYR A 476      76.638 -27.072  14.554  1.00 55.77           C  
ANISOU 3492  CE1 TYR A 476     5331   4600  11260    365  -2189     50       C  
ATOM   3493  CE2 TYR A 476      75.924 -25.027  15.584  1.00 54.60           C  
ANISOU 3493  CE2 TYR A 476     5459   4670  10614    362  -2152    151       C  
ATOM   3494  CZ  TYR A 476      76.021 -26.404  15.598  1.00 55.73           C  
ANISOU 3494  CZ  TYR A 476     5523   4676  10975    381  -2207    205       C  
ATOM   3495  OH  TYR A 476      75.500 -27.114  16.655  1.00 57.05           O  
ANISOU 3495  OH  TYR A 476     5805   4785  11086    418  -2270    417       O  
ATOM   3496  N   GLY A 477      74.416 -24.547  11.425  1.00 50.28           N  
ANISOU 3496  N   GLY A 477     4634   4337  10129    206  -1626   -247       N  
ATOM   3497  CA  GLY A 477      73.030 -24.179  11.704  1.00 48.98           C  
ANISOU 3497  CA  GLY A 477     4599   4250   9760    186  -1539   -138       C  
ATOM   3498  C   GLY A 477      72.145 -25.357  12.059  1.00 48.96           C  
ANISOU 3498  C   GLY A 477     4606   4158   9837    189  -1542    -32       C  
ATOM   3499  O   GLY A 477      72.622 -26.481  12.207  1.00 49.65           O  
ANISOU 3499  O   GLY A 477     4612   4113  10140    211  -1627    -26       O  
ATOM   3500  N   TYR A 478      70.849 -25.083  12.189  1.00 47.92           N  
ANISOU 3500  N   TYR A 478     4561   4087   9558    167  -1444     51       N  
ATOM   3501  CA  TYR A 478      69.861 -26.085  12.576  1.00 48.44           C  
ANISOU 3501  CA  TYR A 478     4634   4064   9703    164  -1420    172       C  
ATOM   3502  C   TYR A 478      69.053 -26.536  11.365  1.00 48.28           C  
ANISOU 3502  C   TYR A 478     4499   4053   9791    128  -1326     48       C  
ATOM   3503  O   TYR A 478      68.323 -25.745  10.766  1.00 47.51           O  
ANISOU 3503  O   TYR A 478     4425   4074   9550    103  -1230     -3       O  
ATOM   3504  CB  TYR A 478      68.929 -25.507  13.642  1.00 48.14           C  
ANISOU 3504  CB  TYR A 478     4766   4080   9444    167  -1369    354       C  
ATOM   3505  CG  TYR A 478      67.823 -26.439  14.101  1.00 48.89           C  
ANISOU 3505  CG  TYR A 478     4871   4085   9619    160  -1312    506       C  
ATOM   3506  CD1 TYR A 478      68.075 -27.456  15.018  1.00 50.44           C  
ANISOU 3506  CD1 TYR A 478     5085   4148   9932    193  -1389    667       C  
ATOM   3507  CD2 TYR A 478      66.518 -26.286  13.634  1.00 48.27           C  
ANISOU 3507  CD2 TYR A 478     4777   4047   9514    122  -1180    501       C  
ATOM   3508  CE1 TYR A 478      67.065 -28.304  15.447  1.00 51.41           C  
ANISOU 3508  CE1 TYR A 478     5206   4175  10150    184  -1318    827       C  
ATOM   3509  CE2 TYR A 478      65.501 -27.129  14.057  1.00 49.25           C  
ANISOU 3509  CE2 TYR A 478     4890   4074   9748    111  -1117    641       C  
ATOM   3510  CZ  TYR A 478      65.778 -28.135  14.964  1.00 50.80           C  
ANISOU 3510  CZ  TYR A 478     5101   4133  10066    140  -1176    810       C  
ATOM   3511  OH  TYR A 478      64.770 -28.972  15.388  1.00 51.65           O  
ANISOU 3511  OH  TYR A 478     5188   4129  10306    127  -1095    970       O  
ATOM   3512  N   ASN A 479      69.195 -27.810  11.006  1.00 49.50           N  
ANISOU 3512  N   ASN A 479     4524   4076  10208    133  -1368     -5       N  
ATOM   3513  CA  ASN A 479      68.402 -28.408   9.938  1.00 49.54           C  
ANISOU 3513  CA  ASN A 479     4410   4067  10345    108  -1306   -137       C  
ATOM   3514  C   ASN A 479      66.991 -28.690  10.447  1.00 49.91           C  
ANISOU 3514  C   ASN A 479     4501   4069  10393     86  -1241     11       C  
ATOM   3515  O   ASN A 479      66.782 -29.613  11.231  1.00 51.24           O  
ANISOU 3515  O   ASN A 479     4660   4088  10720     93  -1271    158       O  
ATOM   3516  CB  ASN A 479      69.065 -29.699   9.446  1.00 50.75           C  
ANISOU 3516  CB  ASN A 479     4398   4075  10809    124  -1380   -261       C  
ATOM   3517  CG  ASN A 479      68.367 -30.299   8.240  1.00 51.02           C  
ANISOU 3517  CG  ASN A 479     4298   4105  10981    108  -1336   -451       C  
ATOM   3518  OD1 ASN A 479      67.158 -30.143   8.062  1.00 50.77           O  
ANISOU 3518  OD1 ASN A 479     4287   4112  10889     83  -1271   -428       O  
ATOM   3519  ND2 ASN A 479      69.128 -30.999   7.405  1.00 51.87           N  
ANISOU 3519  ND2 ASN A 479     4261   4163  11283    127  -1377   -655       N  
ATOM   3520  N   ALA A 480      66.031 -27.890   9.993  1.00 49.13           N  
ANISOU 3520  N   ALA A 480     4441   4093  10132     61  -1148    -18       N  
ATOM   3521  CA  ALA A 480      64.651 -27.987  10.467  1.00 49.53           C  
ANISOU 3521  CA  ALA A 480     4527   4112  10179     39  -1069    117       C  
ATOM   3522  C   ALA A 480      63.949 -29.269  10.013  1.00 50.99           C  
ANISOU 3522  C   ALA A 480     4558   4149  10665     22  -1073     65       C  
ATOM   3523  O   ALA A 480      63.041 -29.755  10.693  1.00 52.02           O  
ANISOU 3523  O   ALA A 480     4691   4177  10896      7  -1022    225       O  
ATOM   3524  CB  ALA A 480      63.858 -26.768  10.020  1.00 48.27           C  
ANISOU 3524  CB  ALA A 480     4429   4114   9794     21   -983     79       C  
ATOM   3525  N   ALA A 481      64.368 -29.810   8.870  1.00 51.35           N  
ANISOU 3525  N   ALA A 481     4464   4181  10864     27  -1127   -162       N  
ATOM   3526  CA  ALA A 481      63.768 -31.028   8.325  1.00 52.72           C  
ANISOU 3526  CA  ALA A 481     4471   4209  11350     16  -1151   -262       C  
ATOM   3527  C   ALA A 481      64.132 -32.254   9.160  1.00 54.37           C  
ANISOU 3527  C   ALA A 481     4621   4194  11840     24  -1204   -127       C  
ATOM   3528  O   ALA A 481      63.254 -33.018   9.564  1.00 55.96           O  
ANISOU 3528  O   ALA A 481     4763   4246  12253      4  -1175    -15       O  
ATOM   3529  CB  ALA A 481      64.198 -31.229   6.879  1.00 52.79           C  
ANISOU 3529  CB  ALA A 481     4358   4283  11415     32  -1197   -566       C  
ATOM   3530  N   THR A 482      65.428 -32.430   9.415  1.00 54.39           N  
ANISOU 3530  N   THR A 482     4634   4168  11863     55  -1282   -130       N  
ATOM   3531  CA  THR A 482      65.934 -33.581  10.166  1.00 55.86           C  
ANISOU 3531  CA  THR A 482     4762   4140  12322     73  -1356     -2       C  
ATOM   3532  C   THR A 482      66.010 -33.325  11.674  1.00 56.53           C  
ANISOU 3532  C   THR A 482     5013   4202  12262     88  -1349    313       C  
ATOM   3533  O   THR A 482      66.180 -34.263  12.451  1.00 58.09           O  
ANISOU 3533  O   THR A 482     5186   4221  12663    105  -1396    486       O  
ATOM   3534  CB  THR A 482      67.334 -33.995   9.672  1.00 55.96           C  
ANISOU 3534  CB  THR A 482     4680   4113  12468    107  -1460   -175       C  
ATOM   3535  OG1 THR A 482      68.283 -32.967   9.982  1.00 54.84           O  
ANISOU 3535  OG1 THR A 482     4664   4114  12059    128  -1480   -149       O  
ATOM   3536  CG2 THR A 482      67.327 -34.240   8.169  1.00 55.95           C  
ANISOU 3536  CG2 THR A 482     4526   4157  12573    105  -1457   -504       C  
ATOM   3537  N   GLU A 483      65.882 -32.060  12.077  1.00 55.96           N  
ANISOU 3537  N   GLU A 483     5110   4310  11839     88  -1294    387       N  
ATOM   3538  CA  GLU A 483      66.028 -31.642  13.479  1.00 56.79           C  
ANISOU 3538  CA  GLU A 483     5396   4438  11742    115  -1294    649       C  
ATOM   3539  C   GLU A 483      67.394 -32.026  14.057  1.00 57.48           C  
ANISOU 3539  C   GLU A 483     5498   4451  11887    164  -1439    702       C  
ATOM   3540  O   GLU A 483      67.494 -32.503  15.188  1.00 58.83           O  
ANISOU 3540  O   GLU A 483     5747   4529  12074    195  -1478    940       O  
ATOM   3541  CB  GLU A 483      64.882 -32.186  14.342  1.00 58.66           C  
ANISOU 3541  CB  GLU A 483     5668   4572  12047    102  -1200    897       C  
ATOM   3542  CG  GLU A 483      63.503 -31.770  13.847  1.00 58.68           C  
ANISOU 3542  CG  GLU A 483     5646   4637  12011     56  -1061    851       C  
ATOM   3543  CD  GLU A 483      62.411 -31.965  14.884  1.00 60.40           C  
ANISOU 3543  CD  GLU A 483     5936   4794  12217     47   -934   1122       C  
ATOM   3544  OE1 GLU A 483      62.504 -32.922  15.685  1.00 62.89           O  
ANISOU 3544  OE1 GLU A 483     6245   4949  12699     64   -946   1329       O  
ATOM   3545  OE2 GLU A 483      61.456 -31.157  14.895  1.00 59.47           O  
ANISOU 3545  OE2 GLU A 483     5877   4785  11932     24   -815   1135       O  
ATOM   3546  N   GLU A 484      68.438 -31.808  13.257  1.00 56.56           N  
ANISOU 3546  N   GLU A 484     5305   4379  11805    173  -1514    482       N  
ATOM   3547  CA  GLU A 484      69.820 -32.049  13.661  1.00 57.07           C  
ANISOU 3547  CA  GLU A 484     5359   4381  11943    219  -1660    489       C  
ATOM   3548  C   GLU A 484      70.652 -30.830  13.289  1.00 54.87           C  
ANISOU 3548  C   GLU A 484     5127   4269  11449    225  -1679    340       C  
ATOM   3549  O   GLU A 484      70.354 -30.147  12.311  1.00 53.29           O  
ANISOU 3549  O   GLU A 484     4899   4196  11151    193  -1588    170       O  
ATOM   3550  CB  GLU A 484      70.389 -33.282  12.949  1.00 58.76           C  
ANISOU 3550  CB  GLU A 484     5366   4421  12539    226  -1731    345       C  
ATOM   3551  CG  GLU A 484      69.612 -34.578  13.155  1.00 60.85           C  
ANISOU 3551  CG  GLU A 484     5538   4484  13097    216  -1717    461       C  
ATOM   3552  CD  GLU A 484      69.907 -35.256  14.483  1.00 63.08           C  
ANISOU 3552  CD  GLU A 484     5887   4617  13462    258  -1806    755       C  
ATOM   3553  OE1 GLU A 484      70.179 -36.477  14.477  1.00 64.95           O  
ANISOU 3553  OE1 GLU A 484     5984   4640  14054    273  -1878    780       O  
ATOM   3554  OE2 GLU A 484      69.868 -34.576  15.532  1.00 63.42           O  
ANISOU 3554  OE2 GLU A 484     6123   4755  13217    282  -1808    960       O  
ATOM   3555  N   TYR A 485      71.693 -30.558  14.069  1.00 54.55           N  
ANISOU 3555  N   TYR A 485     5155   4223  11347    269  -1801    409       N  
ATOM   3556  CA  TYR A 485      72.605 -29.457  13.766  1.00 52.90           C  
ANISOU 3556  CA  TYR A 485     4964   4139  10995    274  -1831    269       C  
ATOM   3557  C   TYR A 485      73.695 -29.933  12.808  1.00 52.90           C  
ANISOU 3557  C   TYR A 485     4775   4072  11252    280  -1882     55       C  
ATOM   3558  O   TYR A 485      73.907 -31.135  12.647  1.00 54.08           O  
ANISOU 3558  O   TYR A 485     4798   4063  11685    293  -1935     35       O  
ATOM   3559  CB  TYR A 485      73.229 -28.901  15.048  1.00 53.25           C  
ANISOU 3559  CB  TYR A 485     5156   4206  10868    322  -1955    417       C  
ATOM   3560  CG  TYR A 485      72.230 -28.273  15.996  1.00 52.69           C  
ANISOU 3560  CG  TYR A 485     5284   4232  10503    325  -1891    603       C  
ATOM   3561  CD1 TYR A 485      71.552 -29.044  16.934  1.00 53.99           C  
ANISOU 3561  CD1 TYR A 485     5531   4317  10665    348  -1889    836       C  
ATOM   3562  CD2 TYR A 485      71.969 -26.907  15.961  1.00 51.21           C  
ANISOU 3562  CD2 TYR A 485     5196   4208  10051    309  -1821    549       C  
ATOM   3563  CE1 TYR A 485      70.640 -28.474  17.806  1.00 53.89           C  
ANISOU 3563  CE1 TYR A 485     5698   4399  10376    356  -1807   1001       C  
ATOM   3564  CE2 TYR A 485      71.059 -26.327  16.831  1.00 51.09           C  
ANISOU 3564  CE2 TYR A 485     5355   4280   9776    317  -1754    698       C  
ATOM   3565  CZ  TYR A 485      70.397 -27.117  17.751  1.00 52.40           C  
ANISOU 3565  CZ  TYR A 485     5604   4378   9927    341  -1742    920       C  
ATOM   3566  OH  TYR A 485      69.490 -26.553  18.617  1.00 52.45           O  
ANISOU 3566  OH  TYR A 485     5781   4476   9669    354  -1653   1065       O  
ATOM   3567  N   GLY A 486      74.377 -28.983  12.174  1.00 51.67           N  
ANISOU 3567  N   GLY A 486     4592   4030  11008    271  -1854   -103       N  
ATOM   3568  CA  GLY A 486      75.472 -29.292  11.254  1.00 51.84           C  
ANISOU 3568  CA  GLY A 486     4437   4009  11251    279  -1873   -312       C  
ATOM   3569  C   GLY A 486      75.702 -28.202  10.224  1.00 50.46           C  
ANISOU 3569  C   GLY A 486     4236   3996  10939    251  -1751   -481       C  
ATOM   3570  O   GLY A 486      75.077 -27.141  10.278  1.00 49.59           O  
ANISOU 3570  O   GLY A 486     4247   4024  10572    227  -1673   -431       O  
ATOM   3571  N   ASN A 487      76.604 -28.468   9.283  1.00 50.61           N  
ANISOU 3571  N   ASN A 487     4094   3995  11140    258  -1727   -676       N  
ATOM   3572  CA  ASN A 487      76.882 -27.539   8.191  1.00 49.53           C  
ANISOU 3572  CA  ASN A 487     3916   4009  10891    236  -1589   -830       C  
ATOM   3573  C   ASN A 487      75.717 -27.527   7.207  1.00 48.74           C  
ANISOU 3573  C   ASN A 487     3833   4027  10659    210  -1449   -901       C  
ATOM   3574  O   ASN A 487      75.411 -28.543   6.586  1.00 49.36           O  
ANISOU 3574  O   ASN A 487     3814   4052  10889    217  -1434  -1012       O  
ATOM   3575  CB  ASN A 487      78.181 -27.924   7.480  1.00 50.59           C  
ANISOU 3575  CB  ASN A 487     3866   4086  11267    258  -1586  -1014       C  
ATOM   3576  CG  ASN A 487      78.635 -26.876   6.478  1.00 49.99           C  
ANISOU 3576  CG  ASN A 487     3754   4162  11077    241  -1433  -1137       C  
ATOM   3577  OD1 ASN A 487      77.977 -26.645   5.465  1.00 49.13           O  
ANISOU 3577  OD1 ASN A 487     3655   4188  10824    224  -1290  -1220       O  
ATOM   3578  ND2 ASN A 487      79.775 -26.245   6.750  1.00 50.61           N  
ANISOU 3578  ND2 ASN A 487     3784   4215  11230    247  -1467  -1143       N  
ATOM   3579  N   MET A 488      75.081 -26.368   7.064  1.00 47.60           N  
ANISOU 3579  N   MET A 488     3804   4035  10247    183  -1358   -848       N  
ATOM   3580  CA  MET A 488      73.853 -26.245   6.274  1.00 46.82           C  
ANISOU 3580  CA  MET A 488     3740   4050   9999    162  -1251   -885       C  
ATOM   3581  C   MET A 488      74.097 -26.407   4.773  1.00 47.26           C  
ANISOU 3581  C   MET A 488     3680   4198  10076    171  -1146  -1104       C  
ATOM   3582  O   MET A 488      73.242 -26.924   4.058  1.00 47.06           O  
ANISOU 3582  O   MET A 488     3628   4210  10039    172  -1109  -1193       O  
ATOM   3583  CB  MET A 488      73.181 -24.895   6.541  1.00 45.46           C  
ANISOU 3583  CB  MET A 488     3714   4007   9550    137  -1190   -765       C  
ATOM   3584  CG  MET A 488      72.754 -24.671   7.986  1.00 45.13           C  
ANISOU 3584  CG  MET A 488     3806   3907   9435    135  -1271   -563       C  
ATOM   3585  SD  MET A 488      71.417 -25.737   8.559  1.00 45.55           S  
ANISOU 3585  SD  MET A 488     3898   3867   9542    130  -1297   -450       S  
ATOM   3586  CE  MET A 488      70.037 -25.120   7.601  1.00 44.49           C  
ANISOU 3586  CE  MET A 488     3794   3883   9226    100  -1164   -496       C  
ATOM   3587  N   ILE A 489      75.263 -25.970   4.303  1.00 47.97           N  
ANISOU 3587  N   ILE A 489     3699   4326  10202    182  -1097  -1194       N  
ATOM   3588  CA  ILE A 489      75.615 -26.077   2.884  1.00 48.75           C  
ANISOU 3588  CA  ILE A 489     3695   4529  10297    199   -974  -1397       C  
ATOM   3589  C   ILE A 489      75.867 -27.540   2.516  1.00 49.88           C  
ANISOU 3589  C   ILE A 489     3695   4557  10700    230  -1022  -1567       C  
ATOM   3590  O   ILE A 489      75.424 -28.000   1.463  1.00 50.64           O  
ANISOU 3590  O   ILE A 489     3740   4730  10767    248   -958  -1736       O  
ATOM   3591  CB  ILE A 489      76.862 -25.229   2.524  1.00 49.32           C  
ANISOU 3591  CB  ILE A 489     3712   4656  10368    202   -886  -1434       C  
ATOM   3592  CG1 ILE A 489      76.647 -23.745   2.869  1.00 48.14           C  
ANISOU 3592  CG1 ILE A 489     3688   4602  10000    171   -840  -1275       C  
ATOM   3593  CG2 ILE A 489      77.211 -25.377   1.047  1.00 50.43           C  
ANISOU 3593  CG2 ILE A 489     3756   4922  10483    228   -734  -1636       C  
ATOM   3594  CD1 ILE A 489      75.522 -23.069   2.111  1.00 47.45           C  
ANISOU 3594  CD1 ILE A 489     3696   4689   9641    160   -735  -1251       C  
ATOM   3595  N   ASP A 490      76.573 -28.262   3.386  1.00 50.06           N  
ANISOU 3595  N   ASP A 490     3652   4391  10976    241  -1146  -1529       N  
ATOM   3596  CA  ASP A 490      76.833 -29.690   3.182  1.00 51.18           C  
ANISOU 3596  CA  ASP A 490     3647   4383  11415    271  -1210  -1672       C  
ATOM   3597  C   ASP A 490      75.544 -30.511   3.239  1.00 50.86           C  
ANISOU 3597  C   ASP A 490     3628   4289  11406    264  -1258  -1658       C  
ATOM   3598  O   ASP A 490      75.375 -31.460   2.474  1.00 51.78           O  
ANISOU 3598  O   ASP A 490     3628   4367  11677    286  -1251  -1852       O  
ATOM   3599  CB  ASP A 490      77.824 -30.217   4.227  1.00 51.97           C  
ANISOU 3599  CB  ASP A 490     3681   4280  11782    288  -1353  -1590       C  
ATOM   3600  CG  ASP A 490      79.208 -29.600   4.094  1.00 52.34           C  
ANISOU 3600  CG  ASP A 490     3654   4344  11888    300  -1319  -1647       C  
ATOM   3601  OD1 ASP A 490      79.406 -28.736   3.212  1.00 52.09           O  
ANISOU 3601  OD1 ASP A 490     3624   4479  11686    291  -1165  -1730       O  
ATOM   3602  OD2 ASP A 490      80.102 -29.984   4.877  1.00 53.17           O  
ANISOU 3602  OD2 ASP A 490     3691   4287  12221    319  -1448  -1599       O  
ATOM   3603  N   MET A 491      74.640 -30.135   4.142  1.00 49.55           N  
ANISOU 3603  N   MET A 491     3603   4116  11107    234  -1302  -1440       N  
ATOM   3604  CA  MET A 491      73.353 -30.826   4.291  1.00 49.46           C  
ANISOU 3604  CA  MET A 491     3609   4043  11140    221  -1334  -1397       C  
ATOM   3605  C   MET A 491      72.363 -30.519   3.163  1.00 49.23           C  
ANISOU 3605  C   MET A 491     3596   4180  10929    214  -1240  -1531       C  
ATOM   3606  O   MET A 491      71.305 -31.142   3.083  1.00 49.49           O  
ANISOU 3606  O   MET A 491     3609   4160  11033    205  -1266  -1546       O  
ATOM   3607  CB  MET A 491      72.716 -30.493   5.646  1.00 48.31           C  
ANISOU 3607  CB  MET A 491     3608   3842  10903    196  -1389  -1114       C  
ATOM   3608  CG  MET A 491      73.391 -31.181   6.821  1.00 49.01           C  
ANISOU 3608  CG  MET A 491     3680   3736  11205    214  -1518   -969       C  
ATOM   3609  SD  MET A 491      72.526 -30.931   8.382  1.00 48.21           S  
ANISOU 3609  SD  MET A 491     3759   3586  10970    199  -1565   -640       S  
ATOM   3610  CE  MET A 491      72.773 -29.180   8.642  1.00 46.56           C  
ANISOU 3610  CE  MET A 491     3710   3576  10402    187  -1513   -573       C  
ATOM   3611  N   GLY A 492      72.700 -29.560   2.303  1.00 49.04           N  
ANISOU 3611  N   GLY A 492     3602   4350  10679    220  -1134  -1620       N  
ATOM   3612  CA  GLY A 492      71.896 -29.261   1.121  1.00 49.09           C  
ANISOU 3612  CA  GLY A 492     3623   4533  10494    229  -1055  -1759       C  
ATOM   3613  C   GLY A 492      70.701 -28.378   1.426  1.00 47.67           C  
ANISOU 3613  C   GLY A 492     3585   4446  10080    197  -1036  -1591       C  
ATOM   3614  O   GLY A 492      69.649 -28.521   0.809  1.00 47.79           O  
ANISOU 3614  O   GLY A 492     3601   4526  10029    200  -1033  -1667       O  
ATOM   3615  N   ILE A 493      70.870 -27.465   2.378  1.00 46.48           N  
ANISOU 3615  N   ILE A 493     3547   4296   9817    171  -1031  -1378       N  
ATOM   3616  CA  ILE A 493      69.840 -26.488   2.727  1.00 45.17           C  
ANISOU 3616  CA  ILE A 493     3515   4218   9429    143  -1000  -1218       C  
ATOM   3617  C   ILE A 493      70.435 -25.097   2.560  1.00 44.16           C  
ANISOU 3617  C   ILE A 493     3463   4230   9086    139   -918  -1159       C  
ATOM   3618  O   ILE A 493      71.185 -24.627   3.416  1.00 43.84           O  
ANISOU 3618  O   ILE A 493     3461   4135   9061    129   -940  -1046       O  
ATOM   3619  CB  ILE A 493      69.332 -26.695   4.165  1.00 44.75           C  
ANISOU 3619  CB  ILE A 493     3530   4022   9448    119  -1069  -1007       C  
ATOM   3620  CG1 ILE A 493      68.651 -28.060   4.267  1.00 45.88           C  
ANISOU 3620  CG1 ILE A 493     3585   4015   9831    119  -1132  -1046       C  
ATOM   3621  CG2 ILE A 493      68.360 -25.588   4.564  1.00 43.56           C  
ANISOU 3621  CG2 ILE A 493     3515   3965   9069     94  -1021   -852       C  
ATOM   3622  CD1 ILE A 493      68.192 -28.432   5.656  1.00 45.97           C  
ANISOU 3622  CD1 ILE A 493     3655   3877   9935    101  -1181   -825       C  
ATOM   3623  N   LEU A 494      70.106 -24.454   1.444  1.00 43.83           N  
ANISOU 3623  N   LEU A 494     3437   4362   8852    150   -832  -1237       N  
ATOM   3624  CA  LEU A 494      70.691 -23.168   1.097  1.00 43.19           C  
ANISOU 3624  CA  LEU A 494     3407   4409   8591    147   -735  -1186       C  
ATOM   3625  C   LEU A 494      69.723 -22.285   0.321  1.00 42.60           C  
ANISOU 3625  C   LEU A 494     3408   4505   8272    151   -668  -1159       C  
ATOM   3626  O   LEU A 494      68.874 -22.776  -0.422  1.00 43.25           O  
ANISOU 3626  O   LEU A 494     3471   4649   8313    171   -685  -1263       O  
ATOM   3627  CB  LEU A 494      71.994 -23.372   0.305  1.00 44.38           C  
ANISOU 3627  CB  LEU A 494     3456   4595   8810    175   -667  -1334       C  
ATOM   3628  CG  LEU A 494      72.049 -24.458  -0.781  1.00 45.72           C  
ANISOU 3628  CG  LEU A 494     3519   4800   9051    216   -655  -1569       C  
ATOM   3629  CD1 LEU A 494      71.328 -24.034  -2.053  1.00 46.11           C  
ANISOU 3629  CD1 LEU A 494     3609   5058   8853    245   -577  -1650       C  
ATOM   3630  CD2 LEU A 494      73.498 -24.806  -1.092  1.00 46.89           C  
ANISOU 3630  CD2 LEU A 494     3552   4914   9349    238   -602  -1690       C  
ATOM   3631  N   ASP A 495      69.864 -20.977   0.514  1.00 41.68           N  
ANISOU 3631  N   ASP A 495     3369   4453   8013    133   -606  -1022       N  
ATOM   3632  CA  ASP A 495      69.121 -19.980  -0.243  1.00 41.37           C  
ANISOU 3632  CA  ASP A 495     3397   4571   7748    140   -537   -972       C  
ATOM   3633  C   ASP A 495      70.102 -19.231  -1.134  1.00 41.87           C  
ANISOU 3633  C   ASP A 495     3440   4753   7714    158   -412   -990       C  
ATOM   3634  O   ASP A 495      71.280 -19.114  -0.791  1.00 42.26           O  
ANISOU 3634  O   ASP A 495     3441   4735   7878    147   -381   -984       O  
ATOM   3635  CB  ASP A 495      68.441 -18.989   0.701  1.00 40.19           C  
ANISOU 3635  CB  ASP A 495     3348   4389   7533    108   -553   -785       C  
ATOM   3636  CG  ASP A 495      67.455 -19.656   1.641  1.00 39.91           C  
ANISOU 3636  CG  ASP A 495     3337   4240   7586     91   -646   -741       C  
ATOM   3637  OD1 ASP A 495      66.771 -20.613   1.215  1.00 40.93           O  
ANISOU 3637  OD1 ASP A 495     3419   4362   7771    104   -690   -841       O  
ATOM   3638  OD2 ASP A 495      67.356 -19.217   2.807  1.00 39.06           O  
ANISOU 3638  OD2 ASP A 495     3293   4050   7495     67   -670   -609       O  
ATOM   3639  N   PRO A 496      69.634 -18.738  -2.291  1.00 42.22           N  
ANISOU 3639  N   PRO A 496     3515   4971   7554    188   -339  -1008       N  
ATOM   3640  CA  PRO A 496      70.491 -17.828  -3.047  1.00 43.07           C  
ANISOU 3640  CA  PRO A 496     3618   5190   7553    201   -195   -967       C  
ATOM   3641  C   PRO A 496      70.711 -16.542  -2.258  1.00 42.04           C  
ANISOU 3641  C   PRO A 496     3535   5000   7437    159   -165   -771       C  
ATOM   3642  O   PRO A 496      69.769 -16.037  -1.644  1.00 41.27           O  
ANISOU 3642  O   PRO A 496     3511   4870   7297    138   -226   -662       O  
ATOM   3643  CB  PRO A 496      69.680 -17.542  -4.316  1.00 43.97           C  
ANISOU 3643  CB  PRO A 496     3783   5505   7418    249   -151   -990       C  
ATOM   3644  CG  PRO A 496      68.703 -18.659  -4.420  1.00 44.01           C  
ANISOU 3644  CG  PRO A 496     3774   5498   7446    269   -278  -1133       C  
ATOM   3645  CD  PRO A 496      68.397 -19.068  -3.015  1.00 42.55           C  
ANISOU 3645  CD  PRO A 496     3585   5114   7469    219   -387  -1077       C  
ATOM   3646  N   THR A 497      71.933 -16.015  -2.277  1.00 42.20           N  
ANISOU 3646  N   THR A 497     3503   4996   7535    147    -69   -739       N  
ATOM   3647  CA  THR A 497      72.253 -14.799  -1.532  1.00 41.38           C  
ANISOU 3647  CA  THR A 497     3423   4815   7483    108    -49   -580       C  
ATOM   3648  C   THR A 497      71.316 -13.655  -1.914  1.00 40.97           C  
ANISOU 3648  C   THR A 497     3457   4859   7248    109     -5   -436       C  
ATOM   3649  O   THR A 497      70.995 -12.805  -1.084  1.00 39.92           O  
ANISOU 3649  O   THR A 497     3369   4648   7148     79    -44   -318       O  
ATOM   3650  CB  THR A 497      73.707 -14.351  -1.773  1.00 42.57           C  
ANISOU 3650  CB  THR A 497     3478   4939   7755     99     68   -575       C  
ATOM   3651  OG1 THR A 497      74.581 -15.484  -1.709  1.00 43.17           O  
ANISOU 3651  OG1 THR A 497     3458   4950   7995    111     43   -729       O  
ATOM   3652  CG2 THR A 497      74.142 -13.319  -0.733  1.00 41.91           C  
ANISOU 3652  CG2 THR A 497     3394   4723   7806     56     37   -455       C  
ATOM   3653  N   LYS A 498      70.880 -13.645  -3.172  1.00 41.88           N  
ANISOU 3653  N   LYS A 498     3594   5145   7171    151     69   -452       N  
ATOM   3654  CA  LYS A 498      69.977 -12.611  -3.677  1.00 41.83           C  
ANISOU 3654  CA  LYS A 498     3666   5240   6986    164    103   -311       C  
ATOM   3655  C   LYS A 498      68.618 -12.579  -2.971  1.00 40.38           C  
ANISOU 3655  C   LYS A 498     3551   5007   6782    152    -29   -272       C  
ATOM   3656  O   LYS A 498      68.055 -11.502  -2.778  1.00 39.99           O  
ANISOU 3656  O   LYS A 498     3550   4951   6691    141    -21   -127       O  
ATOM   3657  CB  LYS A 498      69.770 -12.780  -5.185  1.00 43.42           C  
ANISOU 3657  CB  LYS A 498     3885   5650   6961    227    185   -354       C  
ATOM   3658  CG  LYS A 498      69.117 -11.584  -5.856  1.00 43.92           C  
ANISOU 3658  CG  LYS A 498     4020   5828   6839    249    243   -177       C  
ATOM   3659  CD  LYS A 498      69.059 -11.754  -7.363  1.00 45.96           C  
ANISOU 3659  CD  LYS A 498     4307   6311   6843    323    327   -215       C  
ATOM   3660  CE  LYS A 498      68.365 -10.573  -8.020  1.00 46.80           C  
ANISOU 3660  CE  LYS A 498     4491   6530   6761    353    367    -14       C  
ATOM   3661  NZ  LYS A 498      68.196 -10.765  -9.486  1.00 49.06           N  
ANISOU 3661  NZ  LYS A 498     4827   7058   6754    440    426    -48       N  
ATOM   3662  N   VAL A 499      68.095 -13.739  -2.579  1.00 39.82           N  
ANISOU 3662  N   VAL A 499     3473   4889   6764    154   -142   -396       N  
ATOM   3663  CA  VAL A 499      66.774 -13.796  -1.973  1.00 38.92           C  
ANISOU 3663  CA  VAL A 499     3410   4730   6646    145   -247   -362       C  
ATOM   3664  C   VAL A 499      66.839 -13.290  -0.529  1.00 37.55           C  
ANISOU 3664  C   VAL A 499     3262   4401   6603     98   -283   -266       C  
ATOM   3665  O   VAL A 499      65.911 -12.624  -0.047  1.00 37.16           O  
ANISOU 3665  O   VAL A 499     3264   4325   6526     87   -309   -171       O  
ATOM   3666  CB  VAL A 499      66.262 -15.251  -1.701  1.00 38.82           C  
ANISOU 3666  CB  VAL A 499     3366   4662   6720    149   -355   -507       C  
ATOM   3667  CG1 VAL A 499      64.866 -15.227  -1.124  1.00 38.22           C  
ANISOU 3667  CG1 VAL A 499     3330   4538   6653    138   -436   -455       C  
ATOM   3668  CG2 VAL A 499      66.376 -16.373  -2.759  1.00 40.09           C  
ANISOU 3668  CG2 VAL A 499     3471   4914   6846    193   -368   -694       C  
ATOM   3669  N   THR A 500      67.866 -13.734   0.193  1.00 37.06           N  
ANISOU 3669  N   THR A 500     3160   4233   6685     77   -298   -311       N  
ATOM   3670  CA  THR A 500      68.046 -13.367   1.593  1.00 35.99           C  
ANISOU 3670  CA  THR A 500     3055   3961   6656     45   -351   -244       C  
ATOM   3671  C   THR A 500      68.337 -11.872   1.685  1.00 35.84           C  
ANISOU 3671  C   THR A 500     3054   3938   6622     30   -286   -128       C  
ATOM   3672  O   THR A 500      67.802 -11.183   2.551  1.00 34.85           O  
ANISOU 3672  O   THR A 500     2983   3752   6505     15   -319    -54       O  
ATOM   3673  CB  THR A 500      69.193 -14.168   2.245  1.00 36.04           C  
ANISOU 3673  CB  THR A 500     3009   3863   6821     37   -399   -321       C  
ATOM   3674  OG1 THR A 500      68.985 -15.572   2.040  1.00 36.07           O  
ANISOU 3674  OG1 THR A 500     2977   3858   6867     53   -452   -431       O  
ATOM   3675  CG2 THR A 500      69.272 -13.889   3.741  1.00 35.41           C  
ANISOU 3675  CG2 THR A 500     2979   3657   6816     17   -480   -260       C  
ATOM   3676  N   ARG A 501      69.180 -11.385   0.777  1.00 36.85           N  
ANISOU 3676  N   ARG A 501     3132   4128   6741     36   -184   -114       N  
ATOM   3677  CA  ARG A 501      69.519  -9.965   0.708  1.00 37.31           C  
ANISOU 3677  CA  ARG A 501     3184   4172   6818     21   -107      5       C  
ATOM   3678  C   ARG A 501      68.291  -9.117   0.391  1.00 37.23           C  
ANISOU 3678  C   ARG A 501     3238   4223   6685     32    -93    115       C  
ATOM   3679  O   ARG A 501      68.008  -8.145   1.093  1.00 37.05           O  
ANISOU 3679  O   ARG A 501     3240   4122   6714     14   -108    196       O  
ATOM   3680  CB  ARG A 501      70.597  -9.728  -0.352  1.00 38.59           C  
ANISOU 3680  CB  ARG A 501     3271   4399   6991     30     26     13       C  
ATOM   3681  CG  ARG A 501      71.047  -8.280  -0.478  1.00 39.15           C  
ANISOU 3681  CG  ARG A 501     3313   4435   7125     11    122    151       C  
ATOM   3682  CD  ARG A 501      72.073  -8.107  -1.588  1.00 40.70           C  
ANISOU 3682  CD  ARG A 501     3431   4702   7329     21    284    177       C  
ATOM   3683  NE  ARG A 501      71.534  -8.426  -2.910  1.00 41.42           N  
ANISOU 3683  NE  ARG A 501     3562   4983   7191     68    362    189       N  
ATOM   3684  CZ  ARG A 501      70.717  -7.642  -3.611  1.00 41.89           C  
ANISOU 3684  CZ  ARG A 501     3682   5142   7091     92    409    325       C  
ATOM   3685  NH1 ARG A 501      70.308  -6.472  -3.131  1.00 41.67           N  
ANISOU 3685  NH1 ARG A 501     3672   5030   7128     69    396    465       N  
ATOM   3686  NH2 ARG A 501      70.295  -8.034  -4.807  1.00 42.93           N  
ANISOU 3686  NH2 ARG A 501     3854   5459   6998    146    458    314       N  
ATOM   3687  N   SER A 502      67.572  -9.487  -0.668  1.00 37.59           N  
ANISOU 3687  N   SER A 502     3303   4405   6575     66    -74    105       N  
ATOM   3688  CA  SER A 502      66.377  -8.756  -1.088  1.00 37.60           C  
ANISOU 3688  CA  SER A 502     3355   4470   6460     86    -77    207       C  
ATOM   3689  C   SER A 502      65.309  -8.748   0.000  1.00 36.61           C  
ANISOU 3689  C   SER A 502     3273   4254   6382     70   -173    211       C  
ATOM   3690  O   SER A 502      64.721  -7.706   0.289  1.00 36.64           O  
ANISOU 3690  O   SER A 502     3301   4220   6397     65   -167    313       O  
ATOM   3691  CB  SER A 502      65.801  -9.357  -2.369  1.00 38.46           C  
ANISOU 3691  CB  SER A 502     3477   4745   6391    135    -76    161       C  
ATOM   3692  OG  SER A 502      66.704  -9.208  -3.446  1.00 39.89           O  
ANISOU 3692  OG  SER A 502     3632   5035   6490    160     38    178       O  
ATOM   3693  N   ALA A 503      65.069  -9.910   0.603  1.00 36.14           N  
ANISOU 3693  N   ALA A 503     3216   4151   6361     64   -251    103       N  
ATOM   3694  CA  ALA A 503      64.085 -10.036   1.676  1.00 35.41           C  
ANISOU 3694  CA  ALA A 503     3163   3974   6313     50   -319    110       C  
ATOM   3695  C   ALA A 503      64.391  -9.098   2.841  1.00 35.20           C  
ANISOU 3695  C   ALA A 503     3165   3838   6371     25   -313    172       C  
ATOM   3696  O   ALA A 503      63.490  -8.448   3.367  1.00 35.07           O  
ANISOU 3696  O   ALA A 503     3183   3785   6354     24   -320    228       O  
ATOM   3697  CB  ALA A 503      64.018 -11.474   2.164  1.00 35.13           C  
ANISOU 3697  CB  ALA A 503     3118   3895   6333     46   -386      4       C  
ATOM   3698  N   LEU A 504      65.661  -9.025   3.235  1.00 35.67           N  
ANISOU 3698  N   LEU A 504     3200   3840   6511     10   -306    146       N  
ATOM   3699  CA  LEU A 504      66.082  -8.165   4.344  1.00 35.59           C  
ANISOU 3699  CA  LEU A 504     3209   3722   6588     -7   -324    173       C  
ATOM   3700  C   LEU A 504      65.965  -6.679   3.999  1.00 36.20           C  
ANISOU 3700  C   LEU A 504     3273   3794   6685    -10   -261    271       C  
ATOM   3701  O   LEU A 504      65.482  -5.887   4.808  1.00 35.98           O  
ANISOU 3701  O   LEU A 504     3278   3698   6692    -13   -279    298       O  
ATOM   3702  CB  LEU A 504      67.521  -8.491   4.762  1.00 35.73           C  
ANISOU 3702  CB  LEU A 504     3185   3676   6713    -18   -352    109       C  
ATOM   3703  CG  LEU A 504      68.141  -7.647   5.882  1.00 35.83           C  
ANISOU 3703  CG  LEU A 504     3206   3576   6829    -30   -398    106       C  
ATOM   3704  CD1 LEU A 504      67.298  -7.685   7.148  1.00 35.42           C  
ANISOU 3704  CD1 LEU A 504     3246   3481   6731    -20   -466     98       C  
ATOM   3705  CD2 LEU A 504      69.555  -8.120   6.172  1.00 36.23           C  
ANISOU 3705  CD2 LEU A 504     3198   3566   6999    -36   -445     32       C  
ATOM   3706  N   GLN A 505      66.412  -6.310   2.802  1.00 37.26           N  
ANISOU 3706  N   GLN A 505     3359   3998   6800     -5   -181    325       N  
ATOM   3707  CA  GLN A 505      66.400  -4.913   2.370  1.00 38.34           C  
ANISOU 3707  CA  GLN A 505     3471   4120   6977     -7   -110    445       C  
ATOM   3708  C   GLN A 505      64.985  -4.364   2.180  1.00 39.01           C  
ANISOU 3708  C   GLN A 505     3596   4235   6988     11   -118    523       C  
ATOM   3709  O   GLN A 505      64.696  -3.239   2.599  1.00 39.74           O  
ANISOU 3709  O   GLN A 505     3685   4248   7165      6   -109    588       O  
ATOM   3710  CB  GLN A 505      67.206  -4.745   1.080  1.00 39.13           C  
ANISOU 3710  CB  GLN A 505     3514   4300   7053      0     -4    507       C  
ATOM   3711  CG  GLN A 505      68.707  -4.885   1.286  1.00 39.20           C  
ANISOU 3711  CG  GLN A 505     3450   4242   7200    -24     27    453       C  
ATOM   3712  CD  GLN A 505      69.485  -4.880  -0.014  1.00 40.13           C  
ANISOU 3712  CD  GLN A 505     3510   4453   7284    -13    159    507       C  
ATOM   3713  OE1 GLN A 505      69.009  -5.366  -1.039  1.00 40.29           O  
ANISOU 3713  OE1 GLN A 505     3561   4620   7124     20    198    521       O  
ATOM   3714  NE2 GLN A 505      70.694  -4.330   0.022  1.00 40.94           N  
ANISOU 3714  NE2 GLN A 505     3524   4472   7560    -39    232    532       N  
ATOM   3715  N   TYR A 506      64.114  -5.151   1.551  1.00 39.32           N  
ANISOU 3715  N   TYR A 506     3663   4380   6896     37   -143    505       N  
ATOM   3716  CA  TYR A 506      62.721  -4.744   1.338  1.00 39.62           C  
ANISOU 3716  CA  TYR A 506     3726   4446   6882     59   -167    567       C  
ATOM   3717  C   TYR A 506      61.919  -4.720   2.639  1.00 39.29           C  
ANISOU 3717  C   TYR A 506     3714   4304   6907     47   -217    524       C  
ATOM   3718  O   TYR A 506      61.038  -3.877   2.806  1.00 39.61           O  
ANISOU 3718  O   TYR A 506     3758   4309   6982     57   -215    586       O  
ATOM   3719  CB  TYR A 506      62.026  -5.649   0.311  1.00 39.81           C  
ANISOU 3719  CB  TYR A 506     3757   4604   6763     93   -200    536       C  
ATOM   3720  CG  TYR A 506      62.346  -5.300  -1.126  1.00 40.99           C  
ANISOU 3720  CG  TYR A 506     3895   4882   6794    127   -144    619       C  
ATOM   3721  CD1 TYR A 506      61.969  -4.072  -1.663  1.00 41.90           C  
ANISOU 3721  CD1 TYR A 506     4010   5010   6898    147   -108    776       C  
ATOM   3722  CD2 TYR A 506      63.015  -6.197  -1.953  1.00 41.52           C  
ANISOU 3722  CD2 TYR A 506     3954   5060   6759    145   -121    545       C  
ATOM   3723  CE1 TYR A 506      62.258  -3.743  -2.977  1.00 43.28           C  
ANISOU 3723  CE1 TYR A 506     4188   5313   6941    185    -47    879       C  
ATOM   3724  CE2 TYR A 506      63.306  -5.878  -3.269  1.00 42.89           C  
ANISOU 3724  CE2 TYR A 506     4132   5372   6792    185    -54    623       C  
ATOM   3725  CZ  TYR A 506      62.926  -4.651  -3.776  1.00 43.74           C  
ANISOU 3725  CZ  TYR A 506     4250   5499   6869    206    -15    801       C  
ATOM   3726  OH  TYR A 506      63.213  -4.331  -5.081  1.00 45.39           O  
ANISOU 3726  OH  TYR A 506     4474   5855   6915    253     59    904       O  
ATOM   3727  N   ALA A 507      62.217  -5.643   3.550  1.00 39.09           N  
ANISOU 3727  N   ALA A 507     3713   4238   6902     31   -256    424       N  
ATOM   3728  CA  ALA A 507      61.568  -5.660   4.860  1.00 39.10           C  
ANISOU 3728  CA  ALA A 507     3756   4156   6943     26   -285    390       C  
ATOM   3729  C   ALA A 507      61.963  -4.426   5.662  1.00 39.95           C  
ANISOU 3729  C   ALA A 507     3871   4169   7140     18   -269    408       C  
ATOM   3730  O   ALA A 507      61.111  -3.766   6.260  1.00 40.43           O  
ANISOU 3730  O   ALA A 507     3949   4180   7230     26   -260    423       O  
ATOM   3731  CB  ALA A 507      61.934  -6.921   5.623  1.00 38.64           C  
ANISOU 3731  CB  ALA A 507     3726   4077   6877     16   -328    303       C  
ATOM   3732  N   ALA A 508      63.257  -4.118   5.663  1.00 40.76           N  
ANISOU 3732  N   ALA A 508     3945   4236   7303      3   -265    395       N  
ATOM   3733  CA  ALA A 508      63.780  -2.956   6.377  1.00 41.48           C  
ANISOU 3733  CA  ALA A 508     4023   4223   7513     -4   -266    390       C  
ATOM   3734  C   ALA A 508      63.305  -1.641   5.763  1.00 42.48           C  
ANISOU 3734  C   ALA A 508     4105   4324   7708      0   -212    494       C  
ATOM   3735  O   ALA A 508      63.155  -0.642   6.468  1.00 42.71           O  
ANISOU 3735  O   ALA A 508     4128   4257   7840      2   -216    481       O  
ATOM   3736  CB  ALA A 508      65.299  -2.999   6.407  1.00 41.89           C  
ANISOU 3736  CB  ALA A 508     4030   4234   7650    -22   -280    349       C  
ATOM   3737  N   SER A 509      63.079  -1.644   4.451  1.00 43.37           N  
ANISOU 3737  N   SER A 509     4189   4524   7765      8   -166    593       N  
ATOM   3738  CA  SER A 509      62.608  -0.455   3.744  1.00 44.81           C  
ANISOU 3738  CA  SER A 509     4331   4689   8003     21   -119    724       C  
ATOM   3739  C   SER A 509      61.252   0.004   4.276  1.00 45.02           C  
ANISOU 3739  C   SER A 509     4378   4675   8051     39   -142    726       C  
ATOM   3740  O   SER A 509      61.115   1.135   4.743  1.00 45.96           O  
ANISOU 3740  O   SER A 509     4469   4686   8306     40   -130    746       O  
ATOM   3741  CB  SER A 509      62.514  -0.729   2.240  1.00 45.46           C  
ANISOU 3741  CB  SER A 509     4402   4905   7966     41    -79    829       C  
ATOM   3742  OG  SER A 509      61.975   0.384   1.549  1.00 46.46           O  
ANISOU 3742  OG  SER A 509     4499   5022   8131     61    -44    979       O  
ATOM   3743  N   VAL A 510      60.260  -0.880   4.203  1.00 44.53           N  
ANISOU 3743  N   VAL A 510     4353   4688   7878     55   -172    696       N  
ATOM   3744  CA  VAL A 510      58.902  -0.561   4.653  1.00 44.43           C  
ANISOU 3744  CA  VAL A 510     4345   4639   7896     74   -183    696       C  
ATOM   3745  C   VAL A 510      58.822  -0.337   6.164  1.00 44.00           C  
ANISOU 3745  C   VAL A 510     4323   4485   7908     68   -182    593       C  
ATOM   3746  O   VAL A 510      58.051   0.505   6.625  1.00 44.59           O  
ANISOU 3746  O   VAL A 510     4382   4488   8070     83   -164    596       O  
ATOM   3747  CB  VAL A 510      57.883  -1.642   4.214  1.00 44.19           C  
ANISOU 3747  CB  VAL A 510     4326   4700   7762     90   -216    679       C  
ATOM   3748  CG1 VAL A 510      58.158  -2.985   4.882  1.00 43.42           C  
ANISOU 3748  CG1 VAL A 510     4272   4625   7600     73   -236    569       C  
ATOM   3749  CG2 VAL A 510      56.455  -1.188   4.487  1.00 44.44           C  
ANISOU 3749  CG2 VAL A 510     4335   4688   7860    112   -218    697       C  
ATOM   3750  N   ALA A 511      59.617  -1.083   6.927  1.00 43.38           N  
ANISOU 3750  N   ALA A 511     4292   4406   7784     52   -203    499       N  
ATOM   3751  CA  ALA A 511      59.668  -0.907   8.376  1.00 43.31           C  
ANISOU 3751  CA  ALA A 511     4333   4325   7797     56   -212    398       C  
ATOM   3752  C   ALA A 511      60.155   0.496   8.723  1.00 43.86           C  
ANISOU 3752  C   ALA A 511     4365   4289   8010     58   -209    383       C  
ATOM   3753  O   ALA A 511      59.627   1.137   9.631  1.00 44.39           O  
ANISOU 3753  O   ALA A 511     4449   4290   8125     77   -199    319       O  
ATOM   3754  CB  ALA A 511      60.569  -1.952   9.010  1.00 42.87           C  
ANISOU 3754  CB  ALA A 511     4332   4292   7664     46   -256    321       C  
ATOM   3755  N   GLY A 512      61.155   0.969   7.984  1.00 43.88           N  
ANISOU 3755  N   GLY A 512     4308   4269   8093     39   -210    437       N  
ATOM   3756  CA  GLY A 512      61.658   2.329   8.139  1.00 44.70           C  
ANISOU 3756  CA  GLY A 512     4348   4251   8382     35   -205    439       C  
ATOM   3757  C   GLY A 512      60.615   3.385   7.821  1.00 45.05           C  
ANISOU 3757  C   GLY A 512     4346   4241   8529     54   -165    517       C  
ATOM   3758  O   GLY A 512      60.538   4.409   8.500  1.00 45.89           O  
ANISOU 3758  O   GLY A 512     4422   4231   8783     64   -169    458       O  
ATOM   3759  N   LEU A 513      59.815   3.139   6.785  1.00 44.58           N  
ANISOU 3759  N   LEU A 513     4274   4262   8401     64   -139    640       N  
ATOM   3760  CA  LEU A 513      58.752   4.063   6.392  1.00 45.18           C  
ANISOU 3760  CA  LEU A 513     4299   4289   8575     88   -117    730       C  
ATOM   3761  C   LEU A 513      57.636   4.118   7.433  1.00 45.03           C  
ANISOU 3761  C   LEU A 513     4307   4231   8569    111   -115    625       C  
ATOM   3762  O   LEU A 513      57.178   5.202   7.793  1.00 45.82           O  
ANISOU 3762  O   LEU A 513     4359   4221   8829    128    -99    612       O  
ATOM   3763  CB  LEU A 513      58.174   3.681   5.025  1.00 45.16           C  
ANISOU 3763  CB  LEU A 513     4286   4398   8472    103   -116    876       C  
ATOM   3764  CG  LEU A 513      59.130   3.800   3.834  1.00 45.61           C  
ANISOU 3764  CG  LEU A 513     4315   4508   8506     93    -91   1009       C  
ATOM   3765  CD1 LEU A 513      58.524   3.159   2.596  1.00 45.74           C  
ANISOU 3765  CD1 LEU A 513     4349   4673   8356    120   -106   1110       C  
ATOM   3766  CD2 LEU A 513      59.495   5.250   3.555  1.00 46.89           C  
ANISOU 3766  CD2 LEU A 513     4397   4543   8874     91    -52   1127       C  
ATOM   3767  N   MET A 514      57.208   2.954   7.917  1.00 44.17           N  
ANISOU 3767  N   MET A 514     4268   4205   8308    113   -119    551       N  
ATOM   3768  CA  MET A 514      56.150   2.885   8.929  1.00 44.26           C  
ANISOU 3768  CA  MET A 514     4308   4192   8317    135    -88    461       C  
ATOM   3769  C   MET A 514      56.587   3.490  10.265  1.00 44.70           C  
ANISOU 3769  C   MET A 514     4397   4162   8422    146    -82    318       C  
ATOM   3770  O   MET A 514      55.805   4.185  10.916  1.00 45.66           O  
ANISOU 3770  O   MET A 514     4503   4217   8629    173    -43    256       O  
ATOM   3771  CB  MET A 514      55.672   1.443   9.132  1.00 43.60           C  
ANISOU 3771  CB  MET A 514     4283   4206   8074    132    -83    434       C  
ATOM   3772  CG  MET A 514      54.650   0.988   8.098  1.00 43.60           C  
ANISOU 3772  CG  MET A 514     4235   4265   8064    139    -89    526       C  
ATOM   3773  SD  MET A 514      54.051  -0.703   8.309  1.00 43.13           S  
ANISOU 3773  SD  MET A 514     4216   4290   7881    131    -85    489       S  
ATOM   3774  CE  MET A 514      53.788  -0.772  10.081  1.00 43.37           C  
ANISOU 3774  CE  MET A 514     4317   4268   7891    141     -6    379       C  
ATOM   3775  N   ILE A 515      57.828   3.228  10.669  1.00 44.16           N  
ANISOU 3775  N   ILE A 515     4372   4099   8308    130   -127    253       N  
ATOM   3776  CA  ILE A 515      58.381   3.815  11.892  1.00 44.58           C  
ANISOU 3776  CA  ILE A 515     4458   4077   8402    146   -153    101       C  
ATOM   3777  C   ILE A 515      58.383   5.345  11.822  1.00 45.27           C  
ANISOU 3777  C   ILE A 515     4451   4026   8722    155   -149     86       C  
ATOM   3778  O   ILE A 515      58.091   6.014  12.815  1.00 46.18           O  
ANISOU 3778  O   ILE A 515     4578   4073   8896    187   -143    -49       O  
ATOM   3779  CB  ILE A 515      59.805   3.283  12.182  1.00 44.54           C  
ANISOU 3779  CB  ILE A 515     4492   4091   8337    128   -228     43       C  
ATOM   3780  CG1 ILE A 515      59.732   1.832  12.669  1.00 43.81           C  
ANISOU 3780  CG1 ILE A 515     4505   4111   8030    132   -236     23       C  
ATOM   3781  CG2 ILE A 515      60.511   4.130  13.236  1.00 45.71           C  
ANISOU 3781  CG2 ILE A 515     4647   4145   8576    148   -287   -116       C  
ATOM   3782  CD1 ILE A 515      61.041   1.077  12.563  1.00 43.45           C  
ANISOU 3782  CD1 ILE A 515     4477   4095   7935    110   -311     13       C  
ATOM   3783  N   THR A 516      58.687   5.890  10.646  1.00 45.02           N  
ANISOU 3783  N   THR A 516     4327   3953   8824    132   -148    228       N  
ATOM   3784  CA  THR A 516      58.735   7.341  10.445  1.00 46.07           C  
ANISOU 3784  CA  THR A 516     4354   3936   9215    137   -142    250       C  
ATOM   3785  C   THR A 516      57.417   7.931   9.913  1.00 46.18           C  
ANISOU 3785  C   THR A 516     4307   3914   9323    160    -94    351       C  
ATOM   3786  O   THR A 516      57.417   9.016   9.330  1.00 46.85           O  
ANISOU 3786  O   THR A 516     4291   3885   9623    161    -88    447       O  
ATOM   3787  CB  THR A 516      59.877   7.722   9.479  1.00 46.41           C  
ANISOU 3787  CB  THR A 516     4318   3933   9381    101   -154    374       C  
ATOM   3788  OG1 THR A 516      59.682   7.070   8.218  1.00 45.74           O  
ANISOU 3788  OG1 THR A 516     4237   3964   9175     88   -123    557       O  
ATOM   3789  CG2 THR A 516      61.226   7.321  10.059  1.00 46.32           C  
ANISOU 3789  CG2 THR A 516     4334   3918   9344     79   -211    256       C  
ATOM   3790  N   THR A 517      56.302   7.230  10.126  1.00 45.38           N  
ANISOU 3790  N   THR A 517     4257   3899   9086    181    -63    336       N  
ATOM   3791  CA  THR A 517      54.984   7.709   9.710  1.00 45.48           C  
ANISOU 3791  CA  THR A 517     4205   3876   9199    208    -29    413       C  
ATOM   3792  C   THR A 517      54.276   8.379  10.884  1.00 46.22           C  
ANISOU 3792  C   THR A 517     4286   3876   9397    245     12    249       C  
ATOM   3793  O   THR A 517      54.175   7.797  11.966  1.00 46.25           O  
ANISOU 3793  O   THR A 517     4379   3934   9261    258     41    101       O  
ATOM   3794  CB  THR A 517      54.105   6.555   9.189  1.00 44.49           C  
ANISOU 3794  CB  THR A 517     4115   3884   8903    210    -19    487       C  
ATOM   3795  OG1 THR A 517      54.680   6.018   7.994  1.00 44.02           O  
ANISOU 3795  OG1 THR A 517     4060   3915   8750    187    -58    628       O  
ATOM   3796  CG2 THR A 517      52.694   7.033   8.882  1.00 45.21           C  
ANISOU 3796  CG2 THR A 517     4128   3928   9119    243      3    542       C  
ATOM   3797  N   GLU A 518      53.780   9.595  10.656  1.00 46.90           N  
ANISOU 3797  N   GLU A 518     4265   3824   9729    266     21    281       N  
ATOM   3798  CA  GLU A 518      53.060  10.358  11.681  1.00 47.62           C  
ANISOU 3798  CA  GLU A 518     4323   3812   9956    308     68    116       C  
ATOM   3799  C   GLU A 518      51.587  10.616  11.356  1.00 47.85           C  
ANISOU 3799  C   GLU A 518     4273   3807  10098    340    115    178       C  
ATOM   3800  O   GLU A 518      50.856  11.107  12.215  1.00 48.94           O  
ANISOU 3800  O   GLU A 518     4384   3875  10335    378    175     34       O  
ATOM   3801  CB  GLU A 518      53.769  11.694  11.940  1.00 48.94           C  
ANISOU 3801  CB  GLU A 518     4408   3804  10380    313     35     41       C  
ATOM   3802  CG  GLU A 518      54.739  11.656  13.110  1.00 49.27           C  
ANISOU 3802  CG  GLU A 518     4525   3844  10350    315      6   -178       C  
ATOM   3803  CD  GLU A 518      54.043  11.526  14.454  1.00 49.81           C  
ANISOU 3803  CD  GLU A 518     4666   3946  10314    365     64   -400       C  
ATOM   3804  OE1 GLU A 518      52.961  12.120  14.639  1.00 50.55           O  
ANISOU 3804  OE1 GLU A 518     4694   3968  10544    402    129   -440       O  
ATOM   3805  OE2 GLU A 518      54.587  10.836  15.337  1.00 49.51           O  
ANISOU 3805  OE2 GLU A 518     4750   4005  10054    372     48   -532       O  
ATOM   3806  N   CYS A 519      51.146  10.295  10.141  1.00 47.11           N  
ANISOU 3806  N   CYS A 519     4141   3764   9994    331     83    379       N  
ATOM   3807  CA  CYS A 519      49.763  10.569   9.742  1.00 47.61           C  
ANISOU 3807  CA  CYS A 519     4112   3784  10191    365     99    446       C  
ATOM   3808  C   CYS A 519      49.262   9.604   8.674  1.00 47.04           C  
ANISOU 3808  C   CYS A 519     4050   3841   9979    357     54    606       C  
ATOM   3809  O   CYS A 519      50.023   9.169   7.811  1.00 46.34           O  
ANISOU 3809  O   CYS A 519     4003   3840   9762    331     -3    728       O  
ATOM   3810  CB  CYS A 519      49.634  12.007   9.237  1.00 48.77           C  
ANISOU 3810  CB  CYS A 519     4128   3756  10645    388     67    535       C  
ATOM   3811  SG  CYS A 519      47.957  12.481   8.762  1.00 49.21           S  
ANISOU 3811  SG  CYS A 519     4050   3731  10915    439     65    616       S  
ATOM   3812  N   MET A 520      47.972   9.282   8.744  1.00 47.60           N  
ANISOU 3812  N   MET A 520     4074   3920  10089    383     81    589       N  
ATOM   3813  CA  MET A 520      47.325   8.394   7.777  1.00 47.34           C  
ANISOU 3813  CA  MET A 520     4029   3994   9962    384     21    709       C  
ATOM   3814  C   MET A 520      45.985   8.976   7.345  1.00 48.87           C  
ANISOU 3814  C   MET A 520     4088   4098  10380    429     -4    769       C  
ATOM   3815  O   MET A 520      45.236   9.492   8.175  1.00 49.97           O  
ANISOU 3815  O   MET A 520     4162   4132  10691    454     75    657       O  
ATOM   3816  CB  MET A 520      47.104   7.013   8.388  1.00 46.20           C  
ANISOU 3816  CB  MET A 520     3963   3964   9626    362     77    609       C  
ATOM   3817  CG  MET A 520      48.381   6.309   8.816  1.00 44.90           C  
ANISOU 3817  CG  MET A 520     3929   3889   9239    323     88    554       C  
ATOM   3818  SD  MET A 520      48.064   4.666   9.482  1.00 43.79           S  
ANISOU 3818  SD  MET A 520     3870   3866   8901    302    149    471       S  
ATOM   3819  CE  MET A 520      47.655   3.762   7.993  1.00 43.37           C  
ANISOU 3819  CE  MET A 520     3774   3910   8793    294     38    607       C  
ATOM   3820  N   VAL A 521      45.691   8.887   6.049  1.00 49.46           N  
ANISOU 3820  N   VAL A 521     4123   4221  10448    446   -119    941       N  
ATOM   3821  CA  VAL A 521      44.460   9.433   5.482  1.00 51.31           C  
ANISOU 3821  CA  VAL A 521     4223   4373  10896    496   -182   1021       C  
ATOM   3822  C   VAL A 521      43.746   8.362   4.662  1.00 51.76           C  
ANISOU 3822  C   VAL A 521     4270   4553  10841    506   -276   1074       C  
ATOM   3823  O   VAL A 521      44.358   7.717   3.813  1.00 51.58           O  
ANISOU 3823  O   VAL A 521     4324   4667  10606    493   -355   1159       O  
ATOM   3824  CB  VAL A 521      44.751  10.650   4.578  1.00 52.42           C  
ANISOU 3824  CB  VAL A 521     4308   4429  11181    526   -267   1208       C  
ATOM   3825  CG1 VAL A 521      43.457  11.254   4.050  1.00 54.07           C  
ANISOU 3825  CG1 VAL A 521     4374   4540  11630    586   -347   1293       C  
ATOM   3826  CG2 VAL A 521      45.549  11.700   5.338  1.00 52.76           C  
ANISOU 3826  CG2 VAL A 521     4347   4334  11365    511   -186   1147       C  
ATOM   3827  N   THR A 522      42.453   8.179   4.923  1.00 53.06           N  
ANISOU 3827  N   THR A 522     4330   4663  11165    531   -266   1010       N  
ATOM   3828  CA  THR A 522      41.635   7.198   4.201  1.00 53.51           C  
ANISOU 3828  CA  THR A 522     4346   4808  11178    544   -368   1034       C  
ATOM   3829  C   THR A 522      40.162   7.594   4.226  1.00 55.63           C  
ANISOU 3829  C   THR A 522     4444   4954  11738    591   -392   1017       C  
ATOM   3830  O   THR A 522      39.768   8.485   4.975  1.00 56.41           O  
ANISOU 3830  O   THR A 522     4467   4908  12058    607   -296    959       O  
ATOM   3831  CB  THR A 522      41.787   5.780   4.797  1.00 52.02           C  
ANISOU 3831  CB  THR A 522     4232   4720  10811    496   -290    909       C  
ATOM   3832  OG1 THR A 522      40.963   4.859   4.071  1.00 51.97           O  
ANISOU 3832  OG1 THR A 522     4162   4777  10807    509   -400    918       O  
ATOM   3833  CG2 THR A 522      41.401   5.753   6.278  1.00 51.95           C  
ANISOU 3833  CG2 THR A 522     4208   4627  10903    478    -99    753       C  
ATOM   3834  N   ASP A 523      39.355   6.920   3.412  1.00 57.08           N  
ANISOU 3834  N   ASP A 523     4559   5192  11935    615   -526   1051       N  
ATOM   3835  CA  ASP A 523      37.921   7.195   3.352  1.00 59.50           C  
ANISOU 3835  CA  ASP A 523     4685   5382  12540    661   -572   1032       C  
ATOM   3836  C   ASP A 523      37.195   6.654   4.584  1.00 60.12           C  
ANISOU 3836  C   ASP A 523     4698   5391  12754    632   -386    859       C  
ATOM   3837  O   ASP A 523      37.606   5.650   5.171  1.00 59.06           O  
ANISOU 3837  O   ASP A 523     4654   5338  12446    581   -281    773       O  
ATOM   3838  CB  ASP A 523      37.308   6.600   2.078  1.00 60.52           C  
ANISOU 3838  CB  ASP A 523     4757   5594  12641    701   -797   1107       C  
ATOM   3839  CG  ASP A 523      37.743   7.333   0.815  1.00 61.52           C  
ANISOU 3839  CG  ASP A 523     4924   5776  12672    754   -982   1304       C  
ATOM   3840  OD1 ASP A 523      38.590   8.250   0.900  1.00 61.65           O  
ANISOU 3840  OD1 ASP A 523     5010   5760  12654    750   -925   1395       O  
ATOM   3841  OD2 ASP A 523      37.230   6.992  -0.272  1.00 62.67           O  
ANISOU 3841  OD2 ASP A 523     5032   5998  12782    804  -1186   1371       O  
ATOM   3842  N   LEU A 524      36.125   7.344   4.975  1.00 62.42           N  
ANISOU 3842  N   LEU A 524     4828   5526  13363    669   -338    817       N  
ATOM   3843  CA  LEU A 524      35.277   6.918   6.091  1.00 63.60           C  
ANISOU 3843  CA  LEU A 524     4889   5600  13676    652   -144    666       C  
ATOM   3844  C   LEU A 524      34.530   5.619   5.780  1.00 64.66           C  
ANISOU 3844  C   LEU A 524     4949   5782  13834    636   -194    633       C  
ATOM   3845  O   LEU A 524      34.181   5.372   4.627  1.00 65.40           O  
ANISOU 3845  O   LEU A 524     4983   5914  13951    665   -417    709       O  
ATOM   3846  CB  LEU A 524      34.233   7.995   6.427  1.00 65.07           C  
ANISOU 3846  CB  LEU A 524     4891   5599  14233    705    -94    631       C  
ATOM   3847  CG  LEU A 524      34.689   9.417   6.741  1.00 65.38           C  
ANISOU 3847  CG  LEU A 524     4942   5534  14364    733    -51    643       C  
ATOM   3848  CD1 LEU A 524      33.511  10.378   6.744  1.00 67.44           C  
ANISOU 3848  CD1 LEU A 524     4987   5604  15031    795    -63    629       C  
ATOM   3849  CD2 LEU A 524      35.422   9.464   8.072  1.00 64.60           C  
ANISOU 3849  CD2 LEU A 524     4969   5452  14124    696    180    503       C  
ATOM   3850  N   PRO A 525      34.264   4.798   6.816  1.00 65.23           N  
ANISOU 3850  N   PRO A 525     5022   5851  13911    594     10    520       N  
ATOM   3851  CA  PRO A 525      33.485   3.575   6.632  1.00 66.06           C  
ANISOU 3851  CA  PRO A 525     5028   5967  14104    573    -11    483       C  
ATOM   3852  C   PRO A 525      31.984   3.853   6.537  1.00 68.21           C  
ANISOU 3852  C   PRO A 525     5052   6087  14778    614    -28    450       C  
ATOM   3853  O   PRO A 525      31.461   4.053   5.440  1.00 69.31           O  
ANISOU 3853  O   PRO A 525     5080   6203  15048    659   -267    509       O  
ATOM   3854  CB  PRO A 525      33.802   2.769   7.893  1.00 65.37           C  
ANISOU 3854  CB  PRO A 525     5035   5912  13889    518    246    401       C  
ATOM   3855  CG  PRO A 525      34.077   3.800   8.933  1.00 65.41           C  
ANISOU 3855  CG  PRO A 525     5096   5863  13893    533    436    351       C  
ATOM   3856  CD  PRO A 525      34.687   4.975   8.220  1.00 64.90           C  
ANISOU 3856  CD  PRO A 525     5073   5794  13790    568    273    425       C  
TER    3857      PRO A 525                                                      
ATOM   3858  N   ALA B   2      37.864  -8.377  -1.663  1.00 64.41           N  
ANISOU 3858  N   ALA B   2     5892   5526  13053   -579    344   2043       N  
ATOM   3859  CA  ALA B   2      37.007  -7.978  -0.505  1.00 63.80           C  
ANISOU 3859  CA  ALA B   2     5726   5299  13214   -522    268   1836       C  
ATOM   3860  C   ALA B   2      37.725  -8.208   0.820  1.00 62.34           C  
ANISOU 3860  C   ALA B   2     5464   5127  13093   -567    339   1568       C  
ATOM   3861  O   ALA B   2      38.648  -9.023   0.901  1.00 61.39           O  
ANISOU 3861  O   ALA B   2     5353   5175  12796   -614    417   1512       O  
ATOM   3862  CB  ALA B   2      35.694  -8.747  -0.527  1.00 62.82           C  
ANISOU 3862  CB  ALA B   2     5632   5265  12970   -415    165   1769       C  
ATOM   3863  N   ALA B   3      37.297  -7.487   1.854  1.00 62.37           N  
ANISOU 3863  N   ALA B   3     5395   4949  13352   -552    308   1401       N  
ATOM   3864  CA  ALA B   3      37.865  -7.640   3.190  1.00 61.30           C  
ANISOU 3864  CA  ALA B   3     5207   4813  13268   -596    351   1134       C  
ATOM   3865  C   ALA B   3      37.603  -9.050   3.708  1.00 58.94           C  
ANISOU 3865  C   ALA B   3     4944   4741  12707   -552    355    962       C  
ATOM   3866  O   ALA B   3      36.559  -9.637   3.419  1.00 58.20           O  
ANISOU 3866  O   ALA B   3     4884   4725  12501   -468    310    973       O  
ATOM   3867  CB  ALA B   3      37.286  -6.609   4.144  1.00 62.32           C  
ANISOU 3867  CB  ALA B   3     5277   4703  13695   -578    320    977       C  
ATOM   3868  N   LYS B   4      38.555  -9.574   4.479  1.00 57.96           N  
ANISOU 3868  N   LYS B   4     4805   4709  12506   -613    398    810       N  
ATOM   3869  CA  LYS B   4      38.543 -10.969   4.907  1.00 55.84           C  
ANISOU 3869  CA  LYS B   4     4575   4658  11984   -587    404    677       C  
ATOM   3870  C   LYS B   4      38.379 -11.122   6.413  1.00 55.23           C  
ANISOU 3870  C   LYS B   4     4488   4560  11936   -592    392    404       C  
ATOM   3871  O   LYS B   4      38.699 -10.217   7.185  1.00 56.30           O  
ANISOU 3871  O   LYS B   4     4588   4537  12266   -642    388    295       O  
ATOM   3872  CB  LYS B   4      39.848 -11.652   4.497  1.00 55.36           C  
ANISOU 3872  CB  LYS B   4     4511   4746  11776   -648    459    742       C  
ATOM   3873  CG  LYS B   4      40.152 -11.623   3.009  1.00 56.12           C  
ANISOU 3873  CG  LYS B   4     4638   4893  11792   -655    505   1002       C  
ATOM   3874  CD  LYS B   4      39.107 -12.375   2.203  1.00 55.39           C  
ANISOU 3874  CD  LYS B   4     4631   4921  11494   -566    467   1083       C  
ATOM   3875  CE  LYS B   4      39.613 -12.709   0.809  1.00 56.08           C  
ANISOU 3875  CE  LYS B   4     4781   5121  11403   -581    526   1298       C  
ATOM   3876  NZ  LYS B   4      39.866 -11.493  -0.012  1.00 58.32           N  
ANISOU 3876  NZ  LYS B   4     5066   5259  11831   -628    551   1523       N  
ATOM   3877  N   ASP B   5      37.875 -12.286   6.809  1.00 53.91           N  
ANISOU 3877  N   ASP B   5     4365   4553  11566   -544    387    296       N  
ATOM   3878  CA  ASP B   5      37.826 -12.707   8.200  1.00 53.61           C  
ANISOU 3878  CA  ASP B   5     4347   4546  11475   -558    385     55       C  
ATOM   3879  C   ASP B   5      38.911 -13.769   8.368  1.00 52.70           C  
ANISOU 3879  C   ASP B   5     4247   4604  11170   -603    382     32       C  
ATOM   3880  O   ASP B   5      38.894 -14.787   7.675  1.00 51.75           O  
ANISOU 3880  O   ASP B   5     4150   4640  10869   -568    390    121       O  
ATOM   3881  CB  ASP B   5      36.445 -13.300   8.522  1.00 53.08           C  
ANISOU 3881  CB  ASP B   5     4312   4528  11328   -474    389    -31       C  
ATOM   3882  CG  ASP B   5      36.143 -13.338  10.015  1.00 53.20           C  
ANISOU 3882  CG  ASP B   5     4357   4515  11340   -488    413   -280       C  
ATOM   3883  OD1 ASP B   5      37.068 -13.154  10.834  1.00 53.66           O  
ANISOU 3883  OD1 ASP B   5     4432   4555  11398   -563    401   -395       O  
ATOM   3884  OD2 ASP B   5      34.964 -13.565  10.367  1.00 53.02           O  
ANISOU 3884  OD2 ASP B   5     4342   4490  11312   -426    444   -361       O  
ATOM   3885  N   VAL B   6      39.855 -13.526   9.273  1.00 53.37           N  
ANISOU 3885  N   VAL B   6     4315   4651  11309   -681    360    -89       N  
ATOM   3886  CA  VAL B   6      40.988 -14.430   9.470  1.00 52.89           C  
ANISOU 3886  CA  VAL B   6     4245   4729  11122   -726    338   -105       C  
ATOM   3887  C   VAL B   6      40.986 -14.981  10.893  1.00 52.75           C  
ANISOU 3887  C   VAL B   6     4285   4759  10999   -747    286   -318       C  
ATOM   3888  O   VAL B   6      41.002 -14.216  11.857  1.00 53.87           O  
ANISOU 3888  O   VAL B   6     4443   4780  11242   -793    255   -465       O  
ATOM   3889  CB  VAL B   6      42.329 -13.714   9.200  1.00 54.23           C  
ANISOU 3889  CB  VAL B   6     4327   4818  11459   -815    335    -29       C  
ATOM   3890  CG1 VAL B   6      43.488 -14.700   9.243  1.00 53.70           C  
ANISOU 3890  CG1 VAL B   6     4221   4892  11290   -848    318    -24       C  
ATOM   3891  CG2 VAL B   6      42.295 -13.005   7.853  1.00 55.09           C  
ANISOU 3891  CG2 VAL B   6     4397   4857  11677   -807    399    191       C  
ATOM   3892  N   LYS B   7      40.967 -16.308  11.015  1.00 51.85           N  
ANISOU 3892  N   LYS B   7     4212   4813  10675   -716    274   -335       N  
ATOM   3893  CA  LYS B   7      41.034 -16.977  12.316  1.00 51.91           C  
ANISOU 3893  CA  LYS B   7     4289   4883  10549   -741    218   -506       C  
ATOM   3894  C   LYS B   7      42.271 -17.864  12.404  1.00 51.87           C  
ANISOU 3894  C   LYS B   7     4252   4987  10467   -777    154   -482       C  
ATOM   3895  O   LYS B   7      42.774 -18.340  11.386  1.00 51.33           O  
ANISOU 3895  O   LYS B   7     4122   4989  10390   -754    185   -342       O  
ATOM   3896  CB  LYS B   7      39.769 -17.799  12.564  1.00 50.92           C  
ANISOU 3896  CB  LYS B   7     4243   4841  10261   -672    256   -555       C  
ATOM   3897  CG  LYS B   7      38.561 -16.949  12.914  1.00 51.84           C  
ANISOU 3897  CG  LYS B   7     4385   4838  10471   -643    313   -639       C  
ATOM   3898  CD  LYS B   7      37.372 -17.796  13.337  1.00 51.24           C  
ANISOU 3898  CD  LYS B   7     4374   4843  10251   -589    359   -706       C  
ATOM   3899  CE  LYS B   7      36.174 -16.926  13.687  1.00 52.39           C  
ANISOU 3899  CE  LYS B   7     4519   4859  10524   -555    434   -797       C  
ATOM   3900  NZ  LYS B   7      36.332 -16.210  14.984  1.00 53.81           N  
ANISOU 3900  NZ  LYS B   7     4762   4945  10736   -612    446   -996       N  
ATOM   3901  N   PHE B   8      42.749 -18.080  13.628  1.00 52.72           N  
ANISOU 3901  N   PHE B   8     4407   5104  10520   -832     62   -621       N  
ATOM   3902  CA  PHE B   8      43.999 -18.804  13.870  1.00 53.06           C  
ANISOU 3902  CA  PHE B   8     4404   5221  10535   -872    -30   -609       C  
ATOM   3903  C   PHE B   8      43.841 -19.928  14.887  1.00 53.00           C  
ANISOU 3903  C   PHE B   8     4500   5318  10317   -868   -107   -703       C  
ATOM   3904  O   PHE B   8      42.988 -19.865  15.773  1.00 52.98           O  
ANISOU 3904  O   PHE B   8     4617   5306  10206   -871   -103   -824       O  
ATOM   3905  CB  PHE B   8      45.071 -17.842  14.383  1.00 54.50           C  
ANISOU 3905  CB  PHE B   8     4521   5286  10899   -969   -121   -665       C  
ATOM   3906  CG  PHE B   8      45.427 -16.755  13.415  1.00 55.04           C  
ANISOU 3906  CG  PHE B   8     4475   5241  11197   -991    -51   -554       C  
ATOM   3907  CD1 PHE B   8      46.402 -16.961  12.453  1.00 55.09           C  
ANISOU 3907  CD1 PHE B   8     4350   5279  11299   -999    -16   -405       C  
ATOM   3908  CD2 PHE B   8      44.794 -15.522  13.471  1.00 55.80           C  
ANISOU 3908  CD2 PHE B   8     4593   5187  11420  -1006    -12   -596       C  
ATOM   3909  CE1 PHE B   8      46.737 -15.960  11.560  1.00 55.98           C  
ANISOU 3909  CE1 PHE B   8     4368   5287  11613  -1029     61   -285       C  
ATOM   3910  CE2 PHE B   8      45.126 -14.515  12.581  1.00 56.73           C  
ANISOU 3910  CE2 PHE B   8     4612   5186  11755  -1031     45   -474       C  
ATOM   3911  CZ  PHE B   8      46.100 -14.735  11.622  1.00 56.78           C  
ANISOU 3911  CZ  PHE B   8     4500   5236  11838  -1048     84   -311       C  
ATOM   3912  N   GLY B   9      44.685 -20.947  14.749  1.00 53.52           N  
ANISOU 3912  N   GLY B   9     4519   5479  10338   -861   -168   -644       N  
ATOM   3913  CA  GLY B   9      44.828 -22.010  15.743  1.00 54.46           C  
ANISOU 3913  CA  GLY B   9     4723   5680  10287   -870   -276   -709       C  
ATOM   3914  C   GLY B   9      43.535 -22.608  16.263  1.00 54.59           C  
ANISOU 3914  C   GLY B   9     4886   5755  10100   -831   -226   -768       C  
ATOM   3915  O   GLY B   9      42.634 -22.919  15.487  1.00 53.71           O  
ANISOU 3915  O   GLY B   9     4775   5679   9952   -763   -113   -706       O  
ATOM   3916  N   ASN B  10      43.449 -22.752  17.583  1.00 56.53           N  
ANISOU 3916  N   ASN B  10     5259   6007  10213   -883   -313   -886       N  
ATOM   3917  CA  ASN B  10      42.313 -23.404  18.236  1.00 57.17           C  
ANISOU 3917  CA  ASN B  10     5485   6147  10091   -862   -258   -942       C  
ATOM   3918  C   ASN B  10      40.978 -22.802  17.815  1.00 56.99           C  
ANISOU 3918  C   ASN B  10     5472   6080  10100   -816    -92   -964       C  
ATOM   3919  O   ASN B  10      40.028 -23.526  17.518  1.00 56.24           O  
ANISOU 3919  O   ASN B  10     5403   6044   9921   -760     -7   -925       O  
ATOM   3920  CB  ASN B  10      42.462 -23.328  19.760  1.00 59.30           C  
ANISOU 3920  CB  ASN B  10     5907   6410  10211   -942   -361  -1077       C  
ATOM   3921  CG  ASN B  10      41.577 -24.326  20.485  1.00 59.94           C  
ANISOU 3921  CG  ASN B  10     6140   6576  10057   -932   -321  -1100       C  
ATOM   3922  OD1 ASN B  10      40.349 -24.230  20.446  1.00 59.94           O  
ANISOU 3922  OD1 ASN B  10     6186   6575  10013   -899   -167  -1135       O  
ATOM   3923  ND2 ASN B  10      42.200 -25.291  21.160  1.00 60.84           N  
ANISOU 3923  ND2 ASN B  10     6324   6756  10034   -962   -463  -1073       N  
ATOM   3924  N   ASP B  11      40.921 -21.474  17.785  1.00 58.15           N  
ANISOU 3924  N   ASP B  11     5589   6111  10393   -840    -57  -1025       N  
ATOM   3925  CA  ASP B  11      39.727 -20.747  17.358  1.00 58.14           C  
ANISOU 3925  CA  ASP B  11     5574   6039  10477   -793     83  -1042       C  
ATOM   3926  C   ASP B  11      39.278 -21.173  15.954  1.00 56.11           C  
ANISOU 3926  C   ASP B  11     5220   5824  10275   -711    150   -884       C  
ATOM   3927  O   ASP B  11      38.082 -21.285  15.687  1.00 55.58           O  
ANISOU 3927  O   ASP B  11     5161   5759  10196   -657    244   -877       O  
ATOM   3928  CB  ASP B  11      40.004 -19.237  17.405  1.00 60.25           C  
ANISOU 3928  CB  ASP B  11     5799   6152  10937   -832     84  -1109       C  
ATOM   3929  CG  ASP B  11      38.759 -18.397  17.184  1.00 61.48           C  
ANISOU 3929  CG  ASP B  11     5947   6208  11202   -784    217  -1151       C  
ATOM   3930  OD1 ASP B  11      37.630 -18.908  17.366  1.00 61.74           O  
ANISOU 3930  OD1 ASP B  11     6028   6288  11141   -737    309  -1178       O  
ATOM   3931  OD2 ASP B  11      38.918 -17.206  16.835  1.00 62.99           O  
ANISOU 3931  OD2 ASP B  11     6072   6262  11596   -795    227  -1153       O  
ATOM   3932  N   ALA B  12      40.242 -21.415  15.069  1.00 55.30           N  
ANISOU 3932  N   ALA B  12     5025   5753  10232   -705    102   -761       N  
ATOM   3933  CA  ALA B  12      39.962 -21.864  13.705  1.00 54.08           C  
ANISOU 3933  CA  ALA B  12     4802   5649  10096   -635    157   -615       C  
ATOM   3934  C   ALA B  12      39.635 -23.353  13.626  1.00 53.13           C  
ANISOU 3934  C   ALA B  12     4723   5654   9809   -593    151   -584       C  
ATOM   3935  O   ALA B  12      38.802 -23.761  12.818  1.00 52.51           O  
ANISOU 3935  O   ALA B  12     4636   5609   9705   -533    207   -518       O  
ATOM   3936  CB  ALA B  12      41.138 -21.543  12.796  1.00 54.31           C  
ANISOU 3936  CB  ALA B  12     4726   5664  10245   -649    138   -505       C  
ATOM   3937  N   ARG B  13      40.297 -24.164  14.449  1.00 53.65           N  
ANISOU 3937  N   ARG B  13     4835   5778   9771   -626     69   -626       N  
ATOM   3938  CA  ARG B  13      40.099 -25.620  14.423  1.00 53.00           C  
ANISOU 3938  CA  ARG B  13     4791   5798   9549   -590     52   -591       C  
ATOM   3939  C   ARG B  13      38.723 -26.042  14.942  1.00 52.62           C  
ANISOU 3939  C   ARG B  13     4831   5768   9392   -575    114   -643       C  
ATOM   3940  O   ARG B  13      38.096 -26.932  14.367  1.00 51.78           O  
ANISOU 3940  O   ARG B  13     4723   5716   9235   -526    145   -588       O  
ATOM   3941  CB  ARG B  13      41.198 -26.341  15.214  1.00 53.50           C  
ANISOU 3941  CB  ARG B  13     4875   5899   9550   -630    -70   -609       C  
ATOM   3942  CG  ARG B  13      42.582 -26.200  14.607  1.00 53.82           C  
ANISOU 3942  CG  ARG B  13     4795   5931   9721   -636   -124   -545       C  
ATOM   3943  CD  ARG B  13      43.608 -27.073  15.313  1.00 54.20           C  
ANISOU 3943  CD  ARG B  13     4843   6014   9733   -660   -262   -548       C  
ATOM   3944  NE  ARG B  13      44.269 -26.337  16.395  1.00 55.45           N  
ANISOU 3944  NE  ARG B  13     5026   6117   9923   -743   -378   -629       N  
ATOM   3945  CZ  ARG B  13      45.466 -25.734  16.364  1.00 56.49           C  
ANISOU 3945  CZ  ARG B  13     5049   6197  10214   -786   -458   -623       C  
ATOM   3946  NH1 ARG B  13      45.920 -25.110  17.457  1.00 58.06           N  
ANISOU 3946  NH1 ARG B  13     5296   6343  10418   -869   -585   -715       N  
ATOM   3947  NH2 ARG B  13      46.223 -25.739  15.271  1.00 56.41           N  
ANISOU 3947  NH2 ARG B  13     4886   6187  10361   -754   -410   -532       N  
ATOM   3948  N   VAL B  14      38.261 -25.412  16.022  1.00 53.43           N  
ANISOU 3948  N   VAL B  14     5010   5822   9465   -619    139   -756       N  
ATOM   3949  CA  VAL B  14      36.929 -25.711  16.567  1.00 53.59           C  
ANISOU 3949  CA  VAL B  14     5104   5853   9404   -610    232   -813       C  
ATOM   3950  C   VAL B  14      35.815 -25.360  15.579  1.00 53.05           C  
ANISOU 3950  C   VAL B  14     4955   5749   9450   -546    327   -768       C  
ATOM   3951  O   VAL B  14      34.759 -25.989  15.590  1.00 52.80           O  
ANISOU 3951  O   VAL B  14     4937   5746   9379   -520    389   -765       O  
ATOM   3952  CB  VAL B  14      36.644 -25.011  17.922  1.00 55.14           C  
ANISOU 3952  CB  VAL B  14     5406   6001   9543   -671    269   -962       C  
ATOM   3953  CG1 VAL B  14      37.630 -25.474  18.989  1.00 56.16           C  
ANISOU 3953  CG1 VAL B  14     5642   6173   9521   -741    149  -1002       C  
ATOM   3954  CG2 VAL B  14      36.641 -23.491  17.788  1.00 56.04           C  
ANISOU 3954  CG2 VAL B  14     5471   5997   9823   -677    307  -1026       C  
ATOM   3955  N   LYS B  15      36.053 -24.358  14.734  1.00 53.17           N  
ANISOU 3955  N   LYS B  15     4886   5697   9619   -525    329   -724       N  
ATOM   3956  CA  LYS B  15      35.108 -24.006  13.676  1.00 53.05           C  
ANISOU 3956  CA  LYS B  15     4795   5643   9716   -462    383   -654       C  
ATOM   3957  C   LYS B  15      35.001 -25.120  12.640  1.00 52.14           C  
ANISOU 3957  C   LYS B  15     4654   5617   9538   -416    351   -542       C  
ATOM   3958  O   LYS B  15      33.901 -25.474  12.227  1.00 52.27           O  
ANISOU 3958  O   LYS B  15     4651   5641   9568   -375    381   -518       O  
ATOM   3959  CB  LYS B  15      35.506 -22.695  12.994  1.00 53.82           C  
ANISOU 3959  CB  LYS B  15     4823   5644   9982   -458    378   -609       C  
ATOM   3960  CG  LYS B  15      35.258 -21.452  13.834  1.00 55.26           C  
ANISOU 3960  CG  LYS B  15     5016   5703  10276   -488    424   -728       C  
ATOM   3961  CD  LYS B  15      33.775 -21.134  13.944  1.00 55.82           C  
ANISOU 3961  CD  LYS B  15     5065   5711  10430   -442    516   -775       C  
ATOM   3962  CE  LYS B  15      33.548 -19.753  14.529  1.00 57.31           C  
ANISOU 3962  CE  LYS B  15     5246   5750  10777   -456    571   -887       C  
ATOM   3963  NZ  LYS B  15      32.108 -19.501  14.800  1.00 58.12           N  
ANISOU 3963  NZ  LYS B  15     5317   5788  10977   -408    680   -957       N  
ATOM   3964  N   MET B  16      36.138 -25.673  12.228  1.00 52.01           N  
ANISOU 3964  N   MET B  16     4633   5661   9465   -422    289   -483       N  
ATOM   3965  CA  MET B  16      36.143 -26.782  11.271  1.00 51.55           C  
ANISOU 3965  CA  MET B  16     4564   5683   9337   -378    265   -400       C  
ATOM   3966  C   MET B  16      35.519 -28.038  11.873  1.00 50.94           C  
ANISOU 3966  C   MET B  16     4543   5662   9149   -377    259   -438       C  
ATOM   3967  O   MET B  16      34.741 -28.722  11.209  1.00 50.36           O  
ANISOU 3967  O   MET B  16     4460   5617   9056   -339    262   -400       O  
ATOM   3968  CB  MET B  16      37.563 -27.097  10.801  1.00 51.98           C  
ANISOU 3968  CB  MET B  16     4593   5780   9376   -383    223   -347       C  
ATOM   3969  CG  MET B  16      38.204 -26.003   9.969  1.00 52.87           C  
ANISOU 3969  CG  MET B  16     4643   5845   9598   -386    244   -278       C  
ATOM   3970  SD  MET B  16      39.800 -26.498   9.289  1.00 53.73           S  
ANISOU 3970  SD  MET B  16     4698   6010   9705   -387    233   -212       S  
ATOM   3971  CE  MET B  16      40.805 -26.542  10.772  1.00 54.38           C  
ANISOU 3971  CE  MET B  16     4777   6074   9811   -451    155   -303       C  
ATOM   3972  N   LEU B  17      35.872 -28.334  13.123  1.00 51.30           N  
ANISOU 3972  N   LEU B  17     4652   5718   9122   -426    243   -508       N  
ATOM   3973  CA  LEU B  17      35.305 -29.471  13.853  1.00 51.55           C  
ANISOU 3973  CA  LEU B  17     4751   5792   9044   -440    246   -534       C  
ATOM   3974  C   LEU B  17      33.785 -29.369  13.923  1.00 51.71           C  
ANISOU 3974  C   LEU B  17     4761   5783   9099   -427    334   -562       C  
ATOM   3975  O   LEU B  17      33.087 -30.351  13.666  1.00 50.81           O  
ANISOU 3975  O   LEU B  17     4647   5700   8958   -410    339   -532       O  
ATOM   3976  CB  LEU B  17      35.887 -29.544  15.270  1.00 52.57           C  
ANISOU 3976  CB  LEU B  17     4971   5926   9076   -505    213   -601       C  
ATOM   3977  CG  LEU B  17      35.399 -30.671  16.190  1.00 52.83           C  
ANISOU 3977  CG  LEU B  17     5097   5998   8975   -535    218   -614       C  
ATOM   3978  CD1 LEU B  17      35.682 -32.044  15.598  1.00 52.13           C  
ANISOU 3978  CD1 LEU B  17     4993   5954   8856   -501    152   -533       C  
ATOM   3979  CD2 LEU B  17      36.040 -30.540  17.564  1.00 53.90           C  
ANISOU 3979  CD2 LEU B  17     5345   6137   8996   -606    169   -674       C  
ATOM   3980  N   ARG B  18      33.287 -28.181  14.276  1.00 52.78           N  
ANISOU 3980  N   ARG B  18     4881   5852   9321   -436    403   -622       N  
ATOM   3981  CA  ARG B  18      31.849 -27.913  14.328  1.00 53.59           C  
ANISOU 3981  CA  ARG B  18     4943   5908   9507   -417    498   -654       C  
ATOM   3982  C   ARG B  18      31.198 -28.184  12.947  1.00 51.82           C  
ANISOU 3982  C   ARG B  18     4629   5686   9371   -355    462   -561       C  
ATOM   3983  O   ARG B  18      30.133 -28.810  12.853  1.00 51.59           O  
ANISOU 3983  O   ARG B  18     4569   5661   9368   -342    490   -555       O  
ATOM   3984  CB  ARG B  18      31.533 -26.480  14.864  1.00 56.08           C  
ANISOU 3984  CB  ARG B  18     5244   6129   9933   -426    578   -744       C  
ATOM   3985  CG  ARG B  18      31.021 -26.364  16.327  1.00 58.54           C  
ANISOU 3985  CG  ARG B  18     5637   6424  10178   -476    692   -873       C  
ATOM   3986  CD  ARG B  18      30.921 -24.880  16.781  1.00 60.81           C  
ANISOU 3986  CD  ARG B  18     5917   6605  10582   -481    763   -981       C  
ATOM   3987  NE  ARG B  18      29.517 -24.616  17.046  1.00 62.89           N  
ANISOU 3987  NE  ARG B  18     6126   6811  10957   -455    908  -1044       N  
ATOM   3988  CZ  ARG B  18      28.858 -25.080  18.106  1.00 64.73           C  
ANISOU 3988  CZ  ARG B  18     6428   7070  11095   -493   1035  -1130       C  
ATOM   3989  NH1 ARG B  18      29.486 -25.801  19.039  1.00 65.44           N  
ANISOU 3989  NH1 ARG B  18     6667   7242  10955   -562   1018  -1158       N  
ATOM   3990  NH2 ARG B  18      27.566 -24.818  18.240  1.00 66.06           N  
ANISOU 3990  NH2 ARG B  18     6516   7178  11406   -463   1181  -1182       N  
ATOM   3991  N   GLY B  19      31.873 -27.757  11.882  1.00 50.48           N  
ANISOU 3991  N   GLY B  19     4425   5515   9238   -325    395   -486       N  
ATOM   3992  CA  GLY B  19      31.383 -27.928  10.514  1.00 49.63           C  
ANISOU 3992  CA  GLY B  19     4262   5415   9179   -273    344   -394       C  
ATOM   3993  C   GLY B  19      31.312 -29.366  10.037  1.00 48.47           C  
ANISOU 3993  C   GLY B  19     4140   5345   8931   -261    290   -360       C  
ATOM   3994  O   GLY B  19      30.301 -29.788   9.476  1.00 48.61           O  
ANISOU 3994  O   GLY B  19     4121   5358   8990   -236    265   -336       O  
ATOM   3995  N   VAL B  20      32.391 -30.116  10.246  1.00 47.64           N  
ANISOU 3995  N   VAL B  20     4090   5297   8713   -279    262   -362       N  
ATOM   3996  CA  VAL B  20      32.437 -31.531   9.849  1.00 47.00           C  
ANISOU 3996  CA  VAL B  20     4037   5273   8546   -266    212   -342       C  
ATOM   3997  C   VAL B  20      31.507 -32.397  10.696  1.00 46.38           C  
ANISOU 3997  C   VAL B  20     3975   5190   8454   -294    238   -382       C  
ATOM   3998  O   VAL B  20      31.017 -33.416  10.220  1.00 46.23           O  
ANISOU 3998  O   VAL B  20     3954   5187   8421   -281    199   -364       O  
ATOM   3999  CB  VAL B  20      33.880 -32.115   9.855  1.00 47.05           C  
ANISOU 3999  CB  VAL B  20     4080   5326   8470   -269    176   -332       C  
ATOM   4000  CG1 VAL B  20      34.776 -31.332   8.907  1.00 47.24           C  
ANISOU 4000  CG1 VAL B  20     4074   5355   8517   -245    174   -282       C  
ATOM   4001  CG2 VAL B  20      34.476 -32.150  11.257  1.00 47.53           C  
ANISOU 4001  CG2 VAL B  20     4183   5382   8492   -319    184   -381       C  
ATOM   4002  N   ASN B  21      31.261 -31.998  11.941  1.00 46.08           N  
ANISOU 4002  N   ASN B  21     3961   5127   8420   -337    310   -439       N  
ATOM   4003  CA  ASN B  21      30.280 -32.694  12.773  1.00 45.97           C  
ANISOU 4003  CA  ASN B  21     3962   5104   8397   -372    370   -470       C  
ATOM   4004  C   ASN B  21      28.869 -32.598  12.191  1.00 45.79           C  
ANISOU 4004  C   ASN B  21     3846   5042   8508   -348    395   -461       C  
ATOM   4005  O   ASN B  21      28.136 -33.583  12.187  1.00 46.06           O  
ANISOU 4005  O   ASN B  21     3865   5079   8556   -361    392   -449       O  
ATOM   4006  CB  ASN B  21      30.299 -32.170  14.217  1.00 46.85           C  
ANISOU 4006  CB  ASN B  21     4136   5201   8463   -427    463   -541       C  
ATOM   4007  CG  ASN B  21      31.467 -32.713  15.026  1.00 46.94           C  
ANISOU 4007  CG  ASN B  21     4254   5254   8325   -467    411   -542       C  
ATOM   4008  OD1 ASN B  21      32.002 -33.781  14.735  1.00 46.57           O  
ANISOU 4008  OD1 ASN B  21     4229   5241   8224   -459    330   -491       O  
ATOM   4009  ND2 ASN B  21      31.864 -31.975  16.056  1.00 47.82           N  
ANISOU 4009  ND2 ASN B  21     4433   5356   8380   -511    448   -606       N  
ATOM   4010  N   VAL B  22      28.496 -31.422  11.691  1.00 45.47           N  
ANISOU 4010  N   VAL B  22     3735   4955   8585   -314    407   -459       N  
ATOM   4011  CA  VAL B  22      27.168 -31.229  11.096  1.00 45.55           C  
ANISOU 4011  CA  VAL B  22     3637   4915   8754   -284    404   -442       C  
ATOM   4012  C   VAL B  22      27.011 -32.072   9.829  1.00 44.88           C  
ANISOU 4012  C   VAL B  22     3535   4860   8654   -255    275   -376       C  
ATOM   4013  O   VAL B  22      25.953 -32.653   9.597  1.00 45.19           O  
ANISOU 4013  O   VAL B  22     3511   4878   8780   -256    251   -370       O  
ATOM   4014  CB  VAL B  22      26.879 -29.740  10.789  1.00 45.96           C  
ANISOU 4014  CB  VAL B  22     3617   4893   8950   -247    424   -441       C  
ATOM   4015  CG1 VAL B  22      25.573 -29.582  10.020  1.00 46.45           C  
ANISOU 4015  CG1 VAL B  22     3556   4900   9193   -208    379   -403       C  
ATOM   4016  CG2 VAL B  22      26.822 -28.934  12.080  1.00 46.71           C  
ANISOU 4016  CG2 VAL B  22     3726   4943   9079   -277    564   -536       C  
ATOM   4017  N   LEU B  23      28.063 -32.135   9.016  1.00 44.07           N  
ANISOU 4017  N   LEU B  23     3491   4804   8448   -232    196   -333       N  
ATOM   4018  CA  LEU B  23      28.055 -32.979   7.821  1.00 43.79           C  
ANISOU 4018  CA  LEU B  23     3472   4804   8360   -206     83   -290       C  
ATOM   4019  C   LEU B  23      28.015 -34.454   8.200  1.00 43.48           C  
ANISOU 4019  C   LEU B  23     3471   4790   8258   -235     71   -318       C  
ATOM   4020  O   LEU B  23      27.147 -35.194   7.747  1.00 44.01           O  
ANISOU 4020  O   LEU B  23     3504   4841   8373   -236     11   -316       O  
ATOM   4021  CB  LEU B  23      29.289 -32.710   6.951  1.00 43.39           C  
ANISOU 4021  CB  LEU B  23     3482   4800   8201   -178     41   -248       C  
ATOM   4022  CG  LEU B  23      29.506 -33.658   5.763  1.00 43.37           C  
ANISOU 4022  CG  LEU B  23     3530   4846   8100   -153    -50   -225       C  
ATOM   4023  CD1 LEU B  23      28.294 -33.696   4.846  1.00 44.12           C  
ANISOU 4023  CD1 LEU B  23     3588   4917   8259   -135   -150   -196       C  
ATOM   4024  CD2 LEU B  23      30.742 -33.259   4.978  1.00 43.21           C  
ANISOU 4024  CD2 LEU B  23     3565   4872   7981   -129    -45   -186       C  
ATOM   4025  N   ALA B  24      28.964 -34.867   9.034  1.00 42.85           N  
ANISOU 4025  N   ALA B  24     3458   4738   8083   -260    116   -341       N  
ATOM   4026  CA  ALA B  24      29.101 -36.266   9.438  1.00 42.27           C  
ANISOU 4026  CA  ALA B  24     3432   4676   7951   -286     98   -353       C  
ATOM   4027  C   ALA B  24      27.849 -36.802  10.127  1.00 42.41           C  
ANISOU 4027  C   ALA B  24     3408   4652   8051   -330    144   -367       C  
ATOM   4028  O   ALA B  24      27.376 -37.885   9.792  1.00 42.63           O  
ANISOU 4028  O   ALA B  24     3428   4664   8101   -340     90   -362       O  
ATOM   4029  CB  ALA B  24      30.311 -36.432  10.347  1.00 42.01           C  
ANISOU 4029  CB  ALA B  24     3472   4669   7821   -306    126   -362       C  
ATOM   4030  N   ASP B  25      27.315 -36.043  11.083  1.00 42.49           N  
ANISOU 4030  N   ASP B  25     3389   4638   8115   -360    254   -390       N  
ATOM   4031  CA  ASP B  25      26.131 -36.471  11.834  1.00 43.11           C  
ANISOU 4031  CA  ASP B  25     3421   4678   8280   -409    340   -404       C  
ATOM   4032  C   ASP B  25      24.903 -36.612  10.932  1.00 43.38           C  
ANISOU 4032  C   ASP B  25     3334   4668   8478   -391    283   -391       C  
ATOM   4033  O   ASP B  25      24.065 -37.486  11.158  1.00 43.83           O  
ANISOU 4033  O   ASP B  25     3347   4694   8611   -431    299   -386       O  
ATOM   4034  CB  ASP B  25      25.816 -35.492  12.978  1.00 43.78           C  
ANISOU 4034  CB  ASP B  25     3500   4744   8388   -438    494   -449       C  
ATOM   4035  CG  ASP B  25      26.908 -35.444  14.043  1.00 43.63           C  
ANISOU 4035  CG  ASP B  25     3614   4765   8198   -473    536   -468       C  
ATOM   4036  OD1 ASP B  25      27.732 -36.378  14.120  1.00 43.19           O  
ANISOU 4036  OD1 ASP B  25     3639   4741   8029   -486    462   -435       O  
ATOM   4037  OD2 ASP B  25      26.946 -34.455  14.806  1.00 44.21           O  
ANISOU 4037  OD2 ASP B  25     3708   4828   8260   -488    634   -522       O  
ATOM   4038  N   ALA B  26      24.800 -35.748   9.924  1.00 42.98           N  
ANISOU 4038  N   ALA B  26     3230   4611   8489   -336    208   -376       N  
ATOM   4039  CA  ALA B  26      23.703 -35.803   8.957  1.00 43.46           C  
ANISOU 4039  CA  ALA B  26     3182   4631   8700   -315    109   -355       C  
ATOM   4040  C   ALA B  26      23.822 -37.002   8.027  1.00 43.26           C  
ANISOU 4040  C   ALA B  26     3198   4623   8613   -314    -35   -342       C  
ATOM   4041  O   ALA B  26      22.819 -37.607   7.654  1.00 44.27           O  
ANISOU 4041  O   ALA B  26     3248   4710   8862   -332   -105   -341       O  
ATOM   4042  CB  ALA B  26      23.653 -34.518   8.146  1.00 43.62           C  
ANISOU 4042  CB  ALA B  26     3155   4635   8781   -258     52   -326       C  
ATOM   4043  N   VAL B  27      25.051 -37.340   7.658  1.00 42.54           N  
ANISOU 4043  N   VAL B  27     3224   4588   8350   -293    -77   -340       N  
ATOM   4044  CA  VAL B  27      25.312 -38.427   6.721  1.00 42.66           C  
ANISOU 4044  CA  VAL B  27     3297   4619   8292   -282   -202   -348       C  
ATOM   4045  C   VAL B  27      25.340 -39.793   7.417  1.00 42.89           C  
ANISOU 4045  C   VAL B  27     3358   4624   8313   -329   -178   -369       C  
ATOM   4046  O   VAL B  27      24.807 -40.767   6.885  1.00 43.43           O  
ANISOU 4046  O   VAL B  27     3413   4658   8428   -344   -272   -386       O  
ATOM   4047  CB  VAL B  27      26.634 -38.180   5.957  1.00 42.13           C  
ANISOU 4047  CB  VAL B  27     3329   4614   8062   -233   -235   -341       C  
ATOM   4048  CG1 VAL B  27      27.048 -39.398   5.147  1.00 42.38           C  
ANISOU 4048  CG1 VAL B  27     3437   4660   8005   -220   -326   -374       C  
ATOM   4049  CG2 VAL B  27      26.490 -36.973   5.042  1.00 42.48           C  
ANISOU 4049  CG2 VAL B  27     3353   4671   8114   -194   -283   -300       C  
ATOM   4050  N   LYS B  28      25.940 -39.862   8.606  1.00 42.78           N  
ANISOU 4050  N   LYS B  28     3389   4620   8243   -357    -67   -365       N  
ATOM   4051  CA  LYS B  28      26.193 -41.152   9.260  1.00 43.10           C  
ANISOU 4051  CA  LYS B  28     3484   4637   8253   -398    -58   -363       C  
ATOM   4052  C   LYS B  28      24.949 -41.866   9.805  1.00 44.19           C  
ANISOU 4052  C   LYS B  28     3554   4709   8525   -465    -23   -353       C  
ATOM   4053  O   LYS B  28      25.019 -43.052  10.129  1.00 44.56           O  
ANISOU 4053  O   LYS B  28     3640   4718   8572   -502    -40   -341       O  
ATOM   4054  CB  LYS B  28      27.264 -41.021  10.358  1.00 42.80           C  
ANISOU 4054  CB  LYS B  28     3530   4631   8101   -411     21   -348       C  
ATOM   4055  CG  LYS B  28      26.817 -40.394  11.675  1.00 43.26           C  
ANISOU 4055  CG  LYS B  28     3580   4686   8169   -464    160   -340       C  
ATOM   4056  CD  LYS B  28      27.999 -39.915  12.505  1.00 42.93           C  
ANISOU 4056  CD  LYS B  28     3629   4687   7995   -466    198   -337       C  
ATOM   4057  CE  LYS B  28      27.590 -39.625  13.943  1.00 43.77           C  
ANISOU 4057  CE  LYS B  28     3773   4789   8068   -534    332   -337       C  
ATOM   4058  NZ  LYS B  28      28.766 -39.463  14.840  1.00 43.72           N  
ANISOU 4058  NZ  LYS B  28     3879   4819   7914   -550    329   -330       N  
ATOM   4059  N   VAL B  29      23.822 -41.163   9.901  1.00 45.19           N  
ANISOU 4059  N   VAL B  29     3569   4813   8788   -482     29   -353       N  
ATOM   4060  CA  VAL B  29      22.556 -41.804  10.300  1.00 46.62           C  
ANISOU 4060  CA  VAL B  29     3652   4925   9137   -548     69   -343       C  
ATOM   4061  C   VAL B  29      22.036 -42.791   9.247  1.00 47.42           C  
ANISOU 4061  C   VAL B  29     3712   4975   9330   -552    -93   -356       C  
ATOM   4062  O   VAL B  29      21.274 -43.701   9.578  1.00 48.71           O  
ANISOU 4062  O   VAL B  29     3820   5071   9615   -617    -81   -343       O  
ATOM   4063  CB  VAL B  29      21.434 -40.788  10.642  1.00 47.38           C  
ANISOU 4063  CB  VAL B  29     3608   4996   9397   -558    175   -348       C  
ATOM   4064  CG1 VAL B  29      21.813 -39.958  11.862  1.00 47.32           C  
ANISOU 4064  CG1 VAL B  29     3652   5022   9304   -571    360   -355       C  
ATOM   4065  CG2 VAL B  29      21.093 -39.897   9.453  1.00 47.37           C  
ANISOU 4065  CG2 VAL B  29     3524   4994   9477   -492     52   -358       C  
ATOM   4066  N   THR B  30      22.457 -42.623   7.995  1.00 47.24           N  
ANISOU 4066  N   THR B  30     3724   4982   9242   -490   -242   -382       N  
ATOM   4067  CA  THR B  30      22.028 -43.507   6.907  1.00 48.20           C  
ANISOU 4067  CA  THR B  30     3833   5060   9418   -492   -416   -414       C  
ATOM   4068  C   THR B  30      22.834 -44.808   6.810  1.00 48.29           C  
ANISOU 4068  C   THR B  30     3959   5051   9335   -497   -465   -442       C  
ATOM   4069  O   THR B  30      22.466 -45.708   6.052  1.00 49.16           O  
ANISOU 4069  O   THR B  30     4070   5108   9500   -510   -598   -484       O  
ATOM   4070  CB  THR B  30      22.123 -42.795   5.543  1.00 48.20           C  
ANISOU 4070  CB  THR B  30     3851   5104   9359   -426   -558   -433       C  
ATOM   4071  OG1 THR B  30      23.489 -42.467   5.259  1.00 47.10           O  
ANISOU 4071  OG1 THR B  30     3841   5040   9014   -368   -537   -440       O  
ATOM   4072  CG2 THR B  30      21.279 -41.528   5.531  1.00 48.68           C  
ANISOU 4072  CG2 THR B  30     3787   5162   9546   -413   -541   -398       C  
ATOM   4073  N   LEU B  31      23.923 -44.910   7.572  1.00 47.83           N  
ANISOU 4073  N   LEU B  31     3994   5025   9151   -486   -369   -422       N  
ATOM   4074  CA  LEU B  31      24.854 -46.033   7.451  1.00 47.94           C  
ANISOU 4074  CA  LEU B  31     4111   5015   9086   -471   -418   -446       C  
ATOM   4075  C   LEU B  31      24.281 -47.333   8.014  1.00 49.12           C  
ANISOU 4075  C   LEU B  31     4242   5061   9359   -544   -424   -428       C  
ATOM   4076  O   LEU B  31      23.647 -47.336   9.071  1.00 49.72           O  
ANISOU 4076  O   LEU B  31     4267   5108   9514   -613   -317   -368       O  
ATOM   4077  CB  LEU B  31      26.169 -45.701   8.165  1.00 46.84           C  
ANISOU 4077  CB  LEU B  31     4056   4933   8808   -439   -330   -417       C  
ATOM   4078  CG  LEU B  31      27.346 -46.658   7.959  1.00 46.70           C  
ANISOU 4078  CG  LEU B  31     4130   4894   8718   -399   -380   -442       C  
ATOM   4079  CD1 LEU B  31      27.861 -46.597   6.530  1.00 46.59           C  
ANISOU 4079  CD1 LEU B  31     4153   4915   8633   -325   -465   -519       C  
ATOM   4080  CD2 LEU B  31      28.461 -46.334   8.941  1.00 46.10           C  
ANISOU 4080  CD2 LEU B  31     4106   4858   8549   -387   -302   -394       C  
ATOM   4081  N   GLY B  32      24.521 -48.432   7.302  1.00 49.87           N  
ANISOU 4081  N   GLY B  32     4385   5094   9467   -531   -540   -482       N  
ATOM   4082  CA  GLY B  32      24.121 -49.763   7.754  1.00 51.34           C  
ANISOU 4082  CA  GLY B  32     4565   5162   9779   -598   -561   -465       C  
ATOM   4083  C   GLY B  32      22.746 -50.173   7.262  1.00 53.02           C  
ANISOU 4083  C   GLY B  32     4671   5294  10177   -660   -648   -492       C  
ATOM   4084  O   GLY B  32      21.998 -49.343   6.744  1.00 53.32           O  
ANISOU 4084  O   GLY B  32     4626   5373  10259   -656   -682   -509       O  
ATOM   4085  N   PRO B  33      22.402 -51.463   7.424  1.00 54.54           N  
ANISOU 4085  N   PRO B  33     4859   5362  10501   -721   -696   -492       N  
ATOM   4086  CA  PRO B  33      21.108 -51.983   6.983  1.00 56.20           C  
ANISOU 4086  CA  PRO B  33     4956   5475  10920   -793   -794   -520       C  
ATOM   4087  C   PRO B  33      19.930 -51.475   7.819  1.00 56.91           C  
ANISOU 4087  C   PRO B  33     4895   5556  11169   -875   -674   -436       C  
ATOM   4088  O   PRO B  33      18.799 -51.474   7.335  1.00 58.25           O  
ANISOU 4088  O   PRO B  33     4933   5675  11522   -920   -756   -461       O  
ATOM   4089  CB  PRO B  33      21.266 -53.499   7.134  1.00 57.30           C  
ANISOU 4089  CB  PRO B  33     5144   5472  11155   -837   -849   -528       C  
ATOM   4090  CG  PRO B  33      22.275 -53.666   8.213  1.00 56.57           C  
ANISOU 4090  CG  PRO B  33     5146   5395  10952   -823   -720   -441       C  
ATOM   4091  CD  PRO B  33      23.217 -52.503   8.081  1.00 54.91           C  
ANISOU 4091  CD  PRO B  33     4998   5337  10529   -728   -669   -455       C  
ATOM   4092  N   LYS B  34      20.191 -51.056   9.057  1.00 56.40           N  
ANISOU 4092  N   LYS B  34     4850   5537  11040   -895   -482   -343       N  
ATOM   4093  CA  LYS B  34      19.172 -50.418   9.893  1.00 56.83           C  
ANISOU 4093  CA  LYS B  34     4775   5600  11217   -961   -323   -278       C  
ATOM   4094  C   LYS B  34      19.334 -48.893   9.859  1.00 55.15           C  
ANISOU 4094  C   LYS B  34     4545   5511  10899   -892   -255   -292       C  
ATOM   4095  O   LYS B  34      19.037 -48.208  10.842  1.00 54.93           O  
ANISOU 4095  O   LYS B  34     4478   5519  10874   -921    -70   -242       O  
ATOM   4096  CB  LYS B  34      19.265 -50.917  11.340  1.00 57.64           C  
ANISOU 4096  CB  LYS B  34     4927   5671  11303  -1041   -139   -170       C  
ATOM   4097  CG  LYS B  34      19.332 -52.428  11.503  1.00 58.98           C  
ANISOU 4097  CG  LYS B  34     5144   5709  11557  -1105   -199   -131       C  
ATOM   4098  CD  LYS B  34      18.022 -53.117  11.164  1.00 61.07           C  
ANISOU 4098  CD  LYS B  34     5249   5848  12107  -1195   -252   -137       C  
ATOM   4099  CE  LYS B  34      18.087 -54.602  11.501  1.00 62.68           C  
ANISOU 4099  CE  LYS B  34     5503   5904  12407  -1272   -286    -80       C  
ATOM   4100  NZ  LYS B  34      18.091 -54.862  12.971  1.00 63.61           N  
ANISOU 4100  NZ  LYS B  34     5673   6007  12489  -1357    -76     67       N  
ATOM   4101  N   GLY B  35      19.797 -48.369   8.724  1.00 53.64           N  
ANISOU 4101  N   GLY B  35     4388   5377  10612   -805   -397   -362       N  
ATOM   4102  CA  GLY B  35      20.046 -46.941   8.572  1.00 52.14           C  
ANISOU 4102  CA  GLY B  35     4192   5290  10326   -736   -354   -370       C  
ATOM   4103  C   GLY B  35      18.767 -46.129   8.596  1.00 52.51           C  
ANISOU 4103  C   GLY B  35     4059   5321  10570   -759   -314   -359       C  
ATOM   4104  O   GLY B  35      17.709 -46.605   8.183  1.00 53.77           O  
ANISOU 4104  O   GLY B  35     4090   5400  10940   -806   -404   -369       O  
ATOM   4105  N   ARG B  36      18.875 -44.898   9.085  1.00 51.40           N  
ANISOU 4105  N   ARG B  36     3900   5246  10382   -724   -185   -343       N  
ATOM   4106  CA  ARG B  36      17.724 -44.023   9.263  1.00 51.98           C  
ANISOU 4106  CA  ARG B  36     3794   5296  10659   -735   -112   -335       C  
ATOM   4107  C   ARG B  36      17.523 -43.112   8.059  1.00 51.58           C  
ANISOU 4107  C   ARG B  36     3687   5267  10643   -659   -279   -359       C  
ATOM   4108  O   ARG B  36      18.435 -42.895   7.263  1.00 50.43           O  
ANISOU 4108  O   ARG B  36     3668   5182  10310   -596   -395   -378       O  
ATOM   4109  CB  ARG B  36      17.888 -43.185  10.535  1.00 51.76           C  
ANISOU 4109  CB  ARG B  36     3781   5310  10575   -742    134   -315       C  
ATOM   4110  CG  ARG B  36      18.199 -43.994  11.788  1.00 52.05           C  
ANISOU 4110  CG  ARG B  36     3913   5340  10522   -819    298   -275       C  
ATOM   4111  CD  ARG B  36      17.070 -44.945  12.155  1.00 53.87           C  
ANISOU 4111  CD  ARG B  36     4021   5475  10972   -917    355   -241       C  
ATOM   4112  NE  ARG B  36      17.407 -45.770  13.314  1.00 54.31           N  
ANISOU 4112  NE  ARG B  36     4192   5520  10923   -996    501   -180       N  
ATOM   4113  CZ  ARG B  36      17.386 -45.358  14.581  1.00 54.99           C  
ANISOU 4113  CZ  ARG B  36     4323   5639  10928  -1038    738   -151       C  
ATOM   4114  NH1 ARG B  36      17.049 -44.107  14.893  1.00 55.18           N  
ANISOU 4114  NH1 ARG B  36     4281   5705  10980  -1005    874   -194       N  
ATOM   4115  NH2 ARG B  36      17.711 -46.205  15.551  1.00 55.70           N  
ANISOU 4115  NH2 ARG B  36     4539   5718  10905  -1115    837    -79       N  
ATOM   4116  N   ASN B  37      16.311 -42.578   7.950  1.00 52.56           N  
ANISOU 4116  N   ASN B  37     3616   5336  11017   -669   -284   -352       N  
ATOM   4117  CA  ASN B  37      15.917 -41.714   6.839  1.00 52.56           C  
ANISOU 4117  CA  ASN B  37     3540   5337  11094   -604   -463   -354       C  
ATOM   4118  C   ASN B  37      16.357 -40.266   7.060  1.00 51.69           C  
ANISOU 4118  C   ASN B  37     3448   5279  10909   -532   -362   -341       C  
ATOM   4119  O   ASN B  37      16.410 -39.792   8.197  1.00 51.57           O  
ANISOU 4119  O   ASN B  37     3417   5271  10903   -545   -133   -343       O  
ATOM   4120  CB  ASN B  37      14.392 -41.786   6.647  1.00 54.29           C  
ANISOU 4120  CB  ASN B  37     3513   5454  11657   -643   -531   -346       C  
ATOM   4121  CG  ASN B  37      13.965 -42.892   5.700  1.00 55.15           C  
ANISOU 4121  CG  ASN B  37     3607   5509  11836   -685   -778   -367       C  
ATOM   4122  OD1 ASN B  37      13.157 -43.731   6.069  1.00 56.46           O  
ANISOU 4122  OD1 ASN B  37     3648   5592  12211   -767   -754   -368       O  
ATOM   4123  ND2 ASN B  37      14.500 -42.905   4.481  1.00 54.72           N  
ANISOU 4123  ND2 ASN B  37     3683   5498  11608   -636  -1009   -389       N  
ATOM   4124  N   VAL B  38      16.684 -39.580   5.967  1.00 51.26           N  
ANISOU 4124  N   VAL B  38     3441   5259  10773   -463   -533   -329       N  
ATOM   4125  CA  VAL B  38      17.018 -38.156   5.997  1.00 50.75           C  
ANISOU 4125  CA  VAL B  38     3380   5222  10677   -395   -473   -306       C  
ATOM   4126  C   VAL B  38      16.112 -37.432   5.008  1.00 52.14           C  
ANISOU 4126  C   VAL B  38     3419   5345  11044   -352   -663   -268       C  
ATOM   4127  O   VAL B  38      16.064 -37.788   3.831  1.00 52.47           O  
ANISOU 4127  O   VAL B  38     3508   5396  11030   -341   -900   -253       O  
ATOM   4128  CB  VAL B  38      18.495 -37.903   5.624  1.00 49.22           C  
ANISOU 4128  CB  VAL B  38     3399   5123  10177   -350   -490   -302       C  
ATOM   4129  CG1 VAL B  38      18.827 -36.418   5.707  1.00 48.85           C  
ANISOU 4129  CG1 VAL B  38     3348   5088  10123   -291   -423   -275       C  
ATOM   4130  CG2 VAL B  38      19.422 -38.699   6.532  1.00 48.08           C  
ANISOU 4130  CG2 VAL B  38     3385   5023   9860   -389   -346   -333       C  
ATOM   4131  N   VAL B  39      15.393 -36.420   5.488  1.00 53.30           N  
ANISOU 4131  N   VAL B  39     3402   5432  11418   -326   -562   -254       N  
ATOM   4132  CA  VAL B  39      14.446 -35.675   4.657  1.00 55.19           C  
ANISOU 4132  CA  VAL B  39     3479   5598  11890   -280   -744   -206       C  
ATOM   4133  C   VAL B  39      15.117 -34.419   4.106  1.00 55.10           C  
ANISOU 4133  C   VAL B  39     3558   5615  11763   -202   -797   -154       C  
ATOM   4134  O   VAL B  39      15.482 -33.520   4.865  1.00 54.67           O  
ANISOU 4134  O   VAL B  39     3504   5554  11711   -173   -605   -166       O  
ATOM   4135  CB  VAL B  39      13.178 -35.283   5.445  1.00 56.68           C  
ANISOU 4135  CB  VAL B  39     3401   5679  12453   -289   -605   -220       C  
ATOM   4136  CG1 VAL B  39      12.133 -34.682   4.518  1.00 58.48           C  
ANISOU 4136  CG1 VAL B  39     3439   5817  12963   -242   -838   -163       C  
ATOM   4137  CG2 VAL B  39      12.595 -36.494   6.158  1.00 57.29           C  
ANISOU 4137  CG2 VAL B  39     3397   5731  12640   -379   -496   -262       C  
ATOM   4138  N   LEU B  40      15.277 -34.370   2.786  1.00 55.89           N  
ANISOU 4138  N   LEU B  40     3741   5740  11753   -174  -1057    -96       N  
ATOM   4139  CA  LEU B  40      15.906 -33.241   2.109  1.00 56.02           C  
ANISOU 4139  CA  LEU B  40     3856   5780  11649   -108  -1129    -23       C  
ATOM   4140  C   LEU B  40      14.838 -32.385   1.441  1.00 58.66           C  
ANISOU 4140  C   LEU B  40     4020   6014  12252    -61  -1319     57       C  
ATOM   4141  O   LEU B  40      14.100 -32.862   0.582  1.00 59.91           O  
ANISOU 4141  O   LEU B  40     4126   6146  12490    -74  -1566     87       O  
ATOM   4142  CB  LEU B  40      16.905 -33.739   1.065  1.00 55.16           C  
ANISOU 4142  CB  LEU B  40     3986   5775  11198   -111  -1272     -3       C  
ATOM   4143  CG  LEU B  40      17.974 -34.712   1.568  1.00 53.45           C  
ANISOU 4143  CG  LEU B  40     3928   5646  10732   -150  -1125    -80       C  
ATOM   4144  CD1 LEU B  40      18.806 -35.230   0.405  1.00 53.28           C  
ANISOU 4144  CD1 LEU B  40     4116   5711  10415   -146  -1273    -72       C  
ATOM   4145  CD2 LEU B  40      18.865 -34.063   2.616  1.00 52.08           C  
ANISOU 4145  CD2 LEU B  40     3798   5498  10490   -138   -874    -98       C  
ATOM   4146  N   ASP B  41      14.766 -31.119   1.839  1.00 60.10           N  
ANISOU 4146  N   ASP B  41     4117   6132  12585     -7  -1215     91       N  
ATOM   4147  CA  ASP B  41      13.736 -30.205   1.352  1.00 63.34           C  
ANISOU 4147  CA  ASP B  41     4338   6422  13304     48  -1374    172       C  
ATOM   4148  C   ASP B  41      14.031 -29.734  -0.070  1.00 65.62           C  
ANISOU 4148  C   ASP B  41     4760   6733  13437     84  -1659    300       C  
ATOM   4149  O   ASP B  41      15.182 -29.717  -0.506  1.00 64.45           O  
ANISOU 4149  O   ASP B  41     4845   6686  12954     79  -1652    326       O  
ATOM   4150  CB  ASP B  41      13.630 -28.994   2.289  1.00 63.26           C  
ANISOU 4150  CB  ASP B  41     4205   6321  13509     99  -1150    153       C  
ATOM   4151  CG  ASP B  41      12.348 -28.195   2.092  1.00 65.36           C  
ANISOU 4151  CG  ASP B  41     4205   6431  14197    158  -1263    208       C  
ATOM   4152  OD1 ASP B  41      11.327 -28.773   1.664  1.00 66.67           O  
ANISOU 4152  OD1 ASP B  41     4216   6550  14564    142  -1443    226       O  
ATOM   4153  OD2 ASP B  41      12.363 -26.980   2.381  1.00 65.56           O  
ANISOU 4153  OD2 ASP B  41     4165   6368  14375    221  -1174    230       O  
ATOM   4154  N   LYS B  42      12.972 -29.366  -0.784  1.00 70.10           N  
ANISOU 4154  N   LYS B  42     5174   7204  14255    116  -1909    385       N  
ATOM   4155  CA  LYS B  42      13.073 -28.761  -2.110  1.00 73.12           C  
ANISOU 4155  CA  LYS B  42     5668   7587  14527    152  -2198    532       C  
ATOM   4156  C   LYS B  42      12.178 -27.528  -2.159  1.00 76.53           C  
ANISOU 4156  C   LYS B  42     5880   7858  15339    226  -2290    629       C  
ATOM   4157  O   LYS B  42      11.165 -27.463  -1.458  1.00 78.05           O  
ANISOU 4157  O   LYS B  42     5802   7938  15914    242  -2220    577       O  
ATOM   4158  CB  LYS B  42      12.630 -29.752  -3.183  1.00 74.69           C  
ANISOU 4158  CB  LYS B  42     5931   7830  14615    109  -2509    549       C  
ATOM   4159  CG  LYS B  42      13.595 -30.904  -3.418  1.00 73.33           C  
ANISOU 4159  CG  LYS B  42     6010   7808  14042     47  -2464    466       C  
ATOM   4160  CD  LYS B  42      12.914 -32.084  -4.101  1.00 74.99           C  
ANISOU 4160  CD  LYS B  42     6219   8030  14243     -6  -2719    423       C  
ATOM   4161  CE  LYS B  42      12.127 -31.670  -5.338  1.00 77.91           C  
ANISOU 4161  CE  LYS B  42     6569   8346  14685     13  -3106    548       C  
ATOM   4162  NZ  LYS B  42      11.539 -32.842  -6.042  1.00 79.47           N  
ANISOU 4162  NZ  LYS B  42     6791   8559  14845    -48  -3374    490       N  
ATOM   4163  N   SER B  43      12.548 -26.557  -2.990  1.00 78.36           N  
ANISOU 4163  N   SER B  43     6224   8071  15478    272  -2439    776       N  
ATOM   4164  CA  SER B  43      11.778 -25.317  -3.115  1.00 81.06           C  
ANISOU 4164  CA  SER B  43     6371   8244  16182    351  -2548    889       C  
ATOM   4165  C   SER B  43      10.375 -25.576  -3.674  1.00 84.24           C  
ANISOU 4165  C   SER B  43     6555   8547  16903    363  -2858    941       C  
ATOM   4166  O   SER B  43       9.393 -25.021  -3.175  1.00 86.32           O  
ANISOU 4166  O   SER B  43     6526   8653  17617    417  -2837    938       O  
ATOM   4167  CB  SER B  43      12.521 -24.305  -3.990  1.00 81.64           C  
ANISOU 4167  CB  SER B  43     6639   8319  16058    385  -2667   1060       C  
ATOM   4168  OG  SER B  43      12.814 -24.846  -5.266  1.00 82.58           O  
ANISOU 4168  OG  SER B  43     6987   8551  15836    346  -2937   1153       O  
ATOM   4169  N   PHE B  44      10.291 -26.422  -4.701  1.00 85.01           N  
ANISOU 4169  N   PHE B  44     6790   8732  16777    314  -3143    980       N  
ATOM   4170  CA  PHE B  44       9.011 -26.808  -5.299  1.00 87.42           C  
ANISOU 4170  CA  PHE B  44     6907   8954  17354    309  -3478   1022       C  
ATOM   4171  C   PHE B  44       8.674 -28.259  -4.959  1.00 85.65           C  
ANISOU 4171  C   PHE B  44     6633   8792  17117    227  -3442    867       C  
ATOM   4172  O   PHE B  44       9.561 -29.114  -4.900  1.00 83.58           O  
ANISOU 4172  O   PHE B  44     6598   8673  16483    167  -3316    776       O  
ATOM   4173  CB  PHE B  44       9.053 -26.629  -6.821  1.00 90.08           C  
ANISOU 4173  CB  PHE B  44     7444   9325  17456    309  -3888   1193       C  
ATOM   4174  CG  PHE B  44       9.160 -25.193  -7.265  1.00 92.16           C  
ANISOU 4174  CG  PHE B  44     7725   9494  17796    388  -3988   1383       C  
ATOM   4175  CD1 PHE B  44       8.017 -24.416  -7.439  1.00 95.23           C  
ANISOU 4175  CD1 PHE B  44     7842   9696  18644    457  -4215   1497       C  
ATOM   4176  CD2 PHE B  44      10.402 -24.617  -7.519  1.00 91.03           C  
ANISOU 4176  CD2 PHE B  44     7860   9436  17289    392  -3858   1455       C  
ATOM   4177  CE1 PHE B  44       8.112 -23.094  -7.851  1.00 96.89           C  
ANISOU 4177  CE1 PHE B  44     8069   9800  18944    531  -4316   1684       C  
ATOM   4178  CE2 PHE B  44      10.503 -23.296  -7.930  1.00 92.65           C  
ANISOU 4178  CE2 PHE B  44     8083   9540  17577    456  -3948   1642       C  
ATOM   4179  CZ  PHE B  44       9.357 -22.533  -8.097  1.00 95.61           C  
ANISOU 4179  CZ  PHE B  44     8198   9723  18406    527  -4182   1760       C  
ATOM   4180  N   GLY B  45       7.389 -28.524  -4.732  1.00 86.18           N  
ANISOU 4180  N   GLY B  45     6389   8739  17617    225  -3552    840       N  
ATOM   4181  CA  GLY B  45       6.903 -29.881  -4.484  1.00 84.99           C  
ANISOU 4181  CA  GLY B  45     6155   8616  17518    140  -3558    713       C  
ATOM   4182  C   GLY B  45       7.181 -30.392  -3.082  1.00 81.63           C  
ANISOU 4182  C   GLY B  45     5663   8219  17131    104  -3124    557       C  
ATOM   4183  O   GLY B  45       7.527 -29.622  -2.183  1.00 80.63           O  
ANISOU 4183  O   GLY B  45     5492   8067  17076    151  -2816    534       O  
ATOM   4184  N   ALA B  46       7.029 -31.702  -2.907  1.00 79.75           N  
ANISOU 4184  N   ALA B  46     5429   8029  16840     16  -3110    451       N  
ATOM   4185  CA  ALA B  46       7.220 -32.354  -1.612  1.00 76.82           C  
ANISOU 4185  CA  ALA B  46     5004   7684  16496    -33  -2728    318       C  
ATOM   4186  C   ALA B  46       8.696 -32.688  -1.379  1.00 72.73           C  
ANISOU 4186  C   ALA B  46     4819   7322  15492    -55  -2521    265       C  
ATOM   4187  O   ALA B  46       9.468 -32.761  -2.334  1.00 72.07           O  
ANISOU 4187  O   ALA B  46     4999   7333  15052    -52  -2698    308       O  
ATOM   4188  CB  ALA B  46       6.375 -33.615  -1.535  1.00 77.95           C  
ANISOU 4188  CB  ALA B  46     4995   7791  16832   -122  -2814    245       C  
ATOM   4189  N   PRO B  47       9.092 -32.904  -0.108  1.00 69.75           N  
ANISOU 4189  N   PRO B  47     4431   6970  15098    -78  -2147    171       N  
ATOM   4190  CA  PRO B  47      10.498 -33.188   0.189  1.00 66.37           C  
ANISOU 4190  CA  PRO B  47     4293   6678  14246    -95  -1957    124       C  
ATOM   4191  C   PRO B  47      10.941 -34.579  -0.254  1.00 64.90           C  
ANISOU 4191  C   PRO B  47     4289   6581  13789   -169  -2059     67       C  
ATOM   4192  O   PRO B  47      10.105 -35.443  -0.518  1.00 66.44           O  
ANISOU 4192  O   PRO B  47     4367   6726  14149   -224  -2219     39       O  
ATOM   4193  CB  PRO B  47      10.576 -33.077   1.722  1.00 65.47           C  
ANISOU 4193  CB  PRO B  47     4085   6547  14243   -107  -1562     42       C  
ATOM   4194  CG  PRO B  47       9.275 -32.500   2.164  1.00 67.90           C  
ANISOU 4194  CG  PRO B  47     4064   6709  15022    -79  -1520     50       C  
ATOM   4195  CD  PRO B  47       8.279 -32.884   1.119  1.00 70.28           C  
ANISOU 4195  CD  PRO B  47     4226   6945  15532    -92  -1879    106       C  
ATOM   4196  N   THR B  48      12.255 -34.776  -0.318  1.00 62.05           N  
ANISOU 4196  N   THR B  48     4199   6339  13038   -170  -1963     44       N  
ATOM   4197  CA  THR B  48      12.848 -36.055  -0.697  1.00 60.68           C  
ANISOU 4197  CA  THR B  48     4217   6246  12591   -228  -2025    -22       C  
ATOM   4198  C   THR B  48      13.287 -36.818   0.550  1.00 58.75           C  
ANISOU 4198  C   THR B  48     3985   6025  12310   -277  -1727   -109       C  
ATOM   4199  O   THR B  48      14.135 -36.344   1.304  1.00 57.24           O  
ANISOU 4199  O   THR B  48     3876   5883  11989   -254  -1487   -116       O  
ATOM   4200  CB  THR B  48      14.077 -35.848  -1.605  1.00 59.52           C  
ANISOU 4200  CB  THR B  48     4361   6213  12038   -195  -2101      7       C  
ATOM   4201  OG1 THR B  48      13.712 -35.036  -2.728  1.00 61.13           O  
ANISOU 4201  OG1 THR B  48     4578   6398  12248   -151  -2366    111       O  
ATOM   4202  CG2 THR B  48      14.621 -37.181  -2.104  1.00 59.02           C  
ANISOU 4202  CG2 THR B  48     4487   6218  11717   -245  -2178    -76       C  
ATOM   4203  N   ILE B  49      12.703 -37.994   0.764  1.00 58.96           N  
ANISOU 4203  N   ILE B  49     3933   6010  12458   -350  -1755   -168       N  
ATOM   4204  CA  ILE B  49      13.110 -38.880   1.852  1.00 57.30           C  
ANISOU 4204  CA  ILE B  49     3759   5817  12196   -407  -1508   -233       C  
ATOM   4205  C   ILE B  49      14.119 -39.873   1.280  1.00 56.02           C  
ANISOU 4205  C   ILE B  49     3846   5732  11705   -426  -1589   -283       C  
ATOM   4206  O   ILE B  49      13.844 -40.514   0.267  1.00 57.17           O  
ANISOU 4206  O   ILE B  49     4038   5866  11818   -447  -1842   -307       O  
ATOM   4207  CB  ILE B  49      11.898 -39.629   2.449  1.00 58.70           C  
ANISOU 4207  CB  ILE B  49     3701   5888  12711   -484  -1473   -258       C  
ATOM   4208  CG1 ILE B  49      10.819 -38.633   2.891  1.00 60.01           C  
ANISOU 4208  CG1 ILE B  49     3594   5966  13239   -456  -1402   -217       C  
ATOM   4209  CG2 ILE B  49      12.324 -40.485   3.633  1.00 57.62           C  
ANISOU 4209  CG2 ILE B  49     3616   5765  12509   -547  -1205   -302       C  
ATOM   4210  CD1 ILE B  49       9.473 -39.264   3.167  1.00 62.10           C  
ANISOU 4210  CD1 ILE B  49     3589   6115  13891   -527  -1426   -229       C  
ATOM   4211  N   THR B  50      15.280 -39.998   1.922  1.00 53.93           N  
ANISOU 4211  N   THR B  50     3739   5540  11209   -418  -1382   -306       N  
ATOM   4212  CA  THR B  50      16.361 -40.836   1.389  1.00 52.99           C  
ANISOU 4212  CA  THR B  50     3851   5492  10791   -419  -1434   -356       C  
ATOM   4213  C   THR B  50      17.277 -41.423   2.466  1.00 51.55           C  
ANISOU 4213  C   THR B  50     3759   5340  10486   -441  -1197   -388       C  
ATOM   4214  O   THR B  50      17.423 -40.860   3.552  1.00 50.74           O  
ANISOU 4214  O   THR B  50     3607   5244  10427   -438   -980   -363       O  
ATOM   4215  CB  THR B  50      17.228 -40.045   0.386  1.00 52.36           C  
ANISOU 4215  CB  THR B  50     3942   5500  10452   -348  -1526   -324       C  
ATOM   4216  OG1 THR B  50      18.222 -40.907  -0.181  1.00 51.75           O  
ANISOU 4216  OG1 THR B  50     4074   5484  10104   -347  -1564   -387       O  
ATOM   4217  CG2 THR B  50      17.912 -38.858   1.061  1.00 51.05           C  
ANISOU 4217  CG2 THR B  50     3788   5377  10230   -299  -1322   -273       C  
ATOM   4218  N   LYS B  51      17.886 -42.563   2.142  1.00 51.51           N  
ANISOU 4218  N   LYS B  51     3893   5348  10329   -461  -1251   -447       N  
ATOM   4219  CA  LYS B  51      18.914 -43.186   2.978  1.00 50.32           C  
ANISOU 4219  CA  LYS B  51     3854   5225  10038   -471  -1074   -469       C  
ATOM   4220  C   LYS B  51      20.261 -43.205   2.244  1.00 49.43           C  
ANISOU 4220  C   LYS B  51     3945   5198   9635   -411  -1104   -500       C  
ATOM   4221  O   LYS B  51      21.128 -44.027   2.547  1.00 48.82           O  
ANISOU 4221  O   LYS B  51     3973   5130   9447   -414  -1036   -538       O  
ATOM   4222  CB  LYS B  51      18.502 -44.614   3.360  1.00 51.10           C  
ANISOU 4222  CB  LYS B  51     3923   5240  10253   -547  -1087   -509       C  
ATOM   4223  CG  LYS B  51      17.181 -44.706   4.108  1.00 52.43           C  
ANISOU 4223  CG  LYS B  51     3880   5318  10722   -618  -1030   -476       C  
ATOM   4224  CD  LYS B  51      16.928 -46.107   4.644  1.00 53.21           C  
ANISOU 4224  CD  LYS B  51     3963   5329  10923   -702  -1002   -495       C  
ATOM   4225  CE  LYS B  51      15.747 -46.144   5.607  1.00 54.52           C  
ANISOU 4225  CE  LYS B  51     3923   5416  11376   -780   -872   -447       C  
ATOM   4226  NZ  LYS B  51      15.637 -47.459   6.296  1.00 55.21           N  
ANISOU 4226  NZ  LYS B  51     4014   5419  11541   -868   -802   -440       N  
ATOM   4227  N   ASP B  52      20.430 -42.295   1.285  1.00 49.58           N  
ANISOU 4227  N   ASP B  52     4015   5275   9548   -358  -1200   -476       N  
ATOM   4228  CA  ASP B  52      21.645 -42.216   0.477  1.00 49.12           C  
ANISOU 4228  CA  ASP B  52     4142   5301   9220   -304  -1215   -499       C  
ATOM   4229  C   ASP B  52      22.547 -41.111   1.021  1.00 47.86           C  
ANISOU 4229  C   ASP B  52     4005   5206   8972   -262  -1042   -440       C  
ATOM   4230  O   ASP B  52      22.234 -39.928   0.898  1.00 48.11           O  
ANISOU 4230  O   ASP B  52     3979   5247   9050   -238  -1047   -373       O  
ATOM   4231  CB  ASP B  52      21.284 -41.941  -0.989  1.00 50.59           C  
ANISOU 4231  CB  ASP B  52     4393   5510   9315   -283  -1433   -500       C  
ATOM   4232  CG  ASP B  52      22.469 -42.101  -1.937  1.00 50.67           C  
ANISOU 4232  CG  ASP B  52     4613   5606   9033   -239  -1440   -542       C  
ATOM   4233  OD1 ASP B  52      23.624 -42.203  -1.470  1.00 49.72           O  
ANISOU 4233  OD1 ASP B  52     4559   5527   8804   -213  -1269   -557       O  
ATOM   4234  OD2 ASP B  52      22.242 -42.123  -3.165  1.00 52.02           O  
ANISOU 4234  OD2 ASP B  52     4880   5800   9082   -231  -1618   -561       O  
ATOM   4235  N   GLY B  53      23.670 -41.504   1.615  1.00 46.91           N  
ANISOU 4235  N   GLY B  53     3964   5117   8743   -252   -902   -465       N  
ATOM   4236  CA  GLY B  53      24.617 -40.554   2.196  1.00 45.89           C  
ANISOU 4236  CA  GLY B  53     3855   5041   8538   -221   -748   -420       C  
ATOM   4237  C   GLY B  53      25.241 -39.598   1.194  1.00 46.13           C  
ANISOU 4237  C   GLY B  53     3966   5139   8420   -170   -779   -382       C  
ATOM   4238  O   GLY B  53      25.662 -38.502   1.560  1.00 45.41           O  
ANISOU 4238  O   GLY B  53     3855   5072   8326   -152   -684   -327       O  
ATOM   4239  N   VAL B  54      25.304 -40.013  -0.070  1.00 47.33           N  
ANISOU 4239  N   VAL B  54     4219   5319   8443   -153   -907   -412       N  
ATOM   4240  CA  VAL B  54      25.823 -39.162  -1.140  1.00 48.03           C  
ANISOU 4240  CA  VAL B  54     4406   5475   8367   -114   -938   -363       C  
ATOM   4241  C   VAL B  54      24.849 -38.021  -1.428  1.00 48.84           C  
ANISOU 4241  C   VAL B  54     4427   5552   8575   -113  -1036   -270       C  
ATOM   4242  O   VAL B  54      25.262 -36.872  -1.585  1.00 48.63           O  
ANISOU 4242  O   VAL B  54     4413   5553   8509    -88   -985   -189       O  
ATOM   4243  CB  VAL B  54      26.073 -39.965  -2.436  1.00 49.29           C  
ANISOU 4243  CB  VAL B  54     4718   5673   8335   -102  -1049   -431       C  
ATOM   4244  CG1 VAL B  54      26.502 -39.041  -3.571  1.00 50.18           C  
ANISOU 4244  CG1 VAL B  54     4945   5859   8259    -72  -1076   -362       C  
ATOM   4245  CG2 VAL B  54      27.125 -41.040  -2.199  1.00 48.75           C  
ANISOU 4245  CG2 VAL B  54     4720   5616   8183    -89   -940   -527       C  
ATOM   4246  N   SER B  55      23.561 -38.350  -1.497  1.00 49.90           N  
ANISOU 4246  N   SER B  55     4468   5622   8866   -141  -1180   -279       N  
ATOM   4247  CA  SER B  55      22.515 -37.355  -1.727  1.00 51.07           C  
ANISOU 4247  CA  SER B  55     4508   5725   9169   -135  -1292   -193       C  
ATOM   4248  C   SER B  55      22.407 -36.377  -0.559  1.00 50.36           C  
ANISOU 4248  C   SER B  55     4280   5594   9259   -128  -1131   -146       C  
ATOM   4249  O   SER B  55      22.211 -35.179  -0.765  1.00 50.76           O  
ANISOU 4249  O   SER B  55     4289   5627   9370   -100  -1151    -61       O  
ATOM   4250  CB  SER B  55      21.165 -38.041  -1.945  1.00 52.40           C  
ANISOU 4250  CB  SER B  55     4575   5821   9510   -171  -1477   -225       C  
ATOM   4251  OG  SER B  55      21.248 -39.012  -2.971  1.00 53.41           O  
ANISOU 4251  OG  SER B  55     4842   5978   9473   -185  -1632   -292       O  
ATOM   4252  N   VAL B  56      22.532 -36.896   0.661  1.00 49.53           N  
ANISOU 4252  N   VAL B  56     4115   5469   9235   -156   -976   -204       N  
ATOM   4253  CA  VAL B  56      22.481 -36.068   1.864  1.00 49.05           C  
ANISOU 4253  CA  VAL B  56     3950   5374   9313   -157   -806   -186       C  
ATOM   4254  C   VAL B  56      23.682 -35.131   1.905  1.00 48.53           C  
ANISOU 4254  C   VAL B  56     3969   5359   9110   -124   -699   -148       C  
ATOM   4255  O   VAL B  56      23.524 -33.929   2.104  1.00 48.59           O  
ANISOU 4255  O   VAL B  56     3915   5333   9215   -103   -659    -96       O  
ATOM   4256  CB  VAL B  56      22.443 -36.926   3.150  1.00 48.35           C  
ANISOU 4256  CB  VAL B  56     3817   5263   9288   -203   -664   -251       C  
ATOM   4257  CG1 VAL B  56      22.643 -36.064   4.392  1.00 47.77           C  
ANISOU 4257  CG1 VAL B  56     3690   5175   9284   -206   -473   -247       C  
ATOM   4258  CG2 VAL B  56      21.124 -37.681   3.245  1.00 49.33           C  
ANISOU 4258  CG2 VAL B  56     3819   5318   9607   -245   -742   -274       C  
ATOM   4259  N   ALA B  57      24.876 -35.691   1.717  1.00 48.42           N  
ANISOU 4259  N   ALA B  57     4086   5414   8896   -121   -653   -178       N  
ATOM   4260  CA  ALA B  57      26.117 -34.912   1.740  1.00 48.17           C  
ANISOU 4260  CA  ALA B  57     4125   5429   8746    -98   -549   -145       C  
ATOM   4261  C   ALA B  57      26.063 -33.736   0.772  1.00 49.57           C  
ANISOU 4261  C   ALA B  57     4323   5608   8903    -68   -620    -49       C  
ATOM   4262  O   ALA B  57      26.387 -32.610   1.143  1.00 49.60           O  
ANISOU 4262  O   ALA B  57     4292   5588   8963    -58   -539     -1       O  
ATOM   4263  CB  ALA B  57      27.308 -35.800   1.419  1.00 47.74           C  
ANISOU 4263  CB  ALA B  57     4192   5442   8502    -93   -514   -191       C  
ATOM   4264  N   ARG B  58      25.621 -34.001  -0.456  1.00 51.45           N  
ANISOU 4264  N   ARG B  58     4622   5864   9062    -57   -781    -19       N  
ATOM   4265  CA  ARG B  58      25.545 -32.979  -1.507  1.00 53.11           C  
ANISOU 4265  CA  ARG B  58     4878   6078   9221    -33   -876     92       C  
ATOM   4266  C   ARG B  58      24.829 -31.701  -1.053  1.00 52.97           C  
ANISOU 4266  C   ARG B  58     4725   5971   9427    -19   -878    167       C  
ATOM   4267  O   ARG B  58      25.243 -30.598  -1.405  1.00 53.23           O  
ANISOU 4267  O   ARG B  58     4786   5994   9443      0   -859    262       O  
ATOM   4268  CB  ARG B  58      24.843 -33.540  -2.749  1.00 55.67           C  
ANISOU 4268  CB  ARG B  58     5277   6420   9452    -33  -1089    104       C  
ATOM   4269  CG  ARG B  58      25.207 -32.826  -4.043  1.00 58.15           C  
ANISOU 4269  CG  ARG B  58     5730   6781   9583    -16  -1173    215       C  
ATOM   4270  CD  ARG B  58      24.207 -33.099  -5.162  1.00 61.05           C  
ANISOU 4270  CD  ARG B  58     6149   7143   9903    -19  -1430    248       C  
ATOM   4271  NE  ARG B  58      23.751 -34.492  -5.205  1.00 62.20           N  
ANISOU 4271  NE  ARG B  58     6305   7295  10033    -44  -1517    120       N  
ATOM   4272  CZ  ARG B  58      24.463 -35.525  -5.663  1.00 62.95           C  
ANISOU 4272  CZ  ARG B  58     6549   7462   9907    -52  -1485     22       C  
ATOM   4273  NH1 ARG B  58      25.702 -35.359  -6.126  1.00 63.12           N  
ANISOU 4273  NH1 ARG B  58     6718   7565   9698    -37  -1351     34       N  
ATOM   4274  NH2 ARG B  58      23.930 -36.744  -5.651  1.00 63.47           N  
ANISOU 4274  NH2 ARG B  58     6606   7505  10003    -77  -1579    -92       N  
ATOM   4275  N   GLU B  59      23.765 -31.859  -0.268  1.00 52.67           N  
ANISOU 4275  N   GLU B  59     4538   5859   9612    -28   -887    123       N  
ATOM   4276  CA  GLU B  59      22.955 -30.728   0.188  1.00 52.99           C  
ANISOU 4276  CA  GLU B  59     4430   5800   9903     -7   -881    172       C  
ATOM   4277  C   GLU B  59      23.613 -29.885   1.284  1.00 51.69           C  
ANISOU 4277  C   GLU B  59     4231   5607   9801     -6   -678    149       C  
ATOM   4278  O   GLU B  59      23.249 -28.724   1.460  1.00 52.45           O  
ANISOU 4278  O   GLU B  59     4241   5618  10066     19   -663    199       O  
ATOM   4279  CB  GLU B  59      21.596 -31.222   0.699  1.00 53.79           C  
ANISOU 4279  CB  GLU B  59     4367   5829  10238    -19   -928    120       C  
ATOM   4280  CG  GLU B  59      20.737 -31.922  -0.345  1.00 55.37           C  
ANISOU 4280  CG  GLU B  59     4566   6028  10441    -25  -1164    142       C  
ATOM   4281  CD  GLU B  59      20.327 -31.014  -1.489  1.00 57.19           C  
ANISOU 4281  CD  GLU B  59     4809   6227  10694     11  -1364    270       C  
ATOM   4282  OE1 GLU B  59      20.034 -29.824  -1.242  1.00 57.84           O  
ANISOU 4282  OE1 GLU B  59     4790   6227  10957     45  -1337    339       O  
ATOM   4283  OE2 GLU B  59      20.287 -31.498  -2.639  1.00 58.37           O  
ANISOU 4283  OE2 GLU B  59     5074   6425  10675      4  -1554    303       O  
ATOM   4284  N   ILE B  60      24.569 -30.458   2.014  1.00 49.90           N  
ANISOU 4284  N   ILE B  60     4070   5441   9448    -33   -535     72       N  
ATOM   4285  CA  ILE B  60      25.125 -29.804   3.202  1.00 48.81           C  
ANISOU 4285  CA  ILE B  60     3902   5275   9367    -44   -360     27       C  
ATOM   4286  C   ILE B  60      25.979 -28.584   2.858  1.00 48.70           C  
ANISOU 4286  C   ILE B  60     3933   5247   9322    -27   -330    102       C  
ATOM   4287  O   ILE B  60      27.034 -28.698   2.233  1.00 48.27           O  
ANISOU 4287  O   ILE B  60     3989   5263   9088    -31   -330    141       O  
ATOM   4288  CB  ILE B  60      25.960 -30.781   4.062  1.00 47.66           C  
ANISOU 4288  CB  ILE B  60     3822   5196   9091    -81   -248    -61       C  
ATOM   4289  CG1 ILE B  60      25.097 -31.948   4.569  1.00 47.78           C  
ANISOU 4289  CG1 ILE B  60     3787   5205   9160   -108   -255   -127       C  
ATOM   4290  CG2 ILE B  60      26.606 -30.058   5.239  1.00 47.19           C  
ANISOU 4290  CG2 ILE B  60     3754   5112   9062    -98    -96   -106       C  
ATOM   4291  CD1 ILE B  60      23.948 -31.559   5.481  1.00 48.40           C  
ANISOU 4291  CD1 ILE B  60     3728   5200   9460   -118   -183   -163       C  
ATOM   4292  N   GLU B  61      25.493 -27.419   3.280  1.00 49.27           N  
ANISOU 4292  N   GLU B  61     3910   5219   9591     -9   -294    120       N  
ATOM   4293  CA  GLU B  61      26.221 -26.158   3.194  1.00 49.30           C  
ANISOU 4293  CA  GLU B  61     3934   5175   9620     -1   -248    181       C  
ATOM   4294  C   GLU B  61      25.821 -25.335   4.415  1.00 49.49           C  
ANISOU 4294  C   GLU B  61     3855   5095   9851      0   -129    101       C  
ATOM   4295  O   GLU B  61      24.631 -25.180   4.691  1.00 50.18           O  
ANISOU 4295  O   GLU B  61     3825   5105  10133     23   -141     75       O  
ATOM   4296  CB  GLU B  61      25.861 -25.416   1.905  1.00 50.56           C  
ANISOU 4296  CB  GLU B  61     4101   5293   9816     33   -394    330       C  
ATOM   4297  CG  GLU B  61      26.648 -24.133   1.670  1.00 51.05           C  
ANISOU 4297  CG  GLU B  61     4192   5299   9904     35   -354    420       C  
ATOM   4298  CD  GLU B  61      26.126 -23.320   0.496  1.00 52.70           C  
ANISOU 4298  CD  GLU B  61     4403   5443  10178     69   -506    586       C  
ATOM   4299  OE1 GLU B  61      25.435 -23.889  -0.378  1.00 53.52           O  
ANISOU 4299  OE1 GLU B  61     4530   5583  10220     85   -662    642       O  
ATOM   4300  OE2 GLU B  61      26.411 -22.104   0.445  1.00 53.25           O  
ANISOU 4300  OE2 GLU B  61     4454   5416  10360     76   -482    666       O  
ATOM   4301  N   LEU B  62      26.806 -24.824   5.150  1.00 49.01           N  
ANISOU 4301  N   LEU B  62     3834   5029   9756    -27    -12     52       N  
ATOM   4302  CA  LEU B  62      26.546 -24.129   6.413  1.00 49.40           C  
ANISOU 4302  CA  LEU B  62     3820   4990   9960    -35    114    -55       C  
ATOM   4303  C   LEU B  62      26.651 -22.612   6.269  1.00 50.41           C  
ANISOU 4303  C   LEU B  62     3905   4990  10256    -12    121     -7       C  
ATOM   4304  O   LEU B  62      27.322 -22.110   5.366  1.00 50.44           O  
ANISOU 4304  O   LEU B  62     3956   4993  10213     -9     55    110       O  
ATOM   4305  CB  LEU B  62      27.512 -24.624   7.492  1.00 48.40           C  
ANISOU 4305  CB  LEU B  62     3772   4932   9685    -89    223   -163       C  
ATOM   4306  CG  LEU B  62      27.638 -26.145   7.639  1.00 47.33           C  
ANISOU 4306  CG  LEU B  62     3693   4914   9375   -114    212   -195       C  
ATOM   4307  CD1 LEU B  62      28.590 -26.483   8.773  1.00 46.62           C  
ANISOU 4307  CD1 LEU B  62     3679   4871   9163   -165    301   -286       C  
ATOM   4308  CD2 LEU B  62      26.286 -26.802   7.873  1.00 47.78           C  
ANISOU 4308  CD2 LEU B  62     3673   4954   9525   -105    214   -232       C  
ATOM   4309  N   GLU B  63      25.981 -21.893   7.169  1.00 51.38           N  
ANISOU 4309  N   GLU B  63     3942   4999  10580      1    213   -101       N  
ATOM   4310  CA  GLU B  63      25.950 -20.431   7.129  1.00 52.88           C  
ANISOU 4310  CA  GLU B  63     4077   5037  10976     28    224    -75       C  
ATOM   4311  C   GLU B  63      27.278 -19.840   7.564  1.00 52.62           C  
ANISOU 4311  C   GLU B  63     4129   4998  10865    -19    287   -108       C  
ATOM   4312  O   GLU B  63      27.818 -18.960   6.891  1.00 53.47           O  
ANISOU 4312  O   GLU B  63     4246   5041  11028    -16    236      0       O  
ATOM   4313  CB  GLU B  63      24.840 -19.880   8.026  1.00 54.31           C  
ANISOU 4313  CB  GLU B  63     4137   5089  11406     62    326   -194       C  
ATOM   4314  CG  GLU B  63      24.640 -18.375   7.896  1.00 55.95           C  
ANISOU 4314  CG  GLU B  63     4269   5111  11875    105    324   -165       C  
ATOM   4315  CD  GLU B  63      23.481 -17.849   8.721  1.00 57.61           C  
ANISOU 4315  CD  GLU B  63     4344   5184  12360    151    438   -294       C  
ATOM   4316  OE1 GLU B  63      22.943 -18.600   9.562  1.00 57.72           O  
ANISOU 4316  OE1 GLU B  63     4338   5255  12337    135    554   -422       O  
ATOM   4317  OE2 GLU B  63      23.107 -16.673   8.529  1.00 59.50           O  
ANISOU 4317  OE2 GLU B  63     4494   5248  12862    203    422   -266       O  
ATOM   4318  N   ASP B  64      27.790 -20.312   8.698  1.00 51.96           N  
ANISOU 4318  N   ASP B  64     4103   4976  10662    -69    390   -251       N  
ATOM   4319  CA  ASP B  64      29.086 -19.861   9.201  1.00 51.84           C  
ANISOU 4319  CA  ASP B  64     4163   4961  10571   -125    429   -296       C  
ATOM   4320  C   ASP B  64      30.163 -20.217   8.184  1.00 51.13           C  
ANISOU 4320  C   ASP B  64     4132   4964  10329   -144    346   -158       C  
ATOM   4321  O   ASP B  64      30.307 -21.377   7.802  1.00 50.31           O  
ANISOU 4321  O   ASP B  64     4071   4991  10052   -147    308   -125       O  
ATOM   4322  CB  ASP B  64      29.392 -20.493  10.562  1.00 51.24           C  
ANISOU 4322  CB  ASP B  64     4153   4952  10360   -177    522   -460       C  
ATOM   4323  CG  ASP B  64      30.664 -19.948  11.194  1.00 51.19           C  
ANISOU 4323  CG  ASP B  64     4215   4929  10306   -238    539   -523       C  
ATOM   4324  OD1 ASP B  64      31.749 -20.096  10.596  1.00 50.63           O  
ANISOU 4324  OD1 ASP B  64     4174   4914  10146   -263    474   -432       O  
ATOM   4325  OD2 ASP B  64      30.580 -19.381  12.302  1.00 52.04           O  
ANISOU 4325  OD2 ASP B  64     4343   4965  10465   -263    621   -671       O  
ATOM   4326  N   LYS B  65      30.914 -19.208   7.757  1.00 51.87           N  
ANISOU 4326  N   LYS B  65     4225   4982  10499   -160    329    -82       N  
ATOM   4327  CA  LYS B  65      31.874 -19.355   6.667  1.00 51.95           C  
ANISOU 4327  CA  LYS B  65     4280   5063  10397   -176    276     65       C  
ATOM   4328  C   LYS B  65      32.983 -20.356   6.994  1.00 50.55           C  
ANISOU 4328  C   LYS B  65     4164   5023  10018   -222    299     16       C  
ATOM   4329  O   LYS B  65      33.381 -21.148   6.139  1.00 49.93           O  
ANISOU 4329  O   LYS B  65     4125   5054   9792   -216    267    101       O  
ATOM   4330  CB  LYS B  65      32.498 -17.998   6.334  1.00 53.61           C  
ANISOU 4330  CB  LYS B  65     4468   5145  10756   -198    279    148       C  
ATOM   4331  CG  LYS B  65      31.525 -16.974   5.773  1.00 55.33           C  
ANISOU 4331  CG  LYS B  65     4625   5212  11184   -147    233    241       C  
ATOM   4332  CD  LYS B  65      31.180 -17.268   4.321  1.00 56.03           C  
ANISOU 4332  CD  LYS B  65     4740   5357  11190   -111    135    435       C  
ATOM   4333  CE  LYS B  65      30.619 -16.040   3.619  1.00 58.13           C  
ANISOU 4333  CE  LYS B  65     4960   5459  11667    -76     68    581       C  
ATOM   4334  NZ  LYS B  65      30.938 -16.050   2.165  1.00 59.08           N  
ANISOU 4334  NZ  LYS B  65     5153   5633  11660    -79    -10    802       N  
ATOM   4335  N   PHE B  66      33.476 -20.308   8.230  1.00 49.86           N  
ANISOU 4335  N   PHE B  66     4090   4924   9931   -267    349   -123       N  
ATOM   4336  CA  PHE B  66      34.551 -21.193   8.673  1.00 48.57           C  
ANISOU 4336  CA  PHE B  66     3973   4870   9610   -311    350   -170       C  
ATOM   4337  C   PHE B  66      34.051 -22.622   8.850  1.00 47.44           C  
ANISOU 4337  C   PHE B  66     3867   4845   9312   -290    339   -209       C  
ATOM   4338  O   PHE B  66      34.743 -23.572   8.485  1.00 46.70           O  
ANISOU 4338  O   PHE B  66     3803   4854   9086   -294    315   -174       O  
ATOM   4339  CB  PHE B  66      35.165 -20.686   9.979  1.00 48.81           C  
ANISOU 4339  CB  PHE B  66     4017   4845   9681   -370    375   -307       C  
ATOM   4340  CG  PHE B  66      35.828 -19.345   9.853  1.00 49.66           C  
ANISOU 4340  CG  PHE B  66     4086   4830   9951   -404    377   -278       C  
ATOM   4341  CD1 PHE B  66      37.093 -19.233   9.299  1.00 49.69           C  
ANISOU 4341  CD1 PHE B  66     4070   4856   9954   -442    358   -190       C  
ATOM   4342  CD2 PHE B  66      35.185 -18.194  10.285  1.00 50.58           C  
ANISOU 4342  CD2 PHE B  66     4177   4796  10244   -399    407   -342       C  
ATOM   4343  CE1 PHE B  66      37.706 -17.998   9.180  1.00 50.82           C  
ANISOU 4343  CE1 PHE B  66     4168   4874  10267   -483    363   -155       C  
ATOM   4344  CE2 PHE B  66      35.792 -16.957  10.168  1.00 51.61           C  
ANISOU 4344  CE2 PHE B  66     4270   4793  10544   -435    403   -315       C  
ATOM   4345  CZ  PHE B  66      37.053 -16.858   9.614  1.00 51.74           C  
ANISOU 4345  CZ  PHE B  66     4267   4834  10556   -482    378   -216       C  
ATOM   4346  N   GLU B  67      32.855 -22.770   9.415  1.00 47.43           N  
ANISOU 4346  N   GLU B  67     3856   4817   9347   -269    365   -283       N  
ATOM   4347  CA  GLU B  67      32.248 -24.090   9.581  1.00 46.56           C  
ANISOU 4347  CA  GLU B  67     3772   4799   9120   -255    359   -311       C  
ATOM   4348  C   GLU B  67      31.982 -24.727   8.226  1.00 46.14           C  
ANISOU 4348  C   GLU B  67     3712   4806   9013   -213    291   -193       C  
ATOM   4349  O   GLU B  67      32.219 -25.919   8.042  1.00 45.66           O  
ANISOU 4349  O   GLU B  67     3691   4841   8817   -213    265   -190       O  
ATOM   4350  CB  GLU B  67      30.948 -24.005  10.386  1.00 47.04           C  
ANISOU 4350  CB  GLU B  67     3802   4804   9264   -245    423   -404       C  
ATOM   4351  CG  GLU B  67      31.146 -23.586  11.836  1.00 47.71           C  
ANISOU 4351  CG  GLU B  67     3929   4849   9347   -292    505   -547       C  
ATOM   4352  CD  GLU B  67      29.844 -23.390  12.590  1.00 48.58           C  
ANISOU 4352  CD  GLU B  67     4006   4899   9552   -279    606   -644       C  
ATOM   4353  OE1 GLU B  67      28.781 -23.817  12.090  1.00 48.56           O  
ANISOU 4353  OE1 GLU B  67     3936   4897   9615   -238    605   -601       O  
ATOM   4354  OE2 GLU B  67      29.890 -22.805  13.694  1.00 49.57           O  
ANISOU 4354  OE2 GLU B  67     4171   4971   9691   -313    690   -772       O  
ATOM   4355  N   ASN B  68      31.496 -23.931   7.278  1.00 46.78           N  
ANISOU 4355  N   ASN B  68     3751   4824   9198   -178    255    -97       N  
ATOM   4356  CA  ASN B  68      31.244 -24.422   5.927  1.00 46.77           C  
ANISOU 4356  CA  ASN B  68     3767   4878   9125   -143    174     17       C  
ATOM   4357  C   ASN B  68      32.518 -24.968   5.297  1.00 46.58           C  
ANISOU 4357  C   ASN B  68     3807   4949   8939   -159    173     67       C  
ATOM   4358  O   ASN B  68      32.527 -26.081   4.778  1.00 46.56           O  
ANISOU 4358  O   ASN B  68     3848   5037   8803   -146    138     74       O  
ATOM   4359  CB  ASN B  68      30.660 -23.323   5.041  1.00 47.75           C  
ANISOU 4359  CB  ASN B  68     3851   4910   9382   -109    121    132       C  
ATOM   4360  CG  ASN B  68      30.207 -23.845   3.690  1.00 47.77           C  
ANISOU 4360  CG  ASN B  68     3889   4969   9292    -77     14    245       C  
ATOM   4361  OD1 ASN B  68      29.445 -24.808   3.614  1.00 47.33           O  
ANISOU 4361  OD1 ASN B  68     3830   4962   9191    -61    -36    209       O  
ATOM   4362  ND2 ASN B  68      30.669 -23.212   2.617  1.00 48.50           N  
ANISOU 4362  ND2 ASN B  68     4022   5052   9350    -73    -22    383       N  
ATOM   4363  N   MET B  69      33.594 -24.188   5.364  1.00 47.02           N  
ANISOU 4363  N   MET B  69     3861   4977   9028   -190    217     94       N  
ATOM   4364  CA  MET B  69      34.896 -24.623   4.849  1.00 46.80           C  
ANISOU 4364  CA  MET B  69     3867   5028   8884   -208    242    135       C  
ATOM   4365  C   MET B  69      35.271 -25.997   5.400  1.00 45.62           C  
ANISOU 4365  C   MET B  69     3744   4970   8617   -211    244     44       C  
ATOM   4366  O   MET B  69      35.732 -26.862   4.658  1.00 45.04           O  
ANISOU 4366  O   MET B  69     3708   4979   8424   -194    242     73       O  
ATOM   4367  CB  MET B  69      35.984 -23.604   5.199  1.00 47.45           C  
ANISOU 4367  CB  MET B  69     3914   5049   9066   -254    293    148       C  
ATOM   4368  CG  MET B  69      35.906 -22.318   4.395  1.00 48.81           C  
ANISOU 4368  CG  MET B  69     4069   5132   9345   -255    297    274       C  
ATOM   4369  SD  MET B  69      36.781 -20.956   5.188  1.00 49.87           S  
ANISOU 4369  SD  MET B  69     4141   5138   9669   -317    341    248       S  
ATOM   4370  CE  MET B  69      38.481 -21.419   4.882  1.00 49.75           C  
ANISOU 4370  CE  MET B  69     4114   5208   9579   -360    395    282       C  
ATOM   4371  N   GLY B  70      35.064 -26.185   6.701  1.00 45.29           N  
ANISOU 4371  N   GLY B  70     3693   4907   8608   -234    252    -63       N  
ATOM   4372  CA  GLY B  70      35.294 -27.473   7.349  1.00 44.81           C  
ANISOU 4372  CA  GLY B  70     3663   4915   8446   -241    240   -136       C  
ATOM   4373  C   GLY B  70      34.548 -28.599   6.661  1.00 44.53           C  
ANISOU 4373  C   GLY B  70     3658   4937   8323   -203    202   -121       C  
ATOM   4374  O   GLY B  70      35.141 -29.612   6.289  1.00 44.64           O  
ANISOU 4374  O   GLY B  70     3702   5018   8242   -190    190   -122       O  
ATOM   4375  N   ALA B  71      33.246 -28.406   6.484  1.00 44.87           N  
ANISOU 4375  N   ALA B  71     3683   4943   8419   -184    178   -114       N  
ATOM   4376  CA  ALA B  71      32.382 -29.412   5.873  1.00 44.97           C  
ANISOU 4376  CA  ALA B  71     3714   4994   8376   -157    121   -107       C  
ATOM   4377  C   ALA B  71      32.711 -29.640   4.399  1.00 45.59           C  
ANISOU 4377  C   ALA B  71     3838   5125   8359   -127     77    -28       C  
ATOM   4378  O   ALA B  71      32.724 -30.777   3.936  1.00 45.78           O  
ANISOU 4378  O   ALA B  71     3905   5205   8281   -112     42    -48       O  
ATOM   4379  CB  ALA B  71      30.923 -29.012   6.028  1.00 45.35           C  
ANISOU 4379  CB  ALA B  71     3707   4977   8544   -146     99   -112       C  
ATOM   4380  N   GLN B  72      32.986 -28.562   3.670  1.00 46.71           N  
ANISOU 4380  N   GLN B  72     3978   5242   8526   -121     83     59       N  
ATOM   4381  CA  GLN B  72      33.259 -28.652   2.230  1.00 47.63           C  
ANISOU 4381  CA  GLN B  72     4160   5410   8526    -99     55    147       C  
ATOM   4382  C   GLN B  72      34.604 -29.315   1.935  1.00 47.53           C  
ANISOU 4382  C   GLN B  72     4190   5473   8395   -102    124    130       C  
ATOM   4383  O   GLN B  72      34.781 -29.908   0.872  1.00 47.61           O  
ANISOU 4383  O   GLN B  72     4273   5546   8269    -81    115    153       O  
ATOM   4384  CB  GLN B  72      33.189 -27.264   1.571  1.00 48.75           C  
ANISOU 4384  CB  GLN B  72     4296   5495   8731    -99     48    267       C  
ATOM   4385  CG  GLN B  72      31.846 -26.548   1.729  1.00 49.27           C  
ANISOU 4385  CG  GLN B  72     4305   5470   8946    -83    -27    294       C  
ATOM   4386  CD  GLN B  72      30.723 -27.215   0.944  1.00 49.73           C  
ANISOU 4386  CD  GLN B  72     4390   5551   8951    -54   -153    314       C  
ATOM   4387  OE1 GLN B  72      30.899 -28.285   0.364  1.00 49.65           O  
ANISOU 4387  OE1 GLN B  72     4454   5627   8783    -49   -183    289       O  
ATOM   4388  NE2 GLN B  72      29.565 -26.574   0.915  1.00 50.63           N  
ANISOU 4388  NE2 GLN B  72     4438   5580   9216    -35   -234    355       N  
ATOM   4389  N   MET B  73      35.542 -29.215   2.875  1.00 47.62           N  
ANISOU 4389  N   MET B  73     4154   5473   8465   -127    191     84       N  
ATOM   4390  CA  MET B  73      36.839 -29.882   2.748  1.00 48.10           C  
ANISOU 4390  CA  MET B  73     4220   5590   8463   -125    254     60       C  
ATOM   4391  C   MET B  73      36.676 -31.398   2.789  1.00 47.79           C  
ANISOU 4391  C   MET B  73     4218   5598   8339    -99    219    -19       C  
ATOM   4392  O   MET B  73      37.060 -32.090   1.845  1.00 48.42           O  
ANISOU 4392  O   MET B  73     4350   5733   8314    -70    242    -21       O  
ATOM   4393  CB  MET B  73      37.803 -29.436   3.855  1.00 48.18           C  
ANISOU 4393  CB  MET B  73     4159   5564   8581   -162    295     27       C  
ATOM   4394  CG  MET B  73      38.585 -28.176   3.530  1.00 49.12           C  
ANISOU 4394  CG  MET B  73     4237   5648   8778   -191    357    106       C  
ATOM   4395  SD  MET B  73      39.770 -27.771   4.825  1.00 49.58           S  
ANISOU 4395  SD  MET B  73     4208   5660   8969   -242    373     51       S  
ATOM   4396  CE  MET B  73      38.699 -26.998   6.027  1.00 49.09           C  
ANISOU 4396  CE  MET B  73     4147   5514   8991   -270    316     -7       C  
ATOM   4397  N   VAL B  74      36.124 -31.902   3.893  1.00 47.25           N  
ANISOU 4397  N   VAL B  74     4130   5503   8319   -111    174    -88       N  
ATOM   4398  CA  VAL B  74      35.857 -33.338   4.057  1.00 47.22           C  
ANISOU 4398  CA  VAL B  74     4157   5522   8262    -94    133   -155       C  
ATOM   4399  C   VAL B  74      34.936 -33.902   2.975  1.00 47.91           C  
ANISOU 4399  C   VAL B  74     4303   5631   8268    -67     74   -151       C  
ATOM   4400  O   VAL B  74      35.117 -35.038   2.524  1.00 47.92           O  
ANISOU 4400  O   VAL B  74     4348   5660   8197    -43     58   -199       O  
ATOM   4401  CB  VAL B  74      35.298 -33.686   5.491  1.00 46.52           C  
ANISOU 4401  CB  VAL B  74     4045   5393   8235   -126    104   -208       C  
ATOM   4402  CG1 VAL B  74      34.443 -34.947   5.497  1.00 46.43           C  
ANISOU 4402  CG1 VAL B  74     4065   5381   8193   -118     48   -250       C  
ATOM   4403  CG2 VAL B  74      36.476 -33.855   6.431  1.00 46.47           C  
ANISOU 4403  CG2 VAL B  74     4017   5386   8252   -145    126   -234       C  
ATOM   4404  N   LYS B  75      33.956 -33.107   2.563  1.00 48.97           N  
ANISOU 4404  N   LYS B  75     4436   5743   8427    -71     29    -99       N  
ATOM   4405  CA  LYS B  75      32.988 -33.537   1.560  1.00 50.36           C  
ANISOU 4405  CA  LYS B  75     4663   5932   8537    -52    -61    -90       C  
ATOM   4406  C   LYS B  75      33.632 -33.769   0.193  1.00 51.85           C  
ANISOU 4406  C   LYS B  75     4946   6185   8568    -26    -47    -66       C  
ATOM   4407  O   LYS B  75      33.205 -34.653  -0.550  1.00 52.40           O  
ANISOU 4407  O   LYS B  75     5086   6280   8542    -11   -115   -107       O  
ATOM   4408  CB  LYS B  75      31.849 -32.521   1.441  1.00 50.65           C  
ANISOU 4408  CB  LYS B  75     4661   5918   8665    -58   -125    -25       C  
ATOM   4409  CG  LYS B  75      30.645 -33.055   0.687  1.00 51.35           C  
ANISOU 4409  CG  LYS B  75     4774   6003   8731    -47   -257    -25       C  
ATOM   4410  CD  LYS B  75      29.439 -32.139   0.802  1.00 51.87           C  
ANISOU 4410  CD  LYS B  75     4761   5999   8946    -49   -328     29       C  
ATOM   4411  CE  LYS B  75      29.645 -30.829   0.066  1.00 52.59           C  
ANISOU 4411  CE  LYS B  75     4872   6076   9032    -36   -337    146       C  
ATOM   4412  NZ  LYS B  75      28.377 -30.245  -0.455  1.00 53.56           N  
ANISOU 4412  NZ  LYS B  75     4953   6140   9255    -22   -474    217       N  
ATOM   4413  N   GLU B  76      34.654 -32.980  -0.133  1.00 53.15           N  
ANISOU 4413  N   GLU B  76     5116   6372   8706    -28     48     -6       N  
ATOM   4414  CA  GLU B  76      35.344 -33.107  -1.416  1.00 55.38           C  
ANISOU 4414  CA  GLU B  76     5492   6720   8828     -9    102     21       C  
ATOM   4415  C   GLU B  76      36.127 -34.417  -1.504  1.00 55.96           C  
ANISOU 4415  C   GLU B  76     5594   6832   8836     17    159    -84       C  
ATOM   4416  O   GLU B  76      35.971 -35.166  -2.466  1.00 57.31           O  
ANISOU 4416  O   GLU B  76     5866   7045   8864     40    137   -127       O  
ATOM   4417  CB  GLU B  76      36.287 -31.924  -1.647  1.00 56.42           C  
ANISOU 4417  CB  GLU B  76     5602   6855   8978    -26    214    119       C  
ATOM   4418  CG  GLU B  76      36.849 -31.848  -3.063  1.00 58.66           C  
ANISOU 4418  CG  GLU B  76     5997   7208   9081    -16    288    176       C  
ATOM   4419  CD  GLU B  76      38.044 -30.916  -3.187  1.00 60.04           C  
ANISOU 4419  CD  GLU B  76     6129   7385   9295    -40    439    261       C  
ATOM   4420  OE1 GLU B  76      38.309 -30.131  -2.251  1.00 59.91           O  
ANISOU 4420  OE1 GLU B  76     6001   7306   9453    -67    455    288       O  
ATOM   4421  OE2 GLU B  76      38.727 -30.971  -4.232  1.00 61.89           O  
ANISOU 4421  OE2 GLU B  76     6444   7682   9387    -35    549    296       O  
ATOM   4422  N   VAL B  77      36.965 -34.683  -0.504  1.00 55.44           N  
ANISOU 4422  N   VAL B  77     5441   6745   8878     15    224   -127       N  
ATOM   4423  CA  VAL B  77      37.774 -35.911  -0.482  1.00 55.74           C  
ANISOU 4423  CA  VAL B  77     5481   6798   8899     49    273   -222       C  
ATOM   4424  C   VAL B  77      36.936 -37.181  -0.304  1.00 55.89           C  
ANISOU 4424  C   VAL B  77     5537   6791   8904     62    169   -311       C  
ATOM   4425  O   VAL B  77      37.317 -38.247  -0.787  1.00 57.20           O  
ANISOU 4425  O   VAL B  77     5749   6968   9015     98    190   -393       O  
ATOM   4426  CB  VAL B  77      38.880 -35.882   0.602  1.00 55.13           C  
ANISOU 4426  CB  VAL B  77     5291   6691   8961     43    334   -233       C  
ATOM   4427  CG1 VAL B  77      39.902 -34.799   0.290  1.00 56.07           C  
ANISOU 4427  CG1 VAL B  77     5362   6829   9110     28    450   -158       C  
ATOM   4428  CG2 VAL B  77      38.300 -35.696   1.998  1.00 53.89           C  
ANISOU 4428  CG2 VAL B  77     5077   6481   8917      6    250   -233       C  
ATOM   4429  N   ALA B  78      35.807 -37.069   0.390  1.00 55.21           N  
ANISOU 4429  N   ALA B  78     5425   6664   8887     32     67   -299       N  
ATOM   4430  CA  ALA B  78      34.906 -38.204   0.573  1.00 55.21           C  
ANISOU 4430  CA  ALA B  78     5448   6630   8899     31    -31   -369       C  
ATOM   4431  C   ALA B  78      34.290 -38.638  -0.755  1.00 56.76           C  
ANISOU 4431  C   ALA B  78     5749   6853   8963     48   -100   -401       C  
ATOM   4432  O   ALA B  78      34.070 -39.829  -0.982  1.00 57.35           O  
ANISOU 4432  O   ALA B  78     5867   6907   9014     61   -151   -490       O  
ATOM   4433  CB  ALA B  78      33.817 -37.859   1.576  1.00 54.44           C  
ANISOU 4433  CB  ALA B  78     5286   6482   8913     -9    -97   -341       C  
ATOM   4434  N   SER B  79      34.014 -37.671  -1.628  1.00 57.97           N  
ANISOU 4434  N   SER B  79     5950   7045   9028     43   -114   -327       N  
ATOM   4435  CA  SER B  79      33.448 -37.959  -2.945  1.00 59.79           C  
ANISOU 4435  CA  SER B  79     6304   7310   9101     52   -199   -345       C  
ATOM   4436  C   SER B  79      34.486 -38.544  -3.904  1.00 60.94           C  
ANISOU 4436  C   SER B  79     6556   7513   9083     88    -97   -412       C  
ATOM   4437  O   SER B  79      34.121 -39.222  -4.863  1.00 62.24           O  
ANISOU 4437  O   SER B  79     6842   7699   9107     98   -164   -481       O  
ATOM   4438  CB  SER B  79      32.824 -36.700  -3.556  1.00 60.53           C  
ANISOU 4438  CB  SER B  79     6423   7421   9152     35   -262   -224       C  
ATOM   4439  OG  SER B  79      33.820 -35.807  -4.019  1.00 61.21           O  
ANISOU 4439  OG  SER B  79     6541   7555   9160     41   -133   -144       O  
ATOM   4440  N   LYS B  80      35.767 -38.271  -3.655  1.00 61.04           N  
ANISOU 4440  N   LYS B  80     6522   7546   9121    105     66   -398       N  
ATOM   4441  CA  LYS B  80      36.853 -38.862  -4.444  1.00 62.58           C  
ANISOU 4441  CA  LYS B  80     6789   7787   9202    145    202   -472       C  
ATOM   4442  C   LYS B  80      36.938 -40.368  -4.228  1.00 62.58           C  
ANISOU 4442  C   LYS B  80     6793   7741   9243    178    179   -620       C  
ATOM   4443  O   LYS B  80      37.247 -41.115  -5.157  1.00 64.00           O  
ANISOU 4443  O   LYS B  80     7080   7945   9292    212    226   -721       O  
ATOM   4444  CB  LYS B  80      38.201 -38.221  -4.106  1.00 62.78           C  
ANISOU 4444  CB  LYS B  80     6720   7828   9302    153    379   -420       C  
ATOM   4445  CG  LYS B  80      38.311 -36.755  -4.487  1.00 63.46           C  
ANISOU 4445  CG  LYS B  80     6813   7952   9346    119    431   -275       C  
ATOM   4446  CD  LYS B  80      39.741 -36.259  -4.355  1.00 64.09           C  
ANISOU 4446  CD  LYS B  80     6804   8046   9498    123    619   -238       C  
ATOM   4447  CE  LYS B  80      39.823 -34.752  -4.531  1.00 64.66           C  
ANISOU 4447  CE  LYS B  80     6861   8129   9577     78    659    -84       C  
ATOM   4448  NZ  LYS B  80      41.207 -34.308  -4.850  1.00 65.88           N  
ANISOU 4448  NZ  LYS B  80     6963   8311   9756     76    864    -43       N  
ATOM   4449  N   ALA B  81      36.667 -40.806  -3.001  1.00 61.14           N  
ANISOU 4449  N   ALA B  81     6503   7486   9239    168    111   -632       N  
ATOM   4450  CA  ALA B  81      36.580 -42.230  -2.691  1.00 61.40           C  
ANISOU 4450  CA  ALA B  81     6537   7452   9338    190     61   -750       C  
ATOM   4451  C   ALA B  81      35.449 -42.890  -3.481  1.00 62.33           C  
ANISOU 4451  C   ALA B  81     6768   7557   9356    178    -75   -822       C  
ATOM   4452  O   ALA B  81      35.580 -44.029  -3.933  1.00 63.38           O  
ANISOU 4452  O   ALA B  81     6966   7656   9457    208    -84   -949       O  
ATOM   4453  CB  ALA B  81      36.369 -42.435  -1.200  1.00 60.00           C  
ANISOU 4453  CB  ALA B  81     6241   7204   9351    165      6   -715       C  
ATOM   4454  N   ASN B  82      34.345 -42.164  -3.640  1.00 62.31           N  
ANISOU 4454  N   ASN B  82     6781   7571   9321    134   -192   -746       N  
ATOM   4455  CA  ASN B  82      33.203 -42.639  -4.421  1.00 63.58           C  
ANISOU 4455  CA  ASN B  82     7038   7721   9399    113   -355   -800       C  
ATOM   4456  C   ASN B  82      33.507 -42.671  -5.918  1.00 65.18           C  
ANISOU 4456  C   ASN B  82     7415   7996   9354    136   -332   -855       C  
ATOM   4457  O   ASN B  82      33.078 -43.581  -6.621  1.00 66.30           O  
ANISOU 4457  O   ASN B  82     7664   8120   9407    138   -425   -973       O  
ATOM   4458  CB  ASN B  82      31.971 -41.764  -4.155  1.00 63.31           C  
ANISOU 4458  CB  ASN B  82     6946   7676   9431     66   -488   -691       C  
ATOM   4459  CG  ASN B  82      30.668 -42.536  -4.265  1.00 64.12           C  
ANISOU 4459  CG  ASN B  82     7054   7716   9592     32   -677   -749       C  
ATOM   4460  OD1 ASN B  82      30.062 -42.894  -3.254  1.00 63.16           O  
ANISOU 4460  OD1 ASN B  82     6819   7522   9657      2   -719   -744       O  
ATOM   4461  ND2 ASN B  82      30.237 -42.808  -5.491  1.00 66.04           N  
ANISOU 4461  ND2 ASN B  82     7433   7986   9672     30   -793   -804       N  
ATOM   4462  N   ASP B  83      34.247 -41.678  -6.400  1.00 65.48           N  
ANISOU 4462  N   ASP B  83     7488   8114   9276    147   -204   -771       N  
ATOM   4463  CA  ASP B  83      34.652 -41.635  -7.805  1.00 67.60           C  
ANISOU 4463  CA  ASP B  83     7938   8465   9281    164   -143   -810       C  
ATOM   4464  C   ASP B  83      35.645 -42.750  -8.139  1.00 68.48           C  
ANISOU 4464  C   ASP B  83     8103   8570   9345    216      1   -973       C  
ATOM   4465  O   ASP B  83      35.577 -43.346  -9.215  1.00 70.28           O  
ANISOU 4465  O   ASP B  83     8502   8828   9373    228    -10  -1088       O  
ATOM   4466  CB  ASP B  83      35.276 -40.277  -8.145  1.00 68.08           C  
ANISOU 4466  CB  ASP B  83     8009   8603   9256    156    -14   -661       C  
ATOM   4467  CG  ASP B  83      34.283 -39.132  -8.059  1.00 67.84           C  
ANISOU 4467  CG  ASP B  83     7951   8569   9252    112   -161   -502       C  
ATOM   4468  OD1 ASP B  83      33.084 -39.344  -8.355  1.00 68.76           O  
ANISOU 4468  OD1 ASP B  83     8118   8664   9343     89   -371   -512       O  
ATOM   4469  OD2 ASP B  83      34.713 -38.014  -7.698  1.00 67.49           O  
ANISOU 4469  OD2 ASP B  83     7829   8538   9277    101    -72   -371       O  
ATOM   4470  N   ALA B  84      36.560 -43.025  -7.212  1.00 67.34           N  
ANISOU 4470  N   ALA B  84     7814   8382   9390    249    131   -989       N  
ATOM   4471  CA  ALA B  84      37.608 -44.021  -7.423  1.00 68.25           C  
ANISOU 4471  CA  ALA B  84     7940   8473   9517    311    283  -1134       C  
ATOM   4472  C   ALA B  84      37.067 -45.448  -7.378  1.00 68.60           C  
ANISOU 4472  C   ALA B  84     8024   8424   9616    326    161  -1294       C  
ATOM   4473  O   ALA B  84      37.288 -46.229  -8.303  1.00 70.41           O  
ANISOU 4473  O   ALA B  84     8386   8654   9709    360    207  -1447       O  
ATOM   4474  CB  ALA B  84      38.709 -43.850  -6.387  1.00 67.14           C  
ANISOU 4474  CB  ALA B  84     7615   8301   9593    339    420  -1085       C  
ATOM   4475  N   ALA B  85      36.353 -45.775  -6.302  1.00 67.02           N  
ANISOU 4475  N   ALA B  85     7712   8138   9613    297     16  -1260       N  
ATOM   4476  CA  ALA B  85      35.918 -47.149  -6.035  1.00 67.13           C  
ANISOU 4476  CA  ALA B  85     7729   8038   9740    304    -89  -1389       C  
ATOM   4477  C   ALA B  85      34.427 -47.413  -6.277  1.00 67.27           C  
ANISOU 4477  C   ALA B  85     7810   8022   9727    244   -316  -1407       C  
ATOM   4478  O   ALA B  85      33.995 -48.567  -6.251  1.00 67.93           O  
ANISOU 4478  O   ALA B  85     7915   8006   9886    241   -414  -1525       O  
ATOM   4479  CB  ALA B  85      36.286 -47.527  -4.609  1.00 65.60           C  
ANISOU 4479  CB  ALA B  85     7363   7753   9805    313    -77  -1341       C  
ATOM   4480  N   GLY B  86      33.642 -46.360  -6.500  1.00 66.70           N  
ANISOU 4480  N   GLY B  86     7753   8018   9570    195   -406  -1289       N  
ATOM   4481  CA  GLY B  86      32.205 -46.505  -6.739  1.00 66.99           C  
ANISOU 4481  CA  GLY B  86     7823   8021   9606    137   -634  -1291       C  
ATOM   4482  C   GLY B  86      31.342 -46.529  -5.484  1.00 65.05           C  
ANISOU 4482  C   GLY B  86     7410   7694   9609     89   -732  -1208       C  
ATOM   4483  O   GLY B  86      30.120 -46.669  -5.576  1.00 65.27           O  
ANISOU 4483  O   GLY B  86     7428   7681   9688     37   -913  -1205       O  
ATOM   4484  N   ASP B  87      31.967 -46.384  -4.316  1.00 62.97           N  
ANISOU 4484  N   ASP B  87     7018   7407   9499    102   -613  -1139       N  
ATOM   4485  CA  ASP B  87      31.262 -46.449  -3.035  1.00 61.28           C  
ANISOU 4485  CA  ASP B  87     6663   7121   9499     55   -669  -1063       C  
ATOM   4486  C   ASP B  87      32.171 -45.942  -1.911  1.00 59.31           C  
ANISOU 4486  C   ASP B  87     6310   6883   9339     72   -524   -973       C  
ATOM   4487  O   ASP B  87      33.393 -45.878  -2.074  1.00 59.64           O  
ANISOU 4487  O   ASP B  87     6370   6961   9327    124   -394   -994       O  
ATOM   4488  CB  ASP B  87      30.825 -47.895  -2.746  1.00 61.90           C  
ANISOU 4488  CB  ASP B  87     6734   7076   9707     36   -756  -1163       C  
ATOM   4489  CG  ASP B  87      29.783 -47.995  -1.638  1.00 61.22           C  
ANISOU 4489  CG  ASP B  87     6524   6916   9820    -31   -832  -1084       C  
ATOM   4490  OD1 ASP B  87      28.909 -47.107  -1.542  1.00 61.17           O  
ANISOU 4490  OD1 ASP B  87     6461   6943   9835    -71   -887   -997       O  
ATOM   4491  OD2 ASP B  87      29.835 -48.975  -0.864  1.00 61.20           O  
ANISOU 4491  OD2 ASP B  87     6478   6814   9961    -44   -828  -1105       O  
ATOM   4492  N   GLY B  88      31.568 -45.572  -0.783  1.00 57.41           N  
ANISOU 4492  N   GLY B  88     5962   6613   9238     25   -546   -880       N  
ATOM   4493  CA  GLY B  88      32.314 -45.251   0.434  1.00 55.75           C  
ANISOU 4493  CA  GLY B  88     5667   6399   9117     28   -440   -807       C  
ATOM   4494  C   GLY B  88      32.375 -43.785   0.825  1.00 54.51           C  
ANISOU 4494  C   GLY B  88     5456   6309   8946     14   -381   -699       C  
ATOM   4495  O   GLY B  88      33.285 -43.382   1.549  1.00 53.80           O  
ANISOU 4495  O   GLY B  88     5321   6235   8886     25   -289   -656       O  
ATOM   4496  N   THR B  89      31.412 -42.987   0.365  1.00 54.32           N  
ANISOU 4496  N   THR B  89     5430   6312   8894    -11   -446   -655       N  
ATOM   4497  CA  THR B  89      31.319 -41.582   0.767  1.00 53.06           C  
ANISOU 4497  CA  THR B  89     5212   6191   8754    -26   -400   -555       C  
ATOM   4498  C   THR B  89      30.951 -41.494   2.239  1.00 51.63           C  
ANISOU 4498  C   THR B  89     4938   5963   8716    -67   -370   -515       C  
ATOM   4499  O   THR B  89      31.628 -40.821   3.018  1.00 51.04           O  
ANISOU 4499  O   THR B  89     4827   5905   8660    -69   -283   -471       O  
ATOM   4500  CB  THR B  89      30.256 -40.821  -0.050  1.00 53.97           C  
ANISOU 4500  CB  THR B  89     5339   6325   8842    -40   -499   -513       C  
ATOM   4501  OG1 THR B  89      30.577 -40.901  -1.440  1.00 55.22           O  
ANISOU 4501  OG1 THR B  89     5615   6536   8829     -9   -532   -544       O  
ATOM   4502  CG2 THR B  89      30.185 -39.351   0.364  1.00 53.51           C  
ANISOU 4502  CG2 THR B  89     5214   6285   8829    -48   -447   -412       C  
ATOM   4503  N   THR B  90      29.870 -42.178   2.607  1.00 51.15           N  
ANISOU 4503  N   THR B  90     4841   5839   8751   -107   -442   -533       N  
ATOM   4504  CA  THR B  90      29.411 -42.228   3.989  1.00 50.07           C  
ANISOU 4504  CA  THR B  90     4632   5657   8734   -156   -399   -498       C  
ATOM   4505  C   THR B  90      30.527 -42.719   4.907  1.00 49.29           C  
ANISOU 4505  C   THR B  90     4553   5550   8623   -150   -326   -497       C  
ATOM   4506  O   THR B  90      30.844 -42.067   5.898  1.00 48.66           O  
ANISOU 4506  O   THR B  90     4446   5484   8557   -169   -254   -452       O  
ATOM   4507  CB  THR B  90      28.187 -43.153   4.133  1.00 50.59           C  
ANISOU 4507  CB  THR B  90     4660   5648   8911   -204   -477   -521       C  
ATOM   4508  OG1 THR B  90      27.198 -42.793   3.161  1.00 51.26           O  
ANISOU 4508  OG1 THR B  90     4723   5735   9017   -205   -581   -526       O  
ATOM   4509  CG2 THR B  90      27.581 -43.054   5.530  1.00 50.31           C  
ANISOU 4509  CG2 THR B  90     4551   5573   8988   -262   -403   -473       C  
ATOM   4510  N   THR B  91      31.127 -43.855   4.556  1.00 49.41           N  
ANISOU 4510  N   THR B  91     4617   5537   8618   -122   -355   -551       N  
ATOM   4511  CA  THR B  91      32.188 -44.469   5.361  1.00 48.81           C  
ANISOU 4511  CA  THR B  91     4551   5436   8559   -109   -316   -545       C  
ATOM   4512  C   THR B  91      33.378 -43.528   5.570  1.00 47.86           C  
ANISOU 4512  C   THR B  91     4419   5377   8389    -79   -241   -514       C  
ATOM   4513  O   THR B  91      33.911 -43.431   6.677  1.00 47.65           O  
ANISOU 4513  O   THR B  91     4374   5341   8389    -98   -215   -471       O  
ATOM   4514  CB  THR B  91      32.690 -45.782   4.721  1.00 49.43           C  
ANISOU 4514  CB  THR B  91     4676   5461   8644    -66   -359   -623       C  
ATOM   4515  OG1 THR B  91      31.573 -46.558   4.270  1.00 49.93           O  
ANISOU 4515  OG1 THR B  91     4753   5465   8751    -96   -444   -668       O  
ATOM   4516  CG2 THR B  91      33.501 -46.599   5.721  1.00 49.51           C  
ANISOU 4516  CG2 THR B  91     4679   5409   8721    -62   -352   -599       C  
ATOM   4517  N   ALA B  92      33.784 -42.840   4.505  1.00 47.51           N  
ANISOU 4517  N   ALA B  92     4388   5393   8269    -39   -213   -530       N  
ATOM   4518  CA  ALA B  92      34.902 -41.895   4.569  1.00 46.85           C  
ANISOU 4518  CA  ALA B  92     4281   5361   8158    -16   -137   -497       C  
ATOM   4519  C   ALA B  92      34.594 -40.691   5.459  1.00 46.10           C  
ANISOU 4519  C   ALA B  92     4143   5281   8089    -62   -109   -432       C  
ATOM   4520  O   ALA B  92      35.483 -40.177   6.136  1.00 46.01           O  
ANISOU 4520  O   ALA B  92     4103   5281   8095    -67    -70   -406       O  
ATOM   4521  CB  ALA B  92      35.277 -41.429   3.172  1.00 47.22           C  
ANISOU 4521  CB  ALA B  92     4362   5465   8112     25    -99   -516       C  
ATOM   4522  N   THR B  93      33.338 -40.248   5.453  1.00 45.82           N  
ANISOU 4522  N   THR B  93     4098   5239   8071    -95   -134   -416       N  
ATOM   4523  CA  THR B  93      32.909 -39.097   6.250  1.00 45.17           C  
ANISOU 4523  CA  THR B  93     3975   5158   8028   -133    -96   -374       C  
ATOM   4524  C   THR B  93      32.920 -39.409   7.752  1.00 44.74           C  
ANISOU 4524  C   THR B  93     3917   5072   8009   -180    -75   -367       C  
ATOM   4525  O   THR B  93      33.325 -38.562   8.550  1.00 44.57           O  
ANISOU 4525  O   THR B  93     3885   5060   7988   -202    -31   -351       O  
ATOM   4526  CB  THR B  93      31.507 -38.606   5.812  1.00 45.49           C  
ANISOU 4526  CB  THR B  93     3987   5185   8111   -148   -128   -361       C  
ATOM   4527  OG1 THR B  93      31.493 -38.402   4.394  1.00 45.78           O  
ANISOU 4527  OG1 THR B  93     4053   5253   8087   -109   -173   -357       O  
ATOM   4528  CG2 THR B  93      31.119 -37.293   6.507  1.00 45.31           C  
ANISOU 4528  CG2 THR B  93     3914   5152   8147   -173    -72   -329       C  
ATOM   4529  N   VAL B  94      32.485 -40.612   8.134  1.00 44.77           N  
ANISOU 4529  N   VAL B  94     3941   5035   8035   -200   -110   -379       N  
ATOM   4530  CA  VAL B  94      32.485 -40.999   9.561  1.00 44.81           C  
ANISOU 4530  CA  VAL B  94     3967   5011   8047   -251    -91   -356       C  
ATOM   4531  C   VAL B  94      33.914 -41.257  10.048  1.00 44.55           C  
ANISOU 4531  C   VAL B  94     3960   4984   7981   -234   -111   -344       C  
ATOM   4532  O   VAL B  94      34.247 -40.928  11.189  1.00 44.89           O  
ANISOU 4532  O   VAL B  94     4027   5030   7998   -274    -98   -319       O  
ATOM   4533  CB  VAL B  94      31.518 -42.180   9.936  1.00 45.33           C  
ANISOU 4533  CB  VAL B  94     4044   5018   8160   -293   -114   -350       C  
ATOM   4534  CG1 VAL B  94      30.746 -42.730   8.747  1.00 45.61           C  
ANISOU 4534  CG1 VAL B  94     4056   5030   8243   -271   -170   -385       C  
ATOM   4535  CG2 VAL B  94      32.238 -43.310  10.668  1.00 45.70           C  
ANISOU 4535  CG2 VAL B  94     4142   5024   8195   -303   -151   -324       C  
ATOM   4536  N   LEU B  95      34.746 -41.837   9.186  1.00 44.05           N  
ANISOU 4536  N   LEU B  95     3891   4920   7924   -175   -145   -367       N  
ATOM   4537  CA  LEU B  95      36.161 -42.039   9.500  1.00 43.81           C  
ANISOU 4537  CA  LEU B  95     3853   4889   7904   -147   -166   -357       C  
ATOM   4538  C   LEU B  95      36.882 -40.705   9.678  1.00 43.41           C  
ANISOU 4538  C   LEU B  95     3768   4885   7840   -152   -128   -343       C  
ATOM   4539  O   LEU B  95      37.658 -40.540  10.621  1.00 43.74           O  
ANISOU 4539  O   LEU B  95     3808   4921   7889   -173   -158   -320       O  
ATOM   4540  CB  LEU B  95      36.856 -42.868   8.414  1.00 44.12           C  
ANISOU 4540  CB  LEU B  95     3878   4913   7972    -74   -179   -400       C  
ATOM   4541  CG  LEU B  95      36.530 -44.365   8.395  1.00 44.55           C  
ANISOU 4541  CG  LEU B  95     3964   4893   8070    -63   -236   -421       C  
ATOM   4542  CD1 LEU B  95      36.982 -44.996   7.090  1.00 45.05           C  
ANISOU 4542  CD1 LEU B  95     4024   4945   8146     10   -226   -497       C  
ATOM   4543  CD2 LEU B  95      37.165 -45.080   9.579  1.00 44.88           C  
ANISOU 4543  CD2 LEU B  95     4013   4876   8161    -78   -297   -370       C  
ATOM   4544  N   ALA B  96      36.618 -39.759   8.779  1.00 42.92           N  
ANISOU 4544  N   ALA B  96     3682   4862   7764   -136    -76   -354       N  
ATOM   4545  CA  ALA B  96      37.219 -38.427   8.863  1.00 42.67           C  
ANISOU 4545  CA  ALA B  96     3614   4859   7739   -147    -35   -337       C  
ATOM   4546  C   ALA B  96      36.843 -37.745  10.174  1.00 42.46           C  
ANISOU 4546  C   ALA B  96     3606   4820   7705   -211    -35   -328       C  
ATOM   4547  O   ALA B  96      37.708 -37.217  10.873  1.00 42.98           O  
ANISOU 4547  O   ALA B  96     3661   4886   7782   -233    -51   -323       O  
ATOM   4548  CB  ALA B  96      36.797 -37.562   7.685  1.00 42.52           C  
ANISOU 4548  CB  ALA B  96     3581   4870   7705   -126     13   -331       C  
ATOM   4549  N   GLN B  97      35.556 -37.773  10.506  1.00 41.99           N  
ANISOU 4549  N   GLN B  97     3575   4747   7632   -243    -16   -334       N  
ATOM   4550  CA  GLN B  97      35.064 -37.189  11.751  1.00 42.23           C  
ANISOU 4550  CA  GLN B  97     3637   4765   7643   -304     14   -342       C  
ATOM   4551  C   GLN B  97      35.806 -37.744  12.969  1.00 42.81           C  
ANISOU 4551  C   GLN B  97     3767   4831   7666   -341    -38   -330       C  
ATOM   4552  O   GLN B  97      36.211 -36.987  13.852  1.00 43.15           O  
ANISOU 4552  O   GLN B  97     3837   4877   7678   -381    -38   -344       O  
ATOM   4553  CB  GLN B  97      33.566 -37.455  11.905  1.00 42.36           C  
ANISOU 4553  CB  GLN B  97     3660   4760   7672   -329     56   -349       C  
ATOM   4554  CG  GLN B  97      32.932 -36.773  13.108  1.00 42.86           C  
ANISOU 4554  CG  GLN B  97     3754   4813   7718   -388    129   -372       C  
ATOM   4555  CD  GLN B  97      31.500 -37.216  13.349  1.00 43.29           C  
ANISOU 4555  CD  GLN B  97     3798   4841   7807   -417    189   -375       C  
ATOM   4556  OE1 GLN B  97      31.140 -38.366  13.090  1.00 43.65           O  
ANISOU 4556  OE1 GLN B  97     3846   4871   7865   -417    154   -351       O  
ATOM   4557  NE2 GLN B  97      30.676 -36.309  13.858  1.00 43.74           N  
ANISOU 4557  NE2 GLN B  97     3835   4882   7899   -443    285   -410       N  
ATOM   4558  N   ALA B  98      35.976 -39.064  13.005  1.00 43.18           N  
ANISOU 4558  N   ALA B  98     3838   4859   7708   -328    -94   -305       N  
ATOM   4559  CA  ALA B  98      36.591 -39.746  14.145  1.00 43.89           C  
ANISOU 4559  CA  ALA B  98     3990   4930   7753   -362   -167   -271       C  
ATOM   4560  C   ALA B  98      38.063 -39.387  14.321  1.00 44.26           C  
ANISOU 4560  C   ALA B  98     4006   4985   7823   -346   -242   -265       C  
ATOM   4561  O   ALA B  98      38.525 -39.190  15.446  1.00 44.96           O  
ANISOU 4561  O   ALA B  98     4151   5072   7857   -395   -302   -250       O  
ATOM   4562  CB  ALA B  98      36.435 -41.253  14.003  1.00 44.23           C  
ANISOU 4562  CB  ALA B  98     4053   4931   7819   -344   -217   -237       C  
ATOM   4563  N   ILE B  99      38.793 -39.302  13.211  1.00 44.13           N  
ANISOU 4563  N   ILE B  99     3902   4976   7889   -281   -238   -277       N  
ATOM   4564  CA  ILE B  99      40.212 -38.942  13.252  1.00 44.89           C  
ANISOU 4564  CA  ILE B  99     3933   5072   8049   -264   -294   -271       C  
ATOM   4565  C   ILE B  99      40.365 -37.471  13.641  1.00 45.43           C  
ANISOU 4565  C   ILE B  99     3993   5160   8106   -311   -269   -293       C  
ATOM   4566  O   ILE B  99      41.223 -37.123  14.453  1.00 46.18           O  
ANISOU 4566  O   ILE B  99     4086   5247   8213   -345   -351   -289       O  
ATOM   4567  CB  ILE B  99      40.917 -39.198  11.901  1.00 44.61           C  
ANISOU 4567  CB  ILE B  99     3802   5041   8107   -185   -256   -282       C  
ATOM   4568  CG1 ILE B  99      40.840 -40.681  11.525  1.00 44.87           C  
ANISOU 4568  CG1 ILE B  99     3845   5037   8165   -134   -285   -281       C  
ATOM   4569  CG2 ILE B  99      42.380 -38.778  11.970  1.00 45.17           C  
ANISOU 4569  CG2 ILE B  99     3778   5105   8277   -172   -296   -273       C  
ATOM   4570  CD1 ILE B  99      41.110 -40.961  10.062  1.00 44.85           C  
ANISOU 4570  CD1 ILE B  99     3786   5044   8208    -60   -210   -320       C  
ATOM   4571  N   ILE B 100      39.522 -36.621  13.060  1.00 45.41           N  
ANISOU 4571  N   ILE B 100     3984   5174   8093   -312   -170   -317       N  
ATOM   4572  CA  ILE B 100      39.552 -35.184  13.323  1.00 45.83           C  
ANISOU 4572  CA  ILE B 100     4025   5226   8159   -351   -135   -343       C  
ATOM   4573  C   ILE B 100      39.197 -34.865  14.776  1.00 47.10           C  
ANISOU 4573  C   ILE B 100     4281   5377   8236   -425   -163   -375       C  
ATOM   4574  O   ILE B 100      39.889 -34.083  15.424  1.00 47.75           O  
ANISOU 4574  O   ILE B 100     4367   5447   8325   -466   -209   -400       O  
ATOM   4575  CB  ILE B 100      38.602 -34.423  12.372  1.00 45.21           C  
ANISOU 4575  CB  ILE B 100     3922   5153   8102   -331    -33   -350       C  
ATOM   4576  CG1 ILE B 100      39.148 -34.466  10.940  1.00 44.92           C  
ANISOU 4576  CG1 ILE B 100     3812   5135   8121   -271     -3   -319       C  
ATOM   4577  CG2 ILE B 100      38.433 -32.975  12.816  1.00 45.64           C  
ANISOU 4577  CG2 ILE B 100     3974   5182   8182   -373      3   -383       C  
ATOM   4578  CD1 ILE B 100      38.110 -34.188   9.873  1.00 44.56           C  
ANISOU 4578  CD1 ILE B 100     3767   5098   8064   -241     59   -307       C  
ATOM   4579  N   THR B 101      38.124 -35.471  15.281  1.00 48.11           N  
ANISOU 4579  N   THR B 101     4490   5508   8282   -446   -129   -376       N  
ATOM   4580  CA  THR B 101      37.658 -35.209  16.644  1.00 49.72           C  
ANISOU 4580  CA  THR B 101     4804   5708   8377   -519   -120   -410       C  
ATOM   4581  C   THR B 101      38.741 -35.499  17.684  1.00 51.78           C  
ANISOU 4581  C   THR B 101     5130   5969   8571   -562   -255   -394       C  
ATOM   4582  O   THR B 101      39.060 -34.640  18.509  1.00 53.06           O  
ANISOU 4582  O   THR B 101     5347   6129   8684   -616   -283   -444       O  
ATOM   4583  CB  THR B 101      36.402 -36.037  16.977  1.00 49.63           C  
ANISOU 4583  CB  THR B 101     4859   5699   8300   -538    -51   -395       C  
ATOM   4584  OG1 THR B 101      35.386 -35.777  16.002  1.00 48.76           O  
ANISOU 4584  OG1 THR B 101     4673   5581   8270   -499     46   -408       O  
ATOM   4585  CG2 THR B 101      35.866 -35.682  18.361  1.00 50.77           C  
ANISOU 4585  CG2 THR B 101     5126   5846   8315   -617      0   -435       C  
ATOM   4586  N   GLU B 102      39.304 -36.703  17.631  1.00 52.83           N  
ANISOU 4586  N   GLU B 102     5258   6098   8715   -536   -352   -328       N  
ATOM   4587  CA  GLU B 102      40.355 -37.118  18.566  1.00 54.79           C  
ANISOU 4587  CA  GLU B 102     5558   6336   8922   -568   -514   -292       C  
ATOM   4588  C   GLU B 102      41.702 -36.472  18.244  1.00 55.29           C  
ANISOU 4588  C   GLU B 102     5509   6388   9109   -548   -604   -304       C  
ATOM   4589  O   GLU B 102      42.524 -36.273  19.141  1.00 56.56           O  
ANISOU 4589  O   GLU B 102     5707   6539   9242   -595   -742   -302       O  
ATOM   4590  CB  GLU B 102      40.484 -38.644  18.571  1.00 55.52           C  
ANISOU 4590  CB  GLU B 102     5666   6406   9021   -538   -590   -209       C  
ATOM   4591  CG  GLU B 102      39.225 -39.363  19.032  1.00 56.07           C  
ANISOU 4591  CG  GLU B 102     5848   6476   8979   -574   -513   -181       C  
ATOM   4592  CD  GLU B 102      38.817 -38.976  20.441  1.00 57.55           C  
ANISOU 4592  CD  GLU B 102     6200   6685   8981   -670   -508   -191       C  
ATOM   4593  OE1 GLU B 102      39.620 -39.198  21.371  1.00 58.96           O  
ANISOU 4593  OE1 GLU B 102     6463   6859   9079   -711   -658   -150       O  
ATOM   4594  OE2 GLU B 102      37.697 -38.449  20.617  1.00 57.72           O  
ANISOU 4594  OE2 GLU B 102     6267   6726   8938   -705   -354   -243       O  
ATOM   4595  N   GLY B 103      41.925 -36.151  16.971  1.00 54.65           N  
ANISOU 4595  N   GLY B 103     5292   6306   9164   -486   -528   -313       N  
ATOM   4596  CA  GLY B 103      43.143 -35.464  16.550  1.00 55.25           C  
ANISOU 4596  CA  GLY B 103     5242   6368   9380   -472   -574   -319       C  
ATOM   4597  C   GLY B 103      43.216 -34.045  17.084  1.00 56.06           C  
ANISOU 4597  C   GLY B 103     5366   6463   9472   -538   -571   -380       C  
ATOM   4598  O   GLY B 103      44.198 -33.668  17.722  1.00 57.18           O  
ANISOU 4598  O   GLY B 103     5488   6583   9655   -580   -700   -390       O  
ATOM   4599  N   LEU B 104      42.164 -33.268  16.838  1.00 55.85           N  
ANISOU 4599  N   LEU B 104     5375   6441   9403   -548   -437   -425       N  
ATOM   4600  CA  LEU B 104      42.102 -31.871  17.279  1.00 56.46           C  
ANISOU 4600  CA  LEU B 104     5472   6491   9487   -605   -414   -496       C  
ATOM   4601  C   LEU B 104      42.064 -31.754  18.800  1.00 57.92           C  
ANISOU 4601  C   LEU B 104     5805   6673   9527   -686   -504   -551       C  
ATOM   4602  O   LEU B 104      42.535 -30.763  19.359  1.00 59.00           O  
ANISOU 4602  O   LEU B 104     5958   6779   9681   -742   -558   -617       O  
ATOM   4603  CB  LEU B 104      40.884 -31.161  16.679  1.00 55.72           C  
ANISOU 4603  CB  LEU B 104     5379   6390   9400   -586   -252   -526       C  
ATOM   4604  CG  LEU B 104      40.830 -31.042  15.153  1.00 54.78           C  
ANISOU 4604  CG  LEU B 104     5142   6274   9397   -517   -166   -472       C  
ATOM   4605  CD1 LEU B 104      39.512 -30.417  14.729  1.00 54.16           C  
ANISOU 4605  CD1 LEU B 104     5078   6180   9317   -502    -43   -493       C  
ATOM   4606  CD2 LEU B 104      41.999 -30.237  14.611  1.00 55.44           C  
ANISOU 4606  CD2 LEU B 104     5112   6329   9623   -520   -189   -454       C  
ATOM   4607  N   LYS B 105      41.490 -32.756  19.461  1.00 58.36           N  
ANISOU 4607  N   LYS B 105     5980   6759   9435   -698   -518   -526       N  
ATOM   4608  CA  LYS B 105      41.568 -32.858  20.917  1.00 59.92           C  
ANISOU 4608  CA  LYS B 105     6343   6965   9457   -778   -618   -556       C  
ATOM   4609  C   LYS B 105      43.018 -32.986  21.372  1.00 60.71           C  
ANISOU 4609  C   LYS B 105     6414   7048   9601   -804   -839   -528       C  
ATOM   4610  O   LYS B 105      43.439 -32.301  22.302  1.00 61.88           O  
ANISOU 4610  O   LYS B 105     6647   7184   9679   -878   -941   -592       O  
ATOM   4611  CB  LYS B 105      40.738 -34.039  21.437  1.00 60.54           C  
ANISOU 4611  CB  LYS B 105     6547   7075   9380   -787   -586   -502       C  
ATOM   4612  CG  LYS B 105      39.417 -33.622  22.052  1.00 61.28           C  
ANISOU 4612  CG  LYS B 105     6768   7182   9333   -833   -421   -573       C  
ATOM   4613  CD  LYS B 105      38.559 -34.812  22.428  1.00 61.73           C  
ANISOU 4613  CD  LYS B 105     6921   7263   9269   -844   -364   -504       C  
ATOM   4614  CE  LYS B 105      39.131 -35.614  23.580  1.00 63.47           C  
ANISOU 4614  CE  LYS B 105     7298   7499   9318   -905   -522   -440       C  
ATOM   4615  NZ  LYS B 105      38.183 -36.678  24.012  1.00 63.95           N  
ANISOU 4615  NZ  LYS B 105     7466   7574   9257   -931   -438   -368       N  
ATOM   4616  N   ALA B 106      43.774 -33.854  20.702  1.00 60.09           N  
ANISOU 4616  N   ALA B 106     6212   6964   9653   -741   -915   -439       N  
ATOM   4617  CA  ALA B 106      45.190 -34.059  21.013  1.00 61.25           C  
ANISOU 4617  CA  ALA B 106     6287   7084   9899   -751  -1128   -401       C  
ATOM   4618  C   ALA B 106      46.052 -32.831  20.700  1.00 61.64           C  
ANISOU 4618  C   ALA B 106     6205   7097  10116   -772  -1158   -457       C  
ATOM   4619  O   ALA B 106      47.107 -32.644  21.305  1.00 63.60           O  
ANISOU 4619  O   ALA B 106     6425   7317  10422   -816  -1351   -459       O  
ATOM   4620  CB  ALA B 106      45.725 -35.280  20.278  1.00 60.84           C  
ANISOU 4620  CB  ALA B 106     6113   7021   9981   -665  -1167   -305       C  
ATOM   4621  N   VAL B 107      45.613 -32.004  19.754  1.00 60.18           N  
ANISOU 4621  N   VAL B 107     5937   6906  10019   -745   -979   -494       N  
ATOM   4622  CA  VAL B 107      46.298 -30.745  19.459  1.00 60.53           C  
ANISOU 4622  CA  VAL B 107     5869   6905  10223   -775   -984   -541       C  
ATOM   4623  C   VAL B 107      46.079 -29.741  20.594  1.00 62.19           C  
ANISOU 4623  C   VAL B 107     6219   7090  10321   -871  -1043   -649       C  
ATOM   4624  O   VAL B 107      47.012 -29.041  20.990  1.00 63.57           O  
ANISOU 4624  O   VAL B 107     6344   7217  10591   -929  -1179   -689       O  
ATOM   4625  CB  VAL B 107      45.838 -30.159  18.107  1.00 59.05           C  
ANISOU 4625  CB  VAL B 107     5573   6712  10149   -721   -778   -530       C  
ATOM   4626  CG1 VAL B 107      46.432 -28.780  17.859  1.00 59.62           C  
ANISOU 4626  CG1 VAL B 107     5545   6723  10382   -764   -769   -570       C  
ATOM   4627  CG2 VAL B 107      46.244 -31.083  16.970  1.00 58.36           C  
ANISOU 4627  CG2 VAL B 107     5353   6648  10169   -633   -727   -442       C  
ATOM   4628  N   ALA B 108      44.854 -29.682  21.117  1.00 62.72           N  
ANISOU 4628  N   ALA B 108     6455   7182  10194   -890   -938   -705       N  
ATOM   4629  CA  ALA B 108      44.531 -28.828  22.269  1.00 64.75           C  
ANISOU 4629  CA  ALA B 108     6874   7418  10307   -978   -967   -827       C  
ATOM   4630  C   ALA B 108      45.236 -29.302  23.543  1.00 67.36           C  
ANISOU 4630  C   ALA B 108     7338   7764  10490  -1051  -1200   -832       C  
ATOM   4631  O   ALA B 108      45.586 -28.494  24.408  1.00 69.75           O  
ANISOU 4631  O   ALA B 108     7731   8034  10735  -1134  -1309   -934       O  
ATOM   4632  CB  ALA B 108      43.027 -28.783  22.487  1.00 64.10           C  
ANISOU 4632  CB  ALA B 108     6926   7362  10066   -972   -770   -880       C  
ATOM   4633  N   CYS B 109      45.422 -30.616  23.649  1.00 67.81           N  
ANISOU 4633  N   CYS B 109     7413   7863  10487  -1020  -1286   -722       N  
ATOM   4634  CA  CYS B 109      46.240 -31.246  24.690  1.00 70.02           C  
ANISOU 4634  CA  CYS B 109     7790   8151  10664  -1073  -1545   -681       C  
ATOM   4635  C   CYS B 109      47.647 -30.652  24.816  1.00 70.52           C  
ANISOU 4635  C   CYS B 109     7728   8158  10907  -1112  -1768   -700       C  
ATOM   4636  O   CYS B 109      48.195 -30.589  25.921  1.00 72.71           O  
ANISOU 4636  O   CYS B 109     8129   8429  11066  -1193  -1994   -728       O  
ATOM   4637  CB  CYS B 109      46.313 -32.752  24.413  1.00 70.60           C  
ANISOU 4637  CB  CYS B 109     7831   8250  10743  -1006  -1587   -536       C  
ATOM   4638  SG  CYS B 109      44.766 -33.640  24.788  1.00 72.28           S  
ANISOU 4638  SG  CYS B 109     8248   8520  10694  -1003  -1410   -503       S  
ATOM   4639  N   GLY B 110      48.205 -30.191  23.696  1.00 68.60           N  
ANISOU 4639  N   GLY B 110     7246   7874  10943  -1062  -1704   -685       N  
ATOM   4640  CA  GLY B 110      49.560 -29.637  23.649  1.00 69.16           C  
ANISOU 4640  CA  GLY B 110     7150   7883  11245  -1095  -1887   -691       C  
ATOM   4641  C   GLY B 110      50.512 -30.449  22.786  1.00 68.09           C  
ANISOU 4641  C   GLY B 110     6777   7733  11359  -1015  -1935   -571       C  
ATOM   4642  O   GLY B 110      51.697 -30.127  22.701  1.00 69.45           O  
ANISOU 4642  O   GLY B 110     6774   7850  11761  -1035  -2082   -560       O  
ATOM   4643  N   MET B 111      50.000 -31.496  22.141  1.00 65.81           N  
ANISOU 4643  N   MET B 111     6474   7487  11043   -924  -1806   -488       N  
ATOM   4644  CA  MET B 111      50.830 -32.386  21.331  1.00 65.13           C  
ANISOU 4644  CA  MET B 111     6181   7384  11180   -836  -1829   -389       C  
ATOM   4645  C   MET B 111      51.067 -31.798  19.946  1.00 63.21           C  
ANISOU 4645  C   MET B 111     5728   7124  11162   -785  -1625   -390       C  
ATOM   4646  O   MET B 111      50.269 -31.001  19.454  1.00 61.71           O  
ANISOU 4646  O   MET B 111     5579   6949  10919   -792  -1434   -438       O  
ATOM   4647  CB  MET B 111      50.179 -33.763  21.199  1.00 64.37           C  
ANISOU 4647  CB  MET B 111     6166   7327  10964   -763  -1776   -313       C  
ATOM   4648  CG  MET B 111      49.846 -34.428  22.524  1.00 65.57           C  
ANISOU 4648  CG  MET B 111     6544   7497  10872   -817  -1951   -286       C  
ATOM   4649  SD  MET B 111      49.181 -36.083  22.292  1.00 64.88           S  
ANISOU 4649  SD  MET B 111     6521   7429  10701   -734  -1892   -180       S  
ATOM   4650  CE  MET B 111      48.356 -36.341  23.863  1.00 66.20           C  
ANISOU 4650  CE  MET B 111     7013   7633  10505   -834  -1996   -172       C  
ATOM   4651  N   ASN B 112      52.168 -32.215  19.327  1.00 63.05           N  
ANISOU 4651  N   ASN B 112     5485   7071  11398   -732  -1664   -329       N  
ATOM   4652  CA  ASN B 112      52.596 -31.695  18.032  1.00 62.09           C  
ANISOU 4652  CA  ASN B 112     5157   6934  11499   -691  -1474   -318       C  
ATOM   4653  C   ASN B 112      51.679 -32.182  16.907  1.00 59.94           C  
ANISOU 4653  C   ASN B 112     4915   6715  11142   -603  -1219   -294       C  
ATOM   4654  O   ASN B 112      51.542 -33.388  16.709  1.00 59.77           O  
ANISOU 4654  O   ASN B 112     4907   6715  11088   -529  -1214   -253       O  
ATOM   4655  CB  ASN B 112      54.040 -32.131  17.759  1.00 63.54           C  
ANISOU 4655  CB  ASN B 112     5091   7067  11984   -657  -1577   -264       C  
ATOM   4656  CG  ASN B 112      54.700 -31.335  16.645  1.00 63.69           C  
ANISOU 4656  CG  ASN B 112     4888   7057  12252   -651  -1402   -255       C  
ATOM   4657  OD1 ASN B 112      54.035 -30.790  15.767  1.00 62.15           O  
ANISOU 4657  OD1 ASN B 112     4723   6892  11996   -637  -1170   -263       O  
ATOM   4658  ND2 ASN B 112      56.025 -31.276  16.676  1.00 65.69           N  
ANISOU 4658  ND2 ASN B 112     4913   7248  12796   -663  -1517   -230       N  
ATOM   4659  N   PRO B 113      51.043 -31.248  16.169  1.00 58.73           N  
ANISOU 4659  N   PRO B 113     4777   6575  10960   -613  -1023   -320       N  
ATOM   4660  CA  PRO B 113      50.174 -31.640  15.052  1.00 57.03           C  
ANISOU 4660  CA  PRO B 113     4594   6410  10663   -536   -804   -297       C  
ATOM   4661  C   PRO B 113      50.891 -32.402  13.936  1.00 57.14           C  
ANISOU 4661  C   PRO B 113     4443   6431  10834   -448   -703   -246       C  
ATOM   4662  O   PRO B 113      50.291 -33.271  13.306  1.00 56.24           O  
ANISOU 4662  O   PRO B 113     4382   6357  10629   -375   -601   -233       O  
ATOM   4663  CB  PRO B 113      49.655 -30.301  14.517  1.00 56.50           C  
ANISOU 4663  CB  PRO B 113     4539   6334  10593   -575   -658   -319       C  
ATOM   4664  CG  PRO B 113      49.791 -29.352  15.650  1.00 57.50           C  
ANISOU 4664  CG  PRO B 113     4721   6413  10714   -673   -799   -382       C  
ATOM   4665  CD  PRO B 113      51.014 -29.791  16.394  1.00 59.15           C  
ANISOU 4665  CD  PRO B 113     4837   6589  11046   -699  -1013   -373       C  
ATOM   4666  N   MET B 114      52.158 -32.074  13.700  1.00 58.89           N  
ANISOU 4666  N   MET B 114     4466   6610  11298   -458   -725   -225       N  
ATOM   4667  CA  MET B 114      52.933 -32.709  12.634  1.00 59.73           C  
ANISOU 4667  CA  MET B 114     4399   6717  11576   -376   -598   -188       C  
ATOM   4668  C   MET B 114      53.252 -34.165  12.965  1.00 59.41           C  
ANISOU 4668  C   MET B 114     4339   6665  11567   -303   -711   -177       C  
ATOM   4669  O   MET B 114      53.257 -35.018  12.077  1.00 59.11           O  
ANISOU 4669  O   MET B 114     4261   6645  11552   -213   -577   -172       O  
ATOM   4670  CB  MET B 114      54.231 -31.934  12.374  1.00 62.38           C  
ANISOU 4670  CB  MET B 114     4504   6999  12196   -415   -584   -166       C  
ATOM   4671  CG  MET B 114      54.034 -30.483  11.942  1.00 63.07           C  
ANISOU 4671  CG  MET B 114     4589   7076  12295   -489   -461   -161       C  
ATOM   4672  SD  MET B 114      52.937 -30.250  10.522  1.00 62.62           S  
ANISOU 4672  SD  MET B 114     4646   7088  12055   -441   -172   -134       S  
ATOM   4673  CE  MET B 114      53.749 -31.264   9.284  1.00 63.58           C  
ANISOU 4673  CE  MET B 114     4614   7240  12302   -339     11   -103       C  
ATOM   4674  N   ASP B 115      53.519 -34.442  14.240  1.00 59.41           N  
ANISOU 4674  N   ASP B 115     4377   6630  11565   -343   -964   -175       N  
ATOM   4675  CA  ASP B 115      53.740 -35.812  14.708  1.00 59.30           C  
ANISOU 4675  CA  ASP B 115     4370   6591  11570   -281  -1107   -146       C  
ATOM   4676  C   ASP B 115      52.438 -36.611  14.748  1.00 57.36           C  
ANISOU 4676  C   ASP B 115     4339   6388  11065   -249  -1059   -151       C  
ATOM   4677  O   ASP B 115      52.424 -37.793  14.411  1.00 57.48           O  
ANISOU 4677  O   ASP B 115     4341   6388  11109   -165  -1040   -134       O  
ATOM   4678  CB  ASP B 115      54.401 -35.816  16.092  1.00 60.73           C  
ANISOU 4678  CB  ASP B 115     4547   6720  11804   -345  -1415   -125       C  
ATOM   4679  CG  ASP B 115      55.859 -35.380  16.052  1.00 62.49           C  
ANISOU 4679  CG  ASP B 115     4508   6879  12354   -360  -1504   -111       C  
ATOM   4680  OD1 ASP B 115      56.555 -35.688  15.060  1.00 62.70           O  
ANISOU 4680  OD1 ASP B 115     4329   6885  12609   -283  -1355   -100       O  
ATOM   4681  OD2 ASP B 115      56.315 -34.740  17.024  1.00 63.52           O  
ANISOU 4681  OD2 ASP B 115     4639   6976  12518   -450  -1722   -118       O  
ATOM   4682  N   LEU B 116      51.348 -35.971  15.167  1.00 55.98           N  
ANISOU 4682  N   LEU B 116     4351   6257  10660   -316  -1036   -178       N  
ATOM   4683  CA  LEU B 116      50.031 -36.614  15.167  1.00 54.38           C  
ANISOU 4683  CA  LEU B 116     4336   6094  10231   -296   -969   -183       C  
ATOM   4684  C   LEU B 116      49.651 -37.088  13.765  1.00 53.54           C  
ANISOU 4684  C   LEU B 116     4190   6014  10140   -209   -756   -192       C  
ATOM   4685  O   LEU B 116      49.154 -38.199  13.600  1.00 53.15           O  
ANISOU 4685  O   LEU B 116     4203   5960  10029   -155   -745   -185       O  
ATOM   4686  CB  LEU B 116      48.953 -35.667  15.707  1.00 53.28           C  
ANISOU 4686  CB  LEU B 116     4366   5992   9885   -378   -938   -221       C  
ATOM   4687  CG  LEU B 116      48.936 -35.442  17.221  1.00 54.16           C  
ANISOU 4687  CG  LEU B 116     4606   6091   9880   -466  -1137   -229       C  
ATOM   4688  CD1 LEU B 116      48.083 -34.234  17.573  1.00 53.65           C  
ANISOU 4688  CD1 LEU B 116     4662   6050   9672   -542  -1064   -294       C  
ATOM   4689  CD2 LEU B 116      48.434 -36.675  17.957  1.00 54.34           C  
ANISOU 4689  CD2 LEU B 116     4771   6116   9760   -457  -1235   -184       C  
ATOM   4690  N   LYS B 117      49.900 -36.246  12.765  1.00 53.56           N  
ANISOU 4690  N   LYS B 117     4095   6036  10219   -202   -593   -207       N  
ATOM   4691  CA  LYS B 117      49.625 -36.593  11.370  1.00 53.31           C  
ANISOU 4691  CA  LYS B 117     4038   6036  10180   -128   -390   -219       C  
ATOM   4692  C   LYS B 117      50.487 -37.759  10.892  1.00 54.89           C  
ANISOU 4692  C   LYS B 117     4115   6200  10539    -36   -378   -220       C  
ATOM   4693  O   LYS B 117      49.995 -38.665  10.220  1.00 54.89           O  
ANISOU 4693  O   LYS B 117     4169   6210  10476     30   -294   -244       O  
ATOM   4694  CB  LYS B 117      49.851 -35.382  10.462  1.00 53.29           C  
ANISOU 4694  CB  LYS B 117     3961   6057  10227   -151   -227   -215       C  
ATOM   4695  CG  LYS B 117      49.744 -35.682   8.974  1.00 53.20           C  
ANISOU 4695  CG  LYS B 117     3929   6084  10197    -80    -18   -221       C  
ATOM   4696  CD  LYS B 117      50.050 -34.454   8.133  1.00 53.89           C  
ANISOU 4696  CD  LYS B 117     3950   6192  10333   -114    136   -191       C  
ATOM   4697  CE  LYS B 117      50.528 -34.834   6.739  1.00 54.85           C  
ANISOU 4697  CE  LYS B 117     4004   6343  10493    -45    341   -192       C  
ATOM   4698  NZ  LYS B 117      49.525 -35.645   5.995  1.00 54.15           N  
ANISOU 4698  NZ  LYS B 117     4062   6300  10209     13    410   -226       N  
ATOM   4699  N   ARG B 118      51.773 -37.725  11.233  1.00 56.89           N  
ANISOU 4699  N   ARG B 118     4194   6402  11016    -33   -465   -201       N  
ATOM   4700  CA  ARG B 118      52.721 -38.756  10.797  1.00 58.38           C  
ANISOU 4700  CA  ARG B 118     4229   6540  11412     60   -447   -206       C  
ATOM   4701  C   ARG B 118      52.381 -40.113  11.416  1.00 57.88           C  
ANISOU 4701  C   ARG B 118     4251   6430  11310    107   -594   -197       C  
ATOM   4702  O   ARG B 118      52.535 -41.151  10.771  1.00 58.10           O  
ANISOU 4702  O   ARG B 118     4236   6424  11413    200   -519   -225       O  
ATOM   4703  CB  ARG B 118      54.153 -38.345  11.153  1.00 60.78           C  
ANISOU 4703  CB  ARG B 118     4307   6788  11998     44   -535   -180       C  
ATOM   4704  CG  ARG B 118      55.238 -38.997  10.306  1.00 63.06           C  
ANISOU 4704  CG  ARG B 118     4377   7030  12549    141   -412   -198       C  
ATOM   4705  CD  ARG B 118      56.570 -38.267  10.454  1.00 65.54           C  
ANISOU 4705  CD  ARG B 118     4444   7299  13156    108   -446   -171       C  
ATOM   4706  NE  ARG B 118      56.481 -36.858  10.063  1.00 65.80           N  
ANISOU 4706  NE  ARG B 118     4475   7382  13141     22   -318   -162       N  
ATOM   4707  CZ  ARG B 118      57.433 -35.946  10.271  1.00 67.80           C  
ANISOU 4707  CZ  ARG B 118     4546   7599  13615    -42   -353   -136       C  
ATOM   4708  NH1 ARG B 118      58.580 -36.273  10.865  1.00 69.90           N  
ANISOU 4708  NH1 ARG B 118     4601   7783  14174    -30   -523   -117       N  
ATOM   4709  NH2 ARG B 118      57.237 -34.690   9.878  1.00 67.52           N  
ANISOU 4709  NH2 ARG B 118     4530   7598  13526   -121   -229   -123       N  
ATOM   4710  N   GLY B 119      51.915 -40.093  12.663  1.00 57.20           N  
ANISOU 4710  N   GLY B 119     4295   6337  11102     39   -794   -159       N  
ATOM   4711  CA  GLY B 119      51.449 -41.300  13.342  1.00 56.93           C  
ANISOU 4711  CA  GLY B 119     4374   6258  10996     62   -933   -128       C  
ATOM   4712  C   GLY B 119      50.191 -41.875  12.717  1.00 55.28           C  
ANISOU 4712  C   GLY B 119     4315   6082  10605     90   -797   -162       C  
ATOM   4713  O   GLY B 119      50.063 -43.091  12.581  1.00 55.38           O  
ANISOU 4713  O   GLY B 119     4347   6040  10655    155   -819   -161       O  
ATOM   4714  N   ILE B 120      49.261 -40.998  12.338  1.00 53.65           N  
ANISOU 4714  N   ILE B 120     4209   5953  10222     41   -669   -191       N  
ATOM   4715  CA  ILE B 120      48.032 -41.409  11.654  1.00 52.09           C  
ANISOU 4715  CA  ILE B 120     4138   5789   9865     61   -546   -226       C  
ATOM   4716  C   ILE B 120      48.360 -42.059  10.311  1.00 52.49           C  
ANISOU 4716  C   ILE B 120     4107   5827  10007    158   -395   -281       C  
ATOM   4717  O   ILE B 120      47.843 -43.128   9.994  1.00 52.22           O  
ANISOU 4717  O   ILE B 120     4136   5760   9943    206   -384   -307       O  
ATOM   4718  CB  ILE B 120      47.076 -40.215  11.429  1.00 50.51           C  
ANISOU 4718  CB  ILE B 120     4029   5665   9498     -4   -444   -242       C  
ATOM   4719  CG1 ILE B 120      46.494 -39.742  12.763  1.00 50.15           C  
ANISOU 4719  CG1 ILE B 120     4100   5626   9327    -96   -567   -213       C  
ATOM   4720  CG2 ILE B 120      45.938 -40.596  10.490  1.00 49.52           C  
ANISOU 4720  CG2 ILE B 120     3996   5570   9249     25   -320   -280       C  
ATOM   4721  CD1 ILE B 120      45.963 -38.325  12.734  1.00 49.37           C  
ANISOU 4721  CD1 ILE B 120     4039   5577   9142   -160   -490   -233       C  
ATOM   4722  N   ASP B 121      49.231 -41.414   9.539  1.00 53.30           N  
ANISOU 4722  N   ASP B 121     4074   5951  10225    182   -274   -301       N  
ATOM   4723  CA  ASP B 121      49.617 -41.914   8.218  1.00 54.16           C  
ANISOU 4723  CA  ASP B 121     4114   6060  10402    270    -97   -363       C  
ATOM   4724  C   ASP B 121      50.311 -43.275   8.295  1.00 55.39           C  
ANISOU 4724  C   ASP B 121     4184   6121  10740    361   -154   -388       C  
ATOM   4725  O   ASP B 121      50.055 -44.149   7.466  1.00 55.77           O  
ANISOU 4725  O   ASP B 121     4268   6149  10773    432    -56   -457       O  
ATOM   4726  CB  ASP B 121      50.528 -40.910   7.501  1.00 55.10           C  
ANISOU 4726  CB  ASP B 121     4093   6216  10624    267     53   -364       C  
ATOM   4727  CG  ASP B 121      49.810 -39.621   7.125  1.00 54.08           C  
ANISOU 4727  CG  ASP B 121     4052   6168  10325    193    142   -342       C  
ATOM   4728  OD1 ASP B 121      48.566 -39.634   6.987  1.00 52.79           O  
ANISOU 4728  OD1 ASP B 121     4052   6043   9963    173    143   -351       O  
ATOM   4729  OD2 ASP B 121      50.499 -38.591   6.963  1.00 54.69           O  
ANISOU 4729  OD2 ASP B 121     4024   6261  10491    156    207   -311       O  
ATOM   4730  N   LYS B 122      51.183 -43.450   9.287  1.00 56.17           N  
ANISOU 4730  N   LYS B 122     4172   6152  11017    358   -325   -333       N  
ATOM   4731  CA  LYS B 122      51.872 -44.726   9.492  1.00 57.47           C  
ANISOU 4731  CA  LYS B 122     4242   6204  11388    445   -414   -338       C  
ATOM   4732  C   LYS B 122      50.887 -45.837   9.854  1.00 56.52           C  
ANISOU 4732  C   LYS B 122     4285   6035  11154    456   -510   -332       C  
ATOM   4733  O   LYS B 122      51.033 -46.972   9.400  1.00 57.34           O  
ANISOU 4733  O   LYS B 122     4361   6056  11367    545   -481   -382       O  
ATOM   4734  CB  LYS B 122      52.941 -44.604  10.583  1.00 58.94           C  
ANISOU 4734  CB  LYS B 122     4286   6326  11782    428   -623   -260       C  
ATOM   4735  CG  LYS B 122      53.794 -45.856  10.746  1.00 60.99           C  
ANISOU 4735  CG  LYS B 122     4410   6454  12309    530   -722   -254       C  
ATOM   4736  CD  LYS B 122      54.929 -45.652  11.735  1.00 62.73           C  
ANISOU 4736  CD  LYS B 122     4466   6609  12757    513   -944   -172       C  
ATOM   4737  CE  LYS B 122      55.750 -46.922  11.892  1.00 64.87           C  
ANISOU 4737  CE  LYS B 122     4592   6733  13321    624  -1058   -156       C  
ATOM   4738  NZ  LYS B 122      56.856 -46.758  12.874  1.00 66.78           N  
ANISOU 4738  NZ  LYS B 122     4666   6904  13802    608  -1312    -66       N  
ATOM   4739  N   ALA B 123      49.896 -45.504  10.678  1.00 54.93           N  
ANISOU 4739  N   ALA B 123     4248   5874  10746    363   -613   -276       N  
ATOM   4740  CA  ALA B 123      48.853 -46.453  11.062  1.00 54.14           C  
ANISOU 4740  CA  ALA B 123     4307   5734  10529    352   -688   -257       C  
ATOM   4741  C   ALA B 123      47.991 -46.853   9.867  1.00 53.21           C  
ANISOU 4741  C   ALA B 123     4266   5638  10312    390   -517   -352       C  
ATOM   4742  O   ALA B 123      47.603 -48.013   9.743  1.00 53.34           O  
ANISOU 4742  O   ALA B 123     4334   5574  10357    431   -545   -375       O  
ATOM   4743  CB  ALA B 123      47.984 -45.865  12.163  1.00 53.14           C  
ANISOU 4743  CB  ALA B 123     4330   5658  10201    237   -794   -184       C  
ATOM   4744  N   VAL B 124      47.697 -45.891   8.995  1.00 52.28           N  
ANISOU 4744  N   VAL B 124     4160   5621  10080    371   -355   -402       N  
ATOM   4745  CA  VAL B 124      46.908 -46.153   7.792  1.00 51.84           C  
ANISOU 4745  CA  VAL B 124     4188   5599   9910    400   -209   -492       C  
ATOM   4746  C   VAL B 124      47.699 -46.995   6.793  1.00 53.50           C  
ANISOU 4746  C   VAL B 124     4309   5750  10266    511    -99   -587       C  
ATOM   4747  O   VAL B 124      47.167 -47.954   6.237  1.00 54.18           O  
ANISOU 4747  O   VAL B 124     4470   5789  10326    553    -74   -662       O  
ATOM   4748  CB  VAL B 124      46.434 -44.844   7.124  1.00 50.74           C  
ANISOU 4748  CB  VAL B 124     4090   5579   9609    350    -81   -501       C  
ATOM   4749  CG1 VAL B 124      45.823 -45.113   5.754  1.00 50.68           C  
ANISOU 4749  CG1 VAL B 124     4161   5606   9488    389     57   -593       C  
ATOM   4750  CG2 VAL B 124      45.424 -44.139   8.016  1.00 49.46           C  
ANISOU 4750  CG2 VAL B 124     4031   5460   9302    251   -169   -434       C  
ATOM   4751  N   THR B 125      48.962 -46.640   6.569  1.00 54.75           N  
ANISOU 4751  N   THR B 125     4304   5906  10589    555    -29   -594       N  
ATOM   4752  CA  THR B 125      49.828 -47.406   5.667  1.00 56.51           C  
ANISOU 4752  CA  THR B 125     4420   6069  10980    667    101   -693       C  
ATOM   4753  C   THR B 125      49.905 -48.868   6.102  1.00 57.62           C  
ANISOU 4753  C   THR B 125     4552   6064  11276    734    -22   -712       C  
ATOM   4754  O   THR B 125      49.810 -49.775   5.275  1.00 58.28           O  
ANISOU 4754  O   THR B 125     4663   6091  11387    809     70   -826       O  
ATOM   4755  CB  THR B 125      51.256 -46.828   5.612  1.00 57.76           C  
ANISOU 4755  CB  THR B 125     4366   6228  11353    698    175   -676       C  
ATOM   4756  OG1 THR B 125      51.198 -45.415   5.387  1.00 56.97           O  
ANISOU 4756  OG1 THR B 125     4271   6245  11129    620    263   -634       O  
ATOM   4757  CG2 THR B 125      52.060 -47.478   4.495  1.00 59.67           C  
ANISOU 4757  CG2 THR B 125     4503   6425  11742    811    377   -798       C  
ATOM   4758  N   ALA B 126      50.073 -49.081   7.406  1.00 57.93           N  
ANISOU 4758  N   ALA B 126     4563   6038  11410    702   -239   -600       N  
ATOM   4759  CA  ALA B 126      50.093 -50.423   7.989  1.00 59.06           C  
ANISOU 4759  CA  ALA B 126     4710   6030  11698    751   -392   -579       C  
ATOM   4760  C   ALA B 126      48.738 -51.109   7.854  1.00 58.26           C  
ANISOU 4760  C   ALA B 126     4800   5910  11426    719   -412   -607       C  
ATOM   4761  O   ALA B 126      48.669 -52.299   7.546  1.00 59.57           O  
ANISOU 4761  O   ALA B 126     4977   5955  11699    788   -420   -671       O  
ATOM   4762  CB  ALA B 126      50.501 -50.356   9.453  1.00 59.36           C  
ANISOU 4762  CB  ALA B 126     4708   6020  11823    703   -633   -429       C  
ATOM   4763  N   ALA B 127      47.668 -50.355   8.092  1.00 56.66           N  
ANISOU 4763  N   ALA B 127     4733   5813  10978    615   -420   -563       N  
ATOM   4764  CA  ALA B 127      46.307 -50.882   7.991  1.00 55.91           C  
ANISOU 4764  CA  ALA B 127     4802   5708  10732    570   -439   -582       C  
ATOM   4765  C   ALA B 127      45.969 -51.348   6.577  1.00 56.57           C  
ANISOU 4765  C   ALA B 127     4927   5788  10776    630   -287   -738       C  
ATOM   4766  O   ALA B 127      45.345 -52.390   6.404  1.00 57.05           O  
ANISOU 4766  O   ALA B 127     5063   5756  10856    644   -327   -786       O  
ATOM   4767  CB  ALA B 127      45.298 -49.843   8.460  1.00 54.04           C  
ANISOU 4767  CB  ALA B 127     4672   5590  10270    454   -453   -514       C  
ATOM   4768  N   VAL B 128      46.387 -50.580   5.575  1.00 57.24           N  
ANISOU 4768  N   VAL B 128     4972   5972  10803    658   -117   -814       N  
ATOM   4769  CA  VAL B 128      46.126 -50.928   4.177  1.00 58.50           C  
ANISOU 4769  CA  VAL B 128     5195   6146  10884    710     33   -967       C  
ATOM   4770  C   VAL B 128      46.829 -52.231   3.785  1.00 61.25           C  
ANISOU 4770  C   VAL B 128     5480   6348  11441    823     63  -1077       C  
ATOM   4771  O   VAL B 128      46.260 -53.049   3.063  1.00 62.20           O  
ANISOU 4771  O   VAL B 128     5698   6415  11519    852     92  -1198       O  
ATOM   4772  CB  VAL B 128      46.535 -49.787   3.217  1.00 58.38           C  
ANISOU 4772  CB  VAL B 128     5157   6269  10754    712    221  -1005       C  
ATOM   4773  CG1 VAL B 128      46.499 -50.247   1.764  1.00 59.72           C  
ANISOU 4773  CG1 VAL B 128     5397   6449  10843    777    387  -1170       C  
ATOM   4774  CG2 VAL B 128      45.617 -48.589   3.404  1.00 56.44           C  
ANISOU 4774  CG2 VAL B 128     4998   6147  10296    607    195   -918       C  
ATOM   4775  N   GLU B 129      48.057 -52.422   4.263  1.00 63.29           N  
ANISOU 4775  N   GLU B 129     5572   6534  11941    888     45  -1042       N  
ATOM   4776  CA  GLU B 129      48.790 -53.668   4.020  1.00 65.91           C  
ANISOU 4776  CA  GLU B 129     5816   6702  12523   1006     61  -1138       C  
ATOM   4777  C   GLU B 129      48.126 -54.852   4.715  1.00 66.27           C  
ANISOU 4777  C   GLU B 129     5936   6596  12646    997   -126  -1102       C  
ATOM   4778  O   GLU B 129      48.036 -55.940   4.147  1.00 67.77           O  
ANISOU 4778  O   GLU B 129     6155   6662  12931   1067    -96  -1228       O  
ATOM   4779  CB  GLU B 129      50.249 -53.548   4.477  1.00 67.48           C  
ANISOU 4779  CB  GLU B 129     5791   6848  12998   1074     58  -1086       C  
ATOM   4780  CG  GLU B 129      51.081 -52.583   3.646  1.00 68.42           C  
ANISOU 4780  CG  GLU B 129     5804   7083  13107   1099    282  -1142       C  
ATOM   4781  CD  GLU B 129      51.131 -52.962   2.177  1.00 70.05           C  
ANISOU 4781  CD  GLU B 129     6060   7301  13253   1175    530  -1339       C  
ATOM   4782  OE1 GLU B 129      51.474 -54.125   1.868  1.00 71.96           O  
ANISOU 4782  OE1 GLU B 129     6263   7398  13680   1278    560  -1457       O  
ATOM   4783  OE2 GLU B 129      50.823 -52.095   1.331  1.00 69.88           O  
ANISOU 4783  OE2 GLU B 129     6126   7429  12994   1131    692  -1377       O  
ATOM   4784  N   GLU B 130      47.661 -54.632   5.942  1.00 65.38           N  
ANISOU 4784  N   GLU B 130     5861   6488  12492    907   -312   -932       N  
ATOM   4785  CA  GLU B 130      46.952 -55.663   6.699  1.00 65.76           C  
ANISOU 4785  CA  GLU B 130     5993   6401  12591    875   -486   -863       C  
ATOM   4786  C   GLU B 130      45.596 -55.964   6.058  1.00 65.07           C  
ANISOU 4786  C   GLU B 130     6071   6330  12320    822   -449   -949       C  
ATOM   4787  O   GLU B 130      45.092 -57.084   6.145  1.00 65.82           O  
ANISOU 4787  O   GLU B 130     6224   6282  12503    828   -530   -971       O  
ATOM   4788  CB  GLU B 130      46.762 -55.223   8.155  1.00 65.07           C  
ANISOU 4788  CB  GLU B 130     5927   6340  12455    778   -666   -658       C  
ATOM   4789  CG  GLU B 130      46.667 -56.374   9.145  1.00 66.40           C  
ANISOU 4789  CG  GLU B 130     6120   6333  12774    775   -861   -545       C  
ATOM   4790  CD  GLU B 130      48.002 -57.056   9.389  1.00 68.62           C  
ANISOU 4790  CD  GLU B 130     6239   6465  13368    889   -939   -527       C  
ATOM   4791  OE1 GLU B 130      49.027 -56.351   9.512  1.00 68.75           O  
ANISOU 4791  OE1 GLU B 130     6119   6539  13464    922   -928   -504       O  
ATOM   4792  OE2 GLU B 130      48.025 -58.302   9.469  1.00 70.71           O  
ANISOU 4792  OE2 GLU B 130     6502   6542  13822    945  -1020   -532       O  
ATOM   4793  N   LEU B 131      45.017 -54.948   5.422  1.00 64.08           N  
ANISOU 4793  N   LEU B 131     6015   6373  11958    767   -340   -990       N  
ATOM   4794  CA  LEU B 131      43.745 -55.076   4.708  1.00 63.77           C  
ANISOU 4794  CA  LEU B 131     6119   6367  11741    714   -313  -1075       C  
ATOM   4795  C   LEU B 131      43.891 -55.919   3.436  1.00 65.28           C  
ANISOU 4795  C   LEU B 131     6341   6485  11977    803   -211  -1280       C  
ATOM   4796  O   LEU B 131      42.973 -56.649   3.065  1.00 65.29           O  
ANISOU 4796  O   LEU B 131     6446   6416  11944    778   -258  -1358       O  
ATOM   4797  CB  LEU B 131      43.202 -53.682   4.361  1.00 62.28           C  
ANISOU 4797  CB  LEU B 131     5981   6373  11307    641   -236  -1051       C  
ATOM   4798  CG  LEU B 131      41.709 -53.522   4.079  1.00 61.43           C  
ANISOU 4798  CG  LEU B 131     6005   6316  11017    552   -271  -1063       C  
ATOM   4799  CD1 LEU B 131      40.886 -53.727   5.342  1.00 60.63           C  
ANISOU 4799  CD1 LEU B 131     5932   6167  10937    460   -413   -920       C  
ATOM   4800  CD2 LEU B 131      41.444 -52.141   3.500  1.00 60.49           C  
ANISOU 4800  CD2 LEU B 131     5914   6374  10693    513   -176  -1058       C  
ATOM   4801  N   LYS B 132      45.042 -55.807   2.773  1.00 66.59           N  
ANISOU 4801  N   LYS B 132     6414   6662  12222    903    -65  -1375       N  
ATOM   4802  CA  LYS B 132      45.341 -56.617   1.586  1.00 68.66           C  
ANISOU 4802  CA  LYS B 132     6705   6850  12533    998     60  -1588       C  
ATOM   4803  C   LYS B 132      45.536 -58.092   1.932  1.00 70.19           C  
ANISOU 4803  C   LYS B 132     6863   6811  12992   1066    -37  -1635       C  
ATOM   4804  O   LYS B 132      45.192 -58.968   1.137  1.00 71.46           O  
ANISOU 4804  O   LYS B 132     7109   6877  13164   1105     -5  -1807       O  
ATOM   4805  CB  LYS B 132      46.589 -56.094   0.868  1.00 69.97           C  
ANISOU 4805  CB  LYS B 132     6763   7085  12735   1087    271  -1668       C  
ATOM   4806  CG  LYS B 132      46.374 -54.790   0.120  1.00 69.28           C  
ANISOU 4806  CG  LYS B 132     6743   7208  12370   1032    409  -1669       C  
ATOM   4807  CD  LYS B 132      47.674 -54.269  -0.469  1.00 70.78           C  
ANISOU 4807  CD  LYS B 132     6809   7458  12626   1109    628  -1720       C  
ATOM   4808  CE  LYS B 132      47.487 -52.893  -1.090  1.00 69.96           C  
ANISOU 4808  CE  LYS B 132     6768   7556  12257   1042    753  -1679       C  
ATOM   4809  NZ  LYS B 132      48.774 -52.321  -1.573  1.00 71.30           N  
ANISOU 4809  NZ  LYS B 132     6799   7781  12508   1101    975  -1702       N  
ATOM   4810  N   ALA B 133      46.098 -58.360   3.108  1.00 70.22           N  
ANISOU 4810  N   ALA B 133     6750   6716  13211   1079   -167  -1482       N  
ATOM   4811  CA  ALA B 133      46.278 -59.729   3.591  1.00 71.83           C  
ANISOU 4811  CA  ALA B 133     6917   6684  13689   1137   -291  -1482       C  
ATOM   4812  C   ALA B 133      44.933 -60.392   3.882  1.00 71.29           C  
ANISOU 4812  C   ALA B 133     6994   6537  13553   1043   -432  -1451       C  
ATOM   4813  O   ALA B 133      44.730 -61.567   3.572  1.00 72.84           O  
ANISOU 4813  O   ALA B 133     7225   6552  13897   1087   -467  -1558       O  
ATOM   4814  CB  ALA B 133      47.150 -59.738   4.838  1.00 72.18           C  
ANISOU 4814  CB  ALA B 133     6816   6659  13949   1158   -426  -1292       C  
ATOM   4815  N   LEU B 134      44.024 -59.625   4.479  1.00 69.31           N  
ANISOU 4815  N   LEU B 134     6819   6416  13099    915   -504  -1308       N  
ATOM   4816  CA  LEU B 134      42.671 -60.092   4.783  1.00 68.62           C  
ANISOU 4816  CA  LEU B 134     6853   6276  12943    809   -618  -1263       C  
ATOM   4817  C   LEU B 134      41.821 -60.273   3.518  1.00 68.39           C  
ANISOU 4817  C   LEU B 134     6938   6272  12775    795   -547  -1461       C  
ATOM   4818  O   LEU B 134      40.886 -61.076   3.504  1.00 68.74           O  
ANISOU 4818  O   LEU B 134     7059   6200  12856    742   -638  -1489       O  
ATOM   4819  CB  LEU B 134      41.985 -59.097   5.723  1.00 66.78           C  
ANISOU 4819  CB  LEU B 134     6654   6188  12531    682   -679  -1071       C  
ATOM   4820  CG  LEU B 134      40.619 -59.497   6.298  1.00 66.70           C  
ANISOU 4820  CG  LEU B 134     6740   6127  12475    560   -788   -981       C  
ATOM   4821  CD1 LEU B 134      40.743 -59.940   7.749  1.00 67.15           C  
ANISOU 4821  CD1 LEU B 134     6780   6081  12652    516   -926   -770       C  
ATOM   4822  CD2 LEU B 134      39.632 -58.346   6.186  1.00 65.12           C  
ANISOU 4822  CD2 LEU B 134     6599   6117  12023    458   -743   -953       C  
ATOM   4823  N   SER B 135      42.151 -59.525   2.467  1.00 67.93           N  
ANISOU 4823  N   SER B 135     6893   6359  12556    837   -391  -1591       N  
ATOM   4824  CA  SER B 135      41.392 -59.542   1.216  1.00 68.20           C  
ANISOU 4824  CA  SER B 135     7056   6446  12409    819   -333  -1774       C  
ATOM   4825  C   SER B 135      41.337 -60.921   0.553  1.00 70.46           C  
ANISOU 4825  C   SER B 135     7394   6535  12840    881   -348  -1970       C  
ATOM   4826  O   SER B 135      42.368 -61.560   0.337  1.00 72.42           O  
ANISOU 4826  O   SER B 135     7573   6667  13276    999   -274  -2069       O  
ATOM   4827  CB  SER B 135      41.987 -58.534   0.228  1.00 68.10           C  
ANISOU 4827  CB  SER B 135     7051   6616  12206    864   -148  -1864       C  
ATOM   4828  OG  SER B 135      41.235 -58.486  -0.973  1.00 68.68           O  
ANISOU 4828  OG  SER B 135     7273   6754  12068    839   -110  -2024       O  
ATOM   4829  N   VAL B 136      40.120 -61.359   0.234  1.00 81.59           N  
ANISOU 4829  N   VAL B 136     9544   9514  11940    151   -208  -1323       N  
ATOM   4830  CA  VAL B 136      39.890 -62.584  -0.526  1.00 82.10           C  
ANISOU 4830  CA  VAL B 136     9709   9295  12190    255   -354  -1254       C  
ATOM   4831  C   VAL B 136      39.794 -62.200  -2.006  1.00 81.00           C  
ANISOU 4831  C   VAL B 136     9665   8997  12111    272   -387  -1443       C  
ATOM   4832  O   VAL B 136      38.991 -61.337  -2.360  1.00 79.99           O  
ANISOU 4832  O   VAL B 136     9550   8816  12025    153   -331  -1505       O  
ATOM   4833  CB  VAL B 136      38.579 -63.276  -0.096  1.00 82.91           C  
ANISOU 4833  CB  VAL B 136     9818   9208  12472    172   -416  -1040       C  
ATOM   4834  CG1 VAL B 136      38.402 -64.601  -0.828  1.00 84.15           C  
ANISOU 4834  CG1 VAL B 136    10109   9024  12838    260   -615   -971       C  
ATOM   4835  CG2 VAL B 136      38.551 -63.492   1.413  1.00 84.07           C  
ANISOU 4835  CG2 VAL B 136     9828   9588  12523    127   -364   -825       C  
ATOM   4836  N   PRO B 137      40.610 -62.828  -2.878  1.00 81.54           N  
ANISOU 4836  N   PRO B 137     9790   9020  12169    442   -481  -1536       N  
ATOM   4837  CA  PRO B 137      40.561 -62.484  -4.308  1.00 80.59           C  
ANISOU 4837  CA  PRO B 137     9733   8819  12068    469   -513  -1710       C  
ATOM   4838  C   PRO B 137      39.215 -62.769  -4.976  1.00 80.05           C  
ANISOU 4838  C   PRO B 137     9766   8432  12216    402   -593  -1696       C  
ATOM   4839  O   PRO B 137      38.411 -63.542  -4.453  1.00 80.81           O  
ANISOU 4839  O   PRO B 137     9900   8332  12470    362   -669  -1541       O  
ATOM   4840  CB  PRO B 137      41.649 -63.372  -4.927  1.00 82.04           C  
ANISOU 4840  CB  PRO B 137     9941   9049  12180    722   -617  -1800       C  
ATOM   4841  CG  PRO B 137      42.559 -63.716  -3.803  1.00 83.15           C  
ANISOU 4841  CG  PRO B 137     9996   9397  12200    799   -589  -1696       C  
ATOM   4842  CD  PRO B 137      41.690 -63.788  -2.584  1.00 83.18           C  
ANISOU 4842  CD  PRO B 137     9985   9310  12307    642   -555  -1498       C  
ATOM   4843  N   CYS B 138      38.989 -62.132  -6.123  1.00 78.83           N  
ANISOU 4843  N   CYS B 138     9637   8256  12057    372   -585  -1833       N  
ATOM   4844  CA  CYS B 138      37.780 -62.333  -6.919  1.00 78.47           C  
ANISOU 4844  CA  CYS B 138     9673   7950  12190    312   -665  -1839       C  
ATOM   4845  C   CYS B 138      38.184 -62.550  -8.378  1.00 78.75           C  
ANISOU 4845  C   CYS B 138     9763   7969  12188    447   -755  -2022       C  
ATOM   4846  O   CYS B 138      38.062 -61.652  -9.215  1.00 77.69           O  
ANISOU 4846  O   CYS B 138     9597   7926  11993    382   -701  -2103       O  
ATOM   4847  CB  CYS B 138      36.851 -61.124  -6.774  1.00 77.11           C  
ANISOU 4847  CB  CYS B 138     9451   7807  12038    124   -547  -1805       C  
ATOM   4848  SG  CYS B 138      35.269 -61.271  -7.637  1.00 76.93           S  
ANISOU 4848  SG  CYS B 138     9487   7527  12217     32   -629  -1777       S  
ATOM   4849  N   SER B 139      38.669 -63.757  -8.666  1.00 80.49           N  
ANISOU 4849  N   SER B 139    10064   8081  12435    651   -904  -2085       N  
ATOM   4850  CA  SER B 139      39.283 -64.073  -9.960  1.00 81.41           C  
ANISOU 4850  CA  SER B 139    10214   8263  12454    856   -994  -2295       C  
ATOM   4851  C   SER B 139      38.307 -64.723 -10.943  1.00 82.22           C  
ANISOU 4851  C   SER B 139    10450   8064  12726    873  -1164  -2383       C  
ATOM   4852  O   SER B 139      37.942 -64.115 -11.950  1.00 81.65           O  
ANISOU 4852  O   SER B 139    10352   8061  12610    819  -1142  -2474       O  
ATOM   4853  CB  SER B 139      40.502 -64.981  -9.759  1.00 83.33           C  
ANISOU 4853  CB  SER B 139    10468   8602  12592   1139  -1072  -2366       C  
ATOM   4854  OG  SER B 139      41.517 -64.321  -9.016  1.00 82.87           O  
ANISOU 4854  OG  SER B 139    10260   8893  12335   1123   -919  -2302       O  
ATOM   4855  N   ASP B 140      37.890 -65.953 -10.647  1.00 83.91           N  
ANISOU 4855  N   ASP B 140    10806   7941  13134    931  -1351  -2341       N  
ATOM   4856  CA  ASP B 140      37.057 -66.734 -11.572  1.00 85.29           C  
ANISOU 4856  CA  ASP B 140    11133   7797  13476    951  -1566  -2444       C  
ATOM   4857  C   ASP B 140      35.641 -66.167 -11.705  1.00 83.94           C  
ANISOU 4857  C   ASP B 140    10936   7517  13440    659  -1529  -2319       C  
ATOM   4858  O   ASP B 140      35.190 -65.388 -10.862  1.00 82.20           O  
ANISOU 4858  O   ASP B 140    10605   7399  13229    460  -1364  -2127       O  
ATOM   4859  CB  ASP B 140      37.011 -68.214 -11.159  1.00 88.07           C  
ANISOU 4859  CB  ASP B 140    11666   7769  14025   1064  -1818  -2407       C  
ATOM   4860  CG  ASP B 140      36.399 -68.431  -9.781  1.00 88.10           C  
ANISOU 4860  CG  ASP B 140    11649   7626  14196    837  -1803  -2079       C  
ATOM   4861  OD1 ASP B 140      36.486 -67.521  -8.929  1.00 86.29           O  
ANISOU 4861  OD1 ASP B 140    11256   7668  13862    703  -1575  -1930       O  
ATOM   4862  OD2 ASP B 140      35.845 -69.525  -9.545  1.00 90.41           O  
ANISOU 4862  OD2 ASP B 140    12088   7544  14719    790  -2037  -1967       O  
ATOM   4863  N   SER B 141      34.950 -66.568 -12.771  1.00 84.93           N  
ANISOU 4863  N   SER B 141    11156   7457  13655    657  -1691  -2442       N  
ATOM   4864  CA  SER B 141      33.620 -66.036 -13.090  1.00 84.06           C  
ANISOU 4864  CA  SER B 141    11004   7286  13649    406  -1668  -2342       C  
ATOM   4865  C   SER B 141      32.519 -66.506 -12.131  1.00 84.64           C  
ANISOU 4865  C   SER B 141    11090   7122  13947    169  -1737  -2066       C  
ATOM   4866  O   SER B 141      31.433 -65.922 -12.111  1.00 83.97           O  
ANISOU 4866  O   SER B 141    10915   7071  13918    -40  -1669  -1930       O  
ATOM   4867  CB  SER B 141      33.236 -66.372 -14.534  1.00 85.15           C  
ANISOU 4867  CB  SER B 141    11227   7331  13794    471  -1837  -2558       C  
ATOM   4868  OG  SER B 141      33.302 -67.766 -14.768  1.00 88.08           O  
ANISOU 4868  OG  SER B 141    11796   7371  14298    604  -2122  -2677       O  
ATOM   4869  N   LYS B 142      32.791 -67.551 -11.351  1.00 86.22           N  
ANISOU 4869  N   LYS B 142    11385   7110  14263    208  -1878  -1962       N  
ATOM   4870  CA  LYS B 142      31.887 -67.963 -10.277  1.00 86.95           C  
ANISOU 4870  CA  LYS B 142    11444   7060  14532    -32  -1926  -1637       C  
ATOM   4871  C   LYS B 142      31.867 -66.901  -9.178  1.00 84.37           C  
ANISOU 4871  C   LYS B 142    10913   7063  14079   -131  -1642  -1457       C  
ATOM   4872  O   LYS B 142      30.799 -66.480  -8.733  1.00 83.82           O  
ANISOU 4872  O   LYS B 142    10723   7070  14055   -342  -1570  -1257       O  
ATOM   4873  CB  LYS B 142      32.317 -69.310  -9.688  1.00 89.99           C  
ANISOU 4873  CB  LYS B 142    11979   7147  15064     41  -2156  -1545       C  
ATOM   4874  CG  LYS B 142      31.347 -69.881  -8.663  1.00 91.73           C  
ANISOU 4874  CG  LYS B 142    12159   7217  15475   -240  -2256  -1160       C  
ATOM   4875  CD  LYS B 142      31.950 -71.053  -7.906  1.00 94.53           C  
ANISOU 4875  CD  LYS B 142    12639   7322  15953   -160  -2452  -1021       C  
ATOM   4876  CE  LYS B 142      31.053 -71.482  -6.755  1.00 96.20           C  
ANISOU 4876  CE  LYS B 142    12751   7490  16310   -469  -2515   -571       C  
ATOM   4877  NZ  LYS B 142      31.650 -72.590  -5.959  1.00 98.99           N  
ANISOU 4877  NZ  LYS B 142    13217   7607  16787   -406  -2711   -384       N  
ATOM   4878  N   ALA B 143      33.056 -66.482  -8.747  1.00 82.89           N  
ANISOU 4878  N   ALA B 143    10684   7090  13718     33  -1495  -1541       N  
ATOM   4879  CA  ALA B 143      33.198 -65.455  -7.715  1.00 80.85           C  
ANISOU 4879  CA  ALA B 143    10257   7141  13320    -33  -1247  -1427       C  
ATOM   4880  C   ALA B 143      32.685 -64.095  -8.186  1.00 78.59           C  
ANISOU 4880  C   ALA B 143     9873   7042  12943   -113  -1075  -1504       C  
ATOM   4881  O   ALA B 143      32.132 -63.331  -7.395  1.00 77.68           O  
ANISOU 4881  O   ALA B 143     9634   7090  12788   -224   -927  -1377       O  
ATOM   4882  CB  ALA B 143      34.651 -65.345  -7.276  1.00 80.60           C  
ANISOU 4882  CB  ALA B 143    10210   7294  13118    150  -1162  -1519       C  
ATOM   4883  N   ILE B 144      32.877 -63.799  -9.470  1.00 77.92           N  
ANISOU 4883  N   ILE B 144     9843   6944  12818    -37  -1104  -1711       N  
ATOM   4884  CA  ILE B 144      32.378 -62.558 -10.069  1.00 76.37           C  
ANISOU 4884  CA  ILE B 144     9571   6885  12558   -109   -977  -1766       C  
ATOM   4885  C   ILE B 144      30.849 -62.502 -10.013  1.00 76.74           C  
ANISOU 4885  C   ILE B 144     9567   6845  12743   -283  -1002  -1609       C  
ATOM   4886  O   ILE B 144      30.271 -61.446  -9.745  1.00 75.74           O  
ANISOU 4886  O   ILE B 144     9339   6863  12575   -351   -858  -1555       O  
ATOM   4887  CB  ILE B 144      32.876 -62.393 -11.526  1.00 76.14           C  
ANISOU 4887  CB  ILE B 144     9593   6887  12448      1  -1029  -1985       C  
ATOM   4888  CG1 ILE B 144      34.380 -62.096 -11.531  1.00 75.81           C  
ANISOU 4888  CG1 ILE B 144     9530   7061  12211    153   -954  -2108       C  
ATOM   4889  CG2 ILE B 144      32.131 -61.271 -12.241  1.00 75.05           C  
ANISOU 4889  CG2 ILE B 144     9389   6835  12292    -97   -947  -1991       C  
ATOM   4890  CD1 ILE B 144      35.044 -62.225 -12.886  1.00 76.41           C  
ANISOU 4890  CD1 ILE B 144     9630   7234  12167    306  -1027  -2311       C  
ATOM   4891  N   ALA B 145      30.204 -63.639 -10.263  1.00 78.60           N  
ANISOU 4891  N   ALA B 145     9875   6849  13140   -348  -1201  -1536       N  
ATOM   4892  CA  ALA B 145      28.748 -63.742 -10.182  1.00 79.55           C  
ANISOU 4892  CA  ALA B 145     9920   6917  13385   -542  -1252  -1346       C  
ATOM   4893  C   ALA B 145      28.251 -63.555  -8.747  1.00 79.97           C  
ANISOU 4893  C   ALA B 145     9826   7129  13428   -645  -1138  -1092       C  
ATOM   4894  O   ALA B 145      27.266 -62.856  -8.517  1.00 80.00           O  
ANISOU 4894  O   ALA B 145     9688   7295  13412   -732  -1036   -982       O  
ATOM   4895  CB  ALA B 145      28.281 -65.082 -10.730  1.00 81.79           C  
ANISOU 4895  CB  ALA B 145    10329   6896  13851   -620  -1533  -1315       C  
ATOM   4896  N   GLN B 146      28.938 -64.181  -7.792  1.00 80.80           N  
ANISOU 4896  N   GLN B 146     9950   7221  13527   -613  -1156  -1001       N  
ATOM   4897  CA  GLN B 146      28.579 -64.080  -6.372  1.00 81.35           C  
ANISOU 4897  CA  GLN B 146     9862   7497  13550   -697  -1051   -755       C  
ATOM   4898  C   GLN B 146      28.639 -62.642  -5.850  1.00 79.33           C  
ANISOU 4898  C   GLN B 146     9479   7552  13110   -626   -798   -834       C  
ATOM   4899  O   GLN B 146      27.760 -62.216  -5.101  1.00 79.72           O  
ANISOU 4899  O   GLN B 146     9362   7817  13111   -693   -702   -678       O  
ATOM   4900  CB  GLN B 146      29.484 -64.979  -5.518  1.00 82.85           C  
ANISOU 4900  CB  GLN B 146    10103   7628  13748   -650  -1121   -658       C  
ATOM   4901  CG  GLN B 146      29.187 -66.466  -5.654  1.00 85.76           C  
ANISOU 4901  CG  GLN B 146    10584   7670  14330   -755  -1404   -488       C  
ATOM   4902  CD  GLN B 146      30.202 -67.338  -4.930  1.00 87.35           C  
ANISOU 4902  CD  GLN B 146    10865   7775  14548   -661  -1492   -413       C  
ATOM   4903  OE1 GLN B 146      31.401 -67.268  -5.201  1.00 86.73           O  
ANISOU 4903  OE1 GLN B 146    10885   7684  14384   -445  -1461   -642       O  
ATOM   4904  NE2 GLN B 146      29.724 -68.173  -4.009  1.00 89.82           N  
ANISOU 4904  NE2 GLN B 146    11118   8046  14963   -826  -1609    -67       N  
ATOM   4905  N   VAL B 147      29.677 -61.905  -6.242  1.00 77.41           N  
ANISOU 4905  N   VAL B 147     9310   7342  12758   -487   -707  -1075       N  
ATOM   4906  CA  VAL B 147      29.840 -60.509  -5.825  1.00 75.96           C  
ANISOU 4906  CA  VAL B 147     9054   7384  12423   -429   -512  -1179       C  
ATOM   4907  C   VAL B 147      28.767 -59.628  -6.464  1.00 75.37           C  
ANISOU 4907  C   VAL B 147     8931   7331  12375   -457   -468  -1208       C  
ATOM   4908  O   VAL B 147      28.196 -58.761  -5.801  1.00 75.53           O  
ANISOU 4908  O   VAL B 147     8845   7533  12319   -435   -346  -1184       O  
ATOM   4909  CB  VAL B 147      31.248 -59.968  -6.171  1.00 74.75           C  
ANISOU 4909  CB  VAL B 147     8989   7253  12156   -321   -463  -1393       C  
ATOM   4910  CG1 VAL B 147      31.332 -58.464  -5.941  1.00 73.77           C  
ANISOU 4910  CG1 VAL B 147     8830   7282  11916   -298   -316  -1507       C  
ATOM   4911  CG2 VAL B 147      32.308 -60.681  -5.342  1.00 75.40           C  
ANISOU 4911  CG2 VAL B 147     9082   7389  12176   -267   -478  -1355       C  
ATOM   4912  N   GLY B 148      28.503 -59.848  -7.749  1.00 74.95           N  
ANISOU 4912  N   GLY B 148     8953   7107  12415   -481   -574  -1271       N  
ATOM   4913  CA  GLY B 148      27.439 -59.135  -8.453  1.00 74.59           C  
ANISOU 4913  CA  GLY B 148     8856   7079  12406   -510   -554  -1271       C  
ATOM   4914  C   GLY B 148      26.064 -59.432  -7.881  1.00 75.81           C  
ANISOU 4914  C   GLY B 148     8857   7336  12612   -606   -563  -1047       C  
ATOM   4915  O   GLY B 148      25.217 -58.542  -7.794  1.00 75.83           O  
ANISOU 4915  O   GLY B 148     8751   7486  12573   -573   -470  -1025       O  
ATOM   4916  N   THR B 149      25.847 -60.686  -7.490  1.00 77.08           N  
ANISOU 4916  N   THR B 149     9000   7428  12858   -722   -688   -866       N  
ATOM   4917  CA  THR B 149      24.589 -61.117  -6.882  1.00 78.75           C  
ANISOU 4917  CA  THR B 149     9033   7781  13107   -862   -719   -588       C  
ATOM   4918  C   THR B 149      24.353 -60.425  -5.539  1.00 79.09           C  
ANISOU 4918  C   THR B 149     8896   8164  12990   -791   -536   -501       C  
ATOM   4919  O   THR B 149      23.258 -59.926  -5.280  1.00 79.98           O  
ANISOU 4919  O   THR B 149     8827   8516  13046   -791   -464   -393       O  
ATOM   4920  CB  THR B 149      24.569 -62.647  -6.680  1.00 80.63           C  
ANISOU 4920  CB  THR B 149     9313   7838  13484  -1030   -927   -384       C  
ATOM   4921  OG1 THR B 149      24.718 -63.300  -7.948  1.00 80.76           O  
ANISOU 4921  OG1 THR B 149     9509   7535  13641  -1068  -1122   -508       O  
ATOM   4922  CG2 THR B 149      23.264 -63.106  -6.032  1.00 82.93           C  
ANISOU 4922  CG2 THR B 149     9387   8318  13805  -1226   -976    -36       C  
ATOM   4923  N   ILE B 150      25.384 -60.399  -4.696  1.00 78.71           N  
ANISOU 4923  N   ILE B 150     8888   8168  12850   -712   -465   -559       N  
ATOM   4924  CA  ILE B 150      25.302 -59.754  -3.383  1.00 79.43           C  
ANISOU 4924  CA  ILE B 150     8820   8599  12760   -623   -301   -521       C  
ATOM   4925  C   ILE B 150      25.079 -58.247  -3.526  1.00 78.82           C  
ANISOU 4925  C   ILE B 150     8733   8635  12578   -453   -157   -742       C  
ATOM   4926  O   ILE B 150      24.277 -57.660  -2.797  1.00 80.21           O  
ANISOU 4926  O   ILE B 150     8734   9109  12631   -370    -54   -693       O  
ATOM   4927  CB  ILE B 150      26.572 -60.021  -2.539  1.00 79.15           C  
ANISOU 4927  CB  ILE B 150     8845   8585  12641   -575   -269   -563       C  
ATOM   4928  CG1 ILE B 150      26.644 -61.501  -2.147  1.00 80.67           C  
ANISOU 4928  CG1 ILE B 150     9021   8697  12932   -724   -418   -289       C  
ATOM   4929  CG2 ILE B 150      26.589 -59.157  -1.281  1.00 79.71           C  
ANISOU 4929  CG2 ILE B 150     8775   9015  12494   -454    -98   -604       C  
ATOM   4930  CD1 ILE B 150      28.025 -61.964  -1.734  1.00 80.28           C  
ANISOU 4930  CD1 ILE B 150     9086   8563  12854   -666   -440   -347       C  
ATOM   4931  N   SER B 151      25.787 -57.631  -4.470  1.00 77.29           N  
ANISOU 4931  N   SER B 151     8722   8215  12427   -392   -166   -977       N  
ATOM   4932  CA  SER B 151      25.689 -56.188  -4.704  1.00 76.88           C  
ANISOU 4932  CA  SER B 151     8706   8188  12314   -249    -73  -1179       C  
ATOM   4933  C   SER B 151      24.323 -55.761  -5.244  1.00 77.37           C  
ANISOU 4933  C   SER B 151     8664   8312  12418   -220    -72  -1115       C  
ATOM   4934  O   SER B 151      23.907 -54.618  -5.042  1.00 77.99           O  
ANISOU 4934  O   SER B 151     8714   8491  12425    -61     10  -1227       O  
ATOM   4935  CB  SER B 151      26.784 -55.733  -5.671  1.00 75.49           C  
ANISOU 4935  CB  SER B 151     8731   7770  12181   -242   -110  -1378       C  
ATOM   4936  OG  SER B 151      28.068 -56.116  -5.210  1.00 75.20           O  
ANISOU 4936  OG  SER B 151     8767   7718  12086   -257   -112  -1432       O  
ATOM   4937  N   ALA B 152      23.634 -56.678  -5.922  1.00 77.38           N  
ANISOU 4937  N   ALA B 152     8615   8248  12536   -364   -180   -941       N  
ATOM   4938  CA  ALA B 152      22.308 -56.411  -6.477  1.00 78.16           C  
ANISOU 4938  CA  ALA B 152     8586   8439  12669   -364   -193   -845       C  
ATOM   4939  C   ALA B 152      21.179 -56.963  -5.596  1.00 80.14           C  
ANISOU 4939  C   ALA B 152     8574   9017  12857   -426   -177   -574       C  
ATOM   4940  O   ALA B 152      20.115 -57.328  -6.101  1.00 81.12           O  
ANISOU 4940  O   ALA B 152     8570   9211  13038   -530   -248   -400       O  
ATOM   4941  CB  ALA B 152      22.215 -56.990  -7.880  1.00 77.62           C  
ANISOU 4941  CB  ALA B 152     8615   8123  12751   -500   -341   -833       C  
ATOM   4942  N   ASN B 153      21.413 -57.012  -4.284  1.00 80.82           N  
ANISOU 4942  N   ASN B 153     8559   9341  12805   -372    -89   -523       N  
ATOM   4943  CA  ASN B 153      20.411 -57.458  -3.313  1.00 83.16           C  
ANISOU 4943  CA  ASN B 153     8563  10042  12989   -420    -56   -243       C  
ATOM   4944  C   ASN B 153      19.918 -58.888  -3.571  1.00 84.22           C  
ANISOU 4944  C   ASN B 153     8619  10119  13259   -724   -227     85       C  
ATOM   4945  O   ASN B 153      18.719 -59.133  -3.724  1.00 86.00           O  
ANISOU 4945  O   ASN B 153     8636  10553  13485   -828   -270    314       O  
ATOM   4946  CB  ASN B 153      19.239 -56.466  -3.269  1.00 84.58           C  
ANISOU 4946  CB  ASN B 153     8551  10535  13049   -226     44   -262       C  
ATOM   4947  CG  ASN B 153      18.419 -56.580  -1.995  1.00 87.39           C  
ANISOU 4947  CG  ASN B 153     8575  11439  13188   -172    136    -46       C  
ATOM   4948  OD1 ASN B 153      18.965 -56.752  -0.905  1.00 87.88           O  
ANISOU 4948  OD1 ASN B 153     8590  11680  13120   -142    198    -30       O  
ATOM   4949  ND2 ASN B 153      17.101 -56.472  -2.126  1.00 89.47           N  
ANISOU 4949  ND2 ASN B 153     8583  12023  13388   -151    148    129       N  
ATOM   4950  N   SER B 154      20.866 -59.821  -3.621  1.00 83.42           N  
ANISOU 4950  N   SER B 154     8693   9728  13275   -862   -342    106       N  
ATOM   4951  CA  SER B 154      20.587 -61.255  -3.787  1.00 84.81           C  
ANISOU 4951  CA  SER B 154     8858   9756  13610  -1150   -552    397       C  
ATOM   4952  C   SER B 154      19.833 -61.606  -5.080  1.00 85.05           C  
ANISOU 4952  C   SER B 154     8932   9576  13806  -1302   -714    433       C  
ATOM   4953  O   SER B 154      19.036 -62.545  -5.102  1.00 87.46           O  
ANISOU 4953  O   SER B 154     9124   9903  14203  -1558   -879    735       O  
ATOM   4954  CB  SER B 154      19.827 -61.797  -2.568  1.00 87.62           C  
ANISOU 4954  CB  SER B 154     8912  10522  13855  -1285   -543    782       C  
ATOM   4955  OG  SER B 154      20.476 -61.440  -1.361  1.00 87.50           O  
ANISOU 4955  OG  SER B 154     8834  10757  13655  -1132   -389    741       O  
ATOM   4956  N   ASP B 155      20.096 -60.856  -6.149  1.00 82.89           N  
ANISOU 4956  N   ASP B 155     8817   9109  13565  -1165   -684    141       N  
ATOM   4957  CA  ASP B 155      19.520 -61.140  -7.464  1.00 82.84           C  
ANISOU 4957  CA  ASP B 155     8872   8906  13697  -1286   -838    128       C  
ATOM   4958  C   ASP B 155      20.567 -61.859  -8.309  1.00 81.90           C  
ANISOU 4958  C   ASP B 155     9045   8350  13722  -1323  -1000    -56       C  
ATOM   4959  O   ASP B 155      21.553 -61.257  -8.737  1.00 79.96           O  
ANISOU 4959  O   ASP B 155     8966   7974  13440  -1145   -923   -335       O  
ATOM   4960  CB  ASP B 155      19.072 -59.841  -8.146  1.00 81.58           C  
ANISOU 4960  CB  ASP B 155     8674   8859  13464  -1099   -709    -46       C  
ATOM   4961  CG  ASP B 155      18.277 -60.082  -9.428  1.00 81.93           C  
ANISOU 4961  CG  ASP B 155     8715   8800  13614  -1229   -856    -15       C  
ATOM   4962  OD1 ASP B 155      18.337 -61.196  -9.989  1.00 82.60           O  
ANISOU 4962  OD1 ASP B 155     8906   8636  13841  -1438  -1071     40       O  
ATOM   4963  OD2 ASP B 155      17.592 -59.142  -9.882  1.00 81.64           O  
ANISOU 4963  OD2 ASP B 155     8577   8926  13516  -1110   -770    -57       O  
ATOM   4964  N   GLU B 156      20.348 -63.150  -8.544  1.00 83.84           N  
ANISOU 4964  N   GLU B 156     9349   8383  14124  -1552  -1241    104       N  
ATOM   4965  CA  GLU B 156      21.298 -63.975  -9.294  1.00 83.75           C  
ANISOU 4965  CA  GLU B 156     9618   7959  14244  -1554  -1429    -82       C  
ATOM   4966  C   GLU B 156      21.336 -63.642 -10.789  1.00 82.88           C  
ANISOU 4966  C   GLU B 156     9634   7696  14158  -1485  -1486   -346       C  
ATOM   4967  O   GLU B 156      22.321 -63.939 -11.464  1.00 82.10           O  
ANISOU 4967  O   GLU B 156     9749   7355  14087  -1377  -1566   -591       O  
ATOM   4968  CB  GLU B 156      20.983 -65.460  -9.101  1.00 86.66           C  
ANISOU 4968  CB  GLU B 156    10035   8099  14793  -1815  -1713    160       C  
ATOM   4969  CG  GLU B 156      21.149 -65.938  -7.666  1.00 88.08           C  
ANISOU 4969  CG  GLU B 156    10111   8400  14953  -1890  -1688    441       C  
ATOM   4970  CD  GLU B 156      20.998 -67.441  -7.518  1.00 91.16           C  
ANISOU 4970  CD  GLU B 156    10598   8482  15554  -2152  -2011    690       C  
ATOM   4971  OE1 GLU B 156      20.356 -68.071  -8.383  1.00 92.85           O  
ANISOU 4971  OE1 GLU B 156    10887   8466  15923  -2342  -2258    721       O  
ATOM   4972  OE2 GLU B 156      21.522 -67.992  -6.527  1.00 92.15           O  
ANISOU 4972  OE2 GLU B 156    10731   8588  15695  -2174  -2036    862       O  
ATOM   4973  N   THR B 157      20.268 -63.028 -11.298  1.00 83.32           N  
ANISOU 4973  N   THR B 157     9538   7937  14183  -1530  -1445   -288       N  
ATOM   4974  CA  THR B 157      20.202 -62.616 -12.703  1.00 82.66           C  
ANISOU 4974  CA  THR B 157     9534   7774  14098  -1469  -1487   -502       C  
ATOM   4975  C   THR B 157      21.205 -61.507 -13.024  1.00 80.24           C  
ANISOU 4975  C   THR B 157     9315   7500  13670  -1213  -1299   -767       C  
ATOM   4976  O   THR B 157      21.751 -61.461 -14.128  1.00 79.47           O  
ANISOU 4976  O   THR B 157     9353   7277  13565  -1141  -1363   -983       O  
ATOM   4977  CB  THR B 157      18.792 -62.118 -13.080  1.00 83.60           C  
ANISOU 4977  CB  THR B 157     9437   8132  14194  -1562  -1470   -344       C  
ATOM   4978  OG1 THR B 157      17.807 -62.992 -12.519  1.00 86.30           O  
ANISOU 4978  OG1 THR B 157     9629   8547  14614  -1825  -1610    -26       O  
ATOM   4979  CG2 THR B 157      18.619 -62.069 -14.596  1.00 83.56           C  
ANISOU 4979  CG2 THR B 157     9515   8018  14213  -1569  -1591   -516       C  
ATOM   4980  N   VAL B 158      21.437 -60.616 -12.060  1.00 79.31           N  
ANISOU 4980  N   VAL B 158     9113   7571  13449  -1086  -1084   -743       N  
ATOM   4981  CA  VAL B 158      22.374 -59.506 -12.237  1.00 77.36           C  
ANISOU 4981  CA  VAL B 158     8947   7345  13098   -884   -926   -958       C  
ATOM   4982  C   VAL B 158      23.815 -60.018 -12.237  1.00 76.78           C  
ANISOU 4982  C   VAL B 158     9055   7101  13015   -821   -966  -1123       C  
ATOM   4983  O   VAL B 158      24.627 -59.593 -13.059  1.00 75.77           O  
ANISOU 4983  O   VAL B 158     9029   6928  12832   -722   -954  -1315       O  
ATOM   4984  CB  VAL B 158      22.198 -58.431 -11.141  1.00 76.85           C  
ANISOU 4984  CB  VAL B 158     8761   7506  12930   -764   -719   -911       C  
ATOM   4985  CG1 VAL B 158      23.243 -57.332 -11.288  1.00 75.17           C  
ANISOU 4985  CG1 VAL B 158     8663   7263  12635   -601   -602  -1122       C  
ATOM   4986  CG2 VAL B 158      20.798 -57.836 -11.200  1.00 77.93           C  
ANISOU 4986  CG2 VAL B 158     8706   7852  13049   -761   -673   -774       C  
ATOM   4987  N   GLY B 159      24.125 -60.924 -11.311  1.00 77.80           N  
ANISOU 4987  N   GLY B 159     9204   7171  13184   -875  -1017  -1024       N  
ATOM   4988  CA  GLY B 159      25.440 -61.564 -11.258  1.00 77.64           C  
ANISOU 4988  CA  GLY B 159     9344   6995  13159   -798  -1076  -1158       C  
ATOM   4989  C   GLY B 159      25.741 -62.364 -12.513  1.00 78.52           C  
ANISOU 4989  C   GLY B 159     9607   6889  13335   -789  -1277  -1319       C  
ATOM   4990  O   GLY B 159      26.874 -62.375 -12.995  1.00 77.67           O  
ANISOU 4990  O   GLY B 159     9612   6744  13155   -643  -1281  -1523       O  
ATOM   4991  N   LYS B 160      24.717 -63.032 -13.039  1.00 80.62           N  
ANISOU 4991  N   LYS B 160     9864   7044  13721   -941  -1453  -1228       N  
ATOM   4992  CA  LYS B 160      24.813 -63.767 -14.300  1.00 82.10           C  
ANISOU 4992  CA  LYS B 160    10195   7035  13964   -934  -1671  -1407       C  
ATOM   4993  C   LYS B 160      25.128 -62.826 -15.468  1.00 80.69           C  
ANISOU 4993  C   LYS B 160    10010   6997  13649   -804  -1583  -1614       C  
ATOM   4994  O   LYS B 160      25.963 -63.141 -16.315  1.00 80.76           O  
ANISOU 4994  O   LYS B 160    10138   6951  13597   -670  -1668  -1844       O  
ATOM   4995  CB  LYS B 160      23.499 -64.514 -14.560  1.00 84.71           C  
ANISOU 4995  CB  LYS B 160    10490   7252  14444  -1170  -1877  -1239       C  
ATOM   4996  CG  LYS B 160      23.466 -65.374 -15.817  1.00 86.85           C  
ANISOU 4996  CG  LYS B 160    10923   7293  14784  -1184  -2149  -1436       C  
ATOM   4997  CD  LYS B 160      22.089 -65.996 -16.006  1.00 89.45           C  
ANISOU 4997  CD  LYS B 160    11193   7535  15258  -1467  -2356  -1238       C  
ATOM   4998  CE  LYS B 160      21.924 -66.620 -17.384  1.00 91.35           C  
ANISOU 4998  CE  LYS B 160    11576   7596  15536  -1481  -2618  -1468       C  
ATOM   4999  NZ  LYS B 160      22.752 -67.847 -17.555  1.00 93.41           N  
ANISOU 4999  NZ  LYS B 160    12105   7492  15893  -1390  -2880  -1672       N  
ATOM   5000  N   LEU B 161      24.455 -61.677 -15.503  1.00 79.65           N  
ANISOU 5000  N   LEU B 161     9730   7067  13463   -831  -1421  -1521       N  
ATOM   5001  CA  LEU B 161      24.662 -60.680 -16.560  1.00 78.58           C  
ANISOU 5001  CA  LEU B 161     9571   7072  13211   -737  -1343  -1652       C  
ATOM   5002  C   LEU B 161      26.071 -60.098 -16.552  1.00 77.28           C  
ANISOU 5002  C   LEU B 161     9462   6987  12911   -576  -1223  -1800       C  
ATOM   5003  O   LEU B 161      26.700 -59.971 -17.605  1.00 77.46           O  
ANISOU 5003  O   LEU B 161     9523   7078  12830   -489  -1259  -1959       O  
ATOM   5004  CB  LEU B 161      23.644 -59.539 -16.439  1.00 78.08           C  
ANISOU 5004  CB  LEU B 161     9349   7177  13138   -777  -1205  -1497       C  
ATOM   5005  CG  LEU B 161      22.254 -59.793 -17.026  1.00 79.43           C  
ANISOU 5005  CG  LEU B 161     9421   7376  13381   -914  -1318  -1379       C  
ATOM   5006  CD1 LEU B 161      21.254 -58.784 -16.483  1.00 79.27           C  
ANISOU 5006  CD1 LEU B 161     9224   7543  13352   -914  -1167  -1195       C  
ATOM   5007  CD2 LEU B 161      22.295 -59.743 -18.548  1.00 79.74           C  
ANISOU 5007  CD2 LEU B 161     9495   7437  13365   -891  -1421  -1527       C  
ATOM   5008  N   ILE B 162      26.556 -59.736 -15.367  1.00 76.43           N  
ANISOU 5008  N   ILE B 162     9340   6914  12784   -546  -1086  -1736       N  
ATOM   5009  CA  ILE B 162      27.879 -59.127 -15.225  1.00 75.32           C  
ANISOU 5009  CA  ILE B 162     9234   6872  12513   -432   -975  -1844       C  
ATOM   5010  C   ILE B 162      28.975 -60.143 -15.542  1.00 75.99           C  
ANISOU 5010  C   ILE B 162     9423   6902  12547   -326  -1087  -2003       C  
ATOM   5011  O   ILE B 162      29.932 -59.823 -16.245  1.00 75.79           O  
ANISOU 5011  O   ILE B 162     9405   7011  12379   -225  -1068  -2135       O  
ATOM   5012  CB  ILE B 162      28.088 -58.534 -13.813  1.00 74.56           C  
ANISOU 5012  CB  ILE B 162     9097   6832  12402   -431   -820  -1751       C  
ATOM   5013  CG1 ILE B 162      27.117 -57.368 -13.580  1.00 74.33           C  
ANISOU 5013  CG1 ILE B 162     8973   6879  12389   -464   -711  -1650       C  
ATOM   5014  CG2 ILE B 162      29.521 -58.042 -13.634  1.00 73.77           C  
ANISOU 5014  CG2 ILE B 162     9033   6828  12166   -347   -740  -1857       C  
ATOM   5015  CD1 ILE B 162      26.950 -56.978 -12.127  1.00 74.33           C  
ANISOU 5015  CD1 ILE B 162     8917   6944  12379   -451   -590  -1566       C  
ATOM   5016  N   ALA B 163      28.826 -61.363 -15.029  1.00 77.20           N  
ANISOU 5016  N   ALA B 163     9648   6871  12812   -344  -1216  -1975       N  
ATOM   5017  CA  ALA B 163      29.789 -62.438 -15.285  1.00 78.31           C  
ANISOU 5017