CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Elnemo is running on a new server.
Should you encounter any unexpected behaviour,
please let us know.


***  4x19  ***

elNémo ID: 19112910404338009

Job options:

ID        	=	 19112910404338009
JOBID     	=	 4x19
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 4x19

HEADER    ISOMERASE                               24-NOV-14   4X19              
TITLE     CRYSTAL STRUCTURE OF NATIVE 4-OT FROM PSEUDOMONAS PUTIDA MT-2 AT 1.94 
TITLE    2 ANGSTROM                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-HYDROXYMUCONATE TAUTOMERASE;                             
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U,
COMPND   4 V, W, X, Y, Z, a, b, c, d;                                           
COMPND   5 FRAGMENT: UNP RESIDUES 2-263;                                        
COMPND   6 SYNONYM: 4-OXALOCROTONATE TAUTOMERASE,4-OT;                          
COMPND   7 EC: 5.3.2.6;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;                             
SOURCE   3 ORGANISM_TAXID: 303;                                                 
SOURCE   4 GENE: XYLH;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET-20B(+)                                
KEYWDS    4-OXALOCROTONATE TAUTOMERASE, BETA-ALPHA-BETA STRUCTURAL MOTIF,       
KEYWDS   2 TAUTOMERASE SUPERFAMILY, ISOMERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.W.H.THUNNISSEN,H.PODDAR                                           
REVDAT   2   25-MAR-15 4X19    1       JRNL                                     
REVDAT   1   11-MAR-15 4X19    0                                                
JRNL        AUTH   H.PODDAR,M.RAHIMI,E.M.GEERTSEMA,A.M.THUNNISSEN,              
JRNL        AUTH 2 G.J.POELARENDS                                               
JRNL        TITL   EVIDENCE FOR THE FORMATION OF AN ENAMINE SPECIES DURING      
JRNL        TITL 2 ALDOL AND MICHAEL-TYPE ADDITION REACTIONS PROMISCUOUSLY      
JRNL        TITL 3 CATALYZED BY 4-OXALOCROTONATE TAUTOMERASE.                   
JRNL        REF    CHEMBIOCHEM                   V.  16   738 2015              
JRNL        REFN                   ESSN 1439-7633                               
JRNL        PMID   25728471                                                     
JRNL        DOI    10.1002/CBIC.201402687                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.94 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.660                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 226223                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.250                           
REMARK   3   R VALUE            (WORKING SET) : 0.248                           
REMARK   3   FREE R VALUE                     : 0.289                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 11362                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.7527 -  6.0382    0.98     7763   404  0.2215 0.2397        
REMARK   3     2  6.0382 -  4.7941    0.99     7816   407  0.2096 0.2495        
REMARK   3     3  4.7941 -  4.1885    0.97     7708   370  0.1930 0.2123        
REMARK   3     4  4.1885 -  3.8057    0.96     7719   349  0.2180 0.2370        
REMARK   3     5  3.8057 -  3.5330    0.72     5751   285  0.2350 0.2639        
REMARK   3     6  3.5330 -  3.3247    0.98     7766   413  0.2307 0.2723        
REMARK   3     7  3.3247 -  3.1583    0.99     7873   389  0.2516 0.2952        
REMARK   3     8  3.1583 -  3.0208    0.99     7829   416  0.2624 0.3050        
REMARK   3     9  3.0208 -  2.9045    0.96     7663   382  0.2769 0.3459        
REMARK   3    10  2.9045 -  2.8043    0.95     7422   446  0.2577 0.3034        
REMARK   3    11  2.8043 -  2.7166    0.97     7713   420  0.2634 0.2920        
REMARK   3    12  2.7166 -  2.6390    0.97     7681   471  0.2672 0.3139        
REMARK   3    13  2.6390 -  2.5695    0.98     7719   411  0.2718 0.3305        
REMARK   3    14  2.5695 -  2.5068    0.98     7855   411  0.2666 0.3086        
REMARK   3    15  2.5068 -  2.4498    0.98     7669   398  0.2724 0.3229        
REMARK   3    16  2.4498 -  2.3977    0.98     7743   378  0.2716 0.3239        
REMARK   3    17  2.3977 -  2.3497    0.98     7848   370  0.2837 0.3439        
REMARK   3    18  2.3497 -  2.3054    0.98     7789   450  0.2796 0.3098        
REMARK   3    19  2.3054 -  2.2642    0.80     4437   248  0.2833 0.3377        
REMARK   3    20  2.2258 -  2.1899    0.80     5682   289  0.2968 0.3679        
REMARK   3    21  2.1899 -  2.1563    0.96     7519   422  0.3037 0.3687        
REMARK   3    22  2.1563 -  2.1245    0.96     7651   367  0.2946 0.3748        
REMARK   3    23  2.1245 -  2.0946    0.97     7605   461  0.3011 0.3419        
REMARK   3    24  2.0946 -  2.0663    0.96     7605   397  0.2982 0.3635        
REMARK   3    25  2.0663 -  2.0395    0.97     7730   445  0.3007 0.3543        
REMARK   3    26  2.0395 -  2.0140    0.97     7579   409  0.2948 0.3506        
REMARK   3    27  2.0140 -  1.9897    0.97     7866   413  0.2997 0.3624        
REMARK   3    28  1.9897 -  1.9666    0.97     7666   382  0.3098 0.3596        
REMARK   3    29  1.9666 -  1.9445    0.78     6194   359  0.3994 0.4194        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.160           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.95                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006          13185                                  
REMARK   3   ANGLE     :  0.994          17719                                  
REMARK   3   CHIRALITY :  0.042           2138                                  
REMARK   3   PLANARITY :  0.005           2263                                  
REMARK   3   DIHEDRAL  : 11.462           5056                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 30                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  68.6303 -16.8305  69.7309              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1723 T22:   0.2509                                     
REMARK   3      T33:   0.2953 T12:   0.0529                                     
REMARK   3      T13:  -0.0206 T23:  -0.0564                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7344 L22:   3.7770                                     
REMARK   3      L33:   3.1937 L12:   1.2662                                     
REMARK   3      L13:  -0.7475 L23:  -0.8903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1240 S12:  -0.1232 S13:  -0.2855                       
REMARK   3      S21:   0.0878 S22:  -0.0354 S23:  -0.6079                       
REMARK   3      S31:   0.1893 S32:   0.6033 S33:   0.1753                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN 'B' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  63.2159 -14.9617  60.0529              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1856 T22:   0.1991                                     
REMARK   3      T33:   0.2201 T12:   0.0130                                     
REMARK   3      T13:   0.0540 T23:  -0.0534                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7392 L22:   2.7523                                     
REMARK   3      L33:   3.8291 L12:   0.9231                                     
REMARK   3      L13:   1.1447 L23:  -0.0061                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1629 S12:   0.1978 S13:  -0.0151                       
REMARK   3      S21:  -0.3276 S22:  -0.0256 S23:   0.1067                       
REMARK   3      S31:  -0.0077 S32:   0.4260 S33:  -0.1219                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN 'C' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  59.9483   0.6688  77.4055              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1573 T22:   0.1588                                     
REMARK   3      T33:   0.2186 T12:  -0.0113                                     
REMARK   3      T13:  -0.0343 T23:  -0.0301                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4522 L22:   3.4254                                     
REMARK   3      L33:   4.6884 L12:   2.2157                                     
REMARK   3      L13:  -0.0761 L23:   0.9399                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2912 S12:  -0.0720 S13:  -0.0025                       
REMARK   3      S21:   0.2100 S22:   0.2225 S23:  -0.1597                       
REMARK   3      S31:  -0.3105 S32:   0.0566 S33:   0.0270                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN 'D' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  53.2297   1.7225  67.9843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2322 T22:   0.1190                                     
REMARK   3      T33:   0.2413 T12:   0.0083                                     
REMARK   3      T13:  -0.0121 T23:  -0.0322                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5566 L22:   2.7829                                     
REMARK   3      L33:   3.1279 L12:   0.9525                                     
REMARK   3      L13:   0.2319 L23:  -0.4417                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2257 S12:   0.1215 S13:   0.6606                       
REMARK   3      S21:  -0.1963 S22:   0.1383 S23:   0.0667                       
REMARK   3      S31:  -0.5135 S32:   0.0440 S33:   0.0674                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN 'E' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  50.5678 -18.0103  80.4054              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2011 T22:   0.1840                                     
REMARK   3      T33:   0.1857 T12:   0.0013                                     
REMARK   3      T13:   0.0467 T23:   0.0371                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4948 L22:   5.3505                                     
REMARK   3      L33:   3.7038 L12:  -0.0461                                     
REMARK   3      L13:   0.6655 L23:  -0.3575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1948 S12:  -0.4190 S13:  -0.1325                       
REMARK   3      S21:   0.5892 S22:  -0.1756 S23:   0.2213                       
REMARK   3      S31:   0.4826 S32:  -0.2256 S33:  -0.0236                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN 'F' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  45.0731 -17.5166  70.2760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1696 T22:   0.1576                                     
REMARK   3      T33:   0.1905 T12:  -0.0221                                     
REMARK   3      T13:   0.0039 T23:  -0.0216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2905 L22:   2.2559                                     
REMARK   3      L33:   3.8630 L12:  -0.5194                                     
REMARK   3      L13:   0.4928 L23:   0.0506                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0321 S12:   0.2008 S13:  -0.1888                       
REMARK   3      S21:   0.0542 S22:   0.0370 S23:   0.1132                       
REMARK   3      S31:   0.0747 S32:  -0.5708 S33:  -0.0467                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN 'G' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  28.8207 -17.0586  34.7245              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1663 T22:   0.3047                                     
REMARK   3      T33:   0.2061 T12:   0.0091                                     
REMARK   3      T13:  -0.0239 T23:   0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5077 L22:   3.3743                                     
REMARK   3      L33:   3.7267 L12:   0.3403                                     
REMARK   3      L13:   1.4066 L23:  -0.4938                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0142 S12:  -0.2441 S13:  -0.2949                       
REMARK   3      S21:  -0.0563 S22:   0.1143 S23:   0.2406                       
REMARK   3      S31:   0.1456 S32:  -0.2942 S33:  -0.1591                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN 'H' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  33.9563 -17.5522  45.1700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1696 T22:   0.2813                                     
REMARK   3      T33:   0.1631 T12:   0.0203                                     
REMARK   3      T13:   0.0109 T23:   0.0257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0660 L22:   3.4598                                     
REMARK   3      L33:   3.0368 L12:   0.1333                                     
REMARK   3      L13:   1.4055 L23:  -0.7185                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0194 S12:  -0.2286 S13:  -0.1793                       
REMARK   3      S21:   0.4088 S22:   0.1315 S23:  -0.0092                       
REMARK   3      S31:   0.2969 S32:  -0.1994 S33:  -0.1847                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN 'I' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  29.3126   3.8076  36.6674              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3701 T22:   0.2601                                     
REMARK   3      T33:   0.2476 T12:   0.1060                                     
REMARK   3      T13:  -0.0204 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9861 L22:   4.2855                                     
REMARK   3      L33:   3.3492 L12:   0.6334                                     
REMARK   3      L13:   0.8300 L23:  -0.7038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1071 S12:   0.0407 S13:   0.5741                       
REMARK   3      S21:  -0.0038 S22:  -0.0943 S23:   0.2503                       
REMARK   3      S31:  -0.7420 S32:  -0.2904 S33:   0.2007                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN 'J' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  35.7952   3.3607  46.3070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3531 T22:   0.2738                                     
REMARK   3      T33:   0.2684 T12:   0.0783                                     
REMARK   3      T13:  -0.0304 T23:  -0.0681                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1595 L22:   3.2026                                     
REMARK   3      L33:   3.7264 L12:  -0.7842                                     
REMARK   3      L13:   0.2619 L23:  -1.5024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1563 S12:  -0.4813 S13:   0.3995                       
REMARK   3      S21:   0.2215 S22:   0.0936 S23:   0.3713                       
REMARK   3      S31:  -0.6781 S32:  -0.1701 S33:   0.0490                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN 'K' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  44.6688  -5.9860  26.6026              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2244 T22:   0.3855                                     
REMARK   3      T33:   0.1962 T12:  -0.0659                                     
REMARK   3      T13:   0.0132 T23:   0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3270 L22:   2.9560                                     
REMARK   3      L33:   3.7731 L12:  -0.6712                                     
REMARK   3      L13:   0.3696 L23:  -0.0443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0772 S12:   0.6872 S13:   0.1957                       
REMARK   3      S21:  -0.5020 S22:  -0.0561 S23:  -0.2259                       
REMARK   3      S31:  -0.0898 S32:   0.3751 S33:  -0.0042                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN 'L' AND RESID 1 THROUGH 62)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  50.3649  -9.5504  37.2126              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1212 T22:   0.2123                                     
REMARK   3      T33:   0.1856 T12:   0.0303                                     
REMARK   3      T13:  -0.0041 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4631 L22:   2.7381                                     
REMARK   3      L33:   4.1062 L12:   0.8526                                     
REMARK   3      L13:   0.6016 L23:  -0.5266                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0334 S12:   0.1420 S13:  -0.0433                       
REMARK   3      S21:   0.0150 S22:  -0.1756 S23:  -0.2486                       
REMARK   3      S31:  -0.1355 S32:   0.4804 S33:   0.2219                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN 'M' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  74.6356 -47.6681  29.8252              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3352 T22:   0.3970                                     
REMARK   3      T33:   0.2784 T12:  -0.1214                                     
REMARK   3      T13:   0.0001 T23:   0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6579 L22:   3.9279                                     
REMARK   3      L33:   4.2381 L12:  -0.4162                                     
REMARK   3      L13:   1.4630 L23:  -0.8284                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0988 S12:   0.4106 S13:   0.4458                       
REMARK   3      S21:   0.0027 S22:  -0.5749 S23:  -0.1780                       
REMARK   3      S31:  -0.4874 S32:   1.0636 S33:   0.3552                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN 'N' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  68.4270 -45.3097  20.6693              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4022 T22:   0.5111                                     
REMARK   3      T33:   0.2619 T12:  -0.0964                                     
REMARK   3      T13:   0.0682 T23:   0.0642                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9889 L22:   3.1111                                     
REMARK   3      L33:   3.2660 L12:   0.1095                                     
REMARK   3      L13:  -1.1190 L23:   1.2789                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0309 S12:   0.5156 S13:   0.1297                       
REMARK   3      S21:  -0.8625 S22:   0.1644 S23:  -0.3557                       
REMARK   3      S31:  -0.3162 S32:   0.3379 S33:  -0.0992                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN 'O' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  58.4538 -41.0615  41.4844              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2688 T22:   0.1514                                     
REMARK   3      T33:   0.2529 T12:   0.0021                                     
REMARK   3      T13:  -0.0168 T23:  -0.0404                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8581 L22:   1.7080                                     
REMARK   3      L33:   3.1544 L12:  -1.4418                                     
REMARK   3      L13:  -0.1371 L23:  -0.1370                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0991 S12:  -0.2515 S13:   0.2844                       
REMARK   3      S21:   0.2372 S22:   0.0635 S23:  -0.0681                       
REMARK   3      S31:  -0.1977 S32:   0.0570 S33:   0.1014                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN 'P' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  51.6208 -39.9984  32.3687              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2509 T22:   0.2512                                     
REMARK   3      T33:   0.2226 T12:   0.0230                                     
REMARK   3      T13:  -0.0179 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1658 L22:   5.2923                                     
REMARK   3      L33:   3.8805 L12:   1.3587                                     
REMARK   3      L13:   0.7634 L23:   1.1421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3470 S12:   0.1684 S13:   0.2938                       
REMARK   3      S21:  -0.6760 S22:   0.0485 S23:   0.4457                       
REMARK   3      S31:  -0.5285 S32:  -0.2086 S33:   0.3029                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN 'Q' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  60.3125 -61.2076  36.7957              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3265 T22:   0.2007                                     
REMARK   3      T33:   0.2215 T12:  -0.0752                                     
REMARK   3      T13:   0.0214 T23:  -0.0314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7702 L22:   2.9178                                     
REMARK   3      L33:   3.4131 L12:  -0.9511                                     
REMARK   3      L13:  -0.2907 L23:  -1.6510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0218 S12:  -0.0903 S13:  -0.2610                       
REMARK   3      S21:   0.1488 S22:  -0.0656 S23:   0.2158                       
REMARK   3      S31:   0.7269 S32:  -0.0112 S33:   0.0737                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN 'R' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  54.8214 -59.9848  26.7747              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3174 T22:   0.3721                                     
REMARK   3      T33:   0.2074 T12:  -0.0978                                     
REMARK   3      T13:  -0.0004 T23:  -0.0374                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2770 L22:   3.1959                                     
REMARK   3      L33:   2.2872 L12:  -0.0282                                     
REMARK   3      L13:   1.3515 L23:   0.7408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0066 S12:   0.3635 S13:  -0.2994                       
REMARK   3      S21:  -0.1406 S22:   0.0843 S23:   0.1831                       
REMARK   3      S31:   0.2841 S32:  -0.3107 S33:  -0.1121                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN 'S' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  30.5027 -56.1041  51.9756              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2853 T22:   0.3608                                     
REMARK   3      T33:   0.2458 T12:   0.1255                                     
REMARK   3      T13:   0.0512 T23:   0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8440 L22:   2.6773                                     
REMARK   3      L33:   3.6877 L12:   1.0195                                     
REMARK   3      L13:   1.6246 L23:  -0.1343                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0784 S12:   0.4687 S13:  -0.4083                       
REMARK   3      S21:  -0.0399 S22:   0.0596 S23:  -0.0276                       
REMARK   3      S31:   0.3303 S32:   0.7241 S33:  -0.0137                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN 'T' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  36.7174 -58.6526  61.1254              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2943 T22:   0.4367                                     
REMARK   3      T33:   0.5493 T12:   0.1291                                     
REMARK   3      T13:   0.0351 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7424 L22:   3.2044                                     
REMARK   3      L33:   4.9304 L12:   0.7441                                     
REMARK   3      L13:   2.3504 L23:   0.2985                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2936 S12:   0.3927 S13:  -0.3902                       
REMARK   3      S21:   0.1353 S22:   0.1314 S23:  -0.8198                       
REMARK   3      S31:   0.3037 S32:   1.4291 S33:   0.1895                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: (CHAIN 'U' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  13.6605 -63.2810  61.7253              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2188 T22:   0.1159                                     
REMARK   3      T33:   0.2654 T12:   0.0153                                     
REMARK   3      T13:   0.0519 T23:   0.0209                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6916 L22:   3.2206                                     
REMARK   3      L33:   3.9884 L12:   0.0246                                     
REMARK   3      L13:   0.6641 L23:  -0.5375                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0023 S12:  -0.0384 S13:  -0.0825                       
REMARK   3      S21:  -0.1344 S22:   0.1932 S23:   0.1534                       
REMARK   3      S31:   0.2724 S32:  -0.1844 S33:  -0.2044                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: (CHAIN 'V' AND RESID 1 THROUGH 58)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3685 -64.0131  71.9042              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4018 T22:   0.1809                                     
REMARK   3      T33:   0.3164 T12:   0.0410                                     
REMARK   3      T13:   0.0983 T23:   0.0582                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0681 L22:   3.9143                                     
REMARK   3      L33:   2.3041 L12:   0.3406                                     
REMARK   3      L13:   0.2778 L23:   1.1373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1697 S12:  -0.2651 S13:  -0.4640                       
REMARK   3      S21:   0.7524 S22:   0.0135 S23:  -0.1038                       
REMARK   3      S31:   0.8084 S32:   0.0242 S33:   0.1054                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: (CHAIN 'W' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0691 -42.9143  62.7197              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1962 T22:   0.1483                                     
REMARK   3      T33:   0.2330 T12:   0.0637                                     
REMARK   3      T13:   0.0158 T23:  -0.0362                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7326 L22:   2.5855                                     
REMARK   3      L33:   3.4421 L12:   1.1944                                     
REMARK   3      L13:   0.5411 L23:  -0.1478                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1726 S12:  -0.0210 S13:   0.2253                       
REMARK   3      S21:  -0.1259 S22:  -0.0224 S23:   0.1000                       
REMARK   3      S31:  -0.3385 S32:  -0.0110 S33:   0.2111                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: (CHAIN 'X' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  25.0628 -44.2259  71.7684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2413 T22:   0.2302                                     
REMARK   3      T33:   0.2118 T12:   0.0431                                     
REMARK   3      T13:  -0.0706 T23:  -0.0431                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5695 L22:   2.8803                                     
REMARK   3      L33:   4.2983 L12:   1.2611                                     
REMARK   3      L13:  -0.4055 L23:  -0.1074                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3090 S12:  -0.4317 S13:   0.0685                       
REMARK   3      S21:   0.2486 S22:   0.1074 S23:  -0.0772                       
REMARK   3      S31:  -0.2355 S32:   0.3011 S33:   0.1939                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: (CHAIN 'Y' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  34.1097 -42.0978   5.8793              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3806 T22:   0.3443                                     
REMARK   3      T33:   0.2785 T12:   0.0134                                     
REMARK   3      T13:   0.0281 T23:  -0.0998                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5019 L22:   3.6233                                     
REMARK   3      L33:   4.2385 L12:   1.0247                                     
REMARK   3      L13:  -0.2761 L23:  -0.2042                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2058 S12:  -0.2475 S13:   0.4094                       
REMARK   3      S21:   0.5908 S22:   0.0739 S23:  -0.1033                       
REMARK   3      S31:  -0.3491 S32:  -0.2789 S33:  -0.2201                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: (CHAIN 'Z' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4163 -43.9231  -3.7343              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2395 T22:   0.3771                                     
REMARK   3      T33:   0.2276 T12:   0.0309                                     
REMARK   3      T13:   0.0417 T23:   0.0339                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6546 L22:   3.9898                                     
REMARK   3      L33:   2.8771 L12:  -0.4909                                     
REMARK   3      L13:   0.6378 L23:   0.9714                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0130 S12:  -0.2289 S13:   0.0713                       
REMARK   3      S21:  -0.1632 S22:   0.0370 S23:   0.3094                       
REMARK   3      S31:  -0.3622 S32:  -0.5060 S33:  -0.0191                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 1 THROUGH 56)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  45.0359 -59.7831   1.0384              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2390 T22:   0.3545                                     
REMARK   3      T33:   0.2051 T12:  -0.0429                                     
REMARK   3      T13:  -0.0323 T23:   0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8612 L22:   3.3776                                     
REMARK   3      L33:   2.8718 L12:  -1.3593                                     
REMARK   3      L13:   0.6630 L23:   0.2514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1032 S12:  -0.3202 S13:  -0.0051                       
REMARK   3      S21:   0.2630 S22:   0.3119 S23:  -0.2768                       
REMARK   3      S31:   0.2852 S32:   0.3219 S33:  -0.2332                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: (CHAIN 'B' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  39.8822 -60.6015  -9.1409              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2139 T22:   0.3140                                     
REMARK   3      T33:   0.2048 T12:  -0.0353                                     
REMARK   3      T13:  -0.0248 T23:   0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9658 L22:   4.4295                                     
REMARK   3      L33:   3.4934 L12:   0.2761                                     
REMARK   3      L13:   0.1073 L23:   0.2867                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0919 S12:  -0.3679 S13:  -0.1427                       
REMARK   3      S21:  -0.1863 S22:   0.0990 S23:   0.1339                       
REMARK   3      S31:   0.3784 S32:  -0.0650 S33:  -0.0926                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: (CHAIN 'C' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  52.5002 -41.1013  -5.0609              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3114 T22:   0.3154                                     
REMARK   3      T33:   0.3839 T12:  -0.0821                                     
REMARK   3      T13:  -0.0584 T23:  -0.0427                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9459 L22:   3.2950                                     
REMARK   3      L33:   4.2228 L12:  -0.1212                                     
REMARK   3      L13:   0.4708 L23:  -0.9371                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0417 S12:  -0.0099 S13:   0.3966                       
REMARK   3      S21:   0.2878 S22:  -0.2181 S23:  -0.5337                       
REMARK   3      S31:  -0.5424 S32:   0.5408 S33:   0.1733                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: (CHAIN 'D' AND RESID 1 THROUGH 57)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  46.0499 -41.2234 -14.4945              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2256 T22:   0.3117                                     
REMARK   3      T33:   0.3068 T12:  -0.0181                                     
REMARK   3      T13:   0.0470 T23:   0.0314                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6022 L22:   3.5369                                     
REMARK   3      L33:   4.4962 L12:  -0.4545                                     
REMARK   3      L13:   0.6241 L23:   0.1838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0349 S12:   0.6519 S13:   0.4433                       
REMARK   3      S21:  -0.1789 S22:   0.0934 S23:  -0.4492                       
REMARK   3      S31:  -0.2215 S32:   0.4804 S33:  -0.0846                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN E                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN F                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 6                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN G                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 7                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN H                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 8                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN I                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 9                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN J                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 10                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN K                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 11                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN L                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 12                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN M                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 13                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN N                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 14                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN O                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 15                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN P                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 16                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN Q                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 17                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN R                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 18                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN S                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 19                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN T                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 20                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN U                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 21                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN V                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 22                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN W                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 23                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN X                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 24                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN Y                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 25                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN Z                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 26                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN A                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 27                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 28                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 29                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 8201                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4X19 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204887.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.987                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 118466                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.94                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1BJP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEXAAMINE COBALT CHLORIDE, BIS-TRIS      
REMARK 280  PROPANE, 20% PEG3350, PH 8.5, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       44.40800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
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 300 REMARK: THE BIOLOGICAL UNIT IS A HEXAMER. THERE ARE 5 HEXAMERS IN    
REMARK 300 THE ASYMMETRIC UNIT.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 13720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12510 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 14100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, J, K, L                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12520 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 13700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, N, O, P, Q, R                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12770 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 13850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, T, U, V, W, X                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12350 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 14140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: a, b, Y, Z, c, d                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    58                                                      
REMARK 465     LYS A    59                                                      
REMARK 465     VAL A    60                                                      
REMARK 465     ARG A    61                                                      
REMARK 465     ARG A    62                                                      
REMARK 465     ALA B    57                                                      
REMARK 465     SER B    58                                                      
REMARK 465     LYS B    59                                                      
REMARK 465     VAL B    60                                                      
REMARK 465     ARG B    61                                                      
REMARK 465     ARG B    62                                                      
REMARK 465     SER C    58                                                      
REMARK 465     LYS C    59                                                      
REMARK 465     VAL C    60                                                      
REMARK 465     ARG C    61                                                      
REMARK 465     ARG C    62                                                      
REMARK 465     SER D    58                                                      
REMARK 465     LYS D    59                                                      
REMARK 465     VAL D    60                                                      
REMARK 465     ARG D    61                                                      
REMARK 465     ARG D    62                                                      
REMARK 465     SER E    58                                                      
REMARK 465     LYS E    59                                                      
REMARK 465     VAL E    60                                                      
REMARK 465     ARG E    61                                                      
REMARK 465     ARG E    62                                                      
REMARK 465     SER F    58                                                      
REMARK 465     LYS F    59                                                      
REMARK 465     VAL F    60                                                      
REMARK 465     ARG F    61                                                      
REMARK 465     ARG F    62                                                      
REMARK 465     SER G    58                                                      
REMARK 465     LYS G    59                                                      
REMARK 465     VAL G    60                                                      
REMARK 465     ARG G    61                                                      
REMARK 465     ARG G    62                                                      
REMARK 465     SER H    58                                                      
REMARK 465     LYS H    59                                                      
REMARK 465     VAL H    60                                                      
REMARK 465     ARG H    61                                                      
REMARK 465     ARG H    62                                                      
REMARK 465     SER I    58                                                      
REMARK 465     LYS I    59                                                      
REMARK 465     VAL I    60                                                      
REMARK 465     ARG I    61                                                      
REMARK 465     ARG I    62                                                      
REMARK 465     SER J    58                                                      
REMARK 465     LYS J    59                                                      
REMARK 465     VAL J    60                                                      
REMARK 465     ARG J    61                                                      
REMARK 465     ARG J    62                                                      
REMARK 465     SER K    58                                                      
REMARK 465     LYS K    59                                                      
REMARK 465     VAL K    60                                                      
REMARK 465     ARG K    61                                                      
REMARK 465     ARG K    62                                                      
REMARK 465     SER M    58                                                      
REMARK 465     LYS M    59                                                      
REMARK 465     VAL M    60                                                      
REMARK 465     ARG M    61                                                      
REMARK 465     ARG M    62                                                      
REMARK 465     SER N    58                                                      
REMARK 465     LYS N    59                                                      
REMARK 465     VAL N    60                                                      
REMARK 465     ARG N    61                                                      
REMARK 465     ARG N    62                                                      
REMARK 465     SER O    58                                                      
REMARK 465     LYS O    59                                                      
REMARK 465     VAL O    60                                                      
REMARK 465     ARG O    61                                                      
REMARK 465     ARG O    62                                                      
REMARK 465     SER P    58                                                      
REMARK 465     LYS P    59                                                      
REMARK 465     VAL P    60                                                      
REMARK 465     ARG P    61                                                      
REMARK 465     ARG P    62                                                      
REMARK 465     SER Q    58                                                      
REMARK 465     LYS Q    59                                                      
REMARK 465     VAL Q    60                                                      
REMARK 465     ARG Q    61                                                      
REMARK 465     ARG Q    62                                                      
REMARK 465     SER R    58                                                      
REMARK 465     LYS R    59                                                      
REMARK 465     VAL R    60                                                      
REMARK 465     ARG R    61                                                      
REMARK 465     ARG R    62                                                      
REMARK 465     ALA S    57                                                      
REMARK 465     SER S    58                                                      
REMARK 465     LYS S    59                                                      
REMARK 465     VAL S    60                                                      
REMARK 465     ARG S    61                                                      
REMARK 465     ARG S    62                                                      
REMARK 465     SER T    58                                                      
REMARK 465     LYS T    59                                                      
REMARK 465     VAL T    60                                                      
REMARK 465     ARG T    61                                                      
REMARK 465     ARG T    62                                                      
REMARK 465     SER U    58                                                      
REMARK 465     LYS U    59                                                      
REMARK 465     VAL U    60                                                      
REMARK 465     ARG U    61                                                      
REMARK 465     ARG U    62                                                      
REMARK 465     LYS V    59                                                      
REMARK 465     VAL V    60                                                      
REMARK 465     ARG V    61                                                      
REMARK 465     ARG V    62                                                      
REMARK 465     SER W    58                                                      
REMARK 465     LYS W    59                                                      
REMARK 465     VAL W    60                                                      
REMARK 465     ARG W    61                                                      
REMARK 465     ARG W    62                                                      
REMARK 465     SER X    58                                                      
REMARK 465     LYS X    59                                                      
REMARK 465     VAL X    60                                                      
REMARK 465     ARG X    61                                                      
REMARK 465     ARG X    62                                                      
REMARK 465     SER Y    58                                                      
REMARK 465     LYS Y    59                                                      
REMARK 465     VAL Y    60                                                      
REMARK 465     ARG Y    61                                                      
REMARK 465     ARG Y    62                                                      
REMARK 465     SER Z    58                                                      
REMARK 465     LYS Z    59                                                      
REMARK 465     VAL Z    60                                                      
REMARK 465     ARG Z    61                                                      
REMARK 465     ARG Z    62                                                      
REMARK 465     ALA a    57                                                      
REMARK 465     SER a    58                                                      
REMARK 465     LYS a    59                                                      
REMARK 465     VAL a    60                                                      
REMARK 465     ARG a    61                                                      
REMARK 465     ARG a    62                                                      
REMARK 465     SER b    58                                                      
REMARK 465     LYS b    59                                                      
REMARK 465     VAL b    60                                                      
REMARK 465     ARG b    61                                                      
REMARK 465     ARG b    62                                                      
REMARK 465     SER c    58                                                      
REMARK 465     LYS c    59                                                      
REMARK 465     VAL c    60                                                      
REMARK 465     ARG c    61                                                      
REMARK 465     ARG c    62                                                      
REMARK 465     SER d    58                                                      
REMARK 465     LYS d    59                                                      
REMARK 465     VAL d    60                                                      
REMARK 465     ARG d    61                                                      
REMARK 465     ARG d    62                                                      
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 C  11   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG C  11   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 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 L  59      -60.39    -92.97                                   
REMARK 500    ARG L  61        0.25     85.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH Q 115        DISTANCE =  6.00 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NCO F 101                 
DBREF  4X19 A    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 B    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 C    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 D    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 E    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 F    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 G    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 H    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 I    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 J    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 K    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 L    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 M    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 N    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 O    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 P    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 Q    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 R    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 S    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 T    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 U    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 V    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 W    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 X    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 Y    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 Z    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 a    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 b    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 c    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
DBREF  4X19 d    1    62  UNP    Q01468   4OT1_PSEPU       2     63             
SEQRES   1 A   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 A   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 A   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 A   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 A   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 B   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 B   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 B   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 B   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 B   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 C   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 C   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 C   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 C   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 C   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 D   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 D   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 D   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 D   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 D   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 E   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 E   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 E   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 E   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 E   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 F   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 F   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 F   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 F   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 F   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 G   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 G   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 G   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 G   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 G   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 H   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 H   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 H   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 H   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 H   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 I   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 I   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 I   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 I   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 I   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 J   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 J   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 J   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 J   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 J   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 K   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 K   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 K   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 K   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 K   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 L   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 L   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 L   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 L   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 L   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 M   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 M   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 M   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 M   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 M   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 N   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 N   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 N   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 N   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 N   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 O   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 O   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 O   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 O   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 O   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 P   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 P   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 P   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 P   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 P   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 Q   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 Q   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 Q   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 Q   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 Q   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 R   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 R   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 R   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 R   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 R   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 S   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 S   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 S   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 S   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 S   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 T   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 T   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 T   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 T   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 T   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 U   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 U   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 U   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 U   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 U   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 V   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 V   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 V   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 V   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 V   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 W   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 W   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 W   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 W   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 W   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 X   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 X   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 X   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 X   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 X   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 Y   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 Y   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 Y   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 Y   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 Y   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 Z   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 Z   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 Z   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 Z   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 Z   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 a   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 a   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 a   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 a   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 a   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 b   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 b   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 b   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 b   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 b   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 c   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 c   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 c   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 c   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 c   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
SEQRES   1 d   62  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 d   62  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 d   62  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 d   62  VAL ILE ILE THR GLU MET ALA LYS GLY HIS PHE GLY ILE          
SEQRES   5 d   62  GLY GLY GLU LEU ALA SER LYS VAL ARG ARG                      
HET    NCO  F 101       7                                                       
HETNAM     NCO COBALT HEXAMMINE(III)                                            
FORMUL  31  NCO    CO H18 N6 3+                                                 
FORMUL  32  HOH   *449(H2 O)                                                    
HELIX    1 AA1 SER A   12  ASP A   32  1                                  21    
HELIX    2 AA2 PRO A   34  SER A   37  5                                   4    
HELIX    3 AA3 ALA A   46  GLY A   48  5                                   3    
HELIX    4 AA4 SER B   12  ASP B   32  1                                  21    
HELIX    5 AA5 PRO B   34  SER B   37  5                                   4    
HELIX    6 AA6 ALA B   46  GLY B   48  5                                   3    
HELIX    7 AA7 SER C   12  ASP C   32  1                                  21    
HELIX    8 AA8 PRO C   34  SER C   37  5                                   4    
HELIX    9 AA9 ALA C   46  GLY C   48  5                                   3    
HELIX   10 AB1 SER D   12  ASP D   32  1                                  21    
HELIX   11 AB2 PRO D   34  SER D   37  5                                   4    
HELIX   12 AB3 ALA D   46  GLY D   48  5                                   3    
HELIX   13 AB4 SER E   12  ASP E   32  1                                  21    
HELIX   14 AB5 PRO E   34  SER E   37  5                                   4    
HELIX   15 AB6 ALA E   46  GLY E   48  5                                   3    
HELIX   16 AB7 SER F   12  ASP F   32  1                                  21    
HELIX   17 AB8 PRO F   34  SER F   37  5                                   4    
HELIX   18 AB9 ALA F   46  GLY F   48  5                                   3    
HELIX   19 AC1 SER G   12  ASP G   32  1                                  21    
HELIX   20 AC2 PRO G   34  SER G   37  5                                   4    
HELIX   21 AC3 ALA G   46  GLY G   48  5                                   3    
HELIX   22 AC4 SER H   12  ASP H   32  1                                  21    
HELIX   23 AC5 PRO H   34  SER H   37  5                                   4    
HELIX   24 AC6 SER I   12  ASP I   32  1                                  21    
HELIX   25 AC7 PRO I   34  SER I   37  5                                   4    
HELIX   26 AC8 ALA I   46  GLY I   48  5                                   3    
HELIX   27 AC9 SER J   12  ASP J   32  1                                  21    
HELIX   28 AD1 PRO J   34  SER J   37  5                                   4    
HELIX   29 AD2 ALA J   46  GLY J   48  5                                   3    
HELIX   30 AD3 SER K   12  ASP K   32  1                                  21    
HELIX   31 AD4 PRO K   34  SER K   37  5                                   4    
HELIX   32 AD5 ALA K   46  GLY K   48  5                                   3    
HELIX   33 AD6 SER L   12  ASP L   32  1                                  21    
HELIX   34 AD7 PRO L   34  SER L   37  5                                   4    
HELIX   35 AD8 SER M   12  ASP M   32  1                                  21    
HELIX   36 AD9 PRO M   34  SER M   37  5                                   4    
HELIX   37 AE1 ALA M   46  GLY M   48  5                                   3    
HELIX   38 AE2 SER N   12  ASP N   32  1                                  21    
HELIX   39 AE3 PRO N   34  SER N   37  5                                   4    
HELIX   40 AE4 ALA N   46  GLY N   48  5                                   3    
HELIX   41 AE5 SER O   12  ASP O   32  1                                  21    
HELIX   42 AE6 PRO O   34  SER O   37  5                                   4    
HELIX   43 AE7 ALA O   46  GLY O   48  5                                   3    
HELIX   44 AE8 SER P   12  ASP P   32  1                                  21    
HELIX   45 AE9 PRO P   34  SER P   37  5                                   4    
HELIX   46 AF1 ALA P   46  GLY P   48  5                                   3    
HELIX   47 AF2 SER Q   12  ASP Q   32  1                                  21    
HELIX   48 AF3 PRO Q   34  SER Q   37  5                                   4    
HELIX   49 AF4 ALA Q   46  GLY Q   48  5                                   3    
HELIX   50 AF5 SER R   12  ASP R   32  1                                  21    
HELIX   51 AF6 PRO R   34  SER R   37  5                                   4    
HELIX   52 AF7 ALA R   46  GLY R   48  5                                   3    
HELIX   53 AF8 SER S   12  LEU S   31  1                                  20    
HELIX   54 AF9 PRO S   34  SER S   37  5                                   4    
HELIX   55 AG1 ALA S   46  GLY S   48  5                                   3    
HELIX   56 AG2 SER T   12  ASP T   32  1                                  21    
HELIX   57 AG3 PRO T   34  SER T   37  5                                   4    
HELIX   58 AG4 ALA T   46  GLY T   48  5                                   3    
HELIX   59 AG5 SER U   12  ASP U   32  1                                  21    
HELIX   60 AG6 PRO U   34  SER U   37  5                                   4    
HELIX   61 AG7 ALA U   46  GLY U   48  5                                   3    
HELIX   62 AG8 SER V   12  ASP V   32  1                                  21    
HELIX   63 AG9 PRO V   34  SER V   37  5                                   4    
HELIX   64 AH1 ALA V   46  GLY V   48  5                                   3    
HELIX   65 AH2 SER W   12  ASP W   32  1                                  21    
HELIX   66 AH3 PRO W   34  SER W   37  5                                   4    
HELIX   67 AH4 ALA W   46  GLY W   48  5                                   3    
HELIX   68 AH5 SER X   12  ASP X   32  1                                  21    
HELIX   69 AH6 PRO X   34  SER X   37  5                                   4    
HELIX   70 AH7 ALA X   46  GLY X   48  5                                   3    
HELIX   71 AH8 SER Y   12  ASP Y   32  1                                  21    
HELIX   72 AH9 PRO Y   34  SER Y   37  5                                   4    
HELIX   73 AI1 ALA Y   46  GLY Y   48  5                                   3    
HELIX   74 AI2 SER Z   12  ASP Z   32  1                                  21    
HELIX   75 AI3 PRO Z   34  SER Z   37  5                                   4    
HELIX   76 AI4 ALA Z   46  GLY Z   48  5                                   3    
HELIX   77 AI5 SER a   12  ASP a   32  1                                  21    
HELIX   78 AI6 PRO a   34  SER a   37  5                                   4    
HELIX   79 AI7 ALA a   46  GLY a   48  5                                   3    
HELIX   80 AI8 SER b   12  ASP b   32  1                                  21    
HELIX   81 AI9 PRO b   34  SER b   37  5                                   4    
HELIX   82 AJ1 ALA b   46  GLY b   48  5                                   3    
HELIX   83 AJ2 SER c   12  ASP c   32  1                                  21    
HELIX   84 AJ3 PRO c   34  SER c   37  5                                   4    
HELIX   85 AJ4 ALA c   46  GLY c   48  5                                   3    
HELIX   86 AJ5 SER d   12  ASP d   32  1                                  21    
HELIX   87 AJ6 PRO d   34  SER d   37  5                                   4    
HELIX   88 AJ7 ALA d   46  GLY d   48  5                                   3    
SHEET    1 AA1 8 GLU C  55  LEU C  56  0                                        
SHEET    2 AA1 8 PHE C  50  ILE C  52 -1  N  ILE C  52   O  GLU C  55           
SHEET    3 AA1 8 ARG A  39  MET A  45 -1  N  VAL A  40   O  GLY C  51           
SHEET    4 AA1 8 ILE A   2  LEU A   8  1  N  ILE A   5   O  THR A  43           
SHEET    5 AA1 8 ILE B   2  LEU B   8 -1  O  HIS B   6   N  ILE A   2           
SHEET    6 AA1 8 ARG B  39  MET B  45  1  O  ILE B  41   N  ILE B   5           
SHEET    7 AA1 8 PHE F  50  ILE F  52 -1  O  GLY F  51   N  VAL B  40           
SHEET    8 AA1 8 GLU F  55  LEU F  56 -1  O  GLU F  55   N  ILE F  52           
SHEET    1 AA2 8 GLU A  55  LEU A  56  0                                        
SHEET    2 AA2 8 PHE A  50  ILE A  52 -1  N  ILE A  52   O  GLU A  55           
SHEET    3 AA2 8 ARG E  39  MET E  45 -1  O  VAL E  40   N  GLY A  51           
SHEET    4 AA2 8 ILE E   2  LEU E   8  1  N  ALA E   3   O  ILE E  41           
SHEET    5 AA2 8 ILE F   2  LEU F   8 -1  O  ILE F   2   N  HIS E   6           
SHEET    6 AA2 8 ARG F  39  MET F  45  1  O  ILE F  41   N  ALA F   3           
SHEET    7 AA2 8 PHE D  50  ILE D  52 -1  N  GLY D  51   O  VAL F  40           
SHEET    8 AA2 8 GLU D  55  LEU D  56 -1  O  GLU D  55   N  ILE D  52           
SHEET    1 AA3 7 PHE B  50  ILE B  52  0                                        
SHEET    2 AA3 7 ARG D  39  MET D  45 -1  O  VAL D  40   N  GLY B  51           
SHEET    3 AA3 7 ILE D   2  LEU D   8  1  N  ILE D   5   O  ILE D  41           
SHEET    4 AA3 7 ILE C   2  LEU C   8 -1  N  HIS C   6   O  ILE D   2           
SHEET    5 AA3 7 ARG C  39  MET C  45  1  O  ILE C  41   N  ALA C   3           
SHEET    6 AA3 7 PHE E  50  ILE E  52 -1  O  GLY E  51   N  VAL C  40           
SHEET    7 AA3 7 GLU E  55  LEU E  56 -1  O  GLU E  55   N  ILE E  52           
SHEET    1 AA4 8 GLU I  55  LEU I  56  0                                        
SHEET    2 AA4 8 PHE I  50  ILE I  52 -1  N  ILE I  52   O  GLU I  55           
SHEET    3 AA4 8 ARG G  39  MET G  45 -1  N  VAL G  40   O  GLY I  51           
SHEET    4 AA4 8 ILE G   2  LEU G   8  1  N  ALA G   3   O  ILE G  41           
SHEET    5 AA4 8 ILE H   2  LEU H   8 -1  O  GLN H   4   N  GLN G   4           
SHEET    6 AA4 8 ARG H  39  MET H  45  1  O  THR H  43   N  ILE H   5           
SHEET    7 AA4 8 PHE L  50  ILE L  52 -1  O  GLY L  51   N  VAL H  40           
SHEET    8 AA4 8 GLU L  55  LEU L  56 -1  O  GLU L  55   N  ILE L  52           
SHEET    1 AA5 8 GLU G  55  LEU G  56  0                                        
SHEET    2 AA5 8 PHE G  50  ILE G  52 -1  N  ILE G  52   O  GLU G  55           
SHEET    3 AA5 8 ARG K  39  MET K  45 -1  O  VAL K  40   N  GLY G  51           
SHEET    4 AA5 8 ILE K   2  LEU K   8  1  N  ALA K   3   O  ILE K  41           
SHEET    5 AA5 8 ILE L   2  LEU L   8 -1  O  ILE L   2   N  HIS K   6           
SHEET    6 AA5 8 ARG L  39  MET L  45  1  O  ILE L  41   N  ALA L   3           
SHEET    7 AA5 8 PHE J  50  ILE J  52 -1  N  GLY J  51   O  VAL L  40           
SHEET    8 AA5 8 GLU J  55  LEU J  56 -1  O  GLU J  55   N  ILE J  52           
SHEET    1 AA6 8 GLU H  55  LEU H  56  0                                        
SHEET    2 AA6 8 PHE H  50  ILE H  52 -1  N  ILE H  52   O  GLU H  55           
SHEET    3 AA6 8 ARG J  39  MET J  45 -1  O  VAL J  40   N  GLY H  51           
SHEET    4 AA6 8 ILE J   2  LEU J   8  1  N  ALA J   3   O  ILE J  41           
SHEET    5 AA6 8 ILE I   2  LEU I   8 -1  N  ILE I   2   O  HIS J   6           
SHEET    6 AA6 8 ARG I  39  MET I  45  1  O  ILE I  41   N  ILE I   5           
SHEET    7 AA6 8 PHE K  50  ILE K  52 -1  O  GLY K  51   N  VAL I  40           
SHEET    8 AA6 8 GLU K  55  LEU K  56 -1  O  GLU K  55   N  ILE K  52           
SHEET    1 AA7 8 GLU O  55  LEU O  56  0                                        
SHEET    2 AA7 8 PHE O  50  ILE O  52 -1  N  ILE O  52   O  GLU O  55           
SHEET    3 AA7 8 ARG M  39  MET M  45 -1  N  VAL M  40   O  GLY O  51           
SHEET    4 AA7 8 ILE M   2  LEU M   8  1  N  ALA M   3   O  ILE M  41           
SHEET    5 AA7 8 ILE N   2  LEU N   8 -1  O  ILE N   2   N  HIS M   6           
SHEET    6 AA7 8 ARG N  39  MET N  45  1  O  ILE N  41   N  ALA N   3           
SHEET    7 AA7 8 PHE R  50  ILE R  52 -1  O  GLY R  51   N  VAL N  40           
SHEET    8 AA7 8 GLU R  55  LEU R  56 -1  O  GLU R  55   N  ILE R  52           
SHEET    1 AA8 8 GLU M  55  LEU M  56  0                                        
SHEET    2 AA8 8 PHE M  50  ILE M  52 -1  N  ILE M  52   O  GLU M  55           
SHEET    3 AA8 8 ARG Q  39  MET Q  45 -1  O  VAL Q  40   N  GLY M  51           
SHEET    4 AA8 8 ILE Q   2  LEU Q   8  1  N  ILE Q   5   O  ILE Q  41           
SHEET    5 AA8 8 ILE R   2  LEU R   8 -1  O  ILE R   2   N  HIS Q   6           
SHEET    6 AA8 8 ARG R  39  MET R  45  1  O  THR R  43   N  ILE R   5           
SHEET    7 AA8 8 PHE P  50  ILE P  52 -1  N  GLY P  51   O  VAL R  40           
SHEET    8 AA8 8 GLU P  55  LEU P  56 -1  O  GLU P  55   N  ILE P  52           
SHEET    1 AA9 8 GLU N  55  LEU N  56  0                                        
SHEET    2 AA9 8 PHE N  50  ILE N  52 -1  N  ILE N  52   O  GLU N  55           
SHEET    3 AA9 8 ARG P  39  MET P  45 -1  O  VAL P  40   N  GLY N  51           
SHEET    4 AA9 8 ILE P   2  LEU P   8  1  N  ALA P   3   O  ILE P  41           
SHEET    5 AA9 8 ILE O   2  LEU O   8 -1  N  GLN O   4   O  GLN P   4           
SHEET    6 AA9 8 ARG O  39  MET O  45  1  O  ILE O  41   N  ALA O   3           
SHEET    7 AA9 8 PHE Q  50  ILE Q  52 -1  O  GLY Q  51   N  VAL O  40           
SHEET    8 AA9 8 GLU Q  55  LEU Q  56 -1  O  GLU Q  55   N  ILE Q  52           
SHEET    1 AB1 8 GLU U  55  LEU U  56  0                                        
SHEET    2 AB1 8 PHE U  50  ILE U  52 -1  N  ILE U  52   O  GLU U  55           
SHEET    3 AB1 8 ARG S  39  MET S  45 -1  N  VAL S  40   O  GLY U  51           
SHEET    4 AB1 8 ILE S   2  LEU S   8  1  N  ALA S   3   O  ILE S  41           
SHEET    5 AB1 8 ILE T   2  LEU T   8 -1  O  ILE T   2   N  HIS S   6           
SHEET    6 AB1 8 ARG T  39  MET T  45  1  O  ILE T  41   N  ALA T   3           
SHEET    7 AB1 8 PHE X  50  ILE X  52 -1  O  GLY X  51   N  VAL T  40           
SHEET    8 AB1 8 GLU X  55  LEU X  56 -1  O  GLU X  55   N  ILE X  52           
SHEET    1 AB2 7 PHE S  50  ILE S  52  0                                        
SHEET    2 AB2 7 ARG W  39  MET W  45 -1  O  VAL W  40   N  GLY S  51           
SHEET    3 AB2 7 ILE W   2  LEU W   8  1  N  ILE W   5   O  ILE W  41           
SHEET    4 AB2 7 ILE X   2  LEU X   8 -1  O  HIS X   6   N  ILE W   2           
SHEET    5 AB2 7 ARG X  39  MET X  45  1  O  ILE X  41   N  ALA X   3           
SHEET    6 AB2 7 PHE V  50  ILE V  52 -1  N  GLY V  51   O  VAL X  40           
SHEET    7 AB2 7 GLU V  55  LEU V  56 -1  O  GLU V  55   N  ILE V  52           
SHEET    1 AB3 8 GLU T  55  LEU T  56  0                                        
SHEET    2 AB3 8 PHE T  50  ILE T  52 -1  N  ILE T  52   O  GLU T  55           
SHEET    3 AB3 8 ARG V  39  MET V  45 -1  O  VAL V  40   N  GLY T  51           
SHEET    4 AB3 8 ILE V   2  LEU V   8  1  N  ILE V   5   O  ILE V  41           
SHEET    5 AB3 8 ILE U   2  LEU U   8 -1  N  ILE U   2   O  HIS V   6           
SHEET    6 AB3 8 ARG U  39  MET U  45  1  O  ILE U  41   N  ALA U   3           
SHEET    7 AB3 8 PHE W  50  ILE W  52 -1  O  GLY W  51   N  VAL U  40           
SHEET    8 AB3 8 GLU W  55  LEU W  56 -1  O  GLU W  55   N  ILE W  52           
SHEET    1 AB4 7 PHE a  50  ILE a  52  0                                        
SHEET    2 AB4 7 ARG Y  39  MET Y  45 -1  N  VAL Y  40   O  GLY a  51           
SHEET    3 AB4 7 ILE Y   2  LEU Y   8  1  N  ALA Y   3   O  ILE Y  41           
SHEET    4 AB4 7 ILE Z   2  LEU Z   8 -1  O  ILE Z   2   N  HIS Y   6           
SHEET    5 AB4 7 ARG Z  39  MET Z  45  1  O  ILE Z  41   N  ALA Z   3           
SHEET    6 AB4 7 PHE d  50  ILE d  52 -1  O  GLY d  51   N  VAL Z  40           
SHEET    7 AB4 7 GLU d  55  LEU d  56 -1  O  GLU d  55   N  ILE d  52           
SHEET    1 AB5 8 GLU Y  55  LEU Y  56  0                                        
SHEET    2 AB5 8 PHE Y  50  ILE Y  52 -1  N  ILE Y  52   O  GLU Y  55           
SHEET    3 AB5 8 ARG c  39  MET c  45 -1  O  VAL c  40   N  GLY Y  51           
SHEET    4 AB5 8 ILE c   2  LEU c   8  1  N  ALA c   3   O  ILE c  41           
SHEET    5 AB5 8 ILE d   2  LEU d   8 -1  O  ILE d   2   N  HIS c   6           
SHEET    6 AB5 8 ARG d  39  MET d  45  1  O  ILE d  41   N  ALA d   3           
SHEET    7 AB5 8 PHE b  50  ILE b  52 -1  N  GLY b  51   O  VAL d  40           
SHEET    8 AB5 8 GLU b  55  LEU b  56 -1  O  GLU b  55   N  ILE b  52           
SHEET    1 AB6 8 GLU Z  55  LEU Z  56  0                                        
SHEET    2 AB6 8 PHE Z  50  ILE Z  52 -1  N  ILE Z  52   O  GLU Z  55           
SHEET    3 AB6 8 ARG b  39  MET b  45 -1  O  VAL b  40   N  GLY Z  51           
SHEET    4 AB6 8 ILE b   2  LEU b   8  1  N  ALA b   3   O  ILE b  41           
SHEET    5 AB6 8 ILE a   2  LEU a   8 -1  N  HIS a   6   O  ILE b   2           
SHEET    6 AB6 8 ARG a  39  MET a  45  1  O  ILE a  41   N  ALA a   3           
SHEET    7 AB6 8 PHE c  50  ILE c  52 -1  O  GLY c  51   N  VAL a  40           
SHEET    8 AB6 8 GLU c  55  LEU c  56 -1  O  GLU c  55   N  ILE c  52           
SITE     1 AC1  2 ARG F  29  ASP F  32                                          
CRYST1   58.480   88.816  169.877  90.00  94.51  90.00 P 1 21 1     60          
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      0.017100  0.000000  0.001348        0.00000                         
SCALE2      0.000000  0.011259  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005905        0.00000                         
ATOM      1  N   PRO A   1      66.729  -6.223  60.196  1.00 26.78      
ATOM      2  CA  PRO A   1      65.949  -7.377  60.650  1.00 26.49      
ATOM      3  C   PRO A   1      66.118  -7.603  62.147  1.00 29.77      
ATOM      4  O   PRO A   1      67.229  -7.434  62.678  1.00 29.17      
ATOM      5  CB  PRO A   1      66.547  -8.546  59.864  1.00 28.61      
ATOM      6  CG  PRO A   1      67.208  -7.938  58.689  1.00 28.67      
ATOM      7  CD  PRO A   1      67.601  -6.545  59.050  1.00 28.35      
ATOM      8  N   ILE A   2      65.045  -7.995  62.825  1.00     5      
ATOM      9  CA  ILE A   2      65.131  -8.221  64.267  1.00     5      
ATOM     10  C   ILE A   2      64.658  -9.631  64.629  1.00     5      
ATOM     11  O   ILE A   2      63.521 -10.016  64.352  1.00     5      
ATOM     12  CB  ILE A   2      64.320  -7.172  65.047  1.00     5      
ATOM     13  CG1 ILE A   2      64.838  -5.767  64.724  1.00     5      
ATOM     14  CG2 ILE A   2      64.392  -7.448  66.539  1.00     5      
ATOM     15  CD1 ILE A   2      63.947  -4.648  65.203  1.00     5      
ATOM     16  N   ALA A   3      65.543 -10.386  65.271  1.00     6      
ATOM     17  CA  ALA A   3      65.266 -11.760  65.644  1.00     6      
ATOM     18  C   ALA A   3      65.130 -11.875  67.153  1.00     6      
ATOM     19  O   ALA A   3      66.003 -11.421  67.878  1.00     6      
ATOM     20  CB  ALA A   3      66.383 -12.676  65.144  1.00     6      
ATOM     21  N   GLN A   4      64.032 -12.453  67.626  1.00     6      
ATOM     22  CA  GLN A   4      63.915 -12.781  69.047  1.00     6      
ATOM     23  C   GLN A   4      63.932 -14.298  69.175  1.00     6      
ATOM     24  O   GLN A   4      63.168 -15.012  68.504  1.00     6      
ATOM     25  CB  GLN A   4      62.661 -12.184  69.708  1.00     6      
ATOM     26  CG  GLN A   4      62.682 -12.398  71.244  1.00     6      
ATOM     27  CD  GLN A   4      61.487 -11.808  71.978  1.00     6      
ATOM     28  OE1 GLN A   4      61.284 -12.088  73.161  1.00     6      
ATOM     29  NE2 GLN A   4      60.698 -10.984  71.290  1.00     6      
ATOM     30  N   ILE A   5      64.862 -14.794  69.981  1.00     7      
ATOM     31  CA  ILE A   5      65.034 -16.225  70.120  1.00     7      
ATOM     32  C   ILE A   5      64.746 -16.596  71.570  1.00     7      
ATOM     33  O   ILE A   5      65.417 -16.122  72.508  1.00     7      
ATOM     34  CB  ILE A   5      66.460 -16.669  69.701  1.00     7      
ATOM     35  CG1 ILE A   5      66.869 -16.002  68.388  1.00     7      
ATOM     36  CG2 ILE A   5      66.553 -18.195  69.593  1.00     7      
ATOM     37  CD1 ILE A   5      68.272 -16.322  67.939  1.00     7      
ATOM     38  N   HIS A   6      63.706 -17.396  71.758  1.00     2      
ATOM     39  CA  HIS A   6      63.393 -17.926  73.075  1.00     2      
ATOM     40  C   HIS A   6      64.133 -19.256  73.218  1.00     2      
ATOM     41  O   HIS A   6      63.981 -20.147  72.386  1.00     2      
ATOM     42  CB  HIS A   6      61.881 -18.097  73.244  1.00     2      
ATOM     43  CG  HIS A   6      61.137 -16.808  73.429  1.00     2      
ATOM     44  ND1 HIS A   6      60.780 -16.321  74.667  1.00     2      
ATOM     45  CD2 HIS A   6      60.703 -15.895  72.527  1.00     2      
ATOM     46  CE1 HIS A   6      60.141 -15.172  74.519  1.00     2      
ATOM     47  NE2 HIS A   6      60.082 -14.891  73.228  1.00     2      
ATOM     48  N   ILE A   7      64.965 -19.373  74.244  1.00     6      
ATOM     49  CA  ILE A   7      65.700 -20.609  74.490  1.00     6      
ATOM     50  C   ILE A   7      65.571 -21.041  75.950  1.00     6      
ATOM     51  O   ILE A   7      65.304 -20.233  76.834  1.00     6      
ATOM     52  CB  ILE A   7      67.213 -20.472  74.170  1.00     6      
ATOM     53  CG1 ILE A   7      67.901 -19.560  75.195  1.00     6      
ATOM     54  CG2 ILE A   7      67.426 -19.996  72.735  1.00     6      
ATOM     55  CD1 ILE A   7      69.438 -19.486  75.062  1.00     6      
ATOM     56  N   LEU A   8      65.759 -22.326  76.187  1.00     5      
ATOM     57  CA  LEU A   8      65.757 -22.873  77.537  1.00     5      
ATOM     58  C   LEU A   8      67.010 -22.461  78.298  1.00     5      
ATOM     59  O   LEU A   8      68.064 -22.291  77.694  1.00     5      
ATOM     60  CB  LEU A   8      65.646 -24.390  77.478  1.00     5      
ATOM     61  CG  LEU A   8      64.215 -24.809  77.132  1.00     5      
ATOM     62  CD1 LEU A   8      64.140 -26.287  76.745  1.00     5      
ATOM     63  CD2 LEU A   8      63.295 -24.482  78.297  1.00     5      
ATOM     64  N   GLU A   9      66.897 -22.287  79.613  1.00     5      
ATOM     65  CA  GLU A   9      68.073 -21.987  80.439  1.00     5      
ATOM     66  C   GLU A   9      69.114 -23.080  80.316  1.00     5      
ATOM     67  O   GLU A   9      68.786 -24.217  79.998  1.00     5      
ATOM     68  CB  GLU A   9      67.702 -21.861  81.918  1.00     5      
ATOM     69  CG  GLU A   9      67.194 -20.513  82.360  1.00     5      
ATOM     70  CD  GLU A   9      66.892 -20.504  83.845  1.00     5      
ATOM     71  OE1 GLU A   9      66.533 -19.438  84.386  1.00     5      
ATOM     72  OE2 GLU A   9      67.056 -21.567  84.482  1.00     5      
ATOM     73  N   GLY A  10      70.375 -22.749  80.559  1.00     9      
ATOM     74  CA  GLY A  10      71.373 -23.797  80.612  1.00     9      
ATOM     75  C   GLY A  10      72.494 -23.683  79.605  1.00     9      
ATOM     76  O   GLY A  10      73.413 -24.485  79.621  1.00     9      
ATOM     77  N   ARG A  11      72.408 -22.751  78.689  1.00     9      
ATOM     78  CA  ARG A  11      73.428 -22.643  77.697  1.00     9      
ATOM     79  C   ARG A  11      74.601 -21.751  78.144  1.00     9      
ATOM     80  O   ARG A  11      74.426 -20.881  78.926  1.00     9      
ATOM     81  CB  ARG A  11      72.835 -22.177  76.370  1.00     9      
ATOM     82  CG  ARG A  11      71.669 -22.987  75.863  1.00     9      
ATOM     83  CD  ARG A  11      72.057 -24.329  75.266  1.00     9      
ATOM     84  NE  ARG A  11      72.016 -25.301  76.306  1.00     9      
ATOM     85  CZ  ARG A  11      72.505 -26.521  76.262  1.00     9      
ATOM     86  NH1 ARG A  11      72.410 -27.276  77.329  1.00     9      
ATOM     87  NH2 ARG A  11      73.079 -26.981  75.184  1.00     9      
ATOM     88  N   SER A  12      75.785 -22.002  77.606  1.00     6      
ATOM     89  CA  SER A  12      76.990 -21.245  77.955  1.00     6      
ATOM     90  C   SER A  12      77.036 -19.882  77.277  1.00     6      
ATOM     91  O   SER A  12      76.306 -19.635  76.317  1.00     6      
ATOM     92  CB  SER A  12      78.241 -22.034  77.577  1.00     6      
ATOM     93  OG  SER A  12      78.348 -22.150  76.168  1.00     6      
ATOM     94  N   ASP A  13      77.902 -18.996  77.759  1.00     1      
ATOM     95  CA  ASP A  13      78.058 -17.696  77.107  1.00     1      
ATOM     96  C   ASP A  13      78.565 -17.810  75.662  1.00     1      
ATOM     97  O   ASP A  13      78.084 -17.083  74.779  1.00     1      
ATOM     98  CB  ASP A  13      78.994 -16.794  77.915  1.00     1      
ATOM     99  CG  ASP A  13      78.314 -16.185  79.118  1.00     1      
ATOM    100  OD1 ASP A  13      77.105 -16.441  79.309  1.00     1      
ATOM    101  OD2 ASP A  13      78.983 -15.435  79.861  1.00     1      
ATOM    102  N   GLU A  14      79.515 -18.711  75.408  1.00     5      
ATOM    103  CA  GLU A  14      80.042 -18.853  74.048  1.00     5      
ATOM    104  C   GLU A  14      78.939 -19.370  73.123  1.00     5      
ATOM    105  O   GLU A  14      78.822 -18.924  71.984  1.00     5      
ATOM    106  CB  GLU A  14      81.276 -19.762  73.970  1.00     5      
ATOM    107  CG  GLU A  14      81.060 -21.251  74.176  1.00     5      
ATOM    108  CD  GLU A  14      82.376 -22.020  74.153  1.00     5      
ATOM    109  OE1 GLU A  14      83.316 -21.571  73.456  1.00     5      
ATOM    110  OE2 GLU A  14      82.480 -23.061  74.838  1.00     5      
ATOM    111  N   GLN A  15      78.133 -20.302  73.622  1.00     7      
ATOM    112  CA  GLN A  15      77.043 -20.850  72.835  1.00     7      
ATOM    113  C   GLN A  15      76.073 -19.733  72.458  1.00     7      
ATOM    114  O   GLN A  15      75.583 -19.693  71.328  1.00     7      
ATOM    115  CB  GLN A  15      76.320 -21.962  73.610  1.00     7      
ATOM    116  CG  GLN A  15      76.848 -23.373  73.341  1.00     7      
ATOM    117  CD  GLN A  15      76.124 -24.432  74.160  1.00     7      
ATOM    118  OE1 GLN A  15      75.230 -24.122  74.948  1.00     7      
ATOM    119  NE2 GLN A  15      76.481 -25.689  73.948  1.00     7      
ATOM    120  N   LYS A  16      75.802 -18.818  73.387  1.00     9      
ATOM    121  CA  LYS A  16      74.907 -17.698  73.078  1.00     9      
ATOM    122  C   LYS A  16      75.555 -16.646  72.176  1.00     9      
ATOM    123  O   LYS A  16      74.902 -16.084  71.281  1.00     9      
ATOM    124  CB  LYS A  16      74.402 -17.050  74.367  1.00     9      
ATOM    125  CG  LYS A  16      73.407 -17.930  75.109  1.00     9      
ATOM    126  CD  LYS A  16      72.850 -17.264  76.354  1.00     9      
ATOM    127  CE  LYS A  16      73.650 -17.637  77.578  1.00     9      
ATOM    128  NZ  LYS A  16      73.036 -17.128  78.841  1.00     9      
ATOM    129  N   GLU A  17      76.844 -16.401  72.390  1.00     4      
ATOM    130  CA  GLU A  17      77.582 -15.478  71.536  1.00     4      
ATOM    131  C   GLU A  17      77.679 -16.029  70.101  1.00     4      
ATOM    132  O   GLU A  17      77.563 -15.280  69.125  1.00     4      
ATOM    133  CB  GLU A  17      78.962 -15.196  72.118  1.00     4      
ATOM    134  CG  GLU A  17      79.692 -14.092  71.410  1.00     4      
ATOM    135  CD  GLU A  17      81.073 -13.868  71.974  1.00     4      
ATOM    136  OE1 GLU A  17      81.334 -14.324  73.113  1.00     4      
ATOM    137  OE2 GLU A  17      81.894 -13.234  71.280  1.00     4      
ATOM    138  N   THR A  18      77.917 -17.334  69.996  1.00     4      
ATOM    139  CA  THR A  18      77.938 -18.046  68.718  1.00     4      
ATOM    140  C   THR A  18      76.542 -18.031  68.084  1.00     4      
ATOM    141  O   THR A  18      76.401 -17.877  66.869  1.00     4      
ATOM    142  CB  THR A  18      78.419 -19.509  68.889  1.00     4      
ATOM    143  OG1 THR A  18      79.738 -19.521  69.453  1.00     4      
ATOM    144  CG2 THR A  18      78.433 -20.254  67.555  1.00     4      
ATOM    145  N   LEU A  19      75.519 -18.215  68.920  1.00     8      
ATOM    146  CA  LEU A  19      74.129 -18.174  68.481  1.00     8      
ATOM    147  C   LEU A  19      73.825 -16.835  67.824  1.00     8      
ATOM    148  O   LEU A  19      73.266 -16.778  66.736  1.00     8      
ATOM    149  CB  LEU A  19      73.181 -18.413  69.662  1.00     8      
ATOM    150  CG  LEU A  19      71.683 -18.284  69.403  1.00     8      
ATOM    151  CD1 LEU A  19      71.245 -19.374  68.451  1.00     8      
ATOM    152  CD2 LEU A  19      70.880 -18.347  70.693  1.00     8      
ATOM    153  N   ILE A  20      74.227 -15.759  68.491  1.00     7      
ATOM    154  CA  ILE A  20      74.038 -14.407  67.984  1.00     7      
ATOM    155  C   ILE A  20      74.749 -14.172  66.651  1.00     7      
ATOM    156  O   ILE A  20      74.156 -13.600  65.724  1.00     7      
ATOM    157  CB  ILE A  20      74.507 -13.361  69.036  1.00     7      
ATOM    158  CG1 ILE A  20      73.361 -13.065  70.005  1.00     7      
ATOM    159  CG2 ILE A  20      74.869 -12.052  68.389  1.00     7      
ATOM    160  CD1 ILE A  20      73.762 -12.199  71.186  1.00     7      
ATOM    161  N   ARG A  21      76.001 -14.613  66.544  1.00     1      
ATOM    162  CA  ARG A  21      76.773 -14.417  65.321  1.00     1      
ATOM    163  C   ARG A  21      76.227 -15.215  64.125  1.00     1      
ATOM    164  O   ARG A  21      75.990 -14.659  63.053  1.00     1      
ATOM    165  CB  ARG A  21      78.240 -14.799  65.553  1.00     1      
ATOM    166  CG  ARG A  21      79.150 -14.506  64.380  1.00     1      
ATOM    167  CD  ARG A  21      80.569 -14.986  64.632  1.00     1      
ATOM    168  NE  ARG A  21      81.065 -14.509  65.921  1.00     1      
ATOM    169  CZ  ARG A  21      81.254 -15.285  66.987  1.00     1      
ATOM    170  NH1 ARG A  21      81.040 -16.596  66.912  1.00     1      
ATOM    171  NH2 ARG A  21      81.693 -14.755  68.121  1.00     1      
ATOM    172  N   GLU A  22      75.997 -16.508  64.333  1.00     3      
ATOM    173  CA  GLU A  22      75.564 -17.405  63.265  1.00     3      
ATOM    174  C   GLU A  22      74.169 -17.048  62.751  1.00     3      
ATOM    175  O   GLU A  22      73.906 -17.138  61.557  1.00     3      
ATOM    176  CB  GLU A  22      75.572 -18.859  63.748  1.00     3      
ATOM    177  CG  GLU A  22      76.955 -19.421  64.096  1.00     3      
ATOM    178  CD  GLU A  22      77.871 -19.588  62.890  1.00     3      
ATOM    179  OE1 GLU A  22      77.366 -19.782  61.763  1.00     3      
ATOM    180  OE2 GLU A  22      79.107 -19.525  63.074  1.00     3      
ATOM    181  N   VAL A  23      73.272 -16.668  63.657  1.00     6      
ATOM    182  CA  VAL A  23      71.918 -16.284  63.263  1.00     6      
ATOM    183  C   VAL A  23      71.942 -14.954  62.497  1.00     6      
ATOM    184  O   VAL A  23      71.248 -14.797  61.489  1.00     6      
ATOM    185  CB  VAL A  23      70.988 -16.222  64.503  1.00     6      
ATOM    186  CG1 VAL A  23      69.734 -15.456  64.221  1.00     6      
ATOM    187  CG2 VAL A  23      70.666 -17.627  64.974  1.00     6      
ATOM    188  N   SER A  24      72.762 -14.012  62.954  1.00     8      
ATOM    189  CA  SER A  24      72.902 -12.722  62.280  1.00     8      
ATOM    190  C   SER A  24      73.466 -12.887  60.867  1.00     8      
ATOM    191  O   SER A  24      72.999 -12.236  59.921  1.00     8      
ATOM    192  CB  SER A  24      73.818 -11.787  63.080  1.00     8      
ATOM    193  OG  SER A  24      73.263 -11.445  64.334  1.00     8      
ATOM    194  N   GLU A  25      74.480 -13.742  60.724  1.00     1      
ATOM    195  CA  GLU A  25      75.066 -13.983  59.402  1.00     1      
ATOM    196  C   GLU A  25      74.075 -14.708  58.488  1.00     1      
ATOM    197  O   GLU A  25      73.977 -14.386  57.308  1.00     1      
ATOM    198  CB  GLU A  25      76.367 -14.793  59.488  1.00     1      
ATOM    199  CG  GLU A  25      77.532 -14.068  60.132  1.00     1      
ATOM    200  CD  GLU A  25      78.797 -14.914  60.163  1.00     1      
ATOM    201  OE1 GLU A  25      78.721 -16.125  59.858  1.00     1      
ATOM    202  OE2 GLU A  25      79.865 -14.370  60.512  1.00     1      
ATOM    203  N   ALA A  26      73.350 -15.680  59.045  1.00     7      
ATOM    204  CA  ALA A  26      72.344 -16.436  58.289  1.00     7      
ATOM    205  C   ALA A  26      71.250 -15.512  57.784  1.00     7      
ATOM    206  O   ALA A  26      70.775 -15.653  56.654  1.00     7      
ATOM    207  CB  ALA A  26      71.747 -17.554  59.139  1.00     7      
ATOM    208  N   ILE A  27      70.824 -14.590  58.639  1.00     5      
ATOM    209  CA  ILE A  27      69.836 -13.603  58.238  1.00     5      
ATOM    210  C   ILE A  27      70.416 -12.705  57.158  1.00     5      
ATOM    211  O   ILE A  27      69.784 -12.479  56.130  1.00     5      
ATOM    212  CB  ILE A  27      69.368 -12.737  59.423  1.00     5      
ATOM    213  CG1 ILE A  27      68.511 -13.559  60.385  1.00     5      
ATOM    214  CG2 ILE A  27      68.550 -11.545  58.940  1.00     5      
ATOM    215  CD1 ILE A  27      68.148 -12.808  61.662  1.00     5      
ATOM    216  N   SER A  28      71.639 -12.228  57.376  1.00     4      
ATOM    217  CA  SER A  28      72.268 -11.333  56.415  1.00     4      
ATOM    218  C   SER A  28      72.416 -11.943  55.025  1.00     4      
ATOM    219  O   SER A  28      72.072 -11.300  54.041  1.00     4      
ATOM    220  CB  SER A  28      73.639 -10.886  56.910  1.00     4      
ATOM    221  OG  SER A  28      74.215  -9.980  55.989  1.00     4      
ATOM    222  N   ARG A  29      72.940 -13.163  54.931  1.00     1      
ATOM    223  CA  ARG A  29      73.120 -13.790  53.617  1.00     1      
ATOM    224  C   ARG A  29      71.783 -14.163  52.948  1.00     1      
ATOM    225  O   ARG A  29      71.623 -13.970  51.744  1.00     1      
ATOM    226  CB  ARG A  29      74.061 -15.006  53.694  1.00     1      
ATOM    227  CG  ARG A  29      73.599 -16.186  54.520  1.00     1      
ATOM    228  CD  ARG A  29      74.627 -17.323  54.438  1.00     1      
ATOM    229  NE  ARG A  29      74.253 -18.444  55.293  1.00     1      
ATOM    230  CZ  ARG A  29      74.646 -18.595  56.554  1.00     1      
ATOM    231  NH1 ARG A  29      75.463 -17.712  57.116  1.00     1      
ATOM    232  NH2 ARG A  29      74.234 -19.645  57.251  1.00     1      
ATOM    233  N   SER A  30      70.835 -14.706  53.708  1.00     5      
ATOM    234  CA  SER A  30      69.564 -15.139  53.125  1.00     5      
ATOM    235  C   SER A  30      68.779 -13.969  52.538  1.00     5      
ATOM    236  O   SER A  30      68.109 -14.116  51.522  1.00     5      
ATOM    237  CB  SER A  30      68.698 -15.855  54.165  1.00     5      
ATOM    238  OG  SER A  30      69.304 -17.057  54.594  1.00     5      
ATOM    239  N   LEU A  31      68.882 -12.807  53.170  1.00     6      
ATOM    240  CA  LEU A  31      68.084 -11.655  52.777  1.00     6      
ATOM    241  C   LEU A  31      68.901 -10.587  52.050  1.00     6      
ATOM    242  O   LEU A  31      68.346  -9.569  51.627  1.00     6      
ATOM    243  CB  LEU A  31      67.426 -11.029  54.003  1.00     6      
ATOM    244  CG  LEU A  31      66.493 -11.905  54.827  1.00     6      
ATOM    245  CD1 LEU A  31      65.892 -11.085  55.949  1.00     6      
ATOM    246  CD2 LEU A  31      65.401 -12.479  53.935  1.00     6      
ATOM    247  N   ASP A  32      70.203 -10.829  51.899  1.00     1      
ATOM    248  CA  ASP A  32      71.131  -9.835  51.358  1.00     1      
ATOM    249  C   ASP A  32      70.982  -8.494  52.063  1.00     1      
ATOM    250  O   ASP A  32      70.910  -7.439  51.431  1.00     1      
ATOM    251  CB  ASP A  32      70.974  -9.675  49.844  1.00     1      
ATOM    252  CG  ASP A  32      71.608 -10.821  49.071  1.00     1      
ATOM    253  OD1 ASP A  32      72.601 -11.393  49.576  1.00     1      
ATOM    254  OD2 ASP A  32      71.136 -11.139  47.957  1.00     1      
ATOM    255  N   ALA A  33      70.899  -8.559  53.385  1.00     6      
ATOM    256  CA  ALA A  33      70.823  -7.371  54.211  1.00     6      
ATOM    257  C   ALA A  33      72.172  -7.165  54.886  1.00     6      
ATOM    258  O   ALA A  33      72.837  -8.134  55.259  1.00     6      
ATOM    259  CB  ALA A  33      69.707  -7.505  55.238  1.00     6      
ATOM    260  N   PRO A  34      72.586  -5.902  55.043  1.00     2      
ATOM    261  CA  PRO A  34      73.871  -5.650  55.697  1.00     2      
ATOM    262  C   PRO A  34      73.876  -6.212  57.107  1.00     2      
ATOM    263  O   PRO A  34      72.880  -6.072  57.819  1.00     2      
ATOM    264  CB  PRO A  34      73.983  -4.122  55.698  1.00     2      
ATOM    265  CG  PRO A  34      72.599  -3.623  55.496  1.00     2      
ATOM    266  CD  PRO A  34      71.894  -4.656  54.671  1.00     2      
ATOM    267  N   LEU A  35      74.965  -6.871  57.486  1.00     1      
ATOM    268  CA  LEU A  35      75.068  -7.485  58.805  1.00     1      
ATOM    269  C   LEU A  35      74.799  -6.483  59.923  1.00     1      
ATOM    270  O   LEU A  35      74.138  -6.807  60.903  1.00     1      
ATOM    271  CB  LEU A  35      76.454  -8.104  58.988  1.00     1      
ATOM    272  CG  LEU A  35      76.741  -8.836  60.298  1.00     1      
ATOM    273  CD1 LEU A  35      75.730  -9.936  60.551  1.00     1      
ATOM    274  CD2 LEU A  35      78.160  -9.388  60.289  1.00     1      
ATOM    275  N   THR A  36      75.274  -5.255  59.747  1.00     4      
ATOM    276  CA  THR A  36      75.140  -4.216  60.770  1.00     4      
ATOM    277  C   THR A  36      73.701  -3.809  61.096  1.00     4      
ATOM    278  O   THR A  36      73.455  -3.183  62.125  1.00     4      
ATOM    279  CB  THR A  36      75.915  -2.947  60.365  1.00     4      
ATOM    280  OG1 THR A  36      75.464  -2.490  59.081  1.00     4      
ATOM    281  CG2 THR A  36      77.401  -3.243  60.289  1.00     4      
ATOM    282  N   SER A  37      72.758  -4.144  60.218  1.00     4      
ATOM    283  CA  SER A  37      71.351  -3.801  60.442  1.00     4      
ATOM    284  C   SER A  37      70.592  -4.913  61.173  1.00     4      
ATOM    285  O   SER A  37      69.416  -4.759  61.499  1.00     4      
ATOM    286  CB  SER A  37      70.659  -3.474  59.116  1.00     4      
ATOM    287  OG  SER A  37      70.507  -4.636  58.322  1.00     4      
ATOM    288  N   VAL A  38      71.256  -6.042  61.397  1.00     7      
ATOM    289  CA  VAL A  38      70.621  -7.205  62.019  1.00     7      
ATOM    290  C   VAL A  38      70.714  -7.152  63.547  1.00     7      
ATOM    291  O   VAL A  38      71.798  -6.992  64.093  1.00     7      
ATOM    292  CB  VAL A  38      71.246  -8.515  61.520  1.00     7      
ATOM    293  CG1 VAL A  38      70.629  -9.706  62.228  1.00     7      
ATOM    294  CG2 VAL A  38      71.092  -8.636  60.005  1.00     7      
ATOM    295  N   ARG A  39      69.574  -7.266  64.229  1.00     8      
ATOM    296  CA  ARG A  39      69.573  -7.277  65.688  1.00     8      
ATOM    297  C   ARG A  39      69.004  -8.579  66.255  1.00     8      
ATOM    298  O   ARG A  39      67.989  -9.082  65.792  1.00     8      
ATOM    299  CB  ARG A  39      68.805  -6.065  66.193  1.00     8      
ATOM    300  CG  ARG A  39      69.656  -4.838  65.998  1.00     8      
ATOM    301  CD  ARG A  39      68.865  -3.549  66.008  1.00     8      
ATOM    302  NE  ARG A  39      69.766  -2.419  65.811  1.00     8      
ATOM    303  CZ  ARG A  39      70.316  -2.122  64.636  1.00     8      
ATOM    304  NH1 ARG A  39      70.000  -2.832  63.559  1.00     8      
ATOM    305  NH2 ARG A  39      71.140  -1.093  64.521  1.00     8      
ATOM    306  N   VAL A  40      69.651  -9.111  67.286  1.00     8      
ATOM    307  CA  VAL A  40      69.216 -10.376  67.863  1.00     8      
ATOM    308  C   VAL A  40      69.014 -10.276  69.374  1.00     8      
ATOM    309  O   VAL A  40      69.884  -9.812  70.122  1.00     8      
ATOM    310  CB  VAL A  40      70.226 -11.514  67.544  1.00     8      
ATOM    311  CG1 VAL A  40      69.885 -12.803  68.320  1.00     8      
ATOM    312  CG2 VAL A  40      70.275 -11.765  66.043  1.00     8      
ATOM    313  N   ILE A  41      67.835 -10.713  69.802  1.00     3      
ATOM    314  CA  ILE A  41      67.463 -10.753  71.209  1.00     3      
ATOM    315  C   ILE A  41      67.327 -12.198  71.675  1.00     3      
ATOM    316  O   ILE A  41      66.532 -12.972  71.132  1.00     3      
ATOM    317  CB  ILE A  41      66.141 -10.002  71.442  1.00     3      
ATOM    318  CG1 ILE A  41      66.289  -8.523  71.051  1.00     3      
ATOM    319  CG2 ILE A  41      65.671 -10.147  72.879  1.00     3      
ATOM    320  CD1 ILE A  41      64.966  -7.770  71.000  1.00     3      
ATOM    321  N   ILE A  42      68.113 -12.560  72.674  1.00     8      
ATOM    322  CA  ILE A  42      68.002 -13.873  73.279  1.00     8      
ATOM    323  C   ILE A  42      67.146 -13.778  74.526  1.00     8      
ATOM    324  O   ILE A  42      67.453 -12.995  75.432  1.00     8      
ATOM    325  CB  ILE A  42      69.376 -14.436  73.624  1.00     8      
ATOM    326  CG1 ILE A  42      70.222 -14.539  72.354  1.00     8      
ATOM    327  CG2 ILE A  42      69.250 -15.793  74.312  1.00     8      
ATOM    328  CD1 ILE A  42      71.592 -15.087  72.604  1.00     8      
ATOM    329  N   THR A  43      66.090 -14.584  74.595  1.00     2      
ATOM    330  CA  THR A  43      65.255 -14.592  75.784  1.00     2      
ATOM    331  C   THR A  43      65.331 -15.976  76.426  1.00     2      
ATOM    332  O   THR A  43      64.954 -16.963  75.813  1.00     2      
ATOM    333  CB  THR A  43      63.783 -14.248  75.466  1.00     2      
ATOM    334  OG1 THR A  43      63.701 -13.055  74.667  1.00     2      
ATOM    335  CG2 THR A  43      62.985 -14.065  76.754  1.00     2      
ATOM    336  N   GLU A  44      65.882 -16.057  77.635  1.00     8      
ATOM    337  CA  GLU A  44      65.975 -17.333  78.333  1.00     8      
ATOM    338  C   GLU A  44      64.661 -17.661  79.031  1.00     8      
ATOM    339  O   GLU A  44      64.015 -16.784  79.603  1.00     8      
ATOM    340  CB  GLU A  44      67.117 -17.331  79.361  1.00     8      
ATOM    341  CG  GLU A  44      68.513 -17.366  78.774  1.00     8      
ATOM    342  CD  GLU A  44      69.570 -17.553  79.852  1.00     8      
ATOM    343  OE1 GLU A  44      69.477 -16.858  80.887  1.00     8      
ATOM    344  OE2 GLU A  44      70.469 -18.399  79.664  1.00     8      
ATOM    345  N   MET A  45      64.266 -18.927  78.965  1.00     6      
ATOM    346  CA  MET A  45      63.086 -19.415  79.674  1.00     6      
ATOM    347  C   MET A  45      63.448 -20.338  80.841  1.00     6      
ATOM    348  O   MET A  45      64.196 -21.289  80.656  1.00     6      
ATOM    349  CB  MET A  45      62.161 -20.172  78.726  1.00     6      
ATOM    350  CG  MET A  45      61.697 -19.381  77.507  1.00     6      
ATOM    351  SD  MET A  45      60.660 -20.392  76.436  1.00     6      
ATOM    352  CE  MET A  45      61.858 -21.489  75.683  1.00     6      
ATOM    353  N   ALA A  46      62.883 -20.073  82.018  1.00     1      
ATOM    354  CA  ALA A  46      63.008 -20.970  83.172  1.00     1      
ATOM    355  C   ALA A  46      62.268 -22.282  82.906  1.00     1      
ATOM    356  O   ALA A  46      61.289 -22.321  82.148  1.00     1      
ATOM    357  CB  ALA A  46      62.474 -20.301  84.428  1.00     1      
ATOM    358  N   LYS A  47      62.715 -23.356  83.543  1.00     3      
ATOM    359  CA  LYS A  47      62.171 -24.675  83.242  1.00     3      
ATOM    360  C   LYS A  47      60.658 -24.794  83.483  1.00     3      
ATOM    361  O   LYS A  47      59.960 -25.480  82.728  1.00     3      
ATOM    362  CB  LYS A  47      62.924 -25.736  84.043  1.00     3      
ATOM    363  CG  LYS A  47      64.323 -25.982  83.499  1.00     3      
ATOM    364  CD  LYS A  47      65.067 -27.096  84.228  1.00     3      
ATOM    365  CE  LYS A  47      64.615 -28.461  83.742  1.00     3      
ATOM    366  NZ  LYS A  47      64.994 -28.652  82.305  1.00     3      
ATOM    367  N   GLY A  48      60.150 -24.097  84.495  1.00     2      
ATOM    368  CA  GLY A  48      58.730 -24.136  84.802  1.00     2      
ATOM    369  C   GLY A  48      57.887 -23.188  83.959  1.00     2      
ATOM    370  O   GLY A  48      56.690 -23.058  84.176  1.00     2      
ATOM    371  N   HIS A  49      58.505 -22.538  82.983  1.00     6      
ATOM    372  CA  HIS A  49      57.804 -21.507  82.223  1.00     6      
ATOM    373  C   HIS A  49      57.605 -21.908  80.763  1.00     6      
ATOM    374  O   HIS A  49      57.138 -21.101  79.940  1.00     6      
ATOM    375  CB  HIS A  49      58.565 -20.193  82.291  1.00     6      
ATOM    376  CG  HIS A  49      58.581 -19.576  83.656  1.00     6      
ATOM    377  ND1 HIS A  49      59.320 -18.455  83.955  1.00     6      
ATOM    378  CD2 HIS A  49      57.955 -19.932  84.805  1.00     6      
ATOM    379  CE1 HIS A  49      59.159 -18.148  85.232  1.00     6      
ATOM    380  NE2 HIS A  49      58.333 -19.028  85.771  1.00     6      
ATOM    381  N   PHE A  50      57.984 -23.133  80.425  1.00     7      
ATOM    382  CA  PHE A  50      57.858 -23.570  79.034  1.00     7      
ATOM    383  C   PHE A  50      57.048 -24.851  78.937  1.00     7      
ATOM    384  O   PHE A  50      57.389 -25.863  79.557  1.00     7      
ATOM    385  CB  PHE A  50      59.228 -23.753  78.378  1.00     7      
ATOM    386  CG  PHE A  50      59.148 -24.149  76.928  1.00     7      
ATOM    387  CD1 PHE A  50      58.336 -23.439  76.045  1.00     7      
ATOM    388  CD2 PHE A  50      59.890 -25.209  76.441  1.00     7      
ATOM    389  CE1 PHE A  50      58.254 -23.795  74.707  1.00     7      
ATOM    390  CE2 PHE A  50      59.819 -25.571  75.086  1.00     7      
ATOM    391  CZ  PHE A  50      58.999 -24.867  74.228  1.00     7      
ATOM    392  N   GLY A  51      55.950 -24.790  78.184  1.00     6      
ATOM    393  CA  GLY A  51      55.068 -25.930  78.079  1.00     6      
ATOM    394  C   GLY A  51      55.000 -26.522  76.693  1.00     6      
ATOM    395  O   GLY A  51      54.974 -25.785  75.701  1.00     6      
ATOM    396  N   ILE A  52      54.991 -27.851  76.627  1.00     5      
ATOM    397  CA  ILE A  52      54.718 -28.572  75.384  1.00     5      
ATOM    398  C   ILE A  52      53.613 -29.598  75.639  1.00     5      
ATOM    399  O   ILE A  52      53.745 -30.452  76.515  1.00     5      
ATOM    400  CB  ILE A  52      55.962 -29.297  74.835  1.00     5      
ATOM    401  CG1 ILE A  52      57.116 -28.321  74.608  1.00     5      
ATOM    402  CG2 ILE A  52      55.618 -30.055  73.553  1.00     5      
ATOM    403  CD1 ILE A  52      58.421 -29.020  74.249  1.00     5      
ATOM    404  N   GLY A  53      52.531 -29.519  74.876  1.00     5      
ATOM    405  CA  GLY A  53      51.408 -30.419  75.062  1.00     5      
ATOM    406  C   GLY A  53      50.709 -30.287  76.405  1.00     5      
ATOM    407  O   GLY A  53      50.086 -31.229  76.879  1.00     5      
ATOM    408  N   GLY A  54      50.807 -29.118  77.024  1.00     8      
ATOM    409  CA  GLY A  54      50.129 -28.880  78.289  1.00     8      
ATOM    410  C   GLY A  54      50.927 -29.310  79.503  1.00     8      
ATOM    411  O   GLY A  54      50.484 -29.159  80.644  1.00     8      
ATOM    412  N   GLU A  55      52.093 -29.886  79.247  1.00     1      
ATOM    413  CA  GLU A  55      52.997 -30.324  80.295  1.00     1      
ATOM    414  C   GLU A  55      54.317 -29.576  80.150  1.00     1      
ATOM    415  O   GLU A  55      54.645 -29.120  79.055  1.00     1      
ATOM    416  CB  GLU A  55      53.208 -31.835  80.226  1.00     1      
ATOM    417  CG  GLU A  55      51.913 -32.645  80.384  1.00     1      
ATOM    418  CD  GLU A  55      51.181 -32.373  81.696  1.00     1      
ATOM    419  OE1 GLU A  55      51.850 -32.211  82.739  1.00     1      
ATOM    420  OE2 GLU A  55      49.929 -32.336  81.683  1.00     1      
ATOM    421  N   LEU A  56      55.068 -29.439  81.239  1.00     4      
ATOM    422  CA  LEU A  56      56.377 -28.788  81.168  1.00     4      
ATOM    423  C   LEU A  56      57.270 -29.578  80.227  1.00     4      
ATOM    424  O   LEU A  56      57.193 -30.800  80.177  1.00     4      
ATOM    425  CB  LEU A  56      57.037 -28.692  82.553  1.00     4      
ATOM    426  CG  LEU A  56      56.357 -27.866  83.645  1.00     4      
ATOM    427  CD1 LEU A  56      57.161 -27.924  84.963  1.00     4      
ATOM    428  CD2 LEU A  56      56.178 -26.428  83.176  1.00     4      
ATOM    429  N   ALA A  57      58.124 -28.874  79.494  1.00     7      
ATOM    430  CA  ALA A  57      59.026 -29.515  78.543  1.00     7      
ATOM    431  C   ALA A  57      60.140 -30.294  79.240  1.00     7      
ATOM    432  O   ALA A  57      60.598 -29.910  80.316  1.00     7      
ATOM    433  CB  ALA A  57      59.614 -28.469  77.607  1.00     7      
TER     434      ALA A  57                                                      
ATOM    435  N   PRO B   1      63.706 -24.529  70.767  1.00            
ATOM    436  CA  PRO B   1      63.995 -23.107  70.563  1.00            
ATOM    437  C   PRO B   1      63.009 -22.475  69.586  1.00            
ATOM    438  O   PRO B   1      62.652 -23.109  68.592  1.00            
ATOM    439  CB  PRO B   1      65.404 -23.109  69.966  1.00            
ATOM    440  CG  PRO B   1      66.004 -24.395  70.368  1.00            
ATOM    441  CD  PRO B   1      64.895 -25.378  70.574  1.00            
ATOM    442  N   ILE B   2      62.584 -21.247  69.861  1.00            
ATOM    443  CA  ILE B   2      61.636 -20.545  68.999  1.00            
ATOM    444  C   ILE B   2      62.166 -19.168  68.588  1.00            
ATOM    445  O   ILE B   2      62.492 -18.331  69.449  1.00            
ATOM    446  CB  ILE B   2      60.263 -20.372  69.680  1.00            
ATOM    447  CG1 ILE B   2      59.680 -21.737  70.057  1.00            
ATOM    448  CG2 ILE B   2      59.315 -19.615  68.772  1.00            
ATOM    449  CD1 ILE B   2      58.470 -21.663  70.943  1.00            
ATOM    450  N   ALA B   3      62.268 -18.939  67.279  1.00            
ATOM    451  CA  ALA B   3      62.765 -17.661  66.775  1.00            
ATOM    452  C   ALA B   3      61.662 -16.883  66.060  1.00            
ATOM    453  O   ALA B   3      61.037 -17.385  65.127  1.00            
ATOM    454  CB  ALA B   3      63.949 -17.879  65.839  1.00            
ATOM    455  N   GLN B   4      61.437 -15.644  66.485  1.00            
ATOM    456  CA  GLN B   4      60.523 -14.790  65.748  1.00            
ATOM    457  C   GLN B   4      61.345 -13.724  65.074  1.00            
ATOM    458  O   GLN B   4      62.045 -12.944  65.732  1.00            
ATOM    459  CB  GLN B   4      59.447 -14.161  66.643  1.00            
ATOM    460  CG  GLN B   4      58.411 -13.391  65.800  1.00            
ATOM    461  CD  GLN B   4      57.278 -12.773  66.591  1.00            
ATOM    462  OE1 GLN B   4      57.241 -12.838  67.823  1.00            
ATOM    463  NE2 GLN B   4      56.334 -12.163  65.875  1.00            
ATOM    464  N   ILE B   5      61.245 -13.674  63.752  1.00            
ATOM    465  CA  ILE B   5      62.068 -12.749  63.002  1.00            
ATOM    466  C   ILE B   5      61.210 -11.696  62.322  1.00            
ATOM    467  O   ILE B   5      60.408 -12.029  61.454  1.00            
ATOM    468  CB  ILE B   5      62.904 -13.472  61.942  1.00            
ATOM    469  CG1 ILE B   5      63.606 -14.683  62.546  1.00            
ATOM    470  CG2 ILE B   5      63.929 -12.520  61.330  1.00            
ATOM    471  CD1 ILE B   5      64.416 -15.460  61.533  1.00            
ATOM    472  N   HIS B   6      61.401 -10.428  62.709  1.00            
ATOM    473  CA  HIS B   6      60.709  -9.315  62.056  1.00            
ATOM    474  C   HIS B   6      61.521  -8.832  60.865  1.00            
ATOM    475  O   HIS B   6      62.668  -8.421  61.013  1.00            
ATOM    476  CB  HIS B   6      60.475  -8.171  63.045  1.00            
ATOM    477  CG  HIS B   6      59.374  -8.438  64.024  1.00            
ATOM    478  ND1 HIS B   6      58.086  -7.984  63.837  1.00            
ATOM    479  CD2 HIS B   6      59.359  -9.151  65.175  1.00            
ATOM    480  CE1 HIS B   6      57.331  -8.382  64.844  1.00            
ATOM    481  NE2 HIS B   6      58.078  -9.097  65.666  1.00            
ATOM    482  N   ILE B   7      60.929  -8.883  59.675  1.00            
ATOM    483  CA  ILE B   7      61.628  -8.415  58.484  1.00            
ATOM    484  C   ILE B   7      60.724  -7.496  57.695  1.00            
ATOM    485  O   ILE B   7      59.495  -7.542  57.831  1.00            
ATOM    486  CB  ILE B   7      62.090  -9.578  57.579  1.00            
ATOM    487  CG1 ILE B   7      60.890 -10.288  56.955  1.00            
ATOM    488  CG2 ILE B   7      62.974 -10.558  58.359  1.00            
ATOM    489  CD1 ILE B   7      61.272 -11.376  55.981  1.00            
ATOM    490  N   LEU B   8      61.337  -6.648  56.880  1.00            
ATOM    491  CA  LEU B   8      60.572  -5.765  56.032  1.00            
ATOM    492  C   LEU B   8      59.907  -6.589  54.936  1.00            
ATOM    493  O   LEU B   8      60.433  -7.611  54.503  1.00            
ATOM    494  CB  LEU B   8      61.450  -4.668  55.439  1.00            
ATOM    495  CG  LEU B   8      61.794  -3.536  56.410  1.00            
ATOM    496  CD1 LEU B   8      62.905  -2.668  55.836  1.00            
ATOM    497  CD2 LEU B   8      60.551  -2.701  56.727  1.00            
ATOM    498  N   GLU B   9      58.704  -6.172  54.566  1.00            
ATOM    499  CA  GLU B   9      57.960  -6.764  53.461  1.00            
ATOM    500  C   GLU B   9      58.685  -6.590  52.142  1.00            
ATOM    501  O   GLU B   9      59.540  -5.730  52.006  1.00            
ATOM    502  CB  GLU B   9      56.566  -6.143  53.349  1.00            
ATOM    503  CG  GLU B   9      55.516  -6.777  54.230  1.00            
ATOM    504  CD  GLU B   9      54.159  -6.127  54.054  1.00            
ATOM    505  OE1 GLU B   9      53.178  -6.617  54.658  1.00            
ATOM    506  OE2 GLU B   9      54.067  -5.152  53.274  1.00            
ATOM    507  N   GLY B  10      58.358  -7.439  51.182  1.00            
ATOM    508  CA  GLY B  10      58.834  -7.258  49.831  1.00            
ATOM    509  C   GLY B  10      59.612  -8.440  49.322  1.00            
ATOM    510  O   GLY B  10      59.775  -8.602  48.102  1.00            
ATOM    511  N   ARG B  11      60.007  -9.330  50.227  1.00            
ATOM    512  CA  ARG B  11      60.772 -10.482  49.773  1.00            
ATOM    513  C   ARG B  11      59.868 -11.588  49.264  1.00            
ATOM    514  O   ARG B  11      58.714 -11.727  49.683  1.00            
ATOM    515  CB  ARG B  11      61.717 -11.004  50.867  1.00            
ATOM    516  CG  ARG B  11      62.940 -10.115  51.061  1.00            
ATOM    517  CD  ARG B  11      62.724  -8.972  52.011  1.00            
ATOM    518  NE  ARG B  11      63.998  -8.417  52.459  1.00            
ATOM    519  CZ  ARG B  11      64.126  -7.606  53.499  1.00            
ATOM    520  NH1 ARG B  11      63.057  -7.276  54.205  1.00            
ATOM    521  NH2 ARG B  11      65.317  -7.130  53.829  1.00            
ATOM    522  N   SER B  12      60.414 -12.352  48.326  1.00            
ATOM    523  CA  SER B  12      59.719 -13.476  47.718  1.00            
ATOM    524  C   SER B  12      59.708 -14.711  48.617  1.00            
ATOM    525  O   SER B  12      60.448 -14.764  49.622  1.00            
ATOM    526  CB  SER B  12      60.352 -13.762  46.384  1.00            
ATOM    527  OG  SER B  12      61.671 -14.198  46.566  1.00            
ATOM    528  N   ASP B  13      58.847 -15.673  48.275  1.00            
ATOM    529  CA  ASP B  13      58.716 -16.910  49.045  1.00            
ATOM    530  C   ASP B  13      59.971 -17.760  49.139  1.00            
ATOM    531  O   ASP B  13      60.245 -18.310  50.210  1.00            
ATOM    532  CB  ASP B  13      57.583 -17.792  48.503  1.00            
ATOM    533  CG  ASP B  13      56.199 -17.341  48.975  1.00            
ATOM    534  OD1 ASP B  13      56.077 -16.317  49.692  1.00            
ATOM    535  OD2 ASP B  13      55.230 -18.082  48.701  1.00            
ATOM    536  N   GLU B  14      60.735 -17.873  48.056  1.00            
ATOM    537  CA  GLU B  14      61.944 -18.698  48.089  1.00            
ATOM    538  C   GLU B  14      62.980 -18.127  49.061  1.00            
ATOM    539  O   GLU B  14      63.613 -18.868  49.820  1.00            
ATOM    540  CB  GLU B  14      62.543 -18.859  46.681  1.00            
ATOM    541  CG  GLU B  14      63.183 -17.648  46.100  1.00            
ATOM    542  CD  GLU B  14      62.197 -16.668  45.532  1.00            
ATOM    543  OE1 GLU B  14      60.962 -16.865  45.686  1.00            
ATOM    544  OE2 GLU B  14      62.657 -15.634  44.967  1.00            
ATOM    545  N   GLN B  15      63.141 -16.808  49.063  1.00            
ATOM    546  CA  GLN B  15      64.078 -16.173  49.992  1.00            
ATOM    547  C   GLN B  15      63.655 -16.368  51.449  1.00            
ATOM    548  O   GLN B  15      64.495 -16.555  52.338  1.00            
ATOM    549  CB  GLN B  15      64.238 -14.679  49.690  1.00            
ATOM    550  CG  GLN B  15      65.361 -14.394  48.704  1.00            
ATOM    551  CD  GLN B  15      65.584 -12.913  48.456  1.00            
ATOM    552  OE1 GLN B  15      64.929 -12.060  49.062  1.00            
ATOM    553  NE2 GLN B  15      66.512 -12.601  47.554  1.00            
ATOM    554  N   LYS B  16      62.356 -16.312  51.723  1.00            
ATOM    555  CA  LYS B  16      61.902 -16.520  53.101  1.00            
ATOM    556  C   LYS B  16      62.070 -17.978  53.526  1.00            
ATOM    557  O   LYS B  16      62.324 -18.271  54.714  1.00            
ATOM    558  CB  LYS B  16      60.452 -16.071  53.273  1.00            
ATOM    559  CG  LYS B  16      60.288 -14.557  53.213  1.00            
ATOM    560  CD  LYS B  16      58.851 -14.171  53.446  1.00            
ATOM    561  CE  LYS B  16      58.109 -14.081  52.109  1.00            
ATOM    562  NZ  LYS B  16      56.755 -13.584  52.381  1.00            
ATOM    563  N   GLU B  17      61.909 -18.882  52.564  1.00            
ATOM    564  CA  GLU B  17      62.163 -20.304  52.777  1.00            
ATOM    565  C   GLU B  17      63.625 -20.542  53.110  1.00            
ATOM    566  O   GLU B  17      63.952 -21.327  53.997  1.00            
ATOM    567  CB  GLU B  17      61.798 -21.096  51.529  1.00            
ATOM    568  CG  GLU B  17      61.904 -22.601  51.648  1.00            
ATOM    569  CD  GLU B  17      61.642 -23.288  50.309  1.00            
ATOM    570  OE1 GLU B  17      61.068 -22.632  49.413  1.00            
ATOM    571  OE2 GLU B  17      62.019 -24.471  50.146  1.00            
ATOM    572  N   THR B  18      64.500 -19.865  52.379  1.00            
ATOM    573  CA  THR B  18      65.923 -19.948  52.635  1.00            
ATOM    574  C   THR B  18      66.261 -19.379  54.022  1.00            
ATOM    575  O   THR B  18      67.042 -19.980  54.761  1.00            
ATOM    576  CB  THR B  18      66.714 -19.221  51.556  1.00            
ATOM    577  OG1 THR B  18      66.490 -19.879  50.309  1.00            
ATOM    578  CG2 THR B  18      68.204 -19.261  51.869  1.00            
ATOM    579  N   LEU B  19      65.645 -18.251  54.374  1.00            
ATOM    580  CA  LEU B  19      65.827 -17.636  55.682  1.00            
ATOM    581  C   LEU B  19      65.492 -18.615  56.810  1.00            
ATOM    582  O   LEU B  19      66.256 -18.765  57.770  1.00            
ATOM    583  CB  LEU B  19      64.952 -16.393  55.803  1.00            
ATOM    584  CG  LEU B  19      64.913 -15.766  57.197  1.00            
ATOM    585  CD1 LEU B  19      66.275 -15.217  57.548  1.00            
ATOM    586  CD2 LEU B  19      63.857 -14.690  57.230  1.00            
ATOM    587  N   ILE B  20      64.354 -19.291  56.669  1.00            
ATOM    588  CA  ILE B  20      63.909 -20.285  57.641  1.00            
ATOM    589  C   ILE B  20      64.894 -21.447  57.790  1.00            
ATOM    590  O   ILE B  20      65.202 -21.871  58.902  1.00            
ATOM    591  CB  ILE B  20      62.534 -20.866  57.247  1.00            
ATOM    592  CG1 ILE B  20      61.425 -19.875  57.582  1.00            
ATOM    593  CG2 ILE B  20      62.280 -22.182  57.947  1.00            
ATOM    594  CD1 ILE B  20      60.081 -20.273  57.018  1.00            
ATOM    595  N   ARG B  21      65.369 -21.969  56.667  1.00            
ATOM    596  CA  ARG B  21      66.285 -23.103  56.702  1.00            
ATOM    597  C   ARG B  21      67.633 -22.713  57.301  1.00            
ATOM    598  O   ARG B  21      68.183 -23.440  58.126  1.00            
ATOM    599  CB  ARG B  21      66.450 -23.700  55.303  1.00            
ATOM    600  CG  ARG B  21      67.310 -24.956  55.254  1.00            
ATOM    601  CD  ARG B  21      67.443 -25.492  53.826  1.00            
ATOM    602  NE  ARG B  21      66.131 -25.686  53.210  1.00            
ATOM    603  CZ  ARG B  21      65.616 -24.921  52.251  1.00            
ATOM    604  NH1 ARG B  21      66.310 -23.903  51.759  1.00            
ATOM    605  NH2 ARG B  21      64.408 -25.185  51.775  1.00            
ATOM    606  N   GLU B  22      68.168 -21.580  56.852  1.00            
ATOM    607  CA  GLU B  22      69.486 -21.110  57.280  1.00            
ATOM    608  C   GLU B  22      69.492 -20.683  58.752  1.00            
ATOM    609  O   GLU B  22      70.456 -20.923  59.468  1.00            
ATOM    610  CB  GLU B  22      69.944 -19.955  56.381  1.00            
ATOM    611  CG  GLU B  22      70.153 -20.361  54.913  1.00            
ATOM    612  CD  GLU B  22      71.351 -21.257  54.663  1.00            
ATOM    613  OE1 GLU B  22      72.365 -21.141  55.381  1.00            
ATOM    614  OE2 GLU B  22      71.254 -22.121  53.770  1.00            
ATOM    615  N   VAL B  23      68.429 -20.033  59.212  1.00            
ATOM    616  CA  VAL B  23      68.375 -19.645  60.622  1.00            
ATOM    617  C   VAL B  23      68.218 -20.887  61.491  1.00            
ATOM    618  O   VAL B  23      68.915 -21.029  62.491  1.00            
ATOM    619  CB  VAL B  23      67.262 -18.636  60.911  1.00            
ATOM    620  CG1 VAL B  23      66.950 -18.565  62.408  1.00            
ATOM    621  CG2 VAL B  23      67.655 -17.288  60.384  1.00            
ATOM    622  N   SER B  24      67.383 -21.826  61.053  1.00            
ATOM    623  CA  SER B  24      67.161 -23.059  61.810  1.00            
ATOM    624  C   SER B  24      68.422 -23.903  62.009  1.00            
ATOM    625  O   SER B  24      68.629 -24.451  63.097  1.00            
ATOM    626  CB  SER B  24      66.087 -23.913  61.141  1.00            
ATOM    627  OG  SER B  24      64.837 -23.262  61.196  1.00            
ATOM    628  N   GLU B  25      69.257 -24.043  60.981  1.00            
ATOM    629  CA  GLU B  25      70.502 -24.779  61.171  1.00            
ATOM    630  C   GLU B  25      71.447 -24.011  62.111  1.00            
ATOM    631  O   GLU B  25      72.180 -24.624  62.889  1.00            
ATOM    632  CB  GLU B  25      71.208 -25.055  59.853  1.00            
ATOM    633  CG  GLU B  25      71.760 -23.813  59.221  1.00            
ATOM    634  CD  GLU B  25      72.321 -24.064  57.854  1.00            
ATOM    635  OE1 GLU B  25      72.536 -25.245  57.494  1.00            
ATOM    636  OE2 GLU B  25      72.554 -23.074  57.140  1.00            
ATOM    637  N   ALA B  26      71.464 -22.683  61.994  1.00            
ATOM    638  CA  ALA B  26      72.320 -21.842  62.828  1.00            
ATOM    639  C   ALA B  26      71.962 -21.984  64.298  1.00            
ATOM    640  O   ALA B  26      72.839 -22.055  65.150  1.00            
ATOM    641  CB  ALA B  26      72.227 -20.375  62.394  1.00            
ATOM    642  N   ILE B  27      70.666 -22.002  64.591  1.00            
ATOM    643  CA  ILE B  27      70.210 -22.191  65.949  1.00            
ATOM    644  C   ILE B  27      70.586 -23.585  66.454  1.00            
ATOM    645  O   ILE B  27      71.117 -23.735  67.555  1.00            
ATOM    646  CB  ILE B  27      68.673 -22.016  66.079  1.00            
ATOM    647  CG1 ILE B  27      68.245 -20.587  65.736  1.00            
ATOM    648  CG2 ILE B  27      68.198 -22.422  67.485  1.00            
ATOM    649  CD1 ILE B  27      66.730 -20.397  65.711  1.00            
ATOM    650  N   SER B  28      70.316 -24.592  65.628  1.00            
ATOM    651  CA  SER B  28      70.583 -25.988  65.964  1.00            
ATOM    652  C   SER B  28      72.053 -26.281  66.267  1.00            
ATOM    653  O   SER B  28      72.384 -26.968  67.246  1.00            
ATOM    654  CB  SER B  28      70.105 -26.886  64.826  1.00            
ATOM    655  OG  SER B  28      70.334 -28.244  65.142  1.00            
ATOM    656  N   ARG B  29      72.926 -25.782  65.403  1.00            
ATOM    657  CA  ARG B  29      74.358 -25.973  65.557  1.00            
ATOM    658  C   ARG B  29      74.935 -25.239  66.760  1.00            
ATOM    659  O   ARG B  29      75.779 -25.774  67.489  1.00            
ATOM    660  CB  ARG B  29      75.080 -25.538  64.299  1.00            
ATOM    661  CG  ARG B  29      74.846 -26.511  63.197  1.00            
ATOM    662  CD  ARG B  29      75.733 -26.259  62.022  1.00            
ATOM    663  NE  ARG B  29      77.123 -26.312  62.471  1.00            
ATOM    664  CZ  ARG B  29      77.792 -27.436  62.712  1.00            
ATOM    665  NH1 ARG B  29      77.159 -28.596  62.650  1.00            
ATOM    666  NH2 ARG B  29      79.059 -27.399  63.112  1.00            
ATOM    667  N   SER B  30      74.490 -24.004  66.942  1.00            
ATOM    668  CA  SER B  30      74.991 -23.150  68.017  1.00            
ATOM    669  C   SER B  30      74.644 -23.681  69.400  1.00            
ATOM    670  O   SER B  30      75.427 -23.553  70.346  1.00            
ATOM    671  CB  SER B  30      74.428 -21.740  67.867  1.00            
ATOM    672  OG  SER B  30      74.882 -21.142  66.670  1.00            
ATOM    673  N   LEU B  31      73.474 -24.297  69.511  1.00            
ATOM    674  CA  LEU B  31      72.942 -24.691  70.807  1.00            
ATOM    675  C   LEU B  31      73.009 -26.187  71.090  1.00            
ATOM    676  O   LEU B  31      72.628 -26.627  72.178  1.00            
ATOM    677  CB  LEU B  31      71.489 -24.221  70.916  1.00            
ATOM    678  CG  LEU B  31      71.310 -22.711  70.753  1.00            
ATOM    679  CD1 LEU B  31      69.867 -22.332  70.987  1.00            
ATOM    680  CD2 LEU B  31      72.264 -21.953  71.692  1.00            
ATOM    681  N   ASP B  32      73.518 -26.955  70.129  1.00            
ATOM    682  CA  ASP B  32      73.510 -28.418  70.199  1.00            
ATOM    683  C   ASP B  32      72.102 -28.929  70.483  1.00            
ATOM    684  O   ASP B  32      71.899 -29.823  71.307  1.00            
ATOM    685  CB  ASP B  32      74.485 -28.916  71.261  1.00            
ATOM    686  CG  ASP B  32      75.930 -28.738  70.847  1.00            
ATOM    687  OD1 ASP B  32      76.210 -28.781  69.632  1.00            
ATOM    688  OD2 ASP B  32      76.788 -28.561  71.739  1.00            
ATOM    689  N   ALA B  33      71.145 -28.321  69.784  1.00            
ATOM    690  CA  ALA B  33      69.724 -28.643  69.843  1.00            
ATOM    691  C   ALA B  33      69.332 -29.414  68.588  1.00            
ATOM    692  O   ALA B  33      69.930 -29.210  67.541  1.00            
ATOM    693  CB  ALA B  33      68.884 -27.370  69.968  1.00            
ATOM    694  N   PRO B  34      68.365 -30.337  68.710  1.00            
ATOM    695  CA  PRO B  34      67.884 -31.108  67.565  1.00            
ATOM    696  C   PRO B  34      67.301 -30.175  66.510  1.00            
ATOM    697  O   PRO B  34      66.574 -29.268  66.887  1.00            
ATOM    698  CB  PRO B  34      66.777 -31.986  68.161  1.00            
ATOM    699  CG  PRO B  34      67.023 -32.009  69.609  1.00            
ATOM    700  CD  PRO B  34      67.626 -30.677  69.938  1.00            
ATOM    701  N   LEU B  35      67.613 -30.369  65.235  1.00            
ATOM    702  CA  LEU B  35      67.061 -29.495  64.199  1.00            
ATOM    703  C   LEU B  35      65.537 -29.440  64.240  1.00            
ATOM    704  O   LEU B  35      64.930 -28.374  64.141  1.00            
ATOM    705  CB  LEU B  35      67.516 -29.981  62.821  1.00            
ATOM    706  CG  LEU B  35      67.013 -29.211  61.596  1.00            
ATOM    707  CD1 LEU B  35      67.345 -27.719  61.671  1.00            
ATOM    708  CD2 LEU B  35      67.577 -29.852  60.323  1.00            
ATOM    709  N   THR B  36      64.917 -30.592  64.436  1.00            
ATOM    710  CA  THR B  36      63.462 -30.663  64.430  1.00            
ATOM    711  C   THR B  36      62.774 -29.911  65.567  1.00            
ATOM    712  O   THR B  36      61.584 -29.629  65.474  1.00            
ATOM    713  CB  THR B  36      63.006 -32.115  64.447  1.00            
ATOM    714  OG1 THR B  36      63.568 -32.777  65.584  1.00            
ATOM    715  CG2 THR B  36      63.486 -32.803  63.182  1.00            
ATOM    716  N   SER B  37      63.506 -29.562  66.628  1.00            
ATOM    717  CA  SER B  37      62.882 -28.859  67.751  1.00            
ATOM    718  C   SER B  37      62.907 -27.347  67.520  1.00            
ATOM    719  O   SER B  37      62.332 -26.590  68.289  1.00            
ATOM    720  CB  SER B  37      63.574 -29.195  69.079  1.00            
ATOM    721  OG  SER B  37      64.860 -28.606  69.157  1.00            
ATOM    722  N   VAL B  38      63.561 -26.916  66.446  1.00            
ATOM    723  CA  VAL B  38      63.706 -25.498  66.168  1.00            
ATOM    724  C   VAL B  38      62.518 -24.981  65.373  1.00            
ATOM    725  O   VAL B  38      62.207 -25.506  64.299  1.00            
ATOM    726  CB  VAL B  38      64.998 -25.213  65.391  1.00            
ATOM    727  CG1 VAL B  38      65.114 -23.740  65.069  1.00            
ATOM    728  CG2 VAL B  38      66.212 -25.697  66.199  1.00            
ATOM    729  N   ARG B  39      61.876 -23.948  65.904  1.00            
ATOM    730  CA  ARG B  39      60.763 -23.296  65.232  1.00            
ATOM    731  C   ARG B  39      61.075 -21.845  64.880  1.00            
ATOM    732  O   ARG B  39      61.713 -21.114  65.653  1.00            
ATOM    733  CB  ARG B  39      59.496 -23.366  66.087  1.00            
ATOM    734  CG  ARG B  39      58.763 -24.675  65.961  1.00            
ATOM    735  CD  ARG B  39      57.777 -24.901  67.081  1.00            
ATOM    736  NE  ARG B  39      56.910 -26.050  66.808  1.00            
ATOM    737  CZ  ARG B  39      57.294 -27.321  66.834  1.00            
ATOM    738  NH1 ARG B  39      58.548 -27.639  67.116  1.00            
ATOM    739  NH2 ARG B  39      56.417 -28.278  66.569  1.00            
ATOM    740  N   VAL B  40      60.650 -21.445  63.685  1.00            
ATOM    741  CA  VAL B  40      60.889 -20.094  63.197  1.00            
ATOM    742  C   VAL B  40      59.600 -19.463  62.685  1.00            
ATOM    743  O   VAL B  40      58.908 -20.042  61.841  1.00            
ATOM    744  CB  VAL B  40      61.935 -20.084  62.067  1.00            
ATOM    745  CG1 VAL B  40      62.132 -18.669  61.544  1.00            
ATOM    746  CG2 VAL B  40      63.260 -20.642  62.579  1.00            
ATOM    747  N   ILE B  41      59.312 -18.269  63.201  1.00            
ATOM    748  CA  ILE B  41      58.180 -17.448  62.797  1.00            
ATOM    749  C   ILE B  41      58.690 -16.215  62.075  1.00            
ATOM    750  O   ILE B  41      59.465 -15.424  62.631  1.00            
ATOM    751  CB  ILE B  41      57.336 -16.984  64.011  1.00            
ATOM    752  CG1 ILE B  41      56.760 -18.188  64.760  1.00            
ATOM    753  CG2 ILE B  41      56.234 -16.041  63.565  1.00            
ATOM    754  CD1 ILE B  41      56.152 -17.848  66.094  1.00            
ATOM    755  N   ILE B  42      58.251 -16.041  60.840  1.00            
ATOM    756  CA  ILE B  42      58.573 -14.837  60.094  1.00            
ATOM    757  C   ILE B  42      57.434 -13.848  60.186  1.00            
ATOM    758  O   ILE B  42      56.298 -14.165  59.837  1.00            
ATOM    759  CB  ILE B  42      58.841 -15.136  58.605  1.00            
ATOM    760  CG1 ILE B  42      60.024 -16.083  58.466  1.00            
ATOM    761  CG2 ILE B  42      59.093 -13.845  57.847  1.00            
ATOM    762  CD1 ILE B  42      60.363 -16.390  57.055  1.00            
ATOM    763  N   THR B  43      57.738 -12.635  60.619  1.00            
ATOM    764  CA  THR B  43      56.710 -11.614  60.669  1.00            
ATOM    765  C   THR B  43      57.104 -10.499  59.720  1.00            
ATOM    766  O   THR B  43      58.164  -9.880  59.866  1.00            
ATOM    767  CB  THR B  43      56.514 -11.045  62.108  1.00            
ATOM    768  OG1 THR B  43      56.339 -12.123  63.036  1.00            
ATOM    769  CG2 THR B  43      55.294 -10.121  62.161  1.00            
ATOM    770  N   GLU B  44      56.292 -10.281  58.695  1.00            
ATOM    771  CA  GLU B  44      56.596  -9.211  57.763  1.00            
ATOM    772  C   GLU B  44      56.088  -7.867  58.261  1.00            
ATOM    773  O   GLU B  44      54.964  -7.756  58.745  1.00            
ATOM    774  CB  GLU B  44      56.019  -9.516  56.382  1.00            
ATOM    775  CG  GLU B  44      56.775 -10.592  55.637  1.00            
ATOM    776  CD  GLU B  44      56.285 -10.736  54.203  1.00            
ATOM    777  OE1 GLU B  44      55.053 -10.779  53.992  1.00            
ATOM    778  OE2 GLU B  44      57.128 -10.769  53.292  1.00            
ATOM    779  N   MET B  45      56.905  -6.835  58.099  1.00            
ATOM    780  CA  MET B  45      56.481  -5.484  58.456  1.00            
ATOM    781  C   MET B  45      56.259  -4.655  57.199  1.00            
ATOM    782  O   MET B  45      57.121  -4.637  56.317  1.00            
ATOM    783  CB  MET B  45      57.524  -4.792  59.337  1.00            
ATOM    784  CG  MET B  45      57.921  -5.562  60.581  1.00            
ATOM    785  SD  MET B  45      59.214  -4.669  61.514  1.00            
ATOM    786  CE  MET B  45      60.667  -4.897  60.484  1.00            
ATOM    787  N   ALA B  46      55.117  -3.977  57.101  1.00            
ATOM    788  CA  ALA B  46      54.925  -3.022  56.004  1.00            
ATOM    789  C   ALA B  46      55.857  -1.835  56.225  1.00            
ATOM    790  O   ALA B  46      56.202  -1.531  57.368  1.00            
ATOM    791  CB  ALA B  46      53.490  -2.568  55.921  1.00            
ATOM    792  N   LYS B  47      56.239  -1.168  55.157  1.00            
ATOM    793  CA  LYS B  47      57.179  -0.066  55.230  1.00            
ATOM    794  C   LYS B  47      56.717   1.079  56.136  1.00            
ATOM    795  O   LYS B  47      57.519   1.746  56.699  1.00            
ATOM    796  CB  LYS B  47      57.450   0.494  53.839  1.00            
ATOM    797  CG  LYS B  47      58.681  -0.035  53.119  1.00            
ATOM    798  CD  LYS B  47      58.410  -0.217  51.631  1.00            
ATOM    799  CE  LYS B  47      59.682  -0.519  50.838  1.00            
ATOM    800  NZ  LYS B  47      59.618  -1.849  50.174  1.00            
ATOM    801  N   GLY B  48      55.415   1.282  56.244  1.00            
ATOM    802  CA  GLY B  48      54.884   2.332  57.096  1.00            
ATOM    803  C   GLY B  48      54.756   1.929  58.560  1.00            
ATOM    804  O   GLY B  48      54.259   2.711  59.376  1.00            
ATOM    805  N   HIS B  49      55.226   0.731  58.894  1.00            
ATOM    806  CA  HIS B  49      55.068   0.181  60.251  1.00            
ATOM    807  C   HIS B  49      56.391  -0.035  60.978  1.00            
ATOM    808  O   HIS B  49      56.414  -0.518  62.117  1.00            
ATOM    809  CB  HIS B  49      54.325  -1.158  60.204  1.00            
ATOM    810  CG  HIS B  49      52.884  -1.041  59.814  1.00            
ATOM    811  ND1 HIS B  49      52.082  -2.140  59.601  1.00            
ATOM    812  CD2 HIS B  49      52.102   0.044  59.594  1.00            
ATOM    813  CE1 HIS B  49      50.868  -1.737  59.261  1.00            
ATOM    814  NE2 HIS B  49      50.855  -0.418  59.248  1.00            
ATOM    815  N   PHE B  50      57.492   0.319  60.329  1.00            
ATOM    816  CA  PHE B  50      58.804   0.128  60.936  1.00            
ATOM    817  C   PHE B  50      59.608   1.412  60.939  1.00            
ATOM    818  O   PHE B  50      59.933   1.961  59.879  1.00            
ATOM    819  CB  PHE B  50      59.584  -0.957  60.211  1.00            
ATOM    820  CG  PHE B  50      60.924  -1.247  60.830  1.00            
ATOM    821  CD1 PHE B  50      61.028  -1.514  62.185  1.00            
ATOM    822  CD2 PHE B  50      62.073  -1.243  60.061  1.00            
ATOM    823  CE1 PHE B  50      62.257  -1.789  62.760  1.00            
ATOM    824  CE2 PHE B  50      63.301  -1.525  60.625  1.00            
ATOM    825  CZ  PHE B  50      63.397  -1.787  61.983  1.00            
ATOM    826  N   GLY B  51      59.953   1.877  62.134  1.00            
ATOM    827  CA  GLY B  51      60.681   3.118  62.279  1.00            
ATOM    828  C   GLY B  51      62.090   2.949  62.810  1.00            
ATOM    829  O   GLY B  51      62.350   2.144  63.705  1.00            
ATOM    830  N   ILE B  52      63.012   3.721  62.253  1.00            
ATOM    831  CA  ILE B  52      64.359   3.789  62.802  1.00            
ATOM    832  C   ILE B  52      64.654   5.237  63.079  1.00            
ATOM    833  O   ILE B  52      64.556   6.072  62.182  1.00            
ATOM    834  CB  ILE B  52      65.427   3.226  61.845  1.00            
ATOM    835  CG1 ILE B  52      65.132   1.772  61.510  1.00            
ATOM    836  CG2 ILE B  52      66.815   3.359  62.453  1.00            
ATOM    837  CD1 ILE B  52      64.614   1.598  60.102  1.00            
ATOM    838  N   GLY B  53      65.000   5.553  64.321  1.00            
ATOM    839  CA  GLY B  53      65.276   6.936  64.654  1.00            
ATOM    840  C   GLY B  53      64.077   7.850  64.501  1.00            
ATOM    841  O   GLY B  53      64.225   9.023  64.201  1.00            
ATOM    842  N   GLY B  54      62.883   7.293  64.641  1.00            
ATOM    843  CA  GLY B  54      61.646   8.052  64.589  1.00            
ATOM    844  C   GLY B  54      61.092   8.274  63.193  1.00            
ATOM    845  O   GLY B  54      59.998   8.808  63.025  1.00            
ATOM    846  N   GLU B  55      61.855   7.877  62.185  1.00            
ATOM    847  CA  GLU B  55      61.408   7.978  60.792  1.00            
ATOM    848  C   GLU B  55      61.349   6.600  60.134  1.00            
ATOM    849  O   GLU B  55      62.025   5.674  60.569  1.00            
ATOM    850  CB  GLU B  55      62.309   8.920  59.988  1.00            
ATOM    851  CG  GLU B  55      62.273  10.397  60.421  1.00            
ATOM    852  CD  GLU B  55      60.889  11.041  60.257  1.00            
ATOM    853  OE1 GLU B  55      60.206  10.757  59.249  1.00            
ATOM    854  OE2 GLU B  55      60.485  11.841  61.130  1.00            
ATOM    855  N   LEU B  56      60.515   6.448  59.108  1.00            
ATOM    856  CA  LEU B  56      60.436   5.183  58.392  1.00            
ATOM    857  C   LEU B  56      61.764   4.872  57.695  1.00            
ATOM    858  O   LEU B  56      62.369   5.738  57.056  1.00            
ATOM    859  CB  LEU B  56      59.281   5.194  57.371  1.00            
ATOM    860  CG  LEU B  56      57.793   5.324  57.778  1.00            
ATOM    861  CD1 LEU B  56      57.549   5.792  59.221  1.00            
ATOM    862  CD2 LEU B  56      56.998   6.191  56.790  1.00            
TER     863      LEU B  56                                                      
ATOM    864  N   PRO C   1      45.979   0.320  73.335  1.00            
ATOM    865  CA  PRO C   1      47.298  -0.020  72.783  1.00            
ATOM    866  C   PRO C   1      48.196  -0.723  73.784  1.00            
ATOM    867  O   PRO C   1      48.136  -0.433  74.977  1.00            
ATOM    868  CB  PRO C   1      47.892   1.335  72.393  1.00            
ATOM    869  CG  PRO C   1      46.721   2.221  72.175  1.00            
ATOM    870  CD  PRO C   1      45.588   1.708  73.032  1.00            
ATOM    871  N   ILE C   2      49.014  -1.643  73.285  1.00            
ATOM    872  CA  ILE C   2      49.948  -2.393  74.115  1.00            
ATOM    873  C   ILE C   2      51.367  -2.222  73.593  1.00            
ATOM    874  O   ILE C   2      51.681  -2.592  72.459  1.00            
ATOM    875  CB  ILE C   2      49.578  -3.876  74.159  1.00            
ATOM    876  CG1 ILE C   2      48.213  -4.030  74.828  1.00            
ATOM    877  CG2 ILE C   2      50.618  -4.655  74.925  1.00            
ATOM    878  CD1 ILE C   2      47.586  -5.397  74.669  1.00            
ATOM    879  N   ALA C   3      52.238  -1.682  74.441  1.00            
ATOM    880  CA  ALA C   3      53.591  -1.453  74.011  1.00            
ATOM    881  C   ALA C   3      54.576  -2.374  74.728  1.00            
ATOM    882  O   ALA C   3      54.568  -2.446  75.956  1.00            
ATOM    883  CB  ALA C   3      53.935  -0.025  74.231  1.00            
ATOM    884  N   GLN C   4      55.390  -3.113  73.967  1.00            
ATOM    885  CA  GLN C   4      56.482  -3.868  74.587  1.00            
ATOM    886  C   GLN C   4      57.826  -3.299  74.152  1.00            
ATOM    887  O   GLN C   4      58.147  -3.256  72.963  1.00            
ATOM    888  CB  GLN C   4      56.408  -5.365  74.267  1.00            
ATOM    889  CG  GLN C   4      57.468  -6.176  75.038  1.00            
ATOM    890  CD  GLN C   4      57.393  -7.670  74.790  1.00            
ATOM    891  OE1 GLN C   4      58.085  -8.464  75.445  1.00            
ATOM    892  NE2 GLN C   4      56.555  -8.065  73.844  1.00            
ATOM    893  N   ILE C   5      58.613  -2.879  75.132  1.00            
ATOM    894  CA  ILE C   5      59.892  -2.233  74.886  1.00            
ATOM    895  C   ILE C   5      61.038  -3.067  75.451  1.00            
ATOM    896  O   ILE C   5      61.099  -3.311  76.663  1.00            
ATOM    897  CB  ILE C   5      59.910  -0.814  75.515  1.00            
ATOM    898  CG1 ILE C   5      58.627  -0.050  75.143  1.00            
ATOM    899  CG2 ILE C   5      61.159  -0.031  75.103  1.00            
ATOM    900  CD1 ILE C   5      58.542   1.336  75.759  1.00            
ATOM    901  N   HIS C   6      61.923  -3.519  74.567  1.00            
ATOM    902  CA  HIS C   6      63.150  -4.215  74.956  1.00            
ATOM    903  C   HIS C   6      64.288  -3.223  75.181  1.00            
ATOM    904  O   HIS C   6      64.602  -2.421  74.312  1.00            
ATOM    905  CB  HIS C   6      63.567  -5.250  73.894  1.00            
ATOM    906  CG  HIS C   6      62.759  -6.509  73.921  1.00            
ATOM    907  ND1 HIS C   6      61.522  -6.622  73.322  1.00            
ATOM    908  CD2 HIS C   6      63.015  -7.714  74.483  1.00            
ATOM    909  CE1 HIS C   6      61.048  -7.838  73.519  1.00            
ATOM    910  NE2 HIS C   6      61.936  -8.521  74.219  1.00            
ATOM    911  N   ILE C   7      64.870  -3.235  76.377  1.00            
ATOM    912  CA  ILE C   7      66.013  -2.369  76.678  1.00            
ATOM    913  C   ILE C   7      67.109  -3.151  77.407  1.00            
ATOM    914  O   ILE C   7      66.833  -4.156  78.048  1.00            
ATOM    915  CB  ILE C   7      65.608  -1.168  77.533  1.00            
ATOM    916  CG1 ILE C   7      65.071  -1.641  78.885  1.00            
ATOM    917  CG2 ILE C   7      64.544  -0.338  76.852  1.00            
ATOM    918  CD1 ILE C   7      64.772  -0.484  79.861  1.00            
ATOM    919  N   LEU C   8      68.347  -2.690  77.322  1.00            
ATOM    920  CA  LEU C   8      69.418  -3.357  78.033  1.00            
ATOM    921  C   LEU C   8      69.249  -3.110  79.524  1.00            
ATOM    922  O   LEU C   8      68.863  -2.033  79.903  1.00            
ATOM    923  CB  LEU C   8      70.781  -2.844  77.565  1.00            
ATOM    924  CG  LEU C   8      71.331  -3.349  76.235  1.00            
ATOM    925  CD1 LEU C   8      72.529  -2.493  75.836  1.00            
ATOM    926  CD2 LEU C   8      71.720  -4.806  76.383  1.00            
ATOM    927  N   GLU C   9      69.581  -4.082  80.366  1.00            
ATOM    928  CA  GLU C   9      69.531  -3.883  81.820  1.00            
ATOM    929  C   GLU C   9      70.473  -2.764  82.190  1.00            
ATOM    930  O   GLU C   9      71.428  -2.483  81.472  1.00            
ATOM    931  CB  GLU C   9      69.928  -5.138  82.610  1.00            
ATOM    932  CG  GLU C   9      71.387  -5.466  82.600  1.00            
ATOM    933  CD  GLU C   9      71.732  -6.727  83.367  1.00            
ATOM    934  OE1 GLU C   9      70.827  -7.193  84.067  1.00            
ATOM    935  OE2 GLU C   9      72.877  -7.254  83.268  1.00            
ATOM    936  N   GLY C  10      70.238  -2.149  83.338  1.00            
ATOM    937  CA  GLY C  10      71.153  -1.131  83.799  1.00            
ATOM    938  C   GLY C  10      70.490   0.206  84.067  1.00            
ATOM    939  O   GLY C  10      71.130   1.115  84.590  1.00            
ATOM    940  N   ARG C  11      69.221   0.374  83.720  1.00            
ATOM    941  CA  ARG C  11      68.527   1.596  84.019  1.00            
ATOM    942  C   ARG C  11      68.009   1.593  85.421  1.00            
ATOM    943  O   ARG C  11      67.725   0.589  85.949  1.00            
ATOM    944  CB  ARG C  11      67.360   1.811  83.065  1.00            
ATOM    945  CG  ARG C  11      67.766   1.973  81.625  1.00            
ATOM    946  CD  ARG C  11      68.701   3.111  81.484  1.00            
ATOM    947  NE  ARG C  11      70.023   2.610  81.471  1.00            
ATOM    948  CZ  ARG C  11      71.079   3.176  82.029  1.00            
ATOM    949  NH1 ARG C  11      71.032   4.335  82.681  1.00            
ATOM    950  NH2 ARG C  11      72.215   2.526  81.896  1.00            
ATOM    951  N   SER C  12      67.830   2.760  85.983  1.00            
ATOM    952  CA  SER C  12      67.287   2.895  87.328  1.00            
ATOM    953  C   SER C  12      65.781   2.671  87.288  1.00            
ATOM    954  O   SER C  12      65.164   2.716  86.205  1.00            
ATOM    955  CB  SER C  12      67.591   4.275  87.899  1.00            
ATOM    956  OG  SER C  12      66.883   5.274  87.188  1.00            
ATOM    957  N   ASP C  13      65.195   2.425  88.459  1.00            
ATOM    958  CA  ASP C  13      63.751   2.245  88.568  1.00            
ATOM    959  C   ASP C  13      63.041   3.515  88.141  1.00            
ATOM    960  O   ASP C  13      62.003   3.461  87.480  1.00            
ATOM    961  CB  ASP C  13      63.346   1.845  89.985  1.00            
ATOM    962  CG  ASP C  13      63.631   0.374  90.277  1.00            
ATOM    963  OD1 ASP C  13      64.086  -0.331  89.355  1.00            
ATOM    964  OD2 ASP C  13      63.426  -0.076  91.428  1.00            
ATOM    965  N   GLU C  14      63.624   4.650  88.513  1.00            
ATOM    966  CA  GLU C  14      63.078   5.967  88.202  1.00            
ATOM    967  C   GLU C  14      63.076   6.186  86.691  1.00            
ATOM    968  O   GLU C  14      62.125   6.703  86.088  1.00            
ATOM    969  CB  GLU C  14      63.915   7.057  88.893  1.00            
ATOM    970  CG  GLU C  14      63.834   7.027  90.410  1.00            
ATOM    971  CD  GLU C  14      64.807   6.040  91.059  1.00            
ATOM    972  OE1 GLU C  14      65.623   5.406  90.349  1.00            
ATOM    973  OE2 GLU C  14      64.701   5.858  92.289  1.00            
ATOM    974  N   GLN C  15      64.170   5.774  86.078  1.00            
ATOM    975  CA  GLN C  15      64.343   5.898  84.654  1.00            
ATOM    976  C   GLN C  15      63.295   5.066  83.900  1.00            
ATOM    977  O   GLN C  15      62.703   5.559  82.950  1.00            
ATOM    978  CB  GLN C  15      65.769   5.483  84.298  1.00            
ATOM    979  CG  GLN C  15      66.752   6.618  84.220  1.00            
ATOM    980  CD  GLN C  15      68.186   6.123  84.088  1.00            
ATOM    981  OE1 GLN C  15      68.444   4.918  84.101  1.00            
ATOM    982  NE2 GLN C  15      69.123   7.054  83.944  1.00            
ATOM    983  N   LYS C  16      63.010   3.853  84.371  1.00            
ATOM    984  CA  LYS C  16      62.010   2.993  83.731  1.00            
ATOM    985  C   LYS C  16      60.581   3.498  83.960  1.00            
ATOM    986  O   LYS C  16      59.727   3.361  83.074  1.00            
ATOM    987  CB  LYS C  16      62.157   1.555  84.215  1.00            
ATOM    988  CG  LYS C  16      63.407   0.909  83.681  1.00            
ATOM    989  CD  LYS C  16      63.526  -0.518  84.123  1.00            
ATOM    990  CE  LYS C  16      64.340  -0.614  85.428  1.00            
ATOM    991  NZ  LYS C  16      64.614  -2.037  85.757  1.00            
ATOM    992  N   GLU C  17      60.329   4.092  85.133  1.00            
ATOM    993  CA  GLU C  17      59.030   4.723  85.417  1.00            
ATOM    994  C   GLU C  17      58.784   5.887  84.463  1.00            
ATOM    995  O   GLU C  17      57.674   6.081  83.979  1.00            
ATOM    996  CB  GLU C  17      58.945   5.246  86.862  1.00            
ATOM    997  CG  GLU C  17      58.950   4.191  87.949  1.00            
ATOM    998  CD  GLU C  17      58.905   4.786  89.356  1.00            
ATOM    999  OE1 GLU C  17      58.874   4.003  90.327  1.00            
ATOM   1000  OE2 GLU C  17      58.942   6.032  89.497  1.00            
ATOM   1001  N   THR C  18      59.825   6.674  84.221  1.00            
ATOM   1002  CA  THR C  18      59.738   7.802  83.308  1.00            
ATOM   1003  C   THR C  18      59.464   7.329  81.881  1.00            
ATOM   1004  O   THR C  18      58.620   7.896  81.192  1.00            
ATOM   1005  CB  THR C  18      61.014   8.638  83.359  1.00            
ATOM   1006  OG1 THR C  18      61.168   9.167  84.685  1.00            
ATOM   1007  CG2 THR C  18      60.935   9.776  82.369  1.00            
ATOM   1008  N   LEU C  19      60.155   6.269  81.465  1.00            
ATOM   1009  CA  LEU C  19      59.938   5.655  80.154  1.00            
ATOM   1010  C   LEU C  19      58.494   5.221  79.968  1.00            
ATOM   1011  O   LEU C  19      57.866   5.514  78.936  1.00            
ATOM   1012  CB  LEU C  19      60.848   4.444  79.984  1.00            
ATOM   1013  CG  LEU C  19      60.630   3.558  78.749  1.00            
ATOM   1014  CD1 LEU C  19      60.955   4.300  77.455  1.00            
ATOM   1015  CD2 LEU C  19      61.456   2.286  78.881  1.00            
ATOM   1016  N   ILE C  20      57.963   4.527  80.966  1.00            
ATOM   1017  CA  ILE C  20      56.590   4.051  80.896  1.00            
ATOM   1018  C   ILE C  20      55.622   5.228  80.799  1.00            
ATOM   1019  O   ILE C  20      54.725   5.222  79.960  1.00            
ATOM   1020  CB  ILE C  20      56.247   3.159  82.106  1.00            
ATOM   1021  CG1 ILE C  20      56.873   1.773  81.931  1.00            
ATOM   1022  CG2 ILE C  20      54.722   3.022  82.305  1.00            
ATOM   1023  CD1 ILE C  20      56.779   0.918  83.190  1.00            
ATOM   1024  N   ARG C  21      55.808   6.249  81.633  1.00            
ATOM   1025  CA  ARG C  21      54.906   7.401  81.576  1.00            
ATOM   1026  C   ARG C  21      55.027   8.142  80.239  1.00            
ATOM   1027  O   ARG C  21      54.018   8.434  79.596  1.00            
ATOM   1028  CB  ARG C  21      55.157   8.345  82.754  1.00            
ATOM   1029  CG  ARG C  21      54.212   9.541  82.793  1.00            
ATOM   1030  CD  ARG C  21      54.517  10.452  83.959  1.00            
ATOM   1031  NE  ARG C  21      55.941  10.746  84.069  1.00            
ATOM   1032  CZ  ARG C  21      56.594  11.608  83.301  1.00            
ATOM   1033  NH1 ARG C  21      57.892  11.806  83.492  1.00            
ATOM   1034  NH2 ARG C  21      55.959  12.257  82.336  1.00            
ATOM   1035  N   GLU C  22      56.254   8.411  79.804  1.00            
ATOM   1036  CA  GLU C  22      56.486   9.167  78.570  1.00            
ATOM   1037  C   GLU C  22      56.006   8.431  77.315  1.00            
ATOM   1038  O   GLU C  22      55.467   9.044  76.386  1.00            
ATOM   1039  CB  GLU C  22      57.978   9.478  78.418  1.00            
ATOM   1040  CG  GLU C  22      58.555  10.432  79.458  1.00            
ATOM   1041  CD  GLU C  22      58.025  11.839  79.310  1.00            
ATOM   1042  OE1 GLU C  22      57.650  12.214  78.175  1.00            
ATOM   1043  OE2 GLU C  22      57.984  12.570  80.325  1.00            
ATOM   1044  N   VAL C  23      56.218   7.125  77.272  1.00            
ATOM   1045  CA  VAL C  23      55.773   6.356  76.115  1.00            
ATOM   1046  C   VAL C  23      54.246   6.251  76.079  1.00            
ATOM   1047  O   VAL C  23      53.636   6.355  75.005  1.00            
ATOM   1048  CB  VAL C  23      56.448   4.983  76.074  1.00            
ATOM   1049  CG1 VAL C  23      55.691   4.008  75.183  1.00            
ATOM   1050  CG2 VAL C  23      57.898   5.153  75.604  1.00            
ATOM   1051  N   SER C  24      53.639   6.071  77.251  1.00            
ATOM   1052  CA  SER C  24      52.186   5.988  77.367  1.00            
ATOM   1053  C   SER C  24      51.509   7.265  76.914  1.00            
ATOM   1054  O   SER C  24      50.463   7.214  76.285  1.00            
ATOM   1055  CB  SER C  24      51.765   5.670  78.803  1.00            
ATOM   1056  OG  SER C  24      52.174   4.367  79.166  1.00            
ATOM   1057  N   GLU C  25      52.082   8.405  77.285  1.00            
ATOM   1058  CA  GLU C  25      51.564   9.709  76.878  1.00            
ATOM   1059  C   GLU C  25      51.751   9.952  75.379  1.00            
ATOM   1060  O   GLU C  25      50.893  10.538  74.741  1.00            
ATOM   1061  CB  GLU C  25      52.234  10.818  77.688  1.00            
ATOM   1062  CG  GLU C  25      51.825  10.805  79.156  1.00            
ATOM   1063  CD  GLU C  25      52.546  11.854  79.988  1.00            
ATOM   1064  OE1 GLU C  25      52.132  12.075  81.148  1.00            
ATOM   1065  OE2 GLU C  25      53.531  12.445  79.490  1.00            
ATOM   1066  N   ALA C  26      52.896   9.542  74.844  1.00            
ATOM   1067  CA  ALA C  26      53.176   9.669  73.419  1.00            
ATOM   1068  C   ALA C  26      52.173   8.848  72.608  1.00            
ATOM   1069  O   ALA C  26      51.653   9.312  71.580  1.00            
ATOM   1070  CB  ALA C  26      54.616   9.240  73.109  1.00            
ATOM   1071  N   ILE C  27      51.883   7.638  73.071  1.00            
ATOM   1072  CA  ILE C  27      50.884   6.811  72.394  1.00            
ATOM   1073  C   ILE C  27      49.494   7.439  72.480  1.00            
ATOM   1074  O   ILE C  27      48.745   7.472  71.498  1.00            
ATOM   1075  CB  ILE C  27      50.832   5.388  72.965  1.00            
ATOM   1076  CG1 ILE C  27      52.113   4.634  72.610  1.00            
ATOM   1077  CG2 ILE C  27      49.618   4.618  72.424  1.00            
ATOM   1078  CD1 ILE C  27      52.191   3.279  73.255  1.00            
ATOM   1079  N   SER C  28      49.153   7.908  73.672  1.00            
ATOM   1080  CA  SER C  28      47.873   8.548  73.917  1.00            
ATOM   1081  C   SER C  28      47.677   9.774  73.035  1.00            
ATOM   1082  O   SER C  28      46.624   9.916  72.412  1.00            
ATOM   1083  CB  SER C  28      47.747   8.938  75.393  1.00            
ATOM   1084  OG  SER C  28      46.492   9.532  75.656  1.00            
ATOM   1085  N   ARG C  29      48.671  10.662  72.971  1.00            
ATOM   1086  CA  ARG C  29      48.522  11.851  72.125  1.00            
ATOM   1087  C   ARG C  29      48.488  11.482  70.636  1.00            
ATOM   1088  O   ARG C  29      47.676  12.014  69.887  1.00            
ATOM   1089  CB  ARG C  29      49.613  12.900  72.395  1.00            
ATOM   1090  CG  ARG C  29      51.043  12.497  72.098  1.00            
ATOM   1091  CD  ARG C  29      51.972  13.687  72.312  1.00            
ATOM   1092  NE  ARG C  29      53.383  13.338  72.158  1.00            
ATOM   1093  CZ  ARG C  29      54.173  12.979  73.165  1.00            
ATOM   1094  NH1 ARG C  29      53.697  12.957  74.404  1.00            
ATOM   1095  NH2 ARG C  29      55.447  12.677  72.943  1.00            
ATOM   1096  N   SER C  30      49.361  10.577  70.203  1.00            
ATOM   1097  CA  SER C  30      49.424  10.220  68.781  1.00            
ATOM   1098  C   SER C  30      48.154   9.570  68.254  1.00            
ATOM   1099  O   SER C  30      47.805   9.734  67.088  1.00            
ATOM   1100  CB  SER C  30      50.599   9.280  68.500  1.00            
ATOM   1101  OG  SER C  30      51.835   9.930  68.703  1.00            
ATOM   1102  N   LEU C  31      47.465   8.816  69.099  1.00            
ATOM   1103  CA  LEU C  31      46.338   8.034  68.621  1.00            
ATOM   1104  C   LEU C  31      44.989   8.598  69.031  1.00            
ATOM   1105  O   LEU C  31      43.959   8.100  68.585  1.00            
ATOM   1106  CB  LEU C  31      46.462   6.600  69.136  1.00            
ATOM   1107  CG  LEU C  31      47.740   5.899  68.689  1.00            
ATOM   1108  CD1 LEU C  31      47.761   4.477  69.189  1.00            
ATOM   1109  CD2 LEU C  31      47.816   5.909  67.170  1.00            
ATOM   1110  N   ASP C  32      45.003   9.673  69.818  1.00            
ATOM   1111  CA  ASP C  32      43.783  10.198  70.429  1.00            
ATOM   1112  C   ASP C  32      43.062   9.064  71.154  1.00            
ATOM   1113  O   ASP C  32      41.842   8.921  71.063  1.00            
ATOM   1114  CB  ASP C  32      42.865  10.841  69.381  1.00            
ATOM   1115  CG  ASP C  32      43.390  12.175  68.885  1.00            
ATOM   1116  OD1 ASP C  32      44.070  12.873  69.670  1.00            
ATOM   1117  OD2 ASP C  32      43.119  12.529  67.713  1.00            
ATOM   1118  N   ALA C  33      43.843   8.247  71.852  1.00            
ATOM   1119  CA  ALA C  33      43.313   7.132  72.620  1.00            
ATOM   1120  C   ALA C  33      43.374   7.495  74.085  1.00            
ATOM   1121  O   ALA C  33      44.338   8.128  74.512  1.00            
ATOM   1122  CB  ALA C  33      44.103   5.871  72.348  1.00            
ATOM   1123  N   PRO C  34      42.363   7.075  74.865  1.00            
ATOM   1124  CA  PRO C  34      42.400   7.407  76.294  1.00            
ATOM   1125  C   PRO C  34      43.660   6.859  76.939  1.00            
ATOM   1126  O   PRO C  34      44.051   5.721  76.682  1.00            
ATOM   1127  CB  PRO C  34      41.128   6.746  76.856  1.00            
ATOM   1128  CG  PRO C  34      40.709   5.740  75.830  1.00            
ATOM   1129  CD  PRO C  34      41.168   6.292  74.502  1.00            
ATOM   1130  N   LEU C  35      44.309   7.692  77.744  1.00            
ATOM   1131  CA  LEU C  35      45.567   7.314  78.359  1.00            
ATOM   1132  C   LEU C  35      45.392   6.018  79.129  1.00            
ATOM   1133  O   LEU C  35      46.236   5.135  79.065  1.00            
ATOM   1134  CB  LEU C  35      46.064   8.436  79.275  1.00            
ATOM   1135  CG  LEU C  35      47.422   8.290  79.970  1.00            
ATOM   1136  CD1 LEU C  35      48.567   8.047  78.991  1.00            
ATOM   1137  CD2 LEU C  35      47.692   9.533  80.822  1.00            
ATOM   1138  N   THR C  36      44.246   5.884  79.788  1.00            
ATOM   1139  CA  THR C  36      43.957   4.731  80.638  1.00            
ATOM   1140  C   THR C  36      43.918   3.381  79.916  1.00            
ATOM   1141  O   THR C  36      43.994   2.338  80.563  1.00            
ATOM   1142  CB  THR C  36      42.612   4.914  81.340  1.00            
ATOM   1143  OG1 THR C  36      41.593   5.121  80.353  1.00            
ATOM   1144  CG2 THR C  36      42.658   6.112  82.267  1.00            
ATOM   1145  N   SER C  37      43.796   3.386  78.591  1.00            
ATOM   1146  CA  SER C  37      43.734   2.127  77.847  1.00            
ATOM   1147  C   SER C  37      45.123   1.667  77.433  1.00            
ATOM   1148  O   SER C  37      45.287   0.567  76.901  1.00            
ATOM   1149  CB  SER C  37      42.868   2.257  76.585  1.00            
ATOM   1150  OG  SER C  37      43.521   3.028  75.579  1.00            
ATOM   1151  N   VAL C  38      46.121   2.510  77.669  1.00            
ATOM   1152  CA  VAL C  38      47.473   2.224  77.204  1.00            
ATOM   1153  C   VAL C  38      48.248   1.391  78.214  1.00            
ATOM   1154  O   VAL C  38      48.387   1.762  79.387  1.00            
ATOM   1155  CB  VAL C  38      48.240   3.530  76.898  1.00            
ATOM   1156  CG1 VAL C  38      49.650   3.233  76.428  1.00            
ATOM   1157  CG2 VAL C  38      47.493   4.349  75.851  1.00            
ATOM   1158  N   ARG C  39      48.769   0.263  77.741  1.00            
ATOM   1159  CA  ARG C  39      49.578  -0.618  78.566  1.00            
ATOM   1160  C   ARG C  39      50.989  -0.693  78.000  1.00            
ATOM   1161  O   ARG C  39      51.173  -0.711  76.784  1.00            
ATOM   1162  CB  ARG C  39      48.956  -2.010  78.647  1.00            
ATOM   1163  CG  ARG C  39      47.821  -2.112  79.623  1.00            
ATOM   1164  CD  ARG C  39      46.938  -3.300  79.324  1.00            
ATOM   1165  NE  ARG C  39      45.979  -3.539  80.398  1.00            
ATOM   1166  CZ  ARG C  39      44.943  -2.760  80.684  1.00            
ATOM   1167  NH1 ARG C  39      44.707  -1.653  79.992  1.00            
ATOM   1168  NH2 ARG C  39      44.143  -3.090  81.679  1.00            
ATOM   1169  N   VAL C  40      51.981  -0.682  78.888  1.00            
ATOM   1170  CA  VAL C  40      53.378  -0.758  78.486  1.00            
ATOM   1171  C   VAL C  40      54.103  -1.854  79.267  1.00            
ATOM   1172  O   VAL C  40      54.007  -1.931  80.512  1.00            
ATOM   1173  CB  VAL C  40      54.090   0.607  78.657  1.00            
ATOM   1174  CG1 VAL C  40      55.594   0.474  78.427  1.00            
ATOM   1175  CG2 VAL C  40      53.477   1.662  77.715  1.00            
ATOM   1176  N   ILE C  41      54.814  -2.716  78.530  1.00            
ATOM   1177  CA  ILE C  41      55.627  -3.769  79.133  1.00            
ATOM   1178  C   ILE C  41      57.106  -3.526  78.869  1.00            
ATOM   1179  O   ILE C  41      57.525  -3.398  77.728  1.00            
ATOM   1180  CB  ILE C  41      55.238  -5.183  78.614  1.00            
ATOM   1181  CG1 ILE C  41      53.806  -5.534  79.014  1.00            
ATOM   1182  CG2 ILE C  41      56.161  -6.268  79.163  1.00            
ATOM   1183  CD1 ILE C  41      53.295  -6.794  78.351  1.00            
ATOM   1184  N   ILE C  42      57.893  -3.436  79.937  1.00            
ATOM   1185  CA  ILE C  42      59.336  -3.330  79.784  1.00            
ATOM   1186  C   ILE C  42      59.985  -4.694  79.939  1.00            
ATOM   1187  O   ILE C  42      59.740  -5.400  80.921  1.00            
ATOM   1188  CB  ILE C  42      59.971  -2.358  80.794  1.00            
ATOM   1189  CG1 ILE C  42      59.433  -0.940  80.616  1.00            
ATOM   1190  CG2 ILE C  42      61.483  -2.332  80.622  1.00            
ATOM   1191  CD1 ILE C  42      60.086   0.045  81.609  1.00            
ATOM   1192  N   THR C  43      60.813  -5.050  78.959  1.00            
ATOM   1193  CA  THR C  43      61.578  -6.290  78.973  1.00            
ATOM   1194  C   THR C  43      63.066  -5.988  78.963  1.00            
ATOM   1195  O   THR C  43      63.584  -5.442  77.994  1.00            
ATOM   1196  CB  THR C  43      61.234  -7.166  77.752  1.00            
ATOM   1197  OG1 THR C  43      59.816  -7.353  77.693  1.00            
ATOM   1198  CG2 THR C  43      61.921  -8.514  77.832  1.00            
ATOM   1199  N   GLU C  44      63.754  -6.328  80.050  1.00            
ATOM   1200  CA  GLU C  44      65.182  -6.065  80.138  1.00            
ATOM   1201  C   GLU C  44      66.015  -7.153  79.478  1.00            
ATOM   1202  O   GLU C  44      65.717  -8.340  79.592  1.00            
ATOM   1203  CB  GLU C  44      65.615  -5.892  81.598  1.00            
ATOM   1204  CG  GLU C  44      65.129  -4.599  82.215  1.00            
ATOM   1205  CD  GLU C  44      65.744  -4.340  83.583  1.00            
ATOM   1206  OE1 GLU C  44      65.800  -5.280  84.411  1.00            
ATOM   1207  OE2 GLU C  44      66.188  -3.197  83.815  1.00            
ATOM   1208  N   MET C  45      67.073  -6.731  78.787  1.00            
ATOM   1209  CA  MET C  45      68.031  -7.659  78.185  1.00            
ATOM   1210  C   MET C  45      69.350  -7.679  78.951  1.00            
ATOM   1211  O   MET C  45      69.953  -6.632  79.214  1.00            
ATOM   1212  CB  MET C  45      68.295  -7.290  76.723  1.00            
ATOM   1213  CG  MET C  45      67.043  -7.264  75.864  1.00            
ATOM   1214  SD  MET C  45      67.368  -6.753  74.161  1.00            
ATOM   1215  CE  MET C  45      67.601  -4.982  74.358  1.00            
ATOM   1216  N   ALA C  46      69.793  -8.884  79.289  1.00            
ATOM   1217  CA  ALA C  46      71.090  -9.084  79.915  1.00            
ATOM   1218  C   ALA C  46      72.177  -8.742  78.918  1.00            
ATOM   1219  O   ALA C  46      71.959  -8.830  77.700  1.00            
ATOM   1220  CB  ALA C  46      71.240 -10.511  80.401  1.00            
ATOM   1221  N   LYS C  47      73.347  -8.358  79.423  1.00            
ATOM   1222  CA  LYS C  47      74.421  -7.904  78.539  1.00            
ATOM   1223  C   LYS C  47      74.840  -8.917  77.470  1.00            
ATOM   1224  O   LYS C  47      75.145  -8.533  76.337  1.00            
ATOM   1225  CB  LYS C  47      75.660  -7.491  79.355  1.00            
ATOM   1226  CG  LYS C  47      75.710  -6.038  79.855  1.00            
ATOM   1227  CD  LYS C  47      74.657  -5.594  80.822  1.00            
ATOM   1228  CE  LYS C  47      74.854  -4.098  81.128  1.00            
ATOM   1229  NZ  LYS C  47      73.844  -3.512  82.013  1.00            
ATOM   1230  N   GLY C  48      74.817 -10.198  77.808  1.00            
ATOM   1231  CA  GLY C  48      75.196 -11.233  76.861  1.00            
ATOM   1232  C   GLY C  48      74.076 -11.681  75.937  1.00            
ATOM   1233  O   GLY C  48      74.253 -12.620  75.166  1.00            
ATOM   1234  N   HIS C  49      72.929 -11.012  75.992  1.00            
ATOM   1235  CA  HIS C  49      71.761 -11.493  75.261  1.00            
ATOM   1236  C   HIS C  49      71.273 -10.586  74.124  1.00            
ATOM   1237  O   HIS C  49      70.215 -10.838  73.552  1.00            
ATOM   1238  CB  HIS C  49      70.605 -11.737  76.238  1.00            
ATOM   1239  CG  HIS C  49      70.822 -12.907  77.141  1.00            
ATOM   1240  ND1 HIS C  49      69.957 -13.224  78.178  1.00            
ATOM   1241  CD2 HIS C  49      71.792 -13.848  77.172  1.00            
ATOM   1242  CE1 HIS C  49      70.395 -14.296  78.800  1.00            
ATOM   1243  NE2 HIS C  49      71.511 -14.700  78.210  1.00            
ATOM   1244  N   PHE C  50      72.008  -9.521  73.823  1.00            
ATOM   1245  CA  PHE C  50      71.593  -8.619  72.756  1.00            
ATOM   1246  C   PHE C  50      72.707  -8.430  71.741  1.00            
ATOM   1247  O   PHE C  50      73.806  -8.015  72.096  1.00            
ATOM   1248  CB  PHE C  50      71.165  -7.262  73.300  1.00            
ATOM   1249  CG  PHE C  50      70.646  -6.335  72.243  1.00            
ATOM   1250  CD1 PHE C  50      69.643  -6.749  71.375  1.00            
ATOM   1251  CD2 PHE C  50      71.173  -5.066  72.091  1.00            
ATOM   1252  CE1 PHE C  50      69.167  -5.903  70.392  1.00            
ATOM   1253  CE2 PHE C  50      70.693  -4.212  71.104  1.00            
ATOM   1254  CZ  PHE C  50      69.690  -4.635  70.258  1.00            
ATOM   1255  N   GLY C  51      72.423  -8.762  70.484  1.00            
ATOM   1256  CA  GLY C  51      73.404  -8.659  69.420  1.00            
ATOM   1257  C   GLY C  51      73.083  -7.608  68.371  1.00            
ATOM   1258  O   GLY C  51      71.926  -7.404  67.989  1.00            
ATOM   1259  N   ILE C  52      74.112  -6.904  67.924  1.00            
ATOM   1260  CA  ILE C  52      73.984  -6.019  66.780  1.00            
ATOM   1261  C   ILE C  52      75.066  -6.378  65.794  1.00            
ATOM   1262  O   ILE C  52      76.233  -6.409  66.155  1.00            
ATOM   1263  CB  ILE C  52      74.123  -4.539  67.138  1.00            
ATOM   1264  CG1 ILE C  52      73.068  -4.112  68.154  1.00            
ATOM   1265  CG2 ILE C  52      74.022  -3.688  65.870  1.00            
ATOM   1266  CD1 ILE C  52      73.299  -2.705  68.696  1.00            
ATOM   1267  N   GLY C  53      74.683  -6.683  64.561  1.00            
ATOM   1268  CA  GLY C  53      75.657  -7.045  63.549  1.00            
ATOM   1269  C   GLY C  53      76.433  -8.307  63.876  1.00            
ATOM   1270  O   GLY C  53      77.578  -8.455  63.454  1.00            
ATOM   1271  N   GLY C  54      75.831  -9.200  64.660  1.00            
ATOM   1272  CA  GLY C  54      76.483 -10.447  65.018  1.00            
ATOM   1273  C   GLY C  54      77.372 -10.356  66.249  1.00            
ATOM   1274  O   GLY C  54      77.923 -11.357  66.694  1.00            
ATOM   1275  N   GLU C  55      77.469  -9.157  66.820  1.00            
ATOM   1276  CA  GLU C  55      78.303  -8.895  67.997  1.00            
ATOM   1277  C   GLU C  55      77.490  -8.520  69.236  1.00            
ATOM   1278  O   GLU C  55      76.416  -7.936  69.123  1.00            
ATOM   1279  CB  GLU C  55      79.290  -7.763  67.674  1.00            
ATOM   1280  CG  GLU C  55      80.245  -7.367  68.803  1.00            
ATOM   1281  CD  GLU C  55      81.180  -6.225  68.421  1.00            
ATOM   1282  OE1 GLU C  55      81.109  -5.752  67.266  1.00            
ATOM   1283  OE2 GLU C  55      81.944  -5.763  69.296  1.00            
ATOM   1284  N   LEU C  56      78.017  -8.827  70.420  1.00            
ATOM   1285  CA  LEU C  56      77.337  -8.470  71.666  1.00            
ATOM   1286  C   LEU C  56      77.206  -6.961  71.821  1.00            
ATOM   1287  O   LEU C  56      78.038  -6.198  71.330  1.00            
ATOM   1288  CB  LEU C  56      78.056  -9.049  72.886  1.00            
ATOM   1289  CG  LEU C  56      78.147 -10.566  73.017  1.00            
ATOM   1290  CD1 LEU C  56      78.878 -10.925  74.300  1.00            
ATOM   1291  CD2 LEU C  56      76.755 -11.171  73.010  1.00            
ATOM   1292  N   ALA C  57      76.136  -6.543  72.486  1.00            
ATOM   1293  CA  ALA C  57      75.882  -5.131  72.743  1.00            
ATOM   1294  C   ALA C  57      76.872  -4.562  73.751  1.00            
ATOM   1295  O   ALA C  57      77.792  -3.825  73.386  1.00            
ATOM   1296  CB  ALA C  57      74.465  -4.944  73.246  1.00            
TER    1297      ALA C  57                                                      
ATOM   1298  N   PRO D   1      67.164   0.553  71.851  1.00            
ATOM   1299  CA  PRO D   1      65.861   0.131  72.372  1.00            
ATOM   1300  C   PRO D   1      64.895  -0.210  71.241  1.00            
ATOM   1301  O   PRO D   1      64.862   0.485  70.226  1.00            
ATOM   1302  CB  PRO D   1      65.382   1.353  73.156  1.00            
ATOM   1303  CG  PRO D   1      66.609   2.084  73.517  1.00            
ATOM   1304  CD  PRO D   1      67.656   1.779  72.500  1.00            
ATOM   1305  N   ILE D   2      64.111  -1.266  71.441  1.00            
ATOM   1306  CA  ILE D   2      63.158  -1.755  70.456  1.00            
ATOM   1307  C   ILE D   2      61.765  -1.839  71.056  1.00            
ATOM   1308  O   ILE D   2      61.545  -2.595  72.006  1.00            
ATOM   1309  CB  ILE D   2      63.538  -3.161  69.965  1.00            
ATOM   1310  CG1 ILE D   2      64.942  -3.154  69.359  1.00            
ATOM   1311  CG2 ILE D   2      62.509  -3.667  68.964  1.00            
ATOM   1312  CD1 ILE D   2      65.523  -4.522  69.154  1.00            
ATOM   1313  N   ALA D   3      60.827  -1.087  70.492  1.00            
ATOM   1314  CA  ALA D   3      59.451  -1.108  70.979  1.00            
ATOM   1315  C   ALA D   3      58.536  -1.736  69.923  1.00            
ATOM   1316  O   ALA D   3      58.583  -1.352  68.749  1.00            
ATOM   1317  CB  ALA D   3      58.974   0.278  71.326  1.00            
ATOM   1318  N   GLN D   4      57.732  -2.712  70.342  1.00            
ATOM   1319  CA  GLN D   4      56.682  -3.249  69.494  1.00            
ATOM   1320  C   GLN D   4      55.330  -2.803  70.055  1.00            
ATOM   1321  O   GLN D   4      55.037  -3.007  71.238  1.00            
ATOM   1322  CB  GLN D   4      56.740  -4.775  69.393  1.00            
ATOM   1323  CG  GLN D   4      55.722  -5.289  68.353  1.00            
ATOM   1324  CD  GLN D   4      55.713  -6.787  68.170  1.00            
ATOM   1325  OE1 GLN D   4      56.371  -7.513  68.905  1.00            
ATOM   1326  NE2 GLN D   4      54.950  -7.264  67.175  1.00            
ATOM   1327  N   ILE D   5      54.526  -2.140  69.225  1.00            
ATOM   1328  CA  ILE D   5      53.254  -1.621  69.702  1.00            
ATOM   1329  C   ILE D   5      52.110  -2.282  68.962  1.00            
ATOM   1330  O   ILE D   5      51.983  -2.103  67.762  1.00            
ATOM   1331  CB  ILE D   5      53.133  -0.087  69.520  1.00            
ATOM   1332  CG1 ILE D   5      54.434   0.612  69.899  1.00            
ATOM   1333  CG2 ILE D   5      51.897   0.466  70.301  1.00            
ATOM   1334  CD1 ILE D   5      54.407   2.107  69.731  1.00            
ATOM   1335  N   HIS D   6      51.266  -3.007  69.682  1.00            
ATOM   1336  CA  HIS D   6      50.068  -3.576  69.084  1.00            
ATOM   1337  C   HIS D   6      48.927  -2.584  69.159  1.00            
ATOM   1338  O   HIS D   6      48.574  -2.136  70.250  1.00            
ATOM   1339  CB  HIS D   6      49.653  -4.884  69.765  1.00            
ATOM   1340  CG  HIS D   6      50.463  -6.075  69.360  1.00            
ATOM   1341  ND1 HIS D   6      51.688  -6.377  69.915  1.00            
ATOM   1342  CD2 HIS D   6      50.213  -7.047  68.449  1.00            
ATOM   1343  CE1 HIS D   6      52.155  -7.485  69.366  1.00            
ATOM   1344  NE2 HIS D   6      51.281  -7.909  68.471  1.00            
ATOM   1345  N   ILE D   7      48.359  -2.234  67.996  1.00            
ATOM   1346  CA  ILE D   7      47.225  -1.326  67.956  1.00            
ATOM   1347  C   ILE D   7      46.127  -1.916  67.069  1.00            
ATOM   1348  O   ILE D   7      46.410  -2.745  66.220  1.00            
ATOM   1349  CB  ILE D   7      47.628   0.070  67.438  1.00            
ATOM   1350  CG1 ILE D   7      48.101  -0.013  65.980  1.00            
ATOM   1351  CG2 ILE D   7      48.747   0.664  68.330  1.00            
ATOM   1352  CD1 ILE D   7      48.345   1.333  65.320  1.00            
ATOM   1353  N   LEU D   8      44.886  -1.509  67.280  1.00            
ATOM   1354  CA  LEU D   8      43.805  -1.988  66.413  1.00            
ATOM   1355  C   LEU D   8      43.927  -1.393  65.016  1.00            
ATOM   1356  O   LEU D   8      44.347  -0.251  64.854  1.00            
ATOM   1357  CB  LEU D   8      42.440  -1.658  67.012  1.00            
ATOM   1358  CG  LEU D   8      42.039  -2.614  68.136  1.00            
ATOM   1359  CD1 LEU D   8      40.843  -2.090  68.920  1.00            
ATOM   1360  CD2 LEU D   8      41.737  -3.979  67.533  1.00            
ATOM   1361  N   GLU D   9      43.572  -2.179  64.001  1.00            
ATOM   1362  CA  GLU D   9      43.608  -1.704  62.624  1.00            
ATOM   1363  C   GLU D   9      42.670  -0.515  62.397  1.00            
ATOM   1364  O   GLU D   9      41.736  -0.287  63.174  1.00            
ATOM   1365  CB  GLU D   9      43.271  -2.846  61.653  1.00            
ATOM   1366  CG  GLU D   9      41.839  -3.342  61.715  1.00            
ATOM   1367  CD  GLU D   9      41.557  -4.464  60.713  1.00            
ATOM   1368  OE1 GLU D   9      42.422  -4.731  59.848  1.00            
ATOM   1369  OE2 GLU D   9      40.467  -5.077  60.793  1.00            
ATOM   1370  N   GLY D  10      42.944   0.265  61.352  1.00            
ATOM   1371  CA  GLY D  10      42.038   1.327  60.961  1.00            
ATOM   1372  C   GLY D  10      42.589   2.730  60.872  1.00            
ATOM   1373  O   GLY D  10      41.925   3.615  60.330  1.00            
ATOM   1374  N   ARG D  11      43.794   2.963  61.357  1.00            
ATOM   1375  CA  ARG D  11      44.385   4.288  61.312  1.00            
ATOM   1376  C   ARG D  11      44.970   4.571  59.951  1.00            
ATOM   1377  O   ARG D  11      45.292   3.705  59.236  1.00            
ATOM   1378  CB  ARG D  11      45.511   4.439  62.332  1.00            
ATOM   1379  CG  ARG D  11      45.206   4.302  63.818  1.00            
ATOM   1380  CD  ARG D  11      43.802   4.554  64.228  1.00            
ATOM   1381  NE  ARG D  11      43.597   4.295  65.643  1.00            
ATOM   1382  CZ  ARG D  11      43.515   5.207  66.599  1.00            
ATOM   1383  NH1 ARG D  11      43.637   6.486  66.329  1.00            
ATOM   1384  NH2 ARG D  11      43.312   4.831  67.853  1.00            
ATOM   1385  N   SER D  12      45.141   5.819  59.635  1.00            
ATOM   1386  CA  SER D  12      45.774   6.185  58.377  1.00            
ATOM   1387  C   SER D  12      47.295   6.001  58.484  1.00            
ATOM   1388  O   SER D  12      47.826   5.900  59.588  1.00            
ATOM   1389  CB  SER D  12      45.422   7.623  58.016  1.00            
ATOM   1390  OG  SER D  12      45.986   8.504  58.971  1.00            
ATOM   1391  N   ASP D  13      47.985   5.966  57.344  1.00            
ATOM   1392  CA  ASP D  13      49.447   5.885  57.318  1.00            
ATOM   1393  C   ASP D  13      50.142   7.059  58.008  1.00            
ATOM   1394  O   ASP D  13      51.170   6.878  58.654  1.00            
ATOM   1395  CB  ASP D  13      49.950   5.803  55.871  1.00            
ATOM   1396  CG  ASP D  13      49.838   4.409  55.281  1.00            
ATOM   1397  OD1 ASP D  13      49.441   3.468  56.008  1.00            
ATOM   1398  OD2 ASP D  13      50.133   4.265  54.071  1.00            
ATOM   1399  N   GLU D  14      49.628   8.272  57.833  1.00            
ATOM   1400  CA  GLU D  14      50.265   9.424  58.480  1.00            
ATOM   1401  C   GLU D  14      50.153   9.392  60.022  1.00            
ATOM   1402  O   GLU D  14      51.105   9.769  60.710  1.00            
ATOM   1403  CB  GLU D  14      49.751  10.747  57.895  1.00            
ATOM   1404  CG  GLU D  14      48.309  11.082  58.135  1.00            
ATOM   1405  CD  GLU D  14      47.392  10.345  57.172  1.00            
ATOM   1406  OE1 GLU D  14      47.878   9.455  56.432  1.00            
ATOM   1407  OE2 GLU D  14      46.182  10.658  57.155  1.00            
ATOM   1408  N   GLN D  15      49.010   8.968  60.561  1.00            
ATOM   1409  CA  GLN D  15      48.856   8.882  62.015  1.00            
ATOM   1410  C   GLN D  15      49.804   7.871  62.653  1.00            
ATOM   1411  O   GLN D  15      50.296   8.103  63.757  1.00            
ATOM   1412  CB  GLN D  15      47.422   8.542  62.405  1.00            
ATOM   1413  CG  GLN D  15      47.092   8.962  63.832  1.00            
ATOM   1414  CD  GLN D  15      45.619   8.847  64.132  1.00            
ATOM   1415  OE1 GLN D  15      44.825   8.522  63.255  1.00            
ATOM   1416  NE2 GLN D  15      45.237   9.163  65.363  1.00            
ATOM   1417  N   LYS D  16      50.029   6.745  61.977  1.00            
ATOM   1418  CA  LYS D  16      50.957   5.730  62.470  1.00            
ATOM   1419  C   LYS D  16      52.396   6.225  62.360  1.00            
ATOM   1420  O   LYS D  16      53.242   5.895  63.194  1.00            
ATOM   1421  CB  LYS D  16      50.793   4.399  61.709  1.00            
ATOM   1422  CG  LYS D  16      49.525   3.619  62.028  1.00            
ATOM   1423  CD  LYS D  16      49.488   2.296  61.259  1.00            
ATOM   1424  CE  LYS D  16      48.778   2.521  59.927  1.00            
ATOM   1425  NZ  LYS D  16      48.511   1.272  59.118  1.00            
ATOM   1426  N   GLU D  17      52.675   7.006  61.321  1.00            
ATOM   1427  CA  GLU D  17      53.980   7.627  61.175  1.00            
ATOM   1428  C   GLU D  17      54.202   8.613  62.332  1.00            
ATOM   1429  O   GLU D  17      55.308   8.722  62.859  1.00            
ATOM   1430  CB  GLU D  17      54.112   8.314  59.814  1.00            
ATOM   1431  CG  GLU D  17      55.511   8.830  59.516  1.00            
ATOM   1432  CD  GLU D  17      55.610   9.520  58.159  1.00            
ATOM   1433  OE1 GLU D  17      54.711   9.309  57.314  1.00            
ATOM   1434  OE2 GLU D  17      56.598  10.253  57.932  1.00            
ATOM   1435  N   THR D  18      53.150   9.336  62.711  1.00            
ATOM   1436  CA  THR D  18      53.217  10.244  63.857  1.00            
ATOM   1437  C   THR D  18      53.476   9.462  65.153  1.00            
ATOM   1438  O   THR D  18      54.299   9.867  65.976  1.00            
ATOM   1439  CB  THR D  18      51.919  11.066  64.004  1.00            
ATOM   1440  OG1 THR D  18      51.724  11.879  62.834  1.00            
ATOM   1441  CG2 THR D  18      51.986  11.968  65.231  1.00            
ATOM   1442  N   LEU D  19      52.777   8.339  65.312  1.00            
ATOM   1443  CA  LEU D  19      52.948   7.442  66.467  1.00            
ATOM   1444  C   LEU D  19      54.379   6.956  66.604  1.00            
ATOM   1445  O   LEU D  19      54.966   6.974  67.702  1.00            
ATOM   1446  CB  LEU D  19      52.025   6.232  66.339  1.00            
ATOM   1447  CG  LEU D  19      52.170   5.050  67.298  1.00            
ATOM   1448  CD1 LEU D  19      51.797   5.411  68.724  1.00            
ATOM   1449  CD2 LEU D  19      51.369   3.842  66.805  1.00            
ATOM   1450  N   ILE D  20      54.935   6.514  65.483  1.00            
ATOM   1451  CA  ILE D  20      56.300   6.029  65.469  1.00            
ATOM   1452  C   ILE D  20      57.250   7.143  65.899  1.00            
ATOM   1453  O   ILE D  20      58.132   6.922  66.718  1.00            
ATOM   1454  CB  ILE D  20      56.711   5.517  64.078  1.00            
ATOM   1455  CG1 ILE D  20      56.044   4.172  63.787  1.00            
ATOM   1456  CG2 ILE D  20      58.240   5.424  63.968  1.00            
ATOM   1457  CD1 ILE D  20      56.181   3.711  62.334  1.00            
ATOM   1458  N   ARG D  21      57.051   8.343  65.367  1.00            
ATOM   1459  CA  ARG D  21      57.958   9.441  65.674  1.00            
ATOM   1460  C   ARG D  21      57.893   9.840  67.147  1.00            
ATOM   1461  O   ARG D  21      58.925  10.010  67.788  1.00            
ATOM   1462  CB  ARG D  21      57.671  10.663  64.806  1.00            
ATOM   1463  CG  ARG D  21      58.708  11.769  64.991  1.00            
ATOM   1464  CD  ARG D  21      58.347  13.016  64.199  1.00            
ATOM   1465  NE  ARG D  21      58.043  12.698  62.808  1.00            
ATOM   1466  CZ  ARG D  21      56.815  12.715  62.300  1.00            
ATOM   1467  NH1 ARG D  21      55.788  13.052  63.071  1.00            
ATOM   1468  NH2 ARG D  21      56.614  12.406  61.025  1.00            
ATOM   1469  N   GLU D  22      56.680   9.997  67.668  1.00            
ATOM   1470  CA  GLU D  22      56.482  10.470  69.035  1.00            
ATOM   1471  C   GLU D  22      56.944   9.446  70.086  1.00            
ATOM   1472  O   GLU D  22      57.530   9.819  71.102  1.00            
ATOM   1473  CB  GLU D  22      55.015  10.839  69.255  1.00            
ATOM   1474  CG  GLU D  22      54.529  11.992  68.366  1.00            
ATOM   1475  CD  GLU D  22      55.196  13.324  68.668  1.00            
ATOM   1476  OE1 GLU D  22      55.274  14.169  67.749  1.00            
ATOM   1477  OE2 GLU D  22      55.636  13.536  69.818  1.00            
ATOM   1478  N   VAL D  23      56.702   8.165  69.834  1.00            
ATOM   1479  CA  VAL D  23      57.143   7.121  70.756  1.00            
ATOM   1480  C   VAL D  23      58.668   7.062  70.759  1.00            
ATOM   1481  O   VAL D  23      59.289   6.930  71.816  1.00            
ATOM   1482  CB  VAL D  23      56.561   5.721  70.390  1.00            
ATOM   1483  CG1 VAL D  23      57.325   4.620  71.076  1.00            
ATOM   1484  CG2 VAL D  23      55.082   5.637  70.730  1.00            
ATOM   1485  N   SER D  24      59.257   7.209  69.574  1.00            
ATOM   1486  CA  SER D  24      60.705   7.169  69.405  1.00            
ATOM   1487  C   SER D  24      61.405   8.278  70.182  1.00            
ATOM   1488  O   SER D  24      62.433   8.041  70.803  1.00            
ATOM   1489  CB  SER D  24      61.074   7.280  67.930  1.00            
ATOM   1490  OG  SER D  24      60.617   6.163  67.202  1.00            
ATOM   1491  N   GLU D  25      60.835   9.477  70.144  1.00            
ATOM   1492  CA  GLU D  25      61.388  10.627  70.861  1.00            
ATOM   1493  C   GLU D  25      61.290  10.425  72.368  1.00            
ATOM   1494  O   GLU D  25      62.233  10.700  73.100  1.00            
ATOM   1495  CB  GLU D  25      60.636  11.898  70.455  1.00            
ATOM   1496  CG  GLU D  25      60.869  12.324  69.018  1.00            
ATOM   1497  CD  GLU D  25      60.014  13.509  68.612  1.00            
ATOM   1498  OE1 GLU D  25      59.067  13.848  69.357  1.00            
ATOM   1499  OE2 GLU D  25      60.282  14.099  67.544  1.00            
ATOM   1500  N   ALA D  26      60.148   9.914  72.813  1.00            
ATOM   1501  CA  ALA D  26      59.899   9.649  74.221  1.00            
ATOM   1502  C   ALA D  26      60.900   8.648  74.771  1.00            
ATOM   1503  O   ALA D  26      61.472   8.853  75.836  1.00            
ATOM   1504  CB  ALA D  26      58.479   9.129  74.417  1.00            
ATOM   1505  N   ILE D  27      61.132   7.582  74.016  1.00            
ATOM   1506  CA  ILE D  27      62.112   6.576  74.392  1.00            
ATOM   1507  C   ILE D  27      63.500   7.183  74.418  1.00            
ATOM   1508  O   ILE D  27      64.257   6.973  75.366  1.00            
ATOM   1509  CB  ILE D  27      62.088   5.389  73.422  1.00            
ATOM   1510  CG1 ILE D  27      60.810   4.583  73.621  1.00            
ATOM   1511  CG2 ILE D  27      63.278   4.489  73.652  1.00            
ATOM   1512  CD1 ILE D  27      60.620   3.495  72.581  1.00            
ATOM   1513  N   SER D  28      63.826   7.950  73.380  1.00            
ATOM   1514  CA  SER D  28      65.129   8.615  73.303  1.00            
ATOM   1515  C   SER D  28      65.336   9.537  74.506  1.00            
ATOM   1516  O   SER D  28      66.380   9.500  75.169  1.00            
ATOM   1517  CB  SER D  28      65.247   9.410  71.995  1.00            
ATOM   1518  OG  SER D  28      66.506  10.049  71.882  1.00            
ATOM   1519  N   ARG D  29      64.322  10.344  74.801  1.00            
ATOM   1520  CA  ARG D  29      64.400  11.282  75.909  1.00            
ATOM   1521  C   ARG D  29      64.497  10.587  77.267  1.00            
ATOM   1522  O   ARG D  29      65.299  10.980  78.112  1.00            
ATOM   1523  CB  ARG D  29      63.189  12.219  75.893  1.00            
ATOM   1524  CG  ARG D  29      63.238  13.314  74.833  1.00            
ATOM   1525  CD  ARG D  29      62.022  14.241  74.943  1.00            
ATOM   1526  NE  ARG D  29      60.770  13.612  74.513  1.00            
ATOM   1527  CZ  ARG D  29      59.832  13.140  75.332  1.00            
ATOM   1528  NH1 ARG D  29      60.004  13.186  76.645  1.00            
ATOM   1529  NH2 ARG D  29      58.726  12.603  74.834  1.00            
ATOM   1530  N   SER D  30      63.678   9.562  77.474  1.00            
ATOM   1531  CA  SER D  30      63.618   8.885  78.769  1.00            
ATOM   1532  C   SER D  30      64.888   8.118  79.146  1.00            
ATOM   1533  O   SER D  30      65.257   8.062  80.324  1.00            
ATOM   1534  CB  SER D  30      62.418   7.948  78.800  1.00            
ATOM   1535  OG  SER D  30      61.220   8.690  78.693  1.00            
ATOM   1536  N   LEU D  31      65.555   7.542  78.150  1.00            
ATOM   1537  CA  LEU D  31      66.697   6.662  78.393  1.00            
ATOM   1538  C   LEU D  31      68.036   7.310  78.026  1.00            
ATOM   1539  O   LEU D  31      69.093   6.690  78.177  1.00            
ATOM   1540  CB  LEU D  31      66.527   5.351  77.616  1.00            
ATOM   1541  CG  LEU D  31      65.276   4.523  77.932  1.00            
ATOM   1542  CD1 LEU D  31      65.275   3.229  77.155  1.00            
ATOM   1543  CD2 LEU D  31      65.210   4.254  79.426  1.00            
ATOM   1544  N   ASP D  32      67.982   8.552  77.548  1.00            
ATOM   1545  CA  ASP D  32      69.159   9.257  77.046  1.00            
ATOM   1546  C   ASP D  32      69.913   8.421  76.013  1.00            
ATOM   1547  O   ASP D  32      71.143   8.331  76.036  1.00            
ATOM   1548  CB  ASP D  32      70.089   9.643  78.204  1.00            
ATOM   1549  CG  ASP D  32      69.529  10.775  79.053  1.00            
ATOM   1550  OD1 ASP D  32      68.791  11.628  78.515  1.00            
ATOM   1551  OD2 ASP D  32      69.829  10.811  80.266  1.00            
ATOM   1552  N   ALA D  33      69.158   7.801  75.115  1.00            
ATOM   1553  CA  ALA D  33      69.734   6.987  74.062  1.00            
ATOM   1554  C   ALA D  33      69.675   7.747  72.749  1.00            
ATOM   1555  O   ALA D  33      68.718   8.486  72.505  1.00            
ATOM   1556  CB  ALA D  33      68.996   5.673  73.951  1.00            
ATOM   1557  N   PRO D  34      70.703   7.576  71.901  1.00            
ATOM   1558  CA  PRO D  34      70.697   8.241  70.598  1.00            
ATOM   1559  C   PRO D  34      69.469   7.791  69.812  1.00            
ATOM   1560  O   PRO D  34      69.182   6.597  69.745  1.00            
ATOM   1561  CB  PRO D  34      71.992   7.754  69.942  1.00            
ATOM   1562  CG  PRO D  34      72.854   7.305  71.077  1.00            
ATOM   1563  CD  PRO D  34      71.915   6.769  72.109  1.00            
ATOM   1564  N   LEU D  35      68.760   8.743  69.226  1.00            
ATOM   1565  CA  LEU D  35      67.520   8.457  68.528  1.00            
ATOM   1566  C   LEU D  35      67.743   7.410  67.423  1.00            
ATOM   1567  O   LEU D  35      66.886   6.565  67.189  1.00            
ATOM   1568  CB  LEU D  35      66.918   9.769  68.014  1.00            
ATOM   1569  CG  LEU D  35      65.540   9.750  67.364  1.00            
ATOM   1570  CD1 LEU D  35      64.550   9.057  68.277  1.00            
ATOM   1571  CD2 LEU D  35      65.087  11.184  67.147  1.00            
ATOM   1572  N   THR D  36      68.912   7.437  66.785  1.00            
ATOM   1573  CA  THR D  36      69.238   6.483  65.725  1.00            
ATOM   1574  C   THR D  36      69.226   5.026  66.223  1.00            
ATOM   1575  O   THR D  36      69.116   4.089  65.427  1.00            
ATOM   1576  CB  THR D  36      70.630   6.776  65.112  1.00            
ATOM   1577  OG1 THR D  36      71.614   6.799  66.154  1.00            
ATOM   1578  CG2 THR D  36      70.646   8.121  64.421  1.00            
ATOM   1579  N   SER D  37      69.301   4.838  67.538  1.00            
ATOM   1580  CA  SER D  37      69.300   3.498  68.130  1.00            
ATOM   1581  C   SER D  37      67.892   2.976  68.448  1.00            
ATOM   1582  O   SER D  37      67.722   1.824  68.848  1.00            
ATOM   1583  CB  SER D  37      70.124   3.501  69.411  1.00            
ATOM   1584  OG  SER D  37      69.446   4.242  70.412  1.00            
ATOM   1585  N   VAL D  38      66.885   3.829  68.297  1.00            
ATOM   1586  CA  VAL D  38      65.521   3.443  68.639  1.00            
ATOM   1587  C   VAL D  38      64.782   2.841  67.466  1.00            
ATOM   1588  O   VAL D  38      64.655   3.472  66.410  1.00            
ATOM   1589  CB  VAL D  38      64.712   4.635  69.161  1.00            
ATOM   1590  CG1 VAL D  38      63.298   4.224  69.431  1.00            
ATOM   1591  CG2 VAL D  38      65.382   5.224  70.424  1.00            
ATOM   1592  N   ARG D  39      64.269   1.633  67.659  1.00            
ATOM   1593  CA  ARG D  39      63.481   0.999  66.626  1.00            
ATOM   1594  C   ARG D  39      62.083   0.779  67.143  1.00            
ATOM   1595  O   ARG D  39      61.896   0.444  68.315  1.00            
ATOM   1596  CB  ARG D  39      64.132  -0.307  66.160  1.00            
ATOM   1597  CG  ARG D  39      65.255  -0.029  65.164  1.00            
ATOM   1598  CD  ARG D  39      66.230  -1.157  64.997  1.00            
ATOM   1599  NE  ARG D  39      67.169  -0.846  63.926  1.00            
ATOM   1600  CZ  ARG D  39      68.117   0.083  64.012  1.00            
ATOM   1601  NH1 ARG D  39      68.253   0.808  65.117  1.00            
ATOM   1602  NH2 ARG D  39      68.924   0.297  62.988  1.00            
ATOM   1603  N   VAL D  40      61.108   1.051  66.279  1.00            
ATOM   1604  CA  VAL D  40      59.704   0.910  66.620  1.00            
ATOM   1605  C   VAL D  40      58.964   0.107  65.545  1.00            
ATOM   1606  O   VAL D  40      59.045   0.417  64.356  1.00            
ATOM   1607  CB  VAL D  40      59.027   2.283  66.802  1.00            
ATOM   1608  CG1 VAL D  40      57.522   2.120  67.027  1.00            
ATOM   1609  CG2 VAL D  40      59.655   3.046  67.974  1.00            
ATOM   1610  N   ILE D  41      58.247  -0.916  65.986  1.00            
ATOM   1611  CA  ILE D  41      57.416  -1.776  65.130  1.00            
ATOM   1612  C   ILE D  41      55.941  -1.606  65.451  1.00            
ATOM   1613  O   ILE D  41      55.528  -1.836  66.587  1.00            
ATOM   1614  CB  ILE D  41      57.778  -3.259  65.325  1.00            
ATOM   1615  CG1 ILE D  41      59.240  -3.503  64.960  1.00            
ATOM   1616  CG2 ILE D  41      56.817  -4.172  64.543  1.00            
ATOM   1617  CD1 ILE D  41      59.772  -4.881  65.426  1.00            
ATOM   1618  N   ILE D  42      55.146  -1.234  64.452  1.00            
ATOM   1619  CA  ILE D  42      53.699  -1.174  64.611  1.00            
ATOM   1620  C   ILE D  42      53.054  -2.475  64.161  1.00            
ATOM   1621  O   ILE D  42      53.246  -2.897  63.031  1.00            
ATOM   1622  CB  ILE D  42      53.088  -0.033  63.778  1.00            
ATOM   1623  CG1 ILE D  42      53.587   1.309  64.286  1.00            
ATOM   1624  CG2 ILE D  42      51.576  -0.057  63.869  1.00            
ATOM   1625  CD1 ILE D  42      53.000   2.465  63.533  1.00            
ATOM   1626  N   THR D  43      52.282  -3.094  65.039  1.00            
ATOM   1627  CA  THR D  43      51.584  -4.311  64.697  1.00            
ATOM   1628  C   THR D  43      50.083  -4.099  64.824  1.00            
ATOM   1629  O   THR D  43      49.548  -3.986  65.924  1.00            
ATOM   1630  CB  THR D  43      52.015  -5.480  65.581  1.00            
ATOM   1631  OG1 THR D  43      53.438  -5.636  65.493  1.00            
ATOM   1632  CG2 THR D  43      51.357  -6.762  65.126  1.00            
ATOM   1633  N   GLU D  44      49.404  -4.116  63.683  1.00            
ATOM   1634  CA  GLU D  44      47.965  -3.900  63.663  1.00            
ATOM   1635  C   GLU D  44      47.211  -5.167  64.001  1.00            
ATOM   1636  O   GLU D  44      47.528  -6.256  63.514  1.00            
ATOM   1637  CB  GLU D  44      47.523  -3.390  62.291  1.00            
ATOM   1638  CG  GLU D  44      47.930  -1.974  61.982  1.00            
ATOM   1639  CD  GLU D  44      47.312  -1.491  60.690  1.00            
ATOM   1640  OE1 GLU D  44      47.363  -2.247  59.689  1.00            
ATOM   1641  OE2 GLU D  44      46.756  -0.373  60.688  1.00            
ATOM   1642  N   MET D  45      46.179  -5.022  64.812  1.00            
ATOM   1643  CA  MET D  45      45.326  -6.157  65.145  1.00            
ATOM   1644  C   MET D  45      43.978  -5.978  64.474  1.00            
ATOM   1645  O   MET D  45      43.389  -4.907  64.551  1.00            
ATOM   1646  CB  MET D  45      45.144  -6.277  66.653  1.00            
ATOM   1647  CG  MET D  45      46.425  -6.366  67.435  1.00            
ATOM   1648  SD  MET D  45      46.060  -6.340  69.199  1.00            
ATOM   1649  CE  MET D  45      45.627  -4.614  69.480  1.00            
ATOM   1650  N   ALA D  46      43.500  -7.013  63.797  1.00            
ATOM   1651  CA  ALA D  46      42.147  -6.996  63.256  1.00            
ATOM   1652  C   ALA D  46      41.146  -7.027  64.410  1.00            
ATOM   1653  O   ALA D  46      41.456  -7.555  65.470  1.00            
ATOM   1654  CB  ALA D  46      41.935  -8.179  62.321  1.00            
ATOM   1655  N   LYS D  47      39.964  -6.487  64.209  1.00            
ATOM   1656  CA  LYS D  47      38.966  -6.444  65.251  1.00            
ATOM   1657  C   LYS D  47      38.654  -7.812  65.846  1.00            
ATOM   1658  O   LYS D  47      38.499  -7.933  67.031  1.00            
ATOM   1659  CB  LYS D  47      37.706  -5.772  64.744  1.00            
ATOM   1660  CG  LYS D  47      37.610  -4.316  65.115  1.00            
ATOM   1661  CD  LYS D  47      38.787  -3.541  64.575  1.00            
ATOM   1662  CE  LYS D  47      38.558  -2.060  64.674  1.00            
ATOM   1663  NZ  LYS D  47      39.521  -1.312  63.865  1.00            
ATOM   1664  N   GLY D  48      38.602  -8.831  65.021  1.00            
ATOM   1665  CA  GLY D  48      38.284 -10.169  65.477  1.00            
ATOM   1666  C   GLY D  48      39.456 -10.878  66.149  1.00            
ATOM   1667  O   GLY D  48      39.361 -12.059  66.477  1.00            
ATOM   1668  N   HIS D  49      40.563 -10.171  66.359  1.00            
ATOM   1669  CA  HIS D  49      41.761 -10.822  66.891  1.00            
ATOM   1670  C   HIS D  49      42.176 -10.276  68.238  1.00            
ATOM   1671  O   HIS D  49      43.228 -10.665  68.736  1.00            
ATOM   1672  CB  HIS D  49      42.958 -10.675  65.951  1.00            
ATOM   1673  CG  HIS D  49      42.824 -11.430  64.665  1.00            
ATOM   1674  ND1 HIS D  49      43.764 -11.352  63.662  1.00            
ATOM   1675  CD2 HIS D  49      41.855 -12.261  64.207  1.00            
ATOM   1676  CE1 HIS D  49      43.394 -12.120  62.651  1.00            
ATOM   1677  NE2 HIS D  49      42.234 -12.675  62.955  1.00            
ATOM   1678  N   PHE D  50      41.397  -9.349  68.793  1.00            
ATOM   1679  CA  PHE D  50      41.753  -8.725  70.067  1.00            
ATOM   1680  C   PHE D  50      40.608  -8.864  71.056  1.00            
ATOM   1681  O   PHE D  50      39.504  -8.368  70.826  1.00            
ATOM   1682  CB  PHE D  50      42.125  -7.250  69.873  1.00            
ATOM   1683  CG  PHE D  50      42.585  -6.555  71.147  1.00            
ATOM   1684  CD1 PHE D  50      43.559  -7.132  71.951  1.00            
ATOM   1685  CD2 PHE D  50      42.075  -5.324  71.505  1.00            
ATOM   1686  CE1 PHE D  50      43.994  -6.500  73.126  1.00            
ATOM   1687  CE2 PHE D  50      42.509  -4.678  72.654  1.00            
ATOM   1688  CZ  PHE D  50      43.468  -5.273  73.472  1.00            
ATOM   1689  N   GLY D  51      40.881  -9.567  72.156  1.00            
ATOM   1690  CA  GLY D  51      39.885  -9.816  73.172  1.00            
ATOM   1691  C   GLY D  51      40.243  -9.146  74.490  1.00            
ATOM   1692  O   GLY D  51      41.401  -9.110  74.890  1.00            
ATOM   1693  N   ILE D  52      39.234  -8.597  75.143  1.00            
ATOM   1694  CA  ILE D  52      39.355  -8.093  76.507  1.00            
ATOM   1695  C   ILE D  52      38.299  -8.798  77.334  1.00            
ATOM   1696  O   ILE D  52      37.131  -8.790  76.977  1.00            
ATOM   1697  CB  ILE D  52      39.144  -6.575  76.616  1.00            
ATOM   1698  CG1 ILE D  52      40.194  -5.815  75.814  1.00            
ATOM   1699  CG2 ILE D  52      39.198  -6.144  78.084  1.00            
ATOM   1700  CD1 ILE D  52      39.910  -4.328  75.707  1.00            
ATOM   1701  N   GLY D  53      38.709  -9.451  78.411  1.00            
ATOM   1702  CA  GLY D  53      37.753 -10.170  79.232  1.00            
ATOM   1703  C   GLY D  53      37.078 -11.309  78.488  1.00            
ATOM   1704  O   GLY D  53      35.954 -11.697  78.815  1.00            
ATOM   1705  N   GLY D  54      37.752 -11.826  77.468  1.00            
ATOM   1706  CA  GLY D  54      37.246 -12.966  76.718  1.00            
ATOM   1707  C   GLY D  54      36.300 -12.618  75.582  1.00            
ATOM   1708  O   GLY D  54      35.839 -13.503  74.860  1.00            
ATOM   1709  N   GLU D  55      36.003 -11.332  75.434  1.00            
ATOM   1710  CA  GLU D  55      35.102 -10.855  74.384  1.00            
ATOM   1711  C   GLU D  55      35.856  -9.932  73.433  1.00            
ATOM   1712  O   GLU D  55      36.860  -9.354  73.817  1.00            
ATOM   1713  CB  GLU D  55      33.902 -10.124  74.983  1.00            
ATOM   1714  CG  GLU D  55      33.032 -10.965  75.921  1.00            
ATOM   1715  CD  GLU D  55      32.460 -12.218  75.267  1.00            
ATOM   1716  OE1 GLU D  55      32.085 -12.170  74.074  1.00            
ATOM   1717  OE2 GLU D  55      32.361 -13.253  75.964  1.00            
ATOM   1718  N   LEU D  56      35.397  -9.791  72.191  1.00            
ATOM   1719  CA  LEU D  56      36.083  -8.872  71.288  1.00            
ATOM   1720  C   LEU D  56      36.002  -7.458  71.879  1.00            
ATOM   1721  O   LEU D  56      34.985  -7.080  72.463  1.00            
ATOM   1722  CB  LEU D  56      35.465  -8.918  69.883  1.00            
ATOM   1723  CG  LEU D  56      35.526 -10.279  69.183  1.00            
ATOM   1724  CD1 LEU D  56      34.888 -10.212  67.799  1.00            
ATOM   1725  CD2 LEU D  56      36.971 -10.772  69.072  1.00            
ATOM   1726  N   ALA D  57      37.064  -6.676  71.717  1.00            
ATOM   1727  CA  ALA D  57      37.090  -5.317  72.262  1.00            
ATOM   1728  C   ALA D  57      36.161  -4.378  71.497  1.00            
ATOM   1729  O   ALA D  57      36.238  -4.277  70.271  1.00            
ATOM   1730  CB  ALA D  57      38.512  -4.770  72.255  1.00            
TER    1731      ALA D  57                                                      
ATOM   1732  N   PRO E   1      50.486 -24.248  67.319  1.00            
ATOM   1733  CA  PRO E   1      50.180 -22.936  67.888  1.00            
ATOM   1734  C   PRO E   1      51.083 -22.626  69.073  1.00            
ATOM   1735  O   PRO E   1      51.409 -23.530  69.829  1.00            
ATOM   1736  CB  PRO E   1      48.717 -23.067  68.339  1.00            
ATOM   1737  CG  PRO E   1      48.445 -24.523  68.380  1.00            
ATOM   1738  CD  PRO E   1      49.314 -25.135  67.331  1.00            
ATOM   1739  N   ILE E   2      51.493 -21.371  69.202  1.00            
ATOM   1740  CA  ILE E   2      52.363 -20.940  70.293  1.00            
ATOM   1741  C   ILE E   2      51.776 -19.746  71.028  1.00            
ATOM   1742  O   ILE E   2      51.466 -18.713  70.431  1.00            
ATOM   1743  CB  ILE E   2      53.778 -20.583  69.808  1.00            
ATOM   1744  CG1 ILE E   2      54.451 -21.807  69.184  1.00            
ATOM   1745  CG2 ILE E   2      54.617 -20.090  70.981  1.00            
ATOM   1746  CD1 ILE E   2      55.738 -21.498  68.421  1.00            
ATOM   1747  N   ALA E   3      51.620 -19.895  72.335  1.00            
ATOM   1748  CA  ALA E   3      51.080 -18.835  73.154  1.00            
ATOM   1749  C   ALA E   3      52.161 -18.286  74.078  1.00            
ATOM   1750  O   ALA E   3      52.870 -19.048  74.745  1.00            
ATOM   1751  CB  ALA E   3      49.895 -19.336  73.953  1.00            
ATOM   1752  N   GLN E   4      52.328 -16.970  74.070  1.00            
ATOM   1753  CA  GLN E   4      53.199 -16.313  75.042  1.00            
ATOM   1754  C   GLN E   4      52.343 -15.514  75.996  1.00            
ATOM   1755  O   GLN E   4      51.592 -14.624  75.592  1.00            
ATOM   1756  CB  GLN E   4      54.233 -15.412  74.365  1.00            
ATOM   1757  CG  GLN E   4      55.240 -14.795  75.350  1.00            
ATOM   1758  CD  GLN E   4      56.289 -13.918  74.678  1.00            
ATOM   1759  OE1 GLN E   4      56.250 -13.691  73.468  1.00            
ATOM   1760  NE2 GLN E   4      57.235 -13.421  75.469  1.00            
ATOM   1761  N   ILE E   5      52.453 -15.824  77.278  1.00            
ATOM   1762  CA  ILE E   5      51.570 -15.178  78.236  1.00            
ATOM   1763  C   ILE E   5      52.372 -14.346  79.219  1.00            
ATOM   1764  O   ILE E   5      53.213 -14.879  79.957  1.00            
ATOM   1765  CB  ILE E   5      50.723 -16.205  78.977  1.00            
ATOM   1766  CG1 ILE E   5      50.125 -17.216  77.989  1.00            
ATOM   1767  CG2 ILE E   5      49.635 -15.511  79.785  1.00            
ATOM   1768  CD1 ILE E   5      49.316 -18.303  78.651  1.00            
ATOM   1769  N   HIS E   6      52.115 -13.040  79.211  1.00            
ATOM   1770  CA  HIS E   6      52.732 -12.132  80.165  1.00            
ATOM   1771  C   HIS E   6      51.910 -12.058  81.440  1.00            
ATOM   1772  O   HIS E   6      50.728 -11.726  81.400  1.00            
ATOM   1773  CB  HIS E   6      52.890 -10.732  79.560  1.00            
ATOM   1774  CG  HIS E   6      54.027 -10.618  78.590  1.00            
ATOM   1775  ND1 HIS E   6      53.939 -11.042  77.284  1.00            
ATOM   1776  CD2 HIS E   6      55.278 -10.123  78.741  1.00            
ATOM   1777  CE1 HIS E   6      55.088 -10.818  76.672  1.00            
ATOM   1778  NE2 HIS E   6      55.917 -10.261  77.534  1.00            
ATOM   1779  N   ILE E   7      52.537 -12.386  82.564  1.00            
ATOM   1780  CA  ILE E   7      51.865 -12.334  83.852  1.00            
ATOM   1781  C   ILE E   7      52.739 -11.612  84.885  1.00            
ATOM   1782  O   ILE E   7      53.951 -11.491  84.723  1.00            
ATOM   1783  CB  ILE E   7      51.490 -13.745  84.388  1.00            
ATOM   1784  CG1 ILE E   7      52.743 -14.565  84.703  1.00            
ATOM   1785  CG2 ILE E   7      50.587 -14.501  83.396  1.00            
ATOM   1786  CD1 ILE E   7      52.448 -15.898  85.359  1.00            
ATOM   1787  N   LEU E   8      52.094 -11.096  85.918  1.00            
ATOM   1788  CA  LEU E   8      52.795 -10.434  87.017  1.00            
ATOM   1789  C   LEU E   8      53.528 -11.442  87.891  1.00            
ATOM   1790  O   LEU E   8      53.073 -12.563  88.063  1.00            
ATOM   1791  CB  LEU E   8      51.816  -9.607  87.851  1.00            
ATOM   1792  CG  LEU E   8      51.443  -8.252  87.251  1.00            
ATOM   1793  CD1 LEU E   8      50.215  -7.664  87.929  1.00            
ATOM   1794  CD2 LEU E   8      52.635  -7.310  87.422  1.00            
ATOM   1795  N   GLU E   9      54.679 -11.046  88.423  1.00            
ATOM   1796  CA  GLU E   9      55.419 -11.919  89.324  1.00            
ATOM   1797  C   GLU E   9      54.568 -12.233  90.536  1.00            
ATOM   1798  O   GLU E   9      53.679 -11.468  90.891  1.00            
ATOM   1799  CB  GLU E   9      56.724 -11.262  89.745  1.00            
ATOM   1800  CG  GLU E   9      57.835 -11.432  88.735  1.00            
ATOM   1801  CD  GLU E   9      59.111 -10.728  89.156  1.00            
ATOM   1802  OE1 GLU E   9      59.113 -10.086  90.230  1.00            
ATOM   1803  OE2 GLU E   9      60.108 -10.816  88.407  1.00            
ATOM   1804  N   GLY E  10      54.833 -13.363  91.175  1.00            
ATOM   1805  CA  GLY E  10      54.148 -13.674  92.416  1.00            
ATOM   1806  C   GLY E  10      53.385 -14.980  92.385  1.00            
ATOM   1807  O   GLY E  10      52.854 -15.404  93.402  1.00            
ATOM   1808  N   ARG E  11      53.310 -15.614  91.216  1.00            
ATOM   1809  CA  ARG E  11      52.550 -16.853  91.081  1.00            
ATOM   1810  C   ARG E  11      53.396 -18.044  91.526  1.00            
ATOM   1811  O   ARG E  11      54.615 -18.063  91.347  1.00            
ATOM   1812  CB  ARG E  11      52.114 -17.072  89.630  1.00            
ATOM   1813  CG  ARG E  11      51.144 -16.040  89.053  1.00            
ATOM   1814  CD  ARG E  11      49.814 -16.000  89.772  1.00            
ATOM   1815  NE  ARG E  11      49.070 -14.770  89.517  1.00            
ATOM   1816  CZ  ARG E  11      48.011 -14.387  90.221  1.00            
ATOM   1817  NH1 ARG E  11      47.561 -15.150  91.206  1.00            
ATOM   1818  NH2 ARG E  11      47.383 -13.258  89.924  1.00            
ATOM   1819  N   SER E  12      52.725 -19.066  92.041  1.00            
ATOM   1820  CA  SER E  12      53.385 -20.289  92.465  1.00            
ATOM   1821  C   SER E  12      53.743 -21.152  91.264  1.00            
ATOM   1822  O   SER E  12      53.284 -20.912  90.139  1.00            
ATOM   1823  CB  SER E  12      52.494 -21.066  93.439  1.00            
ATOM   1824  OG  SER E  12      51.328 -21.530  92.777  1.00            
ATOM   1825  N   ASP E  13      54.610 -22.127  91.499  1.00            
ATOM   1826  CA  ASP E  13      54.976 -23.080  90.469  1.00            
ATOM   1827  C   ASP E  13      53.727 -23.856  90.064  1.00            
ATOM   1828  O   ASP E  13      53.504 -24.146  88.884  1.00            
ATOM   1829  CB  ASP E  13      56.075 -24.014  90.969  1.00            
ATOM   1830  CG  ASP E  13      57.434 -23.332  91.030  1.00            
ATOM   1831  OD1 ASP E  13      57.524 -22.134  90.668  1.00            
ATOM   1832  OD2 ASP E  13      58.413 -23.997  91.426  1.00            
ATOM   1833  N   GLU E  14      52.894 -24.151  91.058  1.00            
ATOM   1834  CA  GLU E  14      51.679 -24.931  90.857  1.00            
ATOM   1835  C   GLU E  14      50.700 -24.202  89.925  1.00            
ATOM   1836  O   GLU E  14      50.131 -24.807  89.026  1.00            
ATOM   1837  CB  GLU E  14      51.015 -25.210  92.209  1.00            
ATOM   1838  CG  GLU E  14      49.756 -26.085  92.179  1.00            
ATOM   1839  CD  GLU E  14      50.018 -27.533  91.772  1.00            
ATOM   1840  OE1 GLU E  14      51.194 -27.960  91.786  1.00            
ATOM   1841  OE2 GLU E  14      49.041 -28.250  91.452  1.00            
ATOM   1842  N   GLN E  15      50.524 -22.904  90.138  1.00            
ATOM   1843  CA  GLN E  15      49.644 -22.085  89.305  1.00            
ATOM   1844  C   GLN E  15      50.122 -21.987  87.851  1.00            
ATOM   1845  O   GLN E  15      49.311 -22.015  86.917  1.00            
ATOM   1846  CB  GLN E  15      49.497 -20.695  89.937  1.00            
ATOM   1847  CG  GLN E  15      48.260 -20.556  90.833  1.00            
ATOM   1848  CD  GLN E  15      48.185 -19.218  91.551  1.00            
ATOM   1849  OE1 GLN E  15      49.095 -18.395  91.462  1.00            
ATOM   1850  NE2 GLN E  15      47.052 -18.958  92.178  1.00            
ATOM   1851  N   LYS E  16      51.435 -21.888  87.659  1.00            
ATOM   1852  CA  LYS E  16      52.005 -21.797  86.325  1.00            
ATOM   1853  C   LYS E  16      51.906 -23.110  85.535  1.00            
ATOM   1854  O   LYS E  16      51.618 -23.097  84.328  1.00            
ATOM   1855  CB  LYS E  16      53.458 -21.317  86.426  1.00            
ATOM   1856  CG  LYS E  16      53.525 -19.851  86.834  1.00            
ATOM   1857  CD  LYS E  16      54.935 -19.280  86.873  1.00            
ATOM   1858  CE  LYS E  16      55.552 -19.361  88.248  1.00            
ATOM   1859  NZ  LYS E  16      56.861 -18.644  88.292  1.00            
ATOM   1860  N   GLU E  17      52.073 -24.241  86.212  1.00            
ATOM   1861  CA  GLU E  17      51.872 -25.534  85.563  1.00            
ATOM   1862  C   GLU E  17      50.409 -25.688  85.145  1.00            
ATOM   1863  O   GLU E  17      50.120 -26.201  84.075  1.00            
ATOM   1864  CB  GLU E  17      52.276 -26.690  86.481  1.00            
ATOM   1865  CG  GLU E  17      53.755 -26.724  86.804  1.00            
ATOM   1866  CD  GLU E  17      54.134 -27.875  87.720  1.00            
ATOM   1867  OE1 GLU E  17      55.332 -27.995  88.056  1.00            
ATOM   1868  OE2 GLU E  17      53.231 -28.628  88.148  1.00            
ATOM   1869  N   THR E  18      49.494 -25.266  86.018  1.00            
ATOM   1870  CA  THR E  18      48.064 -25.300  85.722  1.00            
ATOM   1871  C   THR E  18      47.734 -24.357  84.560  1.00            
ATOM   1872  O   THR E  18      46.953 -24.705  83.671  1.00            
ATOM   1873  CB  THR E  18      47.209 -24.910  86.963  1.00            
ATOM   1874  OG1 THR E  18      47.511 -25.780  88.059  1.00            
ATOM   1875  CG2 THR E  18      45.709 -24.969  86.643  1.00            
ATOM   1876  N   LEU E  19      48.332 -23.167  84.571  1.00            
ATOM   1877  CA  LEU E  19      48.139 -22.199  83.494  1.00            
ATOM   1878  C   LEU E  19      48.538 -22.803  82.148  1.00            
ATOM   1879  O   LEU E  19      47.790 -22.718  81.164  1.00            
ATOM   1880  CB  LEU E  19      48.945 -20.916  83.767  1.00            
ATOM   1881  CG  LEU E  19      49.014 -19.851  82.660  1.00            
ATOM   1882  CD1 LEU E  19      47.632 -19.267  82.384  1.00            
ATOM   1883  CD2 LEU E  19      50.018 -18.733  83.009  1.00            
ATOM   1884  N   ILE E  20      49.707 -23.437  82.111  1.00            
ATOM   1885  CA  ILE E  20      50.190 -24.048  80.877  1.00            
ATOM   1886  C   ILE E  20      49.261 -25.156  80.394  1.00            
ATOM   1887  O   ILE E  20      48.904 -25.198  79.219  1.00            
ATOM   1888  CB  ILE E  20      51.622 -24.580  81.050  1.00            
ATOM   1889  CG1 ILE E  20      52.609 -23.421  80.926  1.00            
ATOM   1890  CG2 ILE E  20      51.949 -25.625  80.006  1.00            
ATOM   1891  CD1 ILE E  20      54.034 -23.768  81.297  1.00            
ATOM   1892  N   ARG E  21      48.844 -26.031  81.302  1.00            
ATOM   1893  CA  ARG E  21      47.949 -27.123  80.943  1.00            
ATOM   1894  C   ARG E  21      46.571 -26.610  80.509  1.00            
ATOM   1895  O   ARG E  21      46.053 -27.030  79.480  1.00            
ATOM   1896  CB  ARG E  21      47.838 -28.116  82.110  1.00            
ATOM   1897  CG  ARG E  21      46.988 -29.335  81.828  1.00            
ATOM   1898  CD  ARG E  21      46.946 -30.303  83.014  1.00            
ATOM   1899  NE  ARG E  21      48.292 -30.695  83.436  1.00            
ATOM   1900  CZ  ARG E  21      48.893 -30.293  84.553  1.00            
ATOM   1901  NH1 ARG E  21      48.258 -29.505  85.412  1.00            
ATOM   1902  NH2 ARG E  21      50.127 -30.701  84.820  1.00            
ATOM   1903  N   GLU E  22      45.979 -25.702  81.282  1.00            
ATOM   1904  CA  GLU E  22      44.632 -25.220  80.974  1.00            
ATOM   1905  C   GLU E  22      44.559 -24.356  79.697  1.00            
ATOM   1906  O   GLU E  22      43.598 -24.474  78.939  1.00            
ATOM   1907  CB  GLU E  22      44.045 -24.469  82.169  1.00            
ATOM   1908  CG  GLU E  22      43.807 -25.364  83.394  1.00            
ATOM   1909  CD  GLU E  22      42.727 -26.414  83.156  1.00            
ATOM   1910  OE1 GLU E  22      41.831 -26.176  82.313  1.00            
ATOM   1911  OE2 GLU E  22      42.779 -27.483  83.808  1.00            
ATOM   1912  N   VAL E  23      45.551 -23.502  79.452  1.00            
ATOM   1913  CA  VAL E  23      45.566 -22.715  78.215  1.00            
ATOM   1914  C   VAL E  23      45.798 -23.629  77.013  1.00            
ATOM   1915  O   VAL E  23      45.169 -23.452  75.955  1.00            
ATOM   1916  CB  VAL E  23      46.637 -21.593  78.231  1.00            
ATOM   1917  CG1 VAL E  23      46.932 -21.083  76.812  1.00            
ATOM   1918  CG2 VAL E  23      46.195 -20.449  79.132  1.00            
ATOM   1919  N   SER E  24      46.681 -24.612  77.179  1.00            
ATOM   1920  CA  SER E  24      46.983 -25.561  76.105  1.00            
ATOM   1921  C   SER E  24      45.760 -26.388  75.692  1.00            
ATOM   1922  O   SER E  24      45.546 -26.628  74.503  1.00            
ATOM   1923  CB  SER E  24      48.126 -26.488  76.509  1.00            
ATOM   1924  OG  SER E  24      49.335 -25.753  76.648  1.00            
ATOM   1925  N   GLU E  25      44.972 -26.836  76.668  1.00            
ATOM   1926  CA  GLU E  25      43.756 -27.587  76.359  1.00            
ATOM   1927  C   GLU E  25      42.714 -26.690  75.683  1.00            
ATOM   1928  O   GLU E  25      42.012 -27.134  74.775  1.00            
ATOM   1929  CB  GLU E  25      43.172 -28.241  77.613  1.00            
ATOM   1930  CG  GLU E  25      44.035 -29.371  78.176  1.00            
ATOM   1931  CD  GLU E  25      43.437 -30.009  79.423  1.00            
ATOM   1932  OE1 GLU E  25      43.947 -31.070  79.860  1.00            
ATOM   1933  OE2 GLU E  25      42.467 -29.443  79.974  1.00            
ATOM   1934  N   ALA E  26      42.614 -25.440  76.141  1.00            
ATOM   1935  CA  ALA E  26      41.693 -24.459  75.565  1.00            
ATOM   1936  C   ALA E  26      42.030 -24.224  74.099  1.00            
ATOM   1937  O   ALA E  26      41.147 -24.182  73.249  1.00            
ATOM   1938  CB  ALA E  26      41.755 -23.136  76.334  1.00            
ATOM   1939  N   ILE E  27      43.320 -24.097  73.813  1.00            
ATOM   1940  CA  ILE E  27      43.790 -23.924  72.452  1.00            
ATOM   1941  C   ILE E  27      43.474 -25.143  71.599  1.00            
ATOM   1942  O   ILE E  27      42.950 -25.025  70.493  1.00            
ATOM   1943  CB  ILE E  27      45.293 -23.677  72.430  1.00            
ATOM   1944  CG1 ILE E  27      45.596 -22.314  73.052  1.00            
ATOM   1945  CG2 ILE E  27      45.832 -23.760  71.004  1.00            
ATOM   1946  CD1 ILE E  27      47.060 -22.055  73.247  1.00            
ATOM   1947  N   SER E  28      43.765 -26.316  72.148  1.00            
ATOM   1948  CA  SER E  28      43.539 -27.581  71.463  1.00            
ATOM   1949  C   SER E  28      42.067 -27.796  71.095  1.00            
ATOM   1950  O   SER E  28      41.765 -28.211  69.975  1.00            
ATOM   1951  CB  SER E  28      44.058 -28.739  72.322  1.00            
ATOM   1952  OG  SER E  28      43.907 -29.981  71.658  1.00            
ATOM   1953  N   ARG E  29      41.161 -27.543  72.041  1.00            
ATOM   1954  CA  ARG E  29      39.727 -27.715  71.794  1.00            
ATOM   1955  C   ARG E  29      39.192 -26.710  70.788  1.00            
ATOM   1956  O   ARG E  29      38.414 -27.056  69.911  1.00            
ATOM   1957  CB  ARG E  29      38.900 -27.555  73.072  1.00            
ATOM   1958  CG  ARG E  29      38.993 -28.662  74.097  1.00            
ATOM   1959  CD  ARG E  29      37.973 -28.395  75.203  1.00            
ATOM   1960  NE  ARG E  29      38.280 -27.186  75.969  1.00            
ATOM   1961  CZ  ARG E  29      39.058 -27.138  77.044  1.00            
ATOM   1962  NH1 ARG E  29      39.627 -28.240  77.520  1.00            
ATOM   1963  NH2 ARG E  29      39.259 -25.976  77.646  1.00            
ATOM   1964  N   SER E  30      39.591 -25.454  70.958  1.00            
ATOM   1965  CA  SER E  30      39.058 -24.351  70.167  1.00            
ATOM   1966  C   SER E  30      39.407 -24.422  68.686  1.00            
ATOM   1967  O   SER E  30      38.594 -24.050  67.837  1.00            
ATOM   1968  CB  SER E  30      39.555 -23.016  70.736  1.00            
ATOM   1969  OG  SER E  30      39.073 -22.803  72.050  1.00            
ATOM   1970  N   LEU E  31      40.607 -24.907  68.377  1.00            
ATOM   1971  CA  LEU E  31      41.097 -24.884  67.006  1.00            
ATOM   1972  C   LEU E  31      41.105 -26.275  66.375  1.00            
ATOM   1973  O   LEU E  31      41.469 -26.429  65.212  1.00            
ATOM   1974  CB  LEU E  31      42.505 -24.312  66.952  1.00            
ATOM   1975  CG  LEU E  31      42.735 -22.921  67.529  1.00            
ATOM   1976  CD1 LEU E  31      44.164 -22.505  67.242  1.00            
ATOM   1977  CD2 LEU E  31      41.725 -21.924  66.988  1.00            
ATOM   1978  N   ASP E  32      40.684 -27.270  67.148  1.00            
ATOM   1979  CA  ASP E  32      40.784 -28.677  66.772  1.00            
ATOM   1980  C   ASP E  32      42.224 -29.032  66.366  1.00            
ATOM   1981  O   ASP E  32      42.457 -29.731  65.376  1.00            
ATOM   1982  CB  ASP E  32      39.798 -29.009  65.645  1.00            
ATOM   1983  CG  ASP E  32      39.643 -30.502  65.429  1.00            
ATOM   1984  OD1 ASP E  32      40.114 -31.278  66.291  1.00            
ATOM   1985  OD2 ASP E  32      39.044 -30.898  64.404  1.00            
ATOM   1986  N   ALA E  33      43.183 -28.539  67.146  1.00            
ATOM   1987  CA  ALA E  33      44.596 -28.829  66.926  1.00            
ATOM   1988  C   ALA E  33      45.064 -29.847  67.959  1.00            
ATOM   1989  O   ALA E  33      44.617 -29.812  69.104  1.00            
ATOM   1990  CB  ALA E  33      45.427 -27.559  67.012  1.00            
ATOM   1991  N   PRO E  34      45.973 -30.750  67.561  1.00            
ATOM   1992  CA  PRO E  34      46.500 -31.775  68.468  1.00            
ATOM   1993  C   PRO E  34      47.165 -31.152  69.683  1.00            
ATOM   1994  O   PRO E  34      47.924 -30.200  69.519  1.00            
ATOM   1995  CB  PRO E  34      47.532 -32.514  67.614  1.00            
ATOM   1996  CG  PRO E  34      47.867 -31.575  66.507  1.00            
ATOM   1997  CD  PRO E  34      46.632 -30.782  66.246  1.00            
ATOM   1998  N   LEU E  35      46.875 -31.671  70.872  1.00            
ATOM   1999  CA  LEU E  35      47.419 -31.114  72.100  1.00            
ATOM   2000  C   LEU E  35      48.940 -31.072  72.058  1.00            
ATOM   2001  O   LEU E  35      49.547 -30.084  72.471  1.00            
ATOM   2002  CB  LEU E  35      46.951 -31.924  73.314  1.00            
ATOM   2003  CG  LEU E  35      47.383 -31.389  74.687  1.00            
ATOM   2004  CD1 LEU E  35      46.927 -29.951  74.865  1.00            
ATOM   2005  CD2 LEU E  35      46.867 -32.259  75.830  1.00            
ATOM   2006  N   THR E  36      49.546 -32.119  71.502  1.00            
ATOM   2007  CA  THR E  36      51.001 -32.234  71.447  1.00            
ATOM   2008  C   THR E  36      51.669 -31.141  70.611  1.00            
ATOM   2009  O   THR E  36      52.884 -30.955  70.701  1.00            
ATOM   2010  CB  THR E  36      51.437 -33.603  70.901  1.00            
ATOM   2011  OG1 THR E  36      50.858 -33.813  69.605  1.00            
ATOM   2012  CG2 THR E  36      50.984 -34.711  71.833  1.00            
ATOM   2013  N   SER E  37      50.887 -30.435  69.791  1.00            
ATOM   2014  CA  SER E  37      51.426 -29.365  68.952  1.00            
ATOM   2015  C   SER E  37      51.380 -27.987  69.627  1.00            
ATOM   2016  O   SER E  37      51.879 -27.007  69.073  1.00            
ATOM   2017  CB  SER E  37      50.685 -29.302  67.608  1.00            
ATOM   2018  OG  SER E  37      49.360 -28.822  67.765  1.00            
ATOM   2019  N   VAL E  38      50.777 -27.906  70.810  1.00            
ATOM   2020  CA  VAL E  38      50.606 -26.623  71.487  1.00            
ATOM   2021  C   VAL E  38      51.804 -26.273  72.364  1.00            
ATOM   2022  O   VAL E  38      52.215 -27.080  73.211  1.00            
ATOM   2023  CB  VAL E  38      49.353 -26.612  72.368  1.00            
ATOM   2024  CG1 VAL E  38      49.219 -25.257  73.044  1.00            
ATOM   2025  CG2 VAL E  38      48.117 -26.933  71.551  1.00            
ATOM   2026  N   ARG E  39      52.366 -25.088  72.162  1.00            
ATOM   2027  CA  ARG E  39      53.477 -24.629  73.000  1.00            
ATOM   2028  C   ARG E  39      53.128 -23.375  73.778  1.00            
ATOM   2029  O   ARG E  39      52.482 -22.470  73.265  1.00            
ATOM   2030  CB  ARG E  39      54.724 -24.399  72.141  1.00            
ATOM   2031  CG  ARG E  39      55.448 -25.679  71.851  1.00            
ATOM   2032  CD  ARG E  39      56.358 -25.576  70.661  1.00            
ATOM   2033  NE  ARG E  39      57.201 -26.762  70.522  1.00            
ATOM   2034  CZ  ARG E  39      56.766 -27.965  70.162  1.00            
ATOM   2035  NH1 ARG E  39      55.478 -28.170  69.925  1.00            
ATOM   2036  NH2 ARG E  39      57.621 -28.972  70.052  1.00            
ATOM   2037  N   VAL E  40      53.538 -23.315  75.039  1.00            
ATOM   2038  CA  VAL E  40      53.212 -22.140  75.832  1.00            
ATOM   2039  C   VAL E  40      54.452 -21.566  76.497  1.00            
ATOM   2040  O   VAL E  40      55.227 -22.303  77.098  1.00            
ATOM   2041  CB  VAL E  40      52.172 -22.443  76.907  1.00            
ATOM   2042  CG1 VAL E  40      51.940 -21.198  77.747  1.00            
ATOM   2043  CG2 VAL E  40      50.863 -22.895  76.281  1.00            
ATOM   2044  N   ILE E  41      54.645 -20.256  76.361  1.00            
ATOM   2045  CA  ILE E  41      55.744 -19.576  77.028  1.00            
ATOM   2046  C   ILE E  41      55.199 -18.634  78.119  1.00            
ATOM   2047  O   ILE E  41      54.385 -17.775  77.842  1.00            
ATOM   2048  CB  ILE E  41      56.610 -18.791  76.019  1.00            
ATOM   2049  CG1 ILE E  41      57.214 -19.755  74.994  1.00            
ATOM   2050  CG2 ILE E  41      57.706 -18.029  76.740  1.00            
ATOM   2051  CD1 ILE E  41      57.885 -19.088  73.819  1.00            
ATOM   2052  N   ILE E  42      55.638 -18.810  79.362  1.00            
ATOM   2053  CA  ILE E  42      55.232 -17.893  80.427  1.00            
ATOM   2054  C   ILE E  42      56.295 -16.816  80.603  1.00            
ATOM   2055  O   ILE E  42      57.476 -17.126  80.765  1.00            
ATOM   2056  CB  ILE E  42      54.995 -18.636  81.766  1.00            
ATOM   2057  CG1 ILE E  42      53.888 -19.670  81.619  1.00            
ATOM   2058  CG2 ILE E  42      54.613 -17.662  82.881  1.00            
ATOM   2059  CD1 ILE E  42      53.579 -20.384  82.926  1.00            
ATOM   2060  N   THR E  43      55.876 -15.554  80.540  1.00            
ATOM   2061  CA  THR E  43      56.770 -14.415  80.743  1.00            
ATOM   2062  C   THR E  43      56.312 -13.590  81.951  1.00            
ATOM   2063  O   THR E  43      55.221 -13.000  81.967  1.00            
ATOM   2064  CB  THR E  43      56.849 -13.506  79.477  1.00            
ATOM   2065  OG1 THR E  43      57.211 -14.302  78.334  1.00            
ATOM   2066  CG2 THR E  43      57.890 -12.410  79.669  1.00            
ATOM   2067  N   GLU E  44      57.146 -13.584  82.982  1.00            
ATOM   2068  CA  GLU E  44      56.848 -12.858  84.216  1.00            
ATOM   2069  C   GLU E  44      57.254 -11.383  84.166  1.00            
ATOM   2070  O   GLU E  44      58.377 -11.052  83.781  1.00            
ATOM   2071  CB  GLU E  44      57.559 -13.547  85.372  1.00            
ATOM   2072  CG  GLU E  44      56.978 -14.898  85.714  1.00            
ATOM   2073  CD  GLU E  44      57.590 -15.495  86.969  1.00            
ATOM   2074  OE1 GLU E  44      58.838 -15.478  87.098  1.00            
ATOM   2075  OE2 GLU E  44      56.813 -15.952  87.836  1.00            
ATOM   2076  N   MET E  45      56.381 -10.505  84.643  1.00            
ATOM   2077  CA  MET E  45      56.698  -9.085  84.723  1.00            
ATOM   2078  C   MET E  45      56.940  -8.644  86.168  1.00            
ATOM   2079  O   MET E  45      56.153  -8.940  87.066  1.00            
ATOM   2080  CB  MET E  45      55.571  -8.250  84.136  1.00            
ATOM   2081  CG  MET E  45      55.200  -8.646  82.711  1.00            
ATOM   2082  SD  MET E  45      53.814  -7.700  82.035  1.00            
ATOM   2083  CE  MET E  45      52.424  -8.366  82.968  1.00            
ATOM   2084  N   ALA E  46      58.054  -7.966  86.382  1.00            
ATOM   2085  CA  ALA E  46      58.312  -7.307  87.649  1.00            
ATOM   2086  C   ALA E  46      57.372  -6.110  87.780  1.00            
ATOM   2087  O   ALA E  46      56.920  -5.559  86.774  1.00            
ATOM   2088  CB  ALA E  46      59.761  -6.881  87.738  1.00            
ATOM   2089  N   LYS E  47      57.060  -5.723  89.014  1.00            
ATOM   2090  CA  LYS E  47      56.123  -4.623  89.268  1.00            
ATOM   2091  C   LYS E  47      56.562  -3.272  88.697  1.00            
ATOM   2092  O   LYS E  47      55.722  -2.440  88.375  1.00            
ATOM   2093  CB  LYS E  47      55.838  -4.501  90.761  1.00            
ATOM   2094  CG  LYS E  47      54.872  -5.563  91.245  1.00            
ATOM   2095  CD  LYS E  47      54.551  -5.418  92.718  1.00            
ATOM   2096  CE  LYS E  47      53.546  -6.481  93.119  1.00            
ATOM   2097  NZ  LYS E  47      54.181  -7.829  93.176  1.00            
ATOM   2098  N   GLY E  48      57.860  -3.027  88.609  1.00            
ATOM   2099  CA  GLY E  48      58.336  -1.779  88.035  1.00            
ATOM   2100  C   GLY E  48      58.414  -1.789  86.507  1.00            
ATOM   2101  O   GLY E  48      58.924  -0.846  85.900  1.00            
ATOM   2102  N   HIS E  49      57.942  -2.863  85.885  1.00            
ATOM   2103  CA  HIS E  49      58.079  -3.038  84.433  1.00            
ATOM   2104  C   HIS E  49      56.746  -3.098  83.703  1.00            
ATOM   2105  O   HIS E  49      56.705  -3.307  82.500  1.00            
ATOM   2106  CB  HIS E  49      58.876  -4.311  84.135  1.00            
ATOM   2107  CG  HIS E  49      60.318  -4.225  84.530  1.00            
ATOM   2108  ND1 HIS E  49      61.175  -5.303  84.460  1.00            
ATOM   2109  CD2 HIS E  49      61.054  -3.192  85.009  1.00            
ATOM   2110  CE1 HIS E  49      62.375  -4.940  84.881  1.00            
ATOM   2111  NE2 HIS E  49      62.327  -3.666  85.225  1.00            
ATOM   2112  N   PHE E  50      55.653  -2.927  84.427  1.00            
ATOM   2113  CA  PHE E  50      54.341  -3.009  83.798  1.00            
ATOM   2114  C   PHE E  50      53.533  -1.757  84.083  1.00            
ATOM   2115  O   PHE E  50      53.254  -1.421  85.234  1.00            
ATOM   2116  CB  PHE E  50      53.612  -4.267  84.279  1.00            
ATOM   2117  CG  PHE E  50      52.267  -4.471  83.660  1.00            
ATOM   2118  CD1 PHE E  50      52.100  -4.428  82.283  1.00            
ATOM   2119  CD2 PHE E  50      51.162  -4.718  84.458  1.00            
ATOM   2120  CE1 PHE E  50      50.847  -4.615  81.715  1.00            
ATOM   2121  CE2 PHE E  50      49.912  -4.914  83.895  1.00            
ATOM   2122  CZ  PHE E  50      49.757  -4.865  82.521  1.00            
ATOM   2123  N   GLY E  51      53.168  -1.053  83.019  1.00            
ATOM   2124  CA  GLY E  51      52.439   0.186  83.152  1.00            
ATOM   2125  C   GLY E  51      51.027   0.109  82.606  1.00            
ATOM   2126  O   GLY E  51      50.778  -0.477  81.539  1.00            
ATOM   2127  N   ILE E  52      50.110   0.718  83.352  1.00            
ATOM   2128  CA  ILE E  52      48.731   0.918  82.926  1.00            
ATOM   2129  C   ILE E  52      48.411   2.408  83.019  1.00            
ATOM   2130  O   ILE E  52      48.549   3.010  84.076  1.00            
ATOM   2131  CB  ILE E  52      47.734   0.121  83.795  1.00            
ATOM   2132  CG1 ILE E  52      48.045  -1.376  83.753  1.00            
ATOM   2133  CG2 ILE E  52      46.308   0.385  83.343  1.00            
ATOM   2134  CD1 ILE E  52      47.228  -2.199  84.740  1.00            
ATOM   2135  N   GLY E  53      48.008   3.016  81.914  1.00            
ATOM   2136  CA  GLY E  53      47.700   4.436  81.928  1.00            
ATOM   2137  C   GLY E  53      48.890   5.326  82.261  1.00            
ATOM   2138  O   GLY E  53      48.711   6.431  82.762  1.00            
ATOM   2139  N   GLY E  54      50.105   4.850  81.992  1.00            
ATOM   2140  CA  GLY E  54      51.296   5.647  82.220  1.00            
ATOM   2141  C   GLY E  54      51.839   5.552  83.635  1.00            
ATOM   2142  O   GLY E  54      52.861   6.158  83.963  1.00            
ATOM   2143  N   GLU E  55      51.139   4.808  84.483  1.00            
ATOM   2144  CA  GLU E  55      51.558   4.627  85.863  1.00            
ATOM   2145  C   GLU E  55      51.824   3.148  86.095  1.00            
ATOM   2146  O   GLU E  55      51.241   2.302  85.417  1.00            
ATOM   2147  CB  GLU E  55      50.485   5.160  86.811  1.00            
ATOM   2148  CG  GLU E  55      50.857   5.159  88.278  1.00            
ATOM   2149  CD  GLU E  55      49.740   5.699  89.150  1.00            
ATOM   2150  OE1 GLU E  55      48.672   6.037  88.594  1.00            
ATOM   2151  OE2 GLU E  55      49.940   5.810  90.382  1.00            
ATOM   2152  N   LEU E  56      52.699   2.824  87.043  1.00            
ATOM   2153  CA  LEU E  56      52.962   1.425  87.347  1.00            
ATOM   2154  C   LEU E  56      51.681   0.774  87.862  1.00            
ATOM   2155  O   LEU E  56      50.929   1.389  88.614  1.00            
ATOM   2156  CB  LEU E  56      54.080   1.302  88.383  1.00            
ATOM   2157  CG  LEU E  56      55.440   1.877  87.980  1.00            
ATOM   2158  CD1 LEU E  56      56.437   1.711  89.113  1.00            
ATOM   2159  CD2 LEU E  56      55.959   1.200  86.732  1.00            
ATOM   2160  N   ALA E  57      51.456  -0.479  87.474  1.00            
ATOM   2161  CA  ALA E  57      50.271  -1.217  87.895  1.00            
ATOM   2162  C   ALA E  57      50.347  -1.628  89.363  1.00            
ATOM   2163  O   ALA E  57      51.385  -2.088  89.840  1.00            
ATOM   2164  CB  ALA E  57      50.067  -2.446  87.000  1.00            
TER    2165      ALA E  57                                                      
ATOM   2166  N   PRO F   1      46.782 -10.146  82.901  1.00            
ATOM   2167  CA  PRO F   1      47.581 -11.009  82.031  1.00            
ATOM   2168  C   PRO F   1      47.331 -10.689  80.551  1.00            
ATOM   2169  O   PRO F   1      46.217 -10.322  80.164  1.00            
ATOM   2170  CB  PRO F   1      47.088 -12.421  82.367  1.00            
ATOM   2171  CG  PRO F   1      46.475 -12.326  83.692  1.00            
ATOM   2172  CD  PRO F   1      45.993 -10.915  83.875  1.00            
ATOM   2173  N   ILE F   2      48.381 -10.793  79.751  1.00            
ATOM   2174  CA  ILE F   2      48.316 -10.541  78.325  1.00            
ATOM   2175  C   ILE F   2      48.841 -11.770  77.602  1.00            
ATOM   2176  O   ILE F   2      49.949 -12.231  77.888  1.00            
ATOM   2177  CB  ILE F   2      49.116  -9.293  77.917  1.00            
ATOM   2178  CG1 ILE F   2      48.490  -8.037  78.533  1.00            
ATOM   2179  CG2 ILE F   2      49.112  -9.124  76.397  1.00            
ATOM   2180  CD1 ILE F   2      49.350  -6.780  78.427  1.00            
ATOM   2181  N   ALA F   3      48.008 -12.342  76.731  1.00            
ATOM   2182  CA  ALA F   3      48.376 -13.531  75.954  1.00            
ATOM   2183  C   ALA F   3      48.454 -13.231  74.448  1.00            
ATOM   2184  O   ALA F   3      47.507 -12.685  73.874  1.00            
ATOM   2185  CB  ALA F   3      47.383 -14.667  76.211  1.00            
ATOM   2186  N   GLN F   4      49.579 -13.563  73.819  1.00            
ATOM   2187  CA  GLN F   4      49.679 -13.496  72.349  1.00            
ATOM   2188  C   GLN F   4      49.786 -14.916  71.854  1.00            
ATOM   2189  O   GLN F   4      50.675 -15.664  72.268  1.00            
ATOM   2190  CB  GLN F   4      50.870 -12.651  71.883  1.00            
ATOM   2191  CG  GLN F   4      50.894 -12.420  70.355  1.00            
ATOM   2192  CD  GLN F   4      52.053 -11.555  69.860  1.00            
ATOM   2193  OE1 GLN F   4      52.940 -11.151  70.625  1.00            
ATOM   2194  NE2 GLN F   4      52.047 -11.271  68.564  1.00            
ATOM   2195  N   ILE F   5      48.848 -15.315  71.000  1.00            
ATOM   2196  CA  ILE F   5      48.806 -16.669  70.494  1.00            
ATOM   2197  C   ILE F   5      49.035 -16.675  68.971  1.00            
ATOM   2198  O   ILE F   5      48.264 -16.074  68.213  1.00            
ATOM   2199  CB  ILE F   5      47.449 -17.357  70.818  1.00            
ATOM   2200  CG1 ILE F   5      47.072 -17.157  72.293  1.00            
ATOM   2201  CG2 ILE F   5      47.499 -18.837  70.466  1.00            
ATOM   2202  CD1 ILE F   5      45.720 -17.757  72.683  1.00            
ATOM   2203  N   HIS F   6      50.109 -17.335  68.546  1.00            
ATOM   2204  CA  HIS F   6      50.389 -17.539  67.134  1.00            
ATOM   2205  C   HIS F   6      49.705 -18.805  66.629  1.00            
ATOM   2206  O   HIS F   6      49.904 -19.890  67.167  1.00            
ATOM   2207  CB  HIS F   6      51.896 -17.607  66.874  1.00            
ATOM   2208  CG  HIS F   6      52.557 -16.270  66.881  1.00            
ATOM   2209  ND1 HIS F   6      52.766 -15.545  65.725  1.00            
ATOM   2210  CD2 HIS F   6      53.025 -15.509  67.896  1.00            
ATOM   2211  CE1 HIS F   6      53.345 -14.399  66.030  1.00            
ATOM   2212  NE2 HIS F   6      53.516 -14.354  67.340  1.00            
ATOM   2213  N   ILE F   7      48.870 -18.643  65.607  1.00            
ATOM   2214  CA  ILE F   7      48.147 -19.762  65.039  1.00            
ATOM   2215  C   ILE F   7      48.282 -19.733  63.510  1.00            
ATOM   2216  O   ILE F   7      48.570 -18.687  62.919  1.00            
ATOM   2217  CB  ILE F   7      46.661 -19.723  65.447  1.00            
ATOM   2218  CG1 ILE F   7      45.978 -18.498  64.838  1.00            
ATOM   2219  CG2 ILE F   7      46.518 -19.703  66.984  1.00            
ATOM   2220  CD1 ILE F   7      44.467 -18.472  65.033  1.00            
ATOM   2221  N   LEU F   8      48.113 -20.882  62.872  1.00            
ATOM   2222  CA  LEU F   8      48.173 -20.912  61.416  1.00            
ATOM   2223  C   LEU F   8      46.916 -20.261  60.827  1.00            
ATOM   2224  O   LEU F   8      45.825 -20.424  61.367  1.00            
ATOM   2225  CB  LEU F   8      48.332 -22.345  60.923  1.00            
ATOM   2226  CG  LEU F   8      49.761 -22.825  61.169  1.00            
ATOM   2227  CD1 LEU F   8      49.876 -24.320  60.949  1.00            
ATOM   2228  CD2 LEU F   8      50.745 -22.042  60.310  1.00            
ATOM   2229  N   GLU F   9      47.061 -19.521  59.734  1.00            
ATOM   2230  CA  GLU F   9      45.878 -18.925  59.101  1.00            
ATOM   2231  C   GLU F   9      44.906 -19.995  58.596  1.00            
ATOM   2232  O   GLU F   9      45.297 -21.127  58.336  1.00            
ATOM   2233  CB  GLU F   9      46.275 -17.992  57.955  1.00            
ATOM   2234  CG  GLU F   9      46.831 -18.689  56.738  1.00            
ATOM   2235  CD  GLU F   9      47.228 -17.711  55.644  1.00            
ATOM   2236  OE1 GLU F   9      46.925 -16.506  55.783  1.00            
ATOM   2237  OE2 GLU F   9      47.836 -18.153  54.646  1.00            
ATOM   2238  N   GLY F  10      43.636 -19.623  58.460  1.00            
ATOM   2239  CA  GLY F  10      42.632 -20.497  57.877  1.00            
ATOM   2240  C   GLY F  10      41.399 -20.768  58.728  1.00            
ATOM   2241  O   GLY F  10      40.432 -21.357  58.249  1.00            
ATOM   2242  N   ARG F  11      41.520 -20.536  60.026  1.00            
ATOM   2243  CA AARG F  11      40.238 -20.521  60.843  0.50            
ATOM   2244  CA BARG F  11      40.271 -20.542  60.815  0.50            
ATOM   2245  C   ARG F  11      39.213 -19.285  60.632  1.00            
ATOM   2246  O   ARG F  11      39.453 -18.100  60.235  1.00            
ATOM   2247  CB AARG F  11      40.634 -20.587  62.320  0.50            
ATOM   2248  CB BARG F  11      40.600 -20.653  62.276  0.50            
ATOM   2249  CG AARG F  11      40.969 -21.988  62.822  0.50            
ATOM   2250  CG BARG F  11      41.753 -21.555  62.579  0.50            
ATOM   2251  CD AARG F  11      42.364 -22.429  62.411  0.50            
ATOM   2252  CD BARG F  11      41.327 -22.946  62.361  0.50            
ATOM   2253  NE AARG F  11      42.803 -23.572  63.205  0.50            
ATOM   2254  NE BARG F  11      41.504 -23.332  60.959  0.50            
ATOM   2255  CZ AARG F  11      44.058 -23.783  63.585  0.50            
ATOM   2256  CZ BARG F  11      40.635 -24.026  60.250  0.50            
ATOM   2257  NH1AARG F  11      45.015 -22.931  63.236  0.50            
ATOM   2258  NH1BARG F  11      39.496 -24.401  60.783  0.50            
ATOM   2259  NH2AARG F  11      44.358 -24.849  64.311  0.50            
ATOM   2260  NH2BARG F  11      40.919 -24.355  59.013  0.50            
ATOM   2261  N   SER F  12      37.955 -19.671  60.887  1.00            
ATOM   2262  CA  SER F  12      36.882 -18.683  60.709  1.00            
ATOM   2263  C   SER F  12      36.890 -17.647  61.829  1.00            
ATOM   2264  O   SER F  12      37.539 -17.862  62.856  1.00            
ATOM   2265  CB  SER F  12      35.516 -19.362  60.676  1.00            
ATOM   2266  OG  SER F  12      35.197 -19.891  61.954  1.00            
ATOM   2267  N   ASP F  13      36.163 -16.539  61.649  1.00            
ATOM   2268  CA  ASP F  13      36.067 -15.526  62.704  1.00            
ATOM   2269  C   ASP F  13      35.480 -16.147  63.972  1.00            
ATOM   2270  O   ASP F  13      35.937 -15.875  65.092  1.00            
ATOM   2271  CB  ASP F  13      35.178 -14.338  62.297  1.00            
ATOM   2272  CG  ASP F  13      35.858 -13.370  61.332  1.00            
ATOM   2273  OD1 ASP F  13      37.020 -13.598  60.933  1.00            
ATOM   2274  OD2 ASP F  13      35.229 -12.341  60.997  1.00            
ATOM   2275  N   GLU F  14      34.490 -17.007  63.761  1.00            
ATOM   2276  CA  GLU F  14      33.738 -17.666  64.819  1.00            
ATOM   2277  C   GLU F  14      34.678 -18.540  65.646  1.00            
ATOM   2278  O   GLU F  14      34.634 -18.537  66.879  1.00            
ATOM   2279  CB  GLU F  14      32.632 -18.517  64.177  1.00            
ATOM   2280  CG  GLU F  14      31.657 -19.242  65.095  1.00            
ATOM   2281  CD  GLU F  14      30.737 -18.303  65.855  1.00            
ATOM   2282  OE1 GLU F  14      30.680 -17.106  65.496  1.00            
ATOM   2283  OE2 GLU F  14      30.028 -18.769  66.778  1.00            
ATOM   2284  N   GLN F  15      35.544 -19.272  64.954  1.00            
ATOM   2285  CA  GLN F  15      36.509 -20.134  65.621  1.00            
ATOM   2286  C   GLN F  15      37.500 -19.331  66.446  1.00            
ATOM   2287  O   GLN F  15      37.849 -19.729  67.563  1.00            
ATOM   2288  CB  GLN F  15      37.277 -20.976  64.613  1.00            
ATOM   2289  CG  GLN F  15      36.672 -22.320  64.273  1.00            
ATOM   2290  CD  GLN F  15      37.534 -23.062  63.271  1.00            
ATOM   2291  OE1 GLN F  15      37.705 -22.623  62.127  1.00            
ATOM   2292  NE2 GLN F  15      38.122 -24.171  63.710  1.00            
ATOM   2293  N   LYS F  16      37.950 -18.197  65.908  1.00            
ATOM   2294  CA  LYS F  16      38.900 -17.341  66.638  1.00            
ATOM   2295  C   LYS F  16      38.207 -16.649  67.802  1.00            
ATOM   2296  O   LYS F  16      38.837 -16.350  68.825  1.00            
ATOM   2297  CB  LYS F  16      39.576 -16.329  65.711  1.00            
ATOM   2298  CG  LYS F  16      40.560 -16.997  64.755  1.00            
ATOM   2299  CD  LYS F  16      41.279 -16.001  63.873  1.00            
ATOM   2300  CE  LYS F  16      40.514 -15.838  62.549  1.00            
ATOM   2301  NZ  LYS F  16      41.246 -14.990  61.554  1.00            
ATOM   2302  N   GLU F  17      36.921 -16.369  67.638  1.00            
ATOM   2303  CA  GLU F  17      36.121 -15.847  68.738  1.00            
ATOM   2304  C   GLU F  17      36.071 -16.853  69.889  1.00            
ATOM   2305  O   GLU F  17      36.226 -16.501  71.058  1.00            
ATOM   2306  CB  GLU F  17      34.699 -15.570  68.266  1.00            
ATOM   2307  CG  GLU F  17      33.822 -14.932  69.302  1.00            
ATOM   2308  CD  GLU F  17      32.394 -14.829  68.831  1.00            
ATOM   2309  OE1 GLU F  17      32.166 -14.936  67.605  1.00            
ATOM   2310  OE2 GLU F  17      31.501 -14.674  69.688  1.00            
ATOM   2311  N   THR F  18      35.864 -18.117  69.545  1.00            
ATOM   2312  CA  THR F  18      35.841 -19.167  70.549  1.00            
ATOM   2313  C   THR F  18      37.193 -19.306  71.228  1.00            
ATOM   2314  O   THR F  18      37.266 -19.467  72.448  1.00            
ATOM   2315  CB  THR F  18      35.423 -20.515  69.941  1.00            
ATOM   2316  OG1 THR F  18      34.098 -20.394  69.416  1.00            
ATOM   2317  CG2 THR F  18      35.446 -21.609  70.990  1.00            
ATOM   2318  N   LEU F  19      38.262 -19.240  70.445  1.00            
ATOM   2319  CA  LEU F  19      39.613 -19.338  70.995  1.00            
ATOM   2320  C   LEU F  19      39.897 -18.262  72.044  1.00            
ATOM   2321  O   LEU F  19      40.454 -18.559  73.104  1.00            
ATOM   2322  CB  LEU F  19      40.652 -19.270  69.874  1.00            
ATOM   2323  CG  LEU F  19      42.137 -19.203  70.230  1.00            
ATOM   2324  CD1 LEU F  19      42.639 -20.483  70.936  1.00            
ATOM   2325  CD2 LEU F  19      42.939 -18.944  68.970  1.00            
ATOM   2326  N   ILE F  20      39.530 -17.020  71.746  1.00            
ATOM   2327  CA  ILE F  20      39.762 -15.909  72.665  1.00            
ATOM   2328  C   ILE F  20      39.018 -16.094  73.978  1.00            
ATOM   2329  O   ILE F  20      39.588 -15.885  75.056  1.00            
ATOM   2330  CB  ILE F  20      39.351 -14.567  72.026  1.00            
ATOM   2331  CG1 ILE F  20      40.385 -14.132  70.985  1.00            
ATOM   2332  CG2 ILE F  20      39.163 -13.489  73.080  1.00            
ATOM   2333  CD1 ILE F  20      39.930 -12.939  70.119  1.00            
ATOM   2334  N   ARG F  21      37.751 -16.494  73.891  1.00            
ATOM   2335  CA  ARG F  21      36.957 -16.696  75.095  1.00            
ATOM   2336  C   ARG F  21      37.492 -17.849  75.931  1.00            
ATOM   2337  O   ARG F  21      37.671 -17.708  77.142  1.00            
ATOM   2338  CB  ARG F  21      35.495 -16.962  74.755  1.00            
ATOM   2339  CG  ARG F  21      34.607 -17.065  75.987  1.00            
ATOM   2340  CD  ARG F  21      33.174 -17.408  75.610  1.00            
ATOM   2341  NE  ARG F  21      32.707 -16.485  74.588  1.00            
ATOM   2342  CZ  ARG F  21      32.552 -16.815  73.309  1.00            
ATOM   2343  NH1 ARG F  21      32.807 -18.056  72.908  1.00            
ATOM   2344  NH2 ARG F  21      32.142 -15.905  72.439  1.00            
ATOM   2345  N   GLU F  22      37.765 -18.981  75.289  1.00            
ATOM   2346  CA  GLU F  22      38.194 -20.169  76.022  1.00            
ATOM   2347  C   GLU F  22      39.550 -19.995  76.694  1.00            
ATOM   2348  O   GLU F  22      39.739 -20.430  77.835  1.00            
ATOM   2349  CB  GLU F  22      38.229 -21.382  75.092  1.00            
ATOM   2350  CG  GLU F  22      36.841 -21.810  74.647  1.00            
ATOM   2351  CD  GLU F  22      36.057 -22.394  75.802  1.00            
ATOM   2352  OE1 GLU F  22      36.701 -22.967  76.714  1.00            
ATOM   2353  OE2 GLU F  22      34.819 -22.241  75.834  1.00            
ATOM   2354  N   VAL F  23      40.476 -19.349  75.998  1.00            
ATOM   2355  CA  VAL F  23      41.788 -19.106  76.554  1.00            
ATOM   2356  C   VAL F  23      41.717 -18.093  77.696  1.00            
ATOM   2357  O   VAL F  23      42.333 -18.300  78.748  1.00            
ATOM   2358  CB  VAL F  23      42.759 -18.617  75.478  1.00            
ATOM   2359  CG1 VAL F  23      43.980 -17.983  76.112  1.00            
ATOM   2360  CG2 VAL F  23      43.149 -19.767  74.559  1.00            
ATOM   2361  N   SER F  24      40.918 -17.042  77.510  1.00            
ATOM   2362  CA  SER F  24      40.744 -16.002  78.521  1.00            
ATOM   2363  C   SER F  24      40.153 -16.562  79.792  1.00            
ATOM   2364  O   SER F  24      40.535 -16.154  80.894  1.00            
ATOM   2365  CB  SER F  24      39.859 -14.866  78.016  1.00            
ATOM   2366  OG  SER F  24      40.491 -14.155  76.971  1.00            
ATOM   2367  N   GLU F  25      39.180 -17.454  79.641  1.00            
ATOM   2368  CA  GLU F  25      38.583 -18.108  80.799  1.00            
ATOM   2369  C   GLU F  25      39.604 -19.043  81.449  1.00            
ATOM   2370  O   GLU F  25      39.648 -19.188  82.678  1.00            
ATOM   2371  CB  GLU F  25      37.308 -18.853  80.396  1.00            
ATOM   2372  CG  GLU F  25      36.187 -17.912  79.987  1.00            
ATOM   2373  CD  GLU F  25      34.922 -18.636  79.556  1.00            
ATOM   2374  OE1 GLU F  25      33.885 -17.962  79.374  1.00            
ATOM   2375  OE2 GLU F  25      34.966 -19.871  79.371  1.00            
ATOM   2376  N   ALA F  26      40.406 -19.712  80.628  1.00            
ATOM   2377  CA  ALA F  26      41.441 -20.597  81.163  1.00            
ATOM   2378  C   ALA F  26      42.466 -19.837  82.029  1.00            
ATOM   2379  O   ALA F  26      42.898 -20.335  83.069  1.00            
ATOM   2380  CB  ALA F  26      42.153 -21.324  80.031  1.00            
ATOM   2381  N   ILE F  27      42.876 -18.660  81.566  1.00            
ATOM   2382  CA  ILE F  27      43.827 -17.810  82.279  1.00            
ATOM   2383  C   ILE F  27      43.248 -17.307  83.603  1.00            
ATOM   2384  O   ILE F  27      43.911 -17.348  84.636  1.00            
ATOM   2385  CB  ILE F  27      44.243 -16.631  81.393  1.00            
ATOM   2386  CG1 ILE F  27      45.007 -17.156  80.177  1.00            
ATOM   2387  CG2 ILE F  27      45.055 -15.590  82.184  1.00            
ATOM   2388  CD1 ILE F  27      45.302 -16.083  79.121  1.00            
ATOM   2389  N   SER F  28      42.000 -16.848  83.553  1.00            
ATOM   2390  CA  SER F  28      41.282 -16.363  84.724  1.00            
ATOM   2391  C   SER F  28      41.163 -17.436  85.811  1.00            
ATOM   2392  O   SER F  28      41.440 -17.182  86.997  1.00            
ATOM   2393  CB  SER F  28      39.893 -15.877  84.312  1.00            
ATOM   2394  OG  SER F  28      39.179 -15.379  85.429  1.00            
ATOM   2395  N   ARG F  29      40.758 -18.631  85.393  1.00            
ATOM   2396  CA  ARG F  29      40.584 -19.771  86.290  1.00            
ATOM   2397  C   ARG F  29      41.904 -20.264  86.883  1.00            
ATOM   2398  O   ARG F  29      42.003 -20.512  88.080  1.00            
ATOM   2399  CB  ARG F  29      39.912 -20.924  85.538  1.00            
ATOM   2400  CG  ARG F  29      38.435 -20.729  85.250  1.00            
ATOM   2401  CD  ARG F  29      37.828 -21.962  84.566  1.00            
ATOM   2402  NE  ARG F  29      38.254 -22.165  83.179  1.00            
ATOM   2403  CZ  ARG F  29      39.156 -23.061  82.786  1.00            
ATOM   2404  NH1 ARG F  29      39.769 -23.829  83.678  1.00            
ATOM   2405  NH2 ARG F  29      39.458 -23.180  81.500  1.00            
ATOM   2406  N   SER F  30      42.917 -20.400  86.035  1.00            
ATOM   2407  CA  SER F  30      44.201 -20.952  86.450  1.00            
ATOM   2408  C   SER F  30      44.903 -20.070  87.471  1.00            
ATOM   2409  O   SER F  30      45.527 -20.571  88.419  1.00            
ATOM   2410  CB  SER F  30      45.122 -21.127  85.234  1.00            
ATOM   2411  OG  SER F  30      44.595 -22.067  84.318  1.00            
ATOM   2412  N   LEU F  31      44.756 -18.759  87.291  1.00            
ATOM   2413  CA  LEU F  31      45.509 -17.767  88.055  1.00            
ATOM   2414  C   LEU F  31      44.697 -17.024  89.093  1.00            
ATOM   2415  O   LEU F  31      45.234 -16.162  89.800  1.00            
ATOM   2416  CB  LEU F  31      46.114 -16.745  87.098  1.00            
ATOM   2417  CG  LEU F  31      47.061 -17.256  86.016  1.00            
ATOM   2418  CD1 LEU F  31      47.579 -16.082  85.220  1.00            
ATOM   2419  CD2 LEU F  31      48.204 -18.000  86.653  1.00            
ATOM   2420  N   ASP F  32      43.407 -17.345  89.178  1.00            
ATOM   2421  CA  ASP F  32      42.484 -16.595  90.028  1.00            
ATOM   2422  C   ASP F  32      42.550 -15.095  89.750  1.00            
ATOM   2423  O   ASP F  32      42.523 -14.287  90.664  1.00            
ATOM   2424  CB  ASP F  32      42.779 -16.898  91.493  1.00            
ATOM   2425  CG  ASP F  32      42.290 -18.271  91.900  1.00            
ATOM   2426  OD1 ASP F  32      41.235 -18.696  91.389  1.00            
ATOM   2427  OD2 ASP F  32      42.996 -18.962  92.655  1.00            
ATOM   2428  N   ALA F  33      42.609 -14.738  88.469  1.00            
ATOM   2429  CA  ALA F  33      42.653 -13.341  88.048  1.00            
ATOM   2430  C   ALA F  33      41.294 -12.907  87.503  1.00            
ATOM   2431  O   ALA F  33      40.594 -13.707  86.882  1.00            
ATOM   2432  CB  ALA F  33      43.749 -13.131  86.983  1.00            
ATOM   2433  N   PRO F  34      40.918 -11.640  87.733  1.00            
ATOM   2434  CA  PRO F  34      39.636 -11.157  87.201  1.00            
ATOM   2435  C   PRO F  34      39.576 -11.310  85.688  1.00            
ATOM   2436  O   PRO F  34      40.541 -10.970  85.004  1.00            
ATOM   2437  CB  PRO F  34      39.615  -9.677  87.605  1.00            
ATOM   2438  CG  PRO F  34      40.550  -9.593  88.782  1.00            
ATOM   2439  CD  PRO F  34      41.616 -10.618  88.533  1.00            
ATOM   2440  N   LEU F  35      38.466 -11.837  85.180  1.00            
ATOM   2441  CA  LEU F  35      38.315 -12.078  83.751  1.00            
ATOM   2442  C   LEU F  35      38.538 -10.815  82.930  1.00            
ATOM   2443  O   LEU F  35      39.114 -10.865  81.835  1.00            
ATOM   2444  CB  LEU F  35      36.935 -12.660  83.454  1.00            
ATOM   2445  CG  LEU F  35      36.660 -12.986  81.988  1.00            
ATOM   2446  CD1 LEU F  35      37.722 -13.909  81.389  1.00            
ATOM   2447  CD2 LEU F  35      35.273 -13.598  81.867  1.00            
ATOM   2448  N   THR F  36      38.078  -9.691  83.470  1.00            
ATOM   2449  CA  THR F  36      38.184  -8.400  82.801  1.00            
ATOM   2450  C   THR F  36      39.631  -7.939  82.623  1.00            
ATOM   2451  O   THR F  36      39.914  -7.078  81.783  1.00            
ATOM   2452  CB  THR F  36      37.419  -7.313  83.578  1.00            
ATOM   2453  OG1 THR F  36      37.942  -7.225  84.908  1.00            
ATOM   2454  CG2 THR F  36      35.929  -7.637  83.632  1.00            
ATOM   2455  N   SER F  37      40.551  -8.531  83.382  1.00            
ATOM   2456  CA  SER F  37      41.951  -8.125  83.312  1.00            
ATOM   2457  C   SER F  37      42.702  -8.900  82.243  1.00            
ATOM   2458  O   SER F  37      43.854  -8.598  81.954  1.00            
ATOM   2459  CB  SER F  37      42.653  -8.343  84.653  1.00            
ATOM   2460  OG  SER F  37      42.838  -9.730  84.887  1.00            
ATOM   2461  N   VAL F  38      42.051  -9.905  81.665  1.00            
ATOM   2462  CA  VAL F  38      42.698 -10.771  80.685  1.00            
ATOM   2463  C   VAL F  38      42.545 -10.259  79.246  1.00            
ATOM   2464  O   VAL F  38      41.428 -10.097  78.757  1.00            
ATOM   2465  CB  VAL F  38      42.126 -12.203  80.773  1.00            
ATOM   2466  CG1 VAL F  38      42.801 -13.114  79.774  1.00            
ATOM   2467  CG2 VAL F  38      42.301 -12.758  82.192  1.00            
ATOM   2468  N   ARG F  39      43.674 -10.049  78.573  1.00            
ATOM   2469  CA  ARG F  39      43.691  -9.653  77.169  1.00            
ATOM   2470  C   ARG F  39      44.383 -10.727  76.340  1.00            
ATOM   2471  O   ARG F  39      45.392 -11.313  76.761  1.00            
ATOM   2472  CB  ARG F  39      44.390  -8.301  76.992  1.00            
ATOM   2473  CG  ARG F  39      43.514  -7.137  77.370  1.00            
ATOM   2474  CD  ARG F  39      44.314  -5.878  77.672  1.00            
ATOM   2475  NE  ARG F  39      43.430  -4.735  77.893  1.00            
ATOM   2476  CZ  ARG F  39      42.673  -4.582  78.977  1.00            
ATOM   2477  NH1 ARG F  39      42.702  -5.490  79.942  1.00            
ATOM   2478  NH2 ARG F  39      41.892  -3.521  79.102  1.00            
ATOM   2479  N   VAL F  40      43.823 -10.992  75.164  1.00            
ATOM   2480  CA  VAL F  40      44.354 -11.989  74.251  1.00            
ATOM   2481  C   VAL F  40      44.535 -11.392  72.844  1.00            
ATOM   2482  O   VAL F  40      43.618 -10.761  72.307  1.00            
ATOM   2483  CB  VAL F  40      43.428 -13.223  74.166  1.00            
ATOM   2484  CG1 VAL F  40      43.914 -14.183  73.087  1.00            
ATOM   2485  CG2 VAL F  40      43.331 -13.915  75.505  1.00            
ATOM   2486  N   ILE F  41      45.727 -11.572  72.277  1.00            
ATOM   2487  CA  ILE F  41      46.020 -11.148  70.912  1.00            
ATOM   2488  C   ILE F  41      46.224 -12.383  70.061  1.00            
ATOM   2489  O   ILE F  41      47.072 -13.214  70.381  1.00            
ATOM   2490  CB  ILE F  41      47.303 -10.289  70.810  1.00            
ATOM   2491  CG1 ILE F  41      47.226  -9.039  71.679  1.00            
ATOM   2492  CG2 ILE F  41      47.596  -9.920  69.355  1.00            
ATOM   2493  CD1 ILE F  41      48.573  -8.322  71.780  1.00            
ATOM   2494  N   ILE F  42      45.452 -12.509  68.983  1.00            
ATOM   2495  CA  ILE F  42      45.654 -13.599  68.044  1.00            
ATOM   2496  C   ILE F  42      46.522 -13.126  66.877  1.00            
ATOM   2497  O   ILE F  42      46.230 -12.121  66.222  1.00            
ATOM   2498  CB  ILE F  42      44.327 -14.137  67.489  1.00            
ATOM   2499  CG1 ILE F  42      43.417 -14.613  68.615  1.00            
ATOM   2500  CG2 ILE F  42      44.593 -15.268  66.504  1.00            
ATOM   2501  CD1 ILE F  42      42.102 -15.152  68.113  1.00            
ATOM   2502  N   THR F  43      47.600 -13.845  66.625  1.00            
ATOM   2503  CA  THR F  43      48.455 -13.506  65.502  1.00            
ATOM   2504  C   THR F  43      48.471 -14.678  64.522  1.00            
ATOM   2505  O   THR F  43      48.867 -15.799  64.853  1.00            
ATOM   2506  CB  THR F  43      49.880 -13.169  65.945  1.00            
ATOM   2507  OG1 THR F  43      49.836 -12.196  66.999  1.00            
ATOM   2508  CG2 THR F  43      50.680 -12.621  64.767  1.00            
ATOM   2509  N   GLU F  44      47.973 -14.427  63.321  1.00            
ATOM   2510  CA  GLU F  44      47.933 -15.462  62.298  1.00            
ATOM   2511  C   GLU F  44      49.251 -15.604  61.540  1.00            
ATOM   2512  O   GLU F  44      49.861 -14.618  61.156  1.00            
ATOM   2513  CB  GLU F  44      46.793 -15.168  61.328  1.00            
ATOM   2514  CG  GLU F  44      45.441 -15.411  61.954  1.00            
ATOM   2515  CD  GLU F  44      44.297 -15.320  60.963  1.00            
ATOM   2516  OE1 GLU F  44      44.251 -14.354  60.165  1.00            
ATOM   2517  OE2 GLU F  44      43.444 -16.231  60.990  1.00            
ATOM   2518  N   MET F  45      49.667 -16.843  61.309  1.00            
ATOM   2519  CA  MET F  45      50.850 -17.112  60.489  1.00            
ATOM   2520  C   MET F  45      50.477 -17.694  59.140  1.00            
ATOM   2521  O   MET F  45      49.754 -18.680  59.066  1.00            
ATOM   2522  CB  MET F  45      51.797 -18.083  61.199  1.00            
ATOM   2523  CG  MET F  45      52.268 -17.622  62.550  1.00            
ATOM   2524  SD  MET F  45      53.318 -18.867  63.315  1.00            
ATOM   2525  CE  MET F  45      52.163 -20.126  63.835  1.00            
ATOM   2526  N   ALA F  46      50.990 -17.091  58.073  1.00            
ATOM   2527  CA  ALA F  46      50.855 -17.651  56.725  1.00            
ATOM   2528  C   ALA F  46      51.699 -18.922  56.596  1.00            
ATOM   2529  O   ALA F  46      52.678 -19.100  57.329  1.00            
ATOM   2530  CB  ALA F  46      51.260 -16.629  55.668  1.00            
ATOM   2531  N   LYS F  47      51.315 -19.799  55.675  1.00            
ATOM   2532  CA  LYS F  47      51.990 -21.079  55.501  1.00            
ATOM   2533  C   LYS F  47      53.472 -20.944  55.163  1.00            
ATOM   2534  O   LYS F  47      54.274 -21.810  55.497  1.00            
ATOM   2535  CB  LYS F  47      51.299 -21.902  54.419  1.00            
ATOM   2536  CG  LYS F  47      49.987 -22.519  54.878  1.00            
ATOM   2537  CD  LYS F  47      49.360 -23.384  53.782  1.00            
ATOM   2538  CE  LYS F  47      48.061 -24.022  54.271  1.00            
ATOM   2539  NZ  LYS F  47      48.321 -25.217  55.126  1.00            
ATOM   2540  N   GLY F  48      53.824 -19.879  54.459  1.00            
ATOM   2541  CA  GLY F  48      55.212 -19.657  54.091  1.00            
ATOM   2542  C   GLY F  48      56.031 -18.972  55.168  1.00            
ATOM   2543  O   GLY F  48      57.196 -18.668  54.944  1.00            
ATOM   2544  N   HIS F  49      55.430 -18.747  56.335  1.00            
ATOM   2545  CA  HIS F  49      56.074 -17.970  57.394  1.00            
ATOM   2546  C   HIS F  49      56.343 -18.750  58.675  1.00            
ATOM   2547  O   HIS F  49      56.775 -18.176  59.685  1.00            
ATOM   2548  CB  HIS F  49      55.222 -16.752  57.743  1.00            
ATOM   2549  CG  HIS F  49      55.199 -15.705  56.674  1.00            
ATOM   2550  ND1 HIS F  49      54.416 -14.576  56.762  1.00            
ATOM   2551  CD2 HIS F  49      55.862 -15.616  55.498  1.00            
ATOM   2552  CE1 HIS F  49      54.591 -13.837  55.679  1.00            
ATOM   2553  NE2 HIS F  49      55.470 -14.443  54.898  1.00            
ATOM   2554  N   PHE F  50      56.034 -20.035  58.667  1.00            
ATOM   2555  CA  PHE F  50      56.225 -20.849  59.855  1.00            
ATOM   2556  C   PHE F  50      57.018 -22.091  59.518  1.00            
ATOM   2557  O   PHE F  50      56.627 -22.900  58.668  1.00            
ATOM   2558  CB  PHE F  50      54.871 -21.190  60.516  1.00            
ATOM   2559  CG  PHE F  50      54.990 -22.009  61.782  1.00            
ATOM   2560  CD1 PHE F  50      55.869 -21.634  62.800  1.00            
ATOM   2561  CD2 PHE F  50      54.201 -23.133  61.972  1.00            
ATOM   2562  CE1 PHE F  50      55.967 -22.390  63.961  1.00            
ATOM   2563  CE2 PHE F  50      54.293 -23.883  63.138  1.00            
ATOM   2564  CZ  PHE F  50      55.184 -23.510  64.125  1.00            
ATOM   2565  N   GLY F  51      58.167 -22.231  60.170  1.00            
ATOM   2566  CA  GLY F  51      59.051 -23.348  59.926  1.00            
ATOM   2567  C   GLY F  51      59.208 -24.251  61.127  1.00            
ATOM   2568  O   GLY F  51      59.246 -23.769  62.258  1.00            
ATOM   2569  N   ILE F  52      59.260 -25.554  60.881  1.00            
ATOM   2570  CA  ILE F  52      59.632 -26.533  61.899  1.00            
ATOM   2571  C   ILE F  52      60.780 -27.346  61.344  1.00            
ATOM   2572  O   ILE F  52      60.681 -27.894  60.264  1.00            
ATOM   2573  CB  ILE F  52      58.498 -27.498  62.293  1.00            
ATOM   2574  CG1 ILE F  52      57.311 -26.748  62.877  1.00            
ATOM   2575  CG2 ILE F  52      59.003 -28.499  63.310  1.00            
ATOM   2576  CD1 ILE F  52      56.104 -27.629  63.100  1.00            
ATOM   2577  N   GLY F  53      61.886 -27.394  62.072  1.00            
ATOM   2578  CA  GLY F  53      63.047 -28.121  61.609  1.00            
ATOM   2579  C   GLY F  53      63.645 -27.553  60.337  1.00            
ATOM   2580  O   GLY F  53      64.290 -28.267  59.580  1.00            
ATOM   2581  N   GLY F  54      63.420 -26.267  60.095  1.00            
ATOM   2582  CA  GLY F  54      64.006 -25.615  58.940  1.00            
ATOM   2583  C   GLY F  54      63.185 -25.772  57.677  1.00            
ATOM   2584  O   GLY F  54      63.555 -25.266  56.614  1.00            
ATOM   2585  N   GLU F  55      62.088 -26.508  57.783  1.00            
ATOM   2586  CA  GLU F  55      61.229 -26.739  56.632  1.00            
ATOM   2587  C   GLU F  55      59.838 -26.183  56.895  1.00            
ATOM   2588  O   GLU F  55      59.422 -26.081  58.048  1.00            
ATOM   2589  CB  GLU F  55      61.158 -28.234  56.311  1.00            
ATOM   2590  CG  GLU F  55      62.499 -28.889  55.983  1.00            
ATOM   2591  CD  GLU F  55      63.209 -28.264  54.791  1.00            
ATOM   2592  OE1 GLU F  55      62.527 -27.883  53.813  1.00            
ATOM   2593  OE2 GLU F  55      64.459 -28.185  54.817  1.00            
ATOM   2594  N   LEU F  56      59.124 -25.810  55.833  1.00            
ATOM   2595  CA  LEU F  56      57.757 -25.320  55.973  1.00            
ATOM   2596  C   LEU F  56      56.822 -26.384  56.509  1.00            
ATOM   2597  O   LEU F  56      57.014 -27.567  56.266  1.00            
ATOM   2598  CB  LEU F  56      57.215 -24.779  54.650  1.00            
ATOM   2599  CG  LEU F  56      57.956 -23.564  54.119  1.00            
ATOM   2600  CD1 LEU F  56      57.334 -23.104  52.832  1.00            
ATOM   2601  CD2 LEU F  56      57.863 -22.477  55.171  1.00            
ATOM   2602  N   ALA F  57      55.815 -25.944  57.258  1.00            
ATOM   2603  CA  ALA F  57      54.807 -26.841  57.810  1.00            
ATOM   2604  C   ALA F  57      53.896 -27.407  56.720  1.00            
ATOM   2605  O   ALA F  57      53.304 -26.667  55.931  1.00            
ATOM   2606  CB  ALA F  57      53.981 -26.113  58.853  1.00            
TER    2607      ALA F  57                                                      
END                                                                             


A second structure was input as follows:


HEADER    ISOMERASE                               16-JUL-15   5CLN              
TITLE     CRYSTAL STRUCTURE OF A 4-OXALOCROTONATE TAUTOMERASE MUTANT AT 2.7     
TITLE    2 ANGSTROM                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-HYDROXYMUCONATE TAUTOMERASE;                             
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 FRAGMENT: UNP RESIDUES 2-58;                                         
COMPND   5 SYNONYM: 4-OXALOCROTONATE TAUTOMERASE,4-OT;                          
COMPND   6 EC: 5.3.2.6;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;                             
SOURCE   3 ORGANISM_TAXID: 303;                                                 
SOURCE   4 GENE: XYLH;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PJEXPRESS 414                             
KEYWDS    4-OXALOCROTONATE TAUTOMERASE, BETA-ALPHA-BETA STRUCTURAL MOTIF,       
KEYWDS   2 TAUTOMERASE SUPERFAMILY, ISOMERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.M.W.H.THUNNISSEN,H.PODDAR                                           
REVDAT   2   16-MAR-16 5CLN    1       JRNL                                     
REVDAT   1   09-MAR-16 5CLN    0                                                
JRNL        AUTH   J.Y.VAN DER MEER,H.PODDAR,B.J.BAAS,Y.MIAO,M.RAHIMI,          
JRNL        AUTH 2 A.KUNZENDORF,R.VAN MERKERK,P.G.TEPPER,E.M.GEERTSEMA,         
JRNL        AUTH 3 A.M.THUNNISSEN,W.J.QUAX,G.J.POELARENDS                       
JRNL        TITL   USING MUTABILITY LANDSCAPES OF A PROMISCUOUS TAUTOMERASE TO  
JRNL        TITL 2 GUIDE THE ENGINEERING OF ENANTIOSELECTIVE MICHAELASES.       
JRNL        REF    NAT COMMUN                    V.   7 10911 2016              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   26952338                                                     
JRNL        DOI    10.1038/NCOMMS10911                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 57.60                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 18170                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.880                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 886                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 57.6308 -  4.9169    0.99     2903   177  0.2180 0.2704        
REMARK   3     2  4.9169 -  3.9029    1.00     2917   140  0.1889 0.2062        
REMARK   3     3  3.9029 -  3.4097    1.00     2912   133  0.2294 0.2563        
REMARK   3     4  3.4097 -  3.0979    1.00     2873   162  0.2563 0.2810        
REMARK   3     5  3.0979 -  2.8759    1.00     2912   127  0.2915 0.3184        
REMARK   3     6  2.8759 -  2.7063    0.97     2767   147  0.2961 0.3246        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.830           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.72                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           5220                                  
REMARK   3   ANGLE     :  0.988           7032                                  
REMARK   3   CHIRALITY :  0.041            852                                  
REMARK   3   PLANARITY :  0.003            900                                  
REMARK   3   DIHEDRAL  : 14.304           1980                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN B                                     
REMARK   3     ATOM PAIRS NUMBER  : 3919                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN C                                     
REMARK   3     ATOM PAIRS NUMBER  : 3919                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN D                                     
REMARK   3     ATOM PAIRS NUMBER  : 3919                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 4                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN E                                     
REMARK   3     ATOM PAIRS NUMBER  : 3919                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 5                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN F                                     
REMARK   3     ATOM PAIRS NUMBER  : 3919                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 6                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN G                                     
REMARK   3     ATOM PAIRS NUMBER  : 3919                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 7                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN H                                     
REMARK   3     ATOM PAIRS NUMBER  : 3919                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 8                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN I                                     
REMARK   3     ATOM PAIRS NUMBER  : 3919                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 9                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN J                                     
REMARK   3     ATOM PAIRS NUMBER  : 3919                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 10                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN K                                     
REMARK   3     ATOM PAIRS NUMBER  : 3919                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 11                                                 
REMARK   3     REFERENCE SELECTION: CHAIN A                                     
REMARK   3     SELECTION          : CHAIN L                                     
REMARK   3     ATOM PAIRS NUMBER  : 3919                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5CLN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211834.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JAN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : HELIOS OPTICS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18204                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.710                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 57.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.14800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 6.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4X19                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.41                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM FORMATE, 0.1 M BIS-TRIS     
REMARK 280  PROPANE, 20% PEG 3350, PH 8.5, VAPOR DIFFUSION, SITTING DROP,       
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       43.58150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       43.62900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       43.58150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       43.62900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 13810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12410 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 14210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -60.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000     -117.44917            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      267.17650            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000     -165.46245            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      178.11767            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J                                     
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000      -43.58150            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000      -43.62900            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L                                     
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000      -43.58150            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000       43.62900            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J                                     
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000     -121.88095            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000      -43.62900            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000      178.11767            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L                                     
REMARK 350   BIOMT1   6 -1.000000  0.000000  0.000000     -121.88095            
REMARK 350   BIOMT2   6  0.000000  1.000000  0.000000       43.62900            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000      178.11767            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -87.25800            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J                                     
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000      -78.29945            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000      -87.25800            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      178.11767            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L                                     
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000      -78.29945            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      178.11767            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K                                     
REMARK 350   BIOMT1   5  1.000000  0.000000  0.000000       43.58150            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000      -43.62900            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K                                     
REMARK 350   BIOMT1   6 -1.000000  0.000000  0.000000     -121.88095            
REMARK 350   BIOMT2   6  0.000000  1.000000  0.000000      -43.62900            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000      178.11767            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13050 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 13990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -48.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -78.29945            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      178.11767            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L                                     
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000       87.25800            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000      -78.29945            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000       87.25800            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      178.11767            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K                                     
REMARK 350   BIOMT1   5  1.000000  0.000000  0.000000       43.58150            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000       43.62900            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   6 -1.000000  0.000000  0.000000     -121.88095            
REMARK 350   BIOMT2   6  0.000000  1.000000  0.000000       43.62900            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000      178.11767            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  32       48.11     39.59                                   
REMARK 500    ASP B  32       48.65     39.80                                   
REMARK 500    ASP C  32       49.27     39.73                                   
REMARK 500    ASP D  32       47.97     39.77                                   
REMARK 500    ASP E  32       49.33     38.12                                   
REMARK 500    ILE E  52      -33.55   -134.84                                   
REMARK 500    LEU H  56      -77.45    -73.86                                   
REMARK 500    ASP J  32       48.67     39.79                                   
REMARK 500    ASP L  32       48.77     39.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5CLN A    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
DBREF  5CLN B    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
DBREF  5CLN C    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
DBREF  5CLN D    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
DBREF  5CLN E    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
DBREF  5CLN F    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
DBREF  5CLN G    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
DBREF  5CLN H    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
DBREF  5CLN I    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
DBREF  5CLN J    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
DBREF  5CLN K    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
DBREF  5CLN L    1    57  UNP    Q01468   4OT1_PSEPU       2     58             
SEQADV 5CLN TYR A   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA A   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQADV 5CLN TYR B   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA B   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQADV 5CLN TYR C   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA C   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQADV 5CLN TYR D   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA D   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQADV 5CLN TYR E   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA E   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQADV 5CLN TYR F   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA F   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQADV 5CLN TYR G   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA G   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQADV 5CLN TYR H   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA H   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQADV 5CLN TYR I   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA I   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQADV 5CLN TYR J   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA J   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQADV 5CLN TYR K   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA K   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQADV 5CLN TYR L   45  UNP  Q01468    MET    46 ENGINEERED MUTATION            
SEQADV 5CLN ALA L   50  UNP  Q01468    PHE    51 ENGINEERED MUTATION            
SEQRES   1 A   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 A   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 A   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 A   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 A   57  GLY GLY GLU LEU ALA                                          
SEQRES   1 B   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 B   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 B   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 B   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 B   57  GLY GLY GLU LEU ALA                                          
SEQRES   1 C   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 C   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 C   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 C   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 C   57  GLY GLY GLU LEU ALA                                          
SEQRES   1 D   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 D   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 D   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 D   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 D   57  GLY GLY GLU LEU ALA                                          
SEQRES   1 E   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 E   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 E   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 E   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 E   57  GLY GLY GLU LEU ALA                                          
SEQRES   1 F   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 F   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 F   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 F   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 F   57  GLY GLY GLU LEU ALA                                          
SEQRES   1 G   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 G   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 G   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 G   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 G   57  GLY GLY GLU LEU ALA                                          
SEQRES   1 H   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 H   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 H   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 H   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 H   57  GLY GLY GLU LEU ALA                                          
SEQRES   1 I   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 I   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 I   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 I   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 I   57  GLY GLY GLU LEU ALA                                          
SEQRES   1 J   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 J   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 J   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 J   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 J   57  GLY GLY GLU LEU ALA                                          
SEQRES   1 K   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 K   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 K   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 K   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 K   57  GLY GLY GLU LEU ALA                                          
SEQRES   1 L   57  PRO ILE ALA GLN ILE HIS ILE LEU GLU GLY ARG SER ASP          
SEQRES   2 L   57  GLU GLN LYS GLU THR LEU ILE ARG GLU VAL SER GLU ALA          
SEQRES   3 L   57  ILE SER ARG SER LEU ASP ALA PRO LEU THR SER VAL ARG          
SEQRES   4 L   57  VAL ILE ILE THR GLU TYR ALA LYS GLY HIS ALA GLY ILE          
SEQRES   5 L   57  GLY GLY GLU LEU ALA                                          
FORMUL  13  HOH   *50(H2 O)                                                     
HELIX    1 AA1 SER A   12  LEU A   31  1                                  20    
HELIX    2 AA2 PRO A   34  SER A   37  5                                   4    
HELIX    3 AA3 ALA A   46  GLY A   48  5                                   3    
HELIX    4 AA4 SER B   12  LEU B   31  1                                  20    
HELIX    5 AA5 PRO B   34  VAL B   38  5                                   5    
HELIX    6 AA6 ALA B   46  GLY B   48  5                                   3    
HELIX    7 AA7 SER C   12  LEU C   31  1                                  20    
HELIX    8 AA8 PRO C   34  SER C   37  5                                   4    
HELIX    9 AA9 ALA C   46  GLY C   48  5                                   3    
HELIX   10 AB1 SER D   12  LEU D   31  1                                  20    
HELIX   11 AB2 PRO D   34  SER D   37  5                                   4    
HELIX   12 AB3 ALA D   46  GLY D   48  5                                   3    
HELIX   13 AB4 SER E   12  LEU E   31  1                                  20    
HELIX   14 AB5 PRO E   34  SER E   37  5                                   4    
HELIX   15 AB6 ALA E   46  GLY E   48  5                                   3    
HELIX   16 AB7 SER F   12  ASP F   32  1                                  21    
HELIX   17 AB8 PRO F   34  SER F   37  5                                   4    
HELIX   18 AB9 ALA F   46  GLY F   48  5                                   3    
HELIX   19 AC1 SER G   12  LEU G   31  1                                  20    
HELIX   20 AC2 PRO G   34  SER G   37  5                                   4    
HELIX   21 AC3 ALA G   46  GLY G   48  5                                   3    
HELIX   22 AC4 SER H   12  LEU H   31  1                                  20    
HELIX   23 AC5 PRO H   34  SER H   37  5                                   4    
HELIX   24 AC6 ALA H   46  GLY H   48  5                                   3    
HELIX   25 AC7 SER I   12  LEU I   31  1                                  20    
HELIX   26 AC8 PRO I   34  SER I   37  5                                   4    
HELIX   27 AC9 ALA I   46  GLY I   48  5                                   3    
HELIX   28 AD1 SER J   12  ASP J   32  1                                  21    
HELIX   29 AD2 PRO J   34  VAL J   38  5                                   5    
HELIX   30 AD3 ALA J   46  ALA J   50  5                                   5    
HELIX   31 AD4 SER K   12  LEU K   31  1                                  20    
HELIX   32 AD5 PRO K   34  VAL K   38  5                                   5    
HELIX   33 AD6 ALA K   46  ALA K   50  5                                   5    
HELIX   34 AD7 SER L   12  LEU L   31  1                                  20    
HELIX   35 AD8 PRO L   34  VAL L   38  5                                   5    
HELIX   36 AD9 ALA L   46  ALA L   50  5                                   5    
SHEET    1 AA1 6 ALA D  50  ILE D  52  0                                        
SHEET    2 AA1 6 ARG A  39  TYR A  45 -1  N  VAL A  40   O  GLY D  51           
SHEET    3 AA1 6 ILE A   2  LEU A   8  1  N  ALA A   3   O  ILE A  41           
SHEET    4 AA1 6 ILE B   2  LEU B   8 -1  O  ILE B   2   N  HIS A   6           
SHEET    5 AA1 6 ARG B  39  TYR B  45  1  O  ARG B  39   N  ALA B   3           
SHEET    6 AA1 6 ALA E  50  GLY E  51 -1  O  GLY E  51   N  VAL B  40           
SHEET    1 AA2 6 ALA A  50  ILE A  52  0                                        
SHEET    2 AA2 6 ARG F  39  TYR F  45 -1  O  VAL F  40   N  GLY A  51           
SHEET    3 AA2 6 ILE F   2  LEU F   8  1  N  ALA F   3   O  ILE F  41           
SHEET    4 AA2 6 ILE E   2  LEU E   8 -1  N  ILE E   2   O  HIS F   6           
SHEET    5 AA2 6 ARG E  39  TYR E  45  1  O  THR E  43   N  ILE E   5           
SHEET    6 AA2 6 ALA C  50  ILE C  52 -1  N  GLY C  51   O  VAL E  40           
SHEET    1 AA3 7 ALA B  50  ILE B  52  0                                        
SHEET    2 AA3 7 ARG C  39  TYR C  45 -1  O  VAL C  40   N  GLY B  51           
SHEET    3 AA3 7 ILE C   2  LEU C   8  1  N  ILE C   5   O  THR C  43           
SHEET    4 AA3 7 ILE D   2  LEU D   8 -1  O  HIS D   6   N  ILE C   2           
SHEET    5 AA3 7 ARG D  39  TYR D  45  1  O  ARG D  39   N  ALA D   3           
SHEET    6 AA3 7 ALA F  50  ILE F  52 -1  O  GLY F  51   N  VAL D  40           
SHEET    7 AA3 7 GLU F  55  LEU F  56 -1  O  GLU F  55   N  ILE F  52           
SHEET    1 AA4 3 ILE G   2  LEU G   8  0                                        
SHEET    2 AA4 3 ARG G  39  TYR G  45  1  O  ARG G  39   N  ALA G   3           
SHEET    3 AA4 3 ALA I  50  ILE I  52 -1  O  GLY I  51   N  VAL G  40           
SHEET    1 AA5 3 ALA G  50  ILE G  52  0                                        
SHEET    2 AA5 3 ARG H  39  TYR H  45 -1  O  VAL H  40   N  GLY G  51           
SHEET    3 AA5 3 ILE H   2  LEU H   8  1  N  ALA H   3   O  ARG H  39           
SHEET    1 AA6 3 ALA H  50  ILE H  52  0                                        
SHEET    2 AA6 3 ARG I  39  TYR I  45 -1  O  VAL I  40   N  GLY H  51           
SHEET    3 AA6 3 ILE I   2  LEU I   8  1  N  ALA I   3   O  ARG I  39           
SHEET    1 AA7 2 ILE J   2  LEU J   8  0                                        
SHEET    2 AA7 2 ARG J  39  TYR J  45  1  O  THR J  43   N  ILE J   5           
SHEET    1 AA8 2 ILE K   2  LEU K   8  0                                        
SHEET    2 AA8 2 ARG K  39  TYR K  45  1  O  ARG K  39   N  ALA K   3           
SHEET    1 AA9 2 ILE L   2  LEU L   8  0                                        
SHEET    2 AA9 2 ARG L  39  TYR L  45  1  O  ARG L  39   N  ALA L   3           
CRYST1   87.163   87.258   97.284  90.00 113.73  90.00 C 1 2 1      48          
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      0.011473  0.000000  0.005043        0.00000                         
SCALE2      0.000000  0.011460  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011228        0.00000                         
ATOM      1  N   PRO A   1     -15.203  -3.515 120.552  1.00     9      
ATOM      2  CA  PRO A   1     -16.098  -4.054 119.523  1.00     9      
ATOM      3  C   PRO A   1     -17.564  -3.819 119.868  1.00     9      
ATOM      4  O   PRO A   1     -17.944  -3.921 121.035  1.00     9      
ATOM      5  CB  PRO A   1     -15.775  -5.557 119.515  1.00     9      
ATOM      6  CG  PRO A   1     -14.487  -5.702 120.259  1.00     9      
ATOM      7  CD  PRO A   1     -14.446  -4.575 121.234  1.00     9      
ATOM      8  N   ILE A   2     -18.370  -3.504 118.860  1.00     4      
ATOM      9  CA  ILE A   2     -19.781  -3.214 119.069  1.00     4      
ATOM     10  C   ILE A   2     -20.641  -4.064 118.148  1.00     4      
ATOM     11  O   ILE A   2     -20.454  -4.066 116.934  1.00     4      
ATOM     12  CB  ILE A   2     -20.085  -1.725 118.838  1.00     4      
ATOM     13  CG1 ILE A   2     -19.369  -0.881 119.890  1.00     4      
ATOM     14  CG2 ILE A   2     -21.585  -1.456 118.910  1.00     4      
ATOM     15  CD1 ILE A   2     -19.168   0.556 119.488  1.00     4      
ATOM     16  N   ALA A   3     -21.586  -4.782 118.743  1.00     5      
ATOM     17  CA  ALA A   3     -22.512  -5.606 117.986  1.00     5      
ATOM     18  C   ALA A   3     -23.914  -5.042 118.118  1.00     5      
ATOM     19  O   ALA A   3     -24.417  -4.863 119.225  1.00     5      
ATOM     20  CB  ALA A   3     -22.467  -7.049 118.473  1.00     5      
ATOM     21  N   GLN A   4     -24.534  -4.755 116.981  1.00     6      
ATOM     22  CA  GLN A   4     -25.929  -4.354 116.954  1.00     6      
ATOM     23  C   GLN A   4     -26.705  -5.495 116.327  1.00     6      
ATOM     24  O   GLN A   4     -26.550  -5.778 115.139  1.00     6      
ATOM     25  CB  GLN A   4     -26.126  -3.057 116.170  1.00     6      
ATOM     26  CG  GLN A   4     -27.487  -2.415 116.392  1.00     6      
ATOM     27  CD  GLN A   4     -27.628  -1.079 115.685  1.00     6      
ATOM     28  OE1 GLN A   4     -26.662  -0.550 115.126  1.00     6      
ATOM     29  NE2 GLN A   4     -28.836  -0.521 115.714  1.00     6      
ATOM     30  N   ILE A   5     -27.535  -6.151 117.132  1.00     7      
ATOM     31  CA  ILE A   5     -28.282  -7.310 116.669  1.00     7      
ATOM     32  C   ILE A   5     -29.745  -6.946 116.481  1.00     7      
ATOM     33  O   ILE A   5     -30.398  -6.437 117.391  1.00     7      
ATOM     34  CB  ILE A   5     -28.154  -8.495 117.646  1.00     7      
ATOM     35  CG1 ILE A   5     -26.675  -8.780 117.923  1.00     7      
ATOM     36  CG2 ILE A   5     -28.821  -9.736 117.064  1.00     7      
ATOM     37  CD1 ILE A   5     -26.428  -9.805 118.999  1.00     7      
ATOM     38  N   HIS A   6     -30.243  -7.232 115.283  1.00     4      
ATOM     39  CA  HIS A   6     -31.603  -6.907 114.892  1.00     4      
ATOM     40  C   HIS A   6     -32.418  -8.180 114.893  1.00     4      
ATOM     41  O   HIS A   6     -32.115  -9.113 114.150  1.00     4      
ATOM     42  CB  HIS A   6     -31.629  -6.268 113.507  1.00     4      
ATOM     43  CG  HIS A   6     -30.768  -5.056 113.386  1.00     4      
ATOM     44  ND1 HIS A   6     -31.182  -3.800 113.766  1.00     4      
ATOM     45  CD2 HIS A   6     -29.499  -4.905 112.924  1.00     4      
ATOM     46  CE1 HIS A   6     -30.217  -2.926 113.543  1.00     4      
ATOM     47  NE2 HIS A   6     -29.185  -3.579 113.033  1.00     4      
ATOM     48  N   ILE A   7     -33.446  -8.224 115.731  1.00     8      
ATOM     49  CA  ILE A   7     -34.245  -9.430 115.876  1.00     8      
ATOM     50  C   ILE A   7     -35.723  -9.091 115.820  1.00     8      
ATOM     51  O   ILE A   7     -36.123  -7.956 116.075  1.00     8      
ATOM     52  CB  ILE A   7     -33.929 -10.160 117.205  1.00     8      
ATOM     53  CG1 ILE A   7     -34.366  -9.318 118.413  1.00     8      
ATOM     54  CG2 ILE A   7     -32.441 -10.474 117.286  1.00     8      
ATOM     55  CD1 ILE A   7     -34.237 -10.031 119.745  1.00     8      
ATOM     56  N   LEU A   8     -36.529 -10.092 115.490  1.00     5      
ATOM     57  CA  LEU A   8     -37.972  -9.948 115.502  1.00     5      
ATOM     58  C   LEU A   8     -38.420  -9.969 116.958  1.00     5      
ATOM     59  O   LEU A   8     -37.862 -10.714 117.762  1.00     5      
ATOM     60  CB  LEU A   8     -38.636 -11.072 114.707  1.00     5      
ATOM     61  CG  LEU A   8     -38.439 -11.049 113.188  1.00     5      
ATOM     62  CD1 LEU A   8     -39.107 -12.262 112.561  1.00     5      
ATOM     63  CD2 LEU A   8     -38.941  -9.763 112.547  1.00     5      
ATOM     64  N   GLU A   9     -39.409  -9.157 117.311  1.00     7      
ATOM     65  CA  GLU A   9     -39.857  -9.118 118.698  1.00     7      
ATOM     66  C   GLU A   9     -40.651 -10.387 118.978  1.00     7      
ATOM     67  O   GLU A   9     -41.134 -11.041 118.052  1.00     7      
ATOM     68  CB  GLU A   9     -40.694  -7.867 118.992  1.00     7      
ATOM     69  CG  GLU A   9     -42.010  -7.776 118.242  1.00     7      
ATOM     70  CD  GLU A   9     -42.770  -6.496 118.559  1.00     7      
ATOM     71  OE1 GLU A   9     -42.121  -5.483 118.898  1.00     7      
ATOM     72  OE2 GLU A   9     -44.016  -6.503 118.474  1.00     7      
ATOM     73  N   GLY A  10     -40.769 -10.734 120.255  1.00     9      
ATOM     74  CA  GLY A  10     -41.501 -11.919 120.659  1.00     9      
ATOM     75  C   GLY A  10     -40.734 -12.769 121.655  1.00     9      
ATOM     76  O   GLY A  10     -41.290 -13.688 122.255  1.00     9      
ATOM     77  N   ARG A  11     -39.455 -12.463 121.839  1.00     9      
ATOM     78  CA  ARG A  11     -38.612 -13.246 122.731  1.00     9      
ATOM     79  C   ARG A  11     -38.748 -12.804 124.172  1.00     9      
ATOM     80  O   ARG A  11     -39.151 -11.678 124.456  1.00     9      
ATOM     81  CB  ARG A  11     -37.151 -13.126 122.316  1.00     9      
ATOM     82  CG  ARG A  11     -36.670 -14.232 121.420  1.00     9      
ATOM     83  CD  ARG A  11     -37.228 -14.051 120.039  1.00     9      
ATOM     84  NE  ARG A  11     -36.707 -15.043 119.104  1.00     9      
ATOM     85  CZ  ARG A  11     -36.299 -14.761 117.869  1.00     9      
ATOM     86  NH1 ARG A  11     -35.847 -15.730 117.087  1.00     9      
ATOM     87  NH2 ARG A  11     -36.280 -13.505 117.429  1.00     9      
ATOM     88  N   SER A  12     -38.396 -13.708 125.078  1.00     6      
ATOM     89  CA  SER A  12     -38.451 -13.428 126.501  1.00     6      
ATOM     90  C   SER A  12     -37.218 -12.628 126.896  1.00     6      
ATOM     91  O   SER A  12     -36.242 -12.583 126.149  1.00     6      
ATOM     92  CB  SER A  12     -38.530 -14.730 127.298  1.00     6      
ATOM     93  OG  SER A  12     -37.281 -15.397 127.300  1.00     6      
ATOM     94  N   ASP A  13     -37.250 -12.005 128.067  1.00     1      
ATOM     95  CA  ASP A  13     -36.081 -11.290 128.551  1.00     1      
ATOM     96  C   ASP A  13     -34.974 -12.300 128.833  1.00     1      
ATOM     97  O   ASP A  13     -33.786 -11.984 128.754  1.00     1      
ATOM     98  CB  ASP A  13     -36.401 -10.476 129.806  1.00     1      
ATOM     99  CG  ASP A  13     -37.076  -9.150 129.490  1.00     1      
ATOM    100  OD1 ASP A  13     -37.208  -8.806 128.295  1.00     1      
ATOM    101  OD2 ASP A  13     -37.470  -8.446 130.443  1.00     1      
ATOM    102  N   GLU A  14     -35.377 -13.531 129.133  1.00     4      
ATOM    103  CA  GLU A  14     -34.436 -14.589 129.473  1.00     4      
ATOM    104  C   GLU A  14     -33.597 -14.941 128.250  1.00     4      
ATOM    105  O   GLU A  14     -32.377 -15.083 128.339  1.00     4      
ATOM    106  CB  GLU A  14     -35.188 -15.822 129.982  1.00     4      
ATOM    107  CG  GLU A  14     -36.043 -15.562 131.231  1.00     4      
ATOM    108  CD  GLU A  14     -36.884 -16.765 131.645  1.00     4      
ATOM    109  OE1 GLU A  14     -37.113 -17.663 130.804  1.00     4      
ATOM    110  OE2 GLU A  14     -37.322 -16.807 132.814  1.00     4      
ATOM    111  N   GLN A  15     -34.261 -15.051 127.102  1.00     8      
ATOM    112  CA  GLN A  15     -33.598 -15.387 125.844  1.00     8      
ATOM    113  C   GLN A  15     -32.631 -14.297 125.395  1.00     8      
ATOM    114  O   GLN A  15     -31.533 -14.578 124.914  1.00     8      
ATOM    115  CB  GLN A  15     -34.635 -15.629 124.742  1.00     8      
ATOM    116  CG  GLN A  15     -35.401 -16.929 124.883  1.00     8      
ATOM    117  CD  GLN A  15     -36.444 -17.119 123.797  1.00     8      
ATOM    118  OE1 GLN A  15     -37.617 -16.794 123.985  1.00     8      
ATOM    119  NE2 GLN A  15     -36.026 -17.670 122.661  1.00     8      
ATOM    120  N   LYS A  16     -33.049 -13.050 125.570  1.00     9      
ATOM    121  CA  LYS A  16     -32.265 -11.897 125.147  1.00     9      
ATOM    122  C   LYS A  16     -31.058 -11.674 126.046  1.00     9      
ATOM    123  O   LYS A  16     -30.053 -11.107 125.625  1.00     9      
ATOM    124  CB  LYS A  16     -33.155 -10.656 125.116  1.00     9      
ATOM    125  CG  LYS A  16     -34.112 -10.643 123.933  1.00     9      
ATOM    126  CD  LYS A  16     -34.954  -9.386 123.899  1.00     9      
ATOM    127  CE  LYS A  16     -36.227  -9.582 124.702  1.00     9      
ATOM    128  NZ  LYS A  16     -37.114  -8.392 124.678  1.00     9      
ATOM    129  N   GLU A  17     -31.158 -12.138 127.284  1.00     1      
ATOM    130  CA  GLU A  17     -30.043 -12.069 128.216  1.00     1      
ATOM    131  C   GLU A  17     -28.991 -13.097 127.822  1.00     1      
ATOM    132  O   GLU A  17     -27.791 -12.856 127.942  1.00     1      
ATOM    133  CB  GLU A  17     -30.546 -12.292 129.643  1.00     1      
ATOM    134  CG  GLU A  17     -29.481 -12.148 130.713  1.00     1      
ATOM    135  CD  GLU A  17     -30.050 -12.194 132.118  1.00     1      
ATOM    136  OE1 GLU A  17     -29.254 -12.285 133.077  1.00     1      
ATOM    137  OE2 GLU A  17     -31.289 -12.116 132.263  1.00     1      
ATOM    138  N   THR A  18     -29.459 -14.241 127.337  1.00     3      
ATOM    139  CA  THR A  18     -28.584 -15.278 126.812  1.00     3      
ATOM    140  C   THR A  18     -27.906 -14.824 125.521  1.00     3      
ATOM    141  O   THR A  18     -26.727 -15.102 125.300  1.00     3      
ATOM    142  CB  THR A  18     -29.367 -16.581 126.554  1.00     3      
ATOM    143  OG1 THR A  18     -29.861 -17.095 127.796  1.00     3      
ATOM    144  CG2 THR A  18     -28.487 -17.635 125.892  1.00     3      
ATOM    145  N   LEU A  19     -28.658 -14.128 124.673  1.00     8      
ATOM    146  CA  LEU A  19     -28.138 -13.649 123.396  1.00     8      
ATOM    147  C   LEU A  19     -26.930 -12.739 123.584  1.00     8      
ATOM    148  O   LEU A  19     -25.887 -12.941 122.963  1.00     8      
ATOM    149  CB  LEU A  19     -29.230 -12.906 122.623  1.00     8      
ATOM    150  CG  LEU A  19     -28.825 -12.325 121.264  1.00     8      
ATOM    151  CD1 LEU A  19     -28.660 -13.425 120.235  1.00     8      
ATOM    152  CD2 LEU A  19     -29.851 -11.307 120.797  1.00     8      
ATOM    153  N   ILE A  20     -27.085 -11.737 124.442  1.00     8      
ATOM    154  CA  ILE A  20     -26.024 -10.777 124.718  1.00     8      
ATOM    155  C   ILE A  20     -24.756 -11.462 125.212  1.00     8      
ATOM    156  O   ILE A  20     -23.654 -11.161 124.758  1.00     8      
ATOM    157  CB  ILE A  20     -26.498  -9.744 125.761  1.00     8      
ATOM    158  CG1 ILE A  20     -27.595  -8.872 125.148  1.00     8      
ATOM    159  CG2 ILE A  20     -25.332  -8.891 126.268  1.00     8      
ATOM    160  CD1 ILE A  20     -28.255  -7.911 126.111  1.00     8      
ATOM    161  N   ARG A  21     -24.927 -12.394 126.138  1.00     1      
ATOM    162  CA  ARG A  21     -23.807 -13.101 126.740  1.00     1      
ATOM    163  C   ARG A  21     -23.117 -14.048 125.767  1.00     1      
ATOM    164  O   ARG A  21     -21.891 -14.051 125.658  1.00     1      
ATOM    165  CB  ARG A  21     -24.291 -13.849 127.980  1.00     1      
ATOM    166  CG  ARG A  21     -23.230 -14.683 128.685  1.00     1      
ATOM    167  CD  ARG A  21     -23.775 -15.217 129.997  1.00     1      
ATOM    168  NE  ARG A  21     -24.152 -14.100 130.865  1.00     1      
ATOM    169  CZ  ARG A  21     -25.223 -14.057 131.654  1.00     1      
ATOM    170  NH1 ARG A  21     -26.078 -15.071 131.705  1.00     1      
ATOM    171  NH2 ARG A  21     -25.443 -12.978 132.392  1.00     1      
ATOM    172  N   GLU A  22     -23.904 -14.847 125.059  1.00     3      
ATOM    173  CA  GLU A  22     -23.348 -15.847 124.159  1.00     3      
ATOM    174  C   GLU A  22     -22.643 -15.173 122.986  1.00     3      
ATOM    175  O   GLU A  22     -21.588 -15.628 122.541  1.00     3      
ATOM    176  CB  GLU A  22     -24.449 -16.787 123.663  1.00     3      
ATOM    177  CG  GLU A  22     -24.937 -17.725 124.750  1.00     3      
ATOM    178  CD  GLU A  22     -23.837 -18.621 125.283  1.00     3      
ATOM    179  OE1 GLU A  22     -23.026 -19.118 124.478  1.00     3      
ATOM    180  OE2 GLU A  22     -23.751 -18.779 126.518  1.00     3      
ATOM    181  N   VAL A  23     -23.225 -14.085 122.491  1.00     7      
ATOM    182  CA  VAL A  23     -22.626 -13.349 121.387  1.00     7      
ATOM    183  C   VAL A  23     -21.371 -12.636 121.872  1.00     7      
ATOM    184  O   VAL A  23     -20.359 -12.612 121.177  1.00     7      
ATOM    185  CB  VAL A  23     -23.611 -12.327 120.780  1.00     7      
ATOM    186  CG1 VAL A  23     -22.877 -11.319 119.891  1.00     7      
ATOM    187  CG2 VAL A  23     -24.693 -13.041 119.991  1.00     7      
ATOM    188  N   SER A  24     -21.440 -12.066 123.070  1.00     8      
ATOM    189  CA  SER A  24     -20.292 -11.382 123.650  1.00     8      
ATOM    190  C   SER A  24     -19.131 -12.353 123.836  1.00     8      
ATOM    191  O   SER A  24     -17.977 -12.014 123.575  1.00     8      
ATOM    192  CB  SER A  24     -20.661 -10.731 124.985  1.00     8      
ATOM    193  OG  SER A  24     -21.682  -9.761 124.820  1.00     8      
ATOM    194  N   GLU A  25     -19.441 -13.561 124.297  1.00     1      
ATOM    195  CA  GLU A  25     -18.422 -14.584 124.500  1.00     1      
ATOM    196  C   GLU A  25     -17.790 -14.984 123.168  1.00     1      
ATOM    197  O   GLU A  25     -16.573 -15.130 123.064  1.00     1      
ATOM    198  CB  GLU A  25     -19.027 -15.817 125.177  1.00     1      
ATOM    199  CG  GLU A  25     -19.223 -15.690 126.685  1.00     1      
ATOM    200  CD  GLU A  25     -17.923 -15.561 127.455  1.00     1      
ATOM    201  OE1 GLU A  25     -16.847 -15.818 126.873  1.00     1      
ATOM    202  OE2 GLU A  25     -17.982 -15.210 128.653  1.00     1      
ATOM    203  N   ALA A  26     -18.634 -15.164 122.156  1.00     8      
ATOM    204  CA  ALA A  26     -18.185 -15.562 120.825  1.00     8      
ATOM    205  C   ALA A  26     -17.266 -14.519 120.195  1.00     8      
ATOM    206  O   ALA A  26     -16.285 -14.862 119.536  1.00     8      
ATOM    207  CB  ALA A  26     -19.381 -15.816 119.924  1.00     8      
ATOM    208  N   ILE A  27     -17.586 -13.247 120.405  1.00     6      
ATOM    209  CA  ILE A  27     -16.779 -12.156 119.871  1.00     6      
ATOM    210  C   ILE A  27     -15.428 -12.107 120.570  1.00     6      
ATOM    211  O   ILE A  27     -14.396 -11.952 119.918  1.00     6      
ATOM    212  CB  ILE A  27     -17.504 -10.804 120.015  1.00     6      
ATOM    213  CG1 ILE A  27     -18.749 -10.797 119.124  1.00     6      
ATOM    214  CG2 ILE A  27     -16.591  -9.653 119.609  1.00     6      
ATOM    215  CD1 ILE A  27     -19.655  -9.594 119.308  1.00     6      
ATOM    216  N   SER A  28     -15.437 -12.236 121.894  1.00     3      
ATOM    217  CA  SER A  28     -14.202 -12.226 122.671  1.00     3      
ATOM    218  C   SER A  28     -13.297 -13.360 122.204  1.00     3      
ATOM    219  O   SER A  28     -12.087 -13.191 122.051  1.00     3      
ATOM    220  CB  SER A  28     -14.501 -12.364 124.163  1.00     3      
ATOM    221  OG  SER A  28     -13.321 -12.225 124.935  1.00     3      
ATOM    222  N   ARG A  29     -13.910 -14.512 121.955  1.00     1      
ATOM    223  CA  ARG A  29     -13.201 -15.676 121.444  1.00     1      
ATOM    224  C   ARG A  29     -12.643 -15.450 120.041  1.00     1      
ATOM    225  O   ARG A  29     -11.462 -15.681 119.791  1.00     1      
ATOM    226  CB  ARG A  29     -14.132 -16.888 121.422  1.00     1      
ATOM    227  CG  ARG A  29     -13.825 -17.977 122.427  1.00     1      
ATOM    228  CD  ARG A  29     -14.815 -19.100 122.219  1.00     1      
ATOM    229  NE  ARG A  29     -16.130 -18.774 122.774  1.00     1      
ATOM    230  CZ  ARG A  29     -17.295 -18.973 122.160  1.00     1      
ATOM    231  NH1 ARG A  29     -17.345 -19.430 120.913  1.00     1      
ATOM    232  NH2 ARG A  29     -18.420 -18.652 122.781  1.00     1      
ATOM    233  N   SER A  30     -13.499 -15.009 119.126  1.00     5      
ATOM    234  CA  SER A  30     -13.117 -14.882 117.724  1.00     5      
ATOM    235  C   SER A  30     -11.975 -13.894 117.494  1.00     5      
ATOM    236  O   SER A  30     -11.108 -14.133 116.655  1.00     5      
ATOM    237  CB  SER A  30     -14.327 -14.454 116.888  1.00     5      
ATOM    238  OG  SER A  30     -15.369 -15.408 116.972  1.00     5      
ATOM    239  N   LEU A  31     -11.968 -12.798 118.247  1.00     5      
ATOM    240  CA  LEU A  31     -11.011 -11.716 118.021  1.00     5      
ATOM    241  C   LEU A  31      -9.956 -11.596 119.121  1.00     5      
ATOM    242  O   LEU A  31      -9.212 -10.615 119.161  1.00     5      
ATOM    243  CB  LEU A  31     -11.761 -10.387 117.894  1.00     5      
ATOM    244  CG  LEU A  31     -12.963 -10.370 116.948  1.00     5      
ATOM    245  CD1 LEU A  31     -13.591  -8.985 116.918  1.00     5      
ATOM    246  CD2 LEU A  31     -12.565 -10.813 115.549  1.00     5      
ATOM    247  N   ASP A  32      -9.868 -12.614 119.973  1.00     2      
ATOM    248  CA  ASP A  32      -8.986 -12.597 121.140  1.00     2      
ATOM    249  C   ASP A  32      -8.979 -11.221 121.810  1.00     2      
ATOM    250  O   ASP A  32      -7.919 -10.664 122.106  1.00     2      
ATOM    251  CB  ASP A  32      -7.564 -12.993 120.733  1.00     2      
ATOM    252  CG  ASP A  32      -6.671 -13.285 121.923  1.00     2      
ATOM    253  OD1 ASP A  32      -7.168 -13.259 123.068  1.00     2      
ATOM    254  OD2 ASP A  32      -5.468 -13.542 121.710  1.00     2      
ATOM    255  N   ALA A  33     -10.174 -10.683 122.032  1.00     6      
ATOM    256  CA  ALA A  33     -10.341  -9.368 122.636  1.00     6      
ATOM    257  C   ALA A  33     -10.889  -9.526 124.049  1.00     6      
ATOM    258  O   ALA A  33     -11.676 -10.436 124.304  1.00     6      
ATOM    259  CB  ALA A  33     -11.271  -8.510 121.794  1.00     6      
ATOM    260  N   PRO A  34     -10.480  -8.643 124.977  1.00     5      
ATOM    261  CA  PRO A  34     -11.041  -8.748 126.328  1.00     5      
ATOM    262  C   PRO A  34     -12.556  -8.584 126.328  1.00     5      
ATOM    263  O   PRO A  34     -13.083  -7.667 125.700  1.00     5      
ATOM    264  CB  PRO A  34     -10.352  -7.607 127.088  1.00     5      
ATOM    265  CG  PRO A  34      -9.881  -6.665 126.031  1.00     5      
ATOM    266  CD  PRO A  34      -9.521  -7.531 124.868  1.00     5      
ATOM    267  N   LEU A  35     -13.237  -9.488 127.023  1.00     1      
ATOM    268  CA  LEU A  35     -14.693  -9.507 127.067  1.00     1      
ATOM    269  C   LEU A  35     -15.271  -8.184 127.558  1.00     1      
ATOM    270  O   LEU A  35     -16.311  -7.737 127.081  1.00     1      
ATOM    271  CB  LEU A  35     -15.167 -10.648 127.966  1.00     1      
ATOM    272  CG  LEU A  35     -16.673 -10.881 128.067  1.00     1      
ATOM    273  CD1 LEU A  35     -17.247 -11.347 126.737  1.00     1      
ATOM    274  CD2 LEU A  35     -16.951 -11.896 129.164  1.00     1      
ATOM    275  N   THR A  36     -14.576  -7.551 128.496  1.00     3      
ATOM    276  CA  THR A  36     -15.073  -6.334 129.129  1.00     3      
ATOM    277  C   THR A  36     -15.147  -5.154 128.162  1.00     3      
ATOM    278  O   THR A  36     -15.724  -4.116 128.490  1.00     3      
ATOM    279  CB  THR A  36     -14.185  -5.934 130.324  1.00     3      
ATOM    280  OG1 THR A  36     -12.826  -5.793 129.889  1.00     3      
ATOM    281  CG2 THR A  36     -14.257  -6.986 131.424  1.00     3      
ATOM    282  N   SER A  37     -14.570  -5.315 126.974  1.00     5      
ATOM    283  CA  SER A  37     -14.598  -4.266 125.960  1.00     5      
ATOM    284  C   SER A  37     -15.735  -4.489 124.965  1.00     5      
ATOM    285  O   SER A  37     -16.018  -3.624 124.135  1.00     5      
ATOM    286  CB  SER A  37     -13.260  -4.197 125.219  1.00     5      
ATOM    287  OG  SER A  37     -12.994  -5.402 124.521  1.00     5      
ATOM    288  N   VAL A  38     -16.390  -5.644 125.056  1.00     8      
ATOM    289  CA  VAL A  38     -17.454  -5.996 124.121  1.00     8      
ATOM    290  C   VAL A  38     -18.794  -5.400 124.534  1.00     8      
ATOM    291  O   VAL A  38     -19.242  -5.571 125.667  1.00     8      
ATOM    292  CB  VAL A  38     -17.609  -7.532 123.997  1.00     8      
ATOM    293  CG1 VAL A  38     -18.720  -7.895 123.011  1.00     8      
ATOM    294  CG2 VAL A  38     -16.292  -8.169 123.585  1.00     8      
ATOM    295  N   ARG A  39     -19.417  -4.695 123.594  1.00     9      
ATOM    296  CA  ARG A  39     -20.750  -4.127 123.781  1.00     9      
ATOM    297  C   ARG A  39     -21.736  -4.685 122.771  1.00     9      
ATOM    298  O   ARG A  39     -21.403  -4.892 121.604  1.00     9      
ATOM    299  CB  ARG A  39     -20.701  -2.603 123.705  1.00     9      
ATOM    300  CG  ARG A  39     -20.125  -2.015 124.966  1.00     9      
ATOM    301  CD  ARG A  39     -19.692  -0.580 124.837  1.00     9      
ATOM    302  NE  ARG A  39     -19.300  -0.078 126.148  1.00     9      
ATOM    303  CZ  ARG A  39     -18.174  -0.426 126.767  1.00     9      
ATOM    304  NH1 ARG A  39     -17.888   0.072 127.962  1.00     9      
ATOM    305  NH2 ARG A  39     -17.339  -1.287 126.198  1.00     9      
ATOM    306  N   VAL A  40     -22.951  -4.929 123.245  1.00     8      
ATOM    307  CA  VAL A  40     -24.020  -5.464 122.418  1.00     8      
ATOM    308  C   VAL A  40     -25.265  -4.604 122.538  1.00     8      
ATOM    309  O   VAL A  40     -25.650  -4.185 123.629  1.00     8      
ATOM    310  CB  VAL A  40     -24.364  -6.916 122.793  1.00     8      
ATOM    311  CG1 VAL A  40     -25.542  -7.423 121.959  1.00     8      
ATOM    312  CG2 VAL A  40     -23.151  -7.809 122.605  1.00     8      
ATOM    313  N   ILE A  41     -25.884  -4.354 121.392  1.00     3      
ATOM    314  CA  ILE A  41     -27.123  -3.603 121.326  1.00     3      
ATOM    315  C   ILE A  41     -28.182  -4.421 120.613  1.00     3      
ATOM    316  O   ILE A  41     -27.978  -4.873 119.486  1.00     3      
ATOM    317  CB  ILE A  41     -26.930  -2.275 120.553  1.00     3      
ATOM    318  CG1 ILE A  41     -26.207  -1.237 121.404  1.00     3      
ATOM    319  CG2 ILE A  41     -28.264  -1.711 120.100  1.00     3      
ATOM    320  CD1 ILE A  41     -25.694  -0.062 120.595  1.00     3      
ATOM    321  N   ILE A  42     -29.314  -4.610 121.283  1.00     8      
ATOM    322  CA  ILE A  42     -30.431  -5.332 120.698  1.00     8      
ATOM    323  C   ILE A  42     -31.486  -4.335 120.245  1.00     8      
ATOM    324  O   ILE A  42     -31.849  -3.422 120.985  1.00     8      
ATOM    325  CB  ILE A  42     -31.037  -6.345 121.684  1.00     8      
ATOM    326  CG1 ILE A  42     -29.989  -7.404 122.034  1.00     8      
ATOM    327  CG2 ILE A  42     -32.263  -7.019 121.073  1.00     8      
ATOM    328  CD1 ILE A  42     -30.413  -8.377 123.110  1.00     8      
ATOM    329  N   THR A  43     -31.973  -4.526 119.025  1.00     3      
ATOM    330  CA  THR A  43     -33.083  -3.750 118.498  1.00     3      
ATOM    331  C   THR A  43     -34.175  -4.714 118.069  1.00     3      
ATOM    332  O   THR A  43     -33.949  -5.569 117.213  1.00     3      
ATOM    333  CB  THR A  43     -32.653  -2.870 117.310  1.00     3      
ATOM    334  OG1 THR A  43     -31.488  -2.118 117.668  1.00     3      
ATOM    335  CG2 THR A  43     -33.765  -1.911 116.916  1.00     3      
ATOM    336  N   GLU A  44     -35.359  -4.571 118.656  1.00     9      
ATOM    337  CA  GLU A  44     -36.475  -5.450 118.332  1.00     9      
ATOM    338  C   GLU A  44     -37.339  -4.834 117.253  1.00     9      
ATOM    339  O   GLU A  44     -37.506  -3.617 117.198  1.00     9      
ATOM    340  CB  GLU A  44     -37.334  -5.735 119.562  1.00     9      
ATOM    341  CG  GLU A  44     -36.667  -6.589 120.614  1.00     9      
ATOM    342  CD  GLU A  44     -37.633  -7.003 121.702  1.00     9      
ATOM    343  OE1 GLU A  44     -38.215  -6.109 122.352  1.00     9      
ATOM    344  OE2 GLU A  44     -37.815  -8.223 121.903  1.00     9      
ATOM    345  N   TYR A  45     -37.880  -5.690 116.394  1.00     6      
ATOM    346  CA  TYR A  45     -38.760  -5.251 115.325  1.00     6      
ATOM    347  C   TYR A  45     -40.099  -5.960 115.357  1.00     6      
ATOM    348  O   TYR A  45     -40.166  -7.184 115.456  1.00     6      
ATOM    349  CB  TYR A  45     -38.079  -5.467 113.976  1.00     6      
ATOM    350  CG  TYR A  45     -36.862  -4.596 113.819  1.00     6      
ATOM    351  CD1 TYR A  45     -36.976  -3.306 113.327  1.00     6      
ATOM    352  CD2 TYR A  45     -35.605  -5.051 114.186  1.00     6      
ATOM    353  CE1 TYR A  45     -35.871  -2.495 113.190  1.00     6      
ATOM    354  CE2 TYR A  45     -34.492  -4.247 114.054  1.00     6      
ATOM    355  CZ  TYR A  45     -34.630  -2.969 113.557  1.00     6      
ATOM    356  OH  TYR A  45     -33.526  -2.159 113.422  1.00     6      
ATOM    357  N   ALA A  46     -41.168  -5.177 115.272  1.00     3      
ATOM    358  CA  ALA A  46     -42.501  -5.739 115.192  1.00     3      
ATOM    359  C   ALA A  46     -42.642  -6.362 113.812  1.00     3      
ATOM    360  O   ALA A  46     -41.965  -5.947 112.873  1.00     3      
ATOM    361  CB  ALA A  46     -43.553  -4.669 115.428  1.00     3      
ATOM    362  N   LYS A  47     -43.502  -7.367 113.695  1.00     1      
ATOM    363  CA  LYS A  47     -43.674  -8.090 112.435  1.00     1      
ATOM    364  C   LYS A  47     -44.004  -7.181 111.252  1.00     1      
ATOM    365  O   LYS A  47     -43.585  -7.461 110.131  1.00     1      
ATOM    366  CB  LYS A  47     -44.709  -9.202 112.613  1.00     1      
ATOM    367  CG  LYS A  47     -44.062 -10.439 113.244  1.00     1      
ATOM    368  CD  LYS A  47     -44.996 -11.315 114.056  1.00     1      
ATOM    369  CE  LYS A  47     -44.245 -12.545 114.575  1.00     1      
ATOM    370  NZ  LYS A  47     -43.759 -13.449 113.484  1.00     1      
ATOM    371  N   GLY A  48     -44.741  -6.101 111.491  1.00     1      
ATOM    372  CA  GLY A  48     -45.098  -5.186 110.420  1.00     1      
ATOM    373  C   GLY A  48     -43.988  -4.193 110.097  1.00     1      
ATOM    374  O   GLY A  48     -44.200  -3.244 109.341  1.00     1      
ATOM    375  N   HIS A  49     -42.802  -4.421 110.663  1.00     6      
ATOM    376  CA  HIS A  49     -41.642  -3.554 110.446  1.00     6      
ATOM    377  C   HIS A  49     -40.466  -4.324 109.848  1.00     6      
ATOM    378  O   HIS A  49     -39.368  -3.784 109.729  1.00     6      
ATOM    379  CB  HIS A  49     -41.199  -2.906 111.764  1.00     6      
ATOM    380  CG  HIS A  49     -42.122  -1.835 112.257  1.00     6      
ATOM    381  ND1 HIS A  49     -42.083  -1.365 113.554  1.00     6      
ATOM    382  CD2 HIS A  49     -43.076  -1.117 111.625  1.00     6      
ATOM    383  CE1 HIS A  49     -42.994  -0.420 113.702  1.00     6      
ATOM    384  NE2 HIS A  49     -43.608  -0.247 112.547  1.00     6      
ATOM    385  N   ALA A  50     -40.700  -5.580 109.472  1.00     6      
ATOM    386  CA  ALA A  50     -39.653  -6.423 108.896  1.00     6      
ATOM    387  C   ALA A  50     -40.167  -7.158 107.659  1.00     6      
ATOM    388  O   ALA A  50     -41.252  -7.740 107.680  1.00     6      
ATOM    389  CB  ALA A  50     -39.142  -7.409 109.934  1.00     6      
ATOM    390  N   GLY A  51     -39.372  -7.129 106.591  1.00     6      
ATOM    391  CA  GLY A  51     -39.719  -7.766 105.330  1.00     6      
ATOM    392  C   GLY A  51     -38.718  -8.794 104.825  1.00     6      
ATOM    393  O   GLY A  51     -37.523  -8.681 105.089  1.00     6      
ATOM    394  N   ILE A  52     -39.216  -9.801 104.106  1.00     6      
ATOM    395  CA  ILE A  52     -38.364 -10.807 103.460  1.00     6      
ATOM    396  C   ILE A  52     -38.890 -11.125 102.060  1.00     6      
ATOM    397  O   ILE A  52     -39.528 -12.157 101.846  1.00     6      
ATOM    398  CB  ILE A  52     -38.265 -12.138 104.246  1.00     6      
ATOM    399  CG1 ILE A  52     -37.767 -11.922 105.669  1.00     6      
ATOM    400  CG2 ILE A  52     -37.345 -13.118 103.526  1.00     6      
ATOM    401  CD1 ILE A  52     -38.871 -11.913 106.685  1.00     6      
ATOM    402  N   GLY A  53     -38.678 -10.208 101.124  1.00     3      
ATOM    403  CA  GLY A  53     -39.105 -10.407  99.750  1.00     3      
ATOM    404  C   GLY A  53     -40.177  -9.408  99.402  1.00     3      
ATOM    405  O   GLY A  53     -40.888  -9.552  98.412  1.00     3      
ATOM    406  N   GLY A  54     -40.296  -8.392 100.248  1.00     9      
ATOM    407  CA  GLY A  54     -41.336  -7.400 100.104  1.00     9      
ATOM    408  C   GLY A  54     -42.547  -7.807 100.924  1.00     9      
ATOM    409  O   GLY A  54     -43.520  -7.057 101.008  1.00     9      
ATOM    410  N   GLU A  55     -42.483  -8.997 101.534  1.00     1      
ATOM    411  CA  GLU A  55     -43.591  -9.517 102.356  1.00     1      
ATOM    412  C   GLU A  55     -43.208  -9.455 103.829  1.00     1      
ATOM    413  O   GLU A  55     -42.030  -9.522 104.174  1.00     1      
ATOM    414  CB  GLU A  55     -43.933 -10.964 102.023  1.00     1      
ATOM    415  CG  GLU A  55     -44.419 -11.189 100.587  1.00     1      
ATOM    416  CD  GLU A  55     -45.574 -10.209 100.162  1.00     1      
ATOM    417  OE1 GLU A  55     -46.472  -9.909 100.992  1.00     1      
ATOM    418  OE2 GLU A  55     -45.595  -9.675  99.005  1.00     1      
ATOM    419  N   LEU A  56     -44.203  -9.317 104.698  1.00     4      
ATOM    420  CA  LEU A  56     -43.935  -9.164 106.123  1.00     4      
ATOM    421  C   LEU A  56     -43.453 -10.495 106.693  1.00     4      
ATOM    422  O   LEU A  56     -43.575 -11.534 106.045  1.00     4      
ATOM    423  CB  LEU A  56     -45.178  -8.686 106.874  1.00     4      
ATOM    424  CG  LEU A  56     -45.692  -7.281 106.531  1.00     4      
ATOM    425  CD1 LEU A  56     -46.923  -6.956 107.362  1.00     4      
ATOM    426  CD2 LEU A  56     -44.622  -6.201 106.692  1.00     4      
ATOM    427  N   ALA A  57     -42.915 -10.457 107.908  1.00     8      
ATOM    428  CA  ALA A  57     -42.397 -11.655 108.563  1.00     8      
ATOM    429  C   ALA A  57     -43.391 -12.187 109.592  1.00     8      
ATOM    430  O   ALA A  57     -44.526 -11.715 109.674  1.00     8      
ATOM    431  CB  ALA A  57     -41.059 -11.358 109.227  1.00     8      
TER     432      ALA A  57                                                      
ATOM    433  N   PRO B   1     -32.802 -12.860 111.723  1.00            
ATOM    434  CA  PRO B   1     -32.021 -11.939 112.558  1.00            
ATOM    435  C   PRO B   1     -30.764 -11.444 111.849  1.00            
ATOM    436  O   PRO B   1     -30.117 -12.213 111.136  1.00            
ATOM    437  CB  PRO B   1     -31.666 -12.778 113.790  1.00            
ATOM    438  CG  PRO B   1     -31.835 -14.194 113.388  1.00            
ATOM    439  CD  PRO B   1     -32.692 -14.261 112.161  1.00            
ATOM    440  N   ILE B   2     -30.429 -10.173 112.062  1.00            
ATOM    441  CA  ILE B   2     -29.305  -9.530 111.387  1.00            
ATOM    442  C   ILE B   2     -28.360  -8.911 112.406  1.00            
ATOM    443  O   ILE B   2     -28.788  -8.134 113.257  1.00            
ATOM    444  CB  ILE B   2     -29.786  -8.418 110.428  1.00            
ATOM    445  CG1 ILE B   2     -30.720  -8.978 109.357  1.00            
ATOM    446  CG2 ILE B   2     -28.597  -7.693 109.793  1.00            
ATOM    447  CD1 ILE B   2     -31.614  -7.919 108.742  1.00            
ATOM    448  N   ALA B   3     -27.082  -9.264 112.326  1.00            
ATOM    449  CA  ALA B   3     -26.072  -8.698 113.215  1.00            
ATOM    450  C   ALA B   3     -25.038  -7.880 112.447  1.00            
ATOM    451  O   ALA B   3     -24.433  -8.382 111.501  1.00            
ATOM    452  CB  ALA B   3     -25.382  -9.806 113.999  1.00            
ATOM    453  N   GLN B   4     -24.851  -6.619 112.835  1.00            
ATOM    454  CA  GLN B   4     -23.744  -5.828 112.305  1.00            
ATOM    455  C   GLN B   4     -22.728  -5.574 113.415  1.00            
ATOM    456  O   GLN B   4     -23.027  -4.898 114.400  1.00            
ATOM    457  CB  GLN B   4     -24.199  -4.500 111.673  1.00            
ATOM    458  CG  GLN B   4     -25.486  -3.868 112.164  1.00            
ATOM    459  CD  GLN B   4     -25.828  -2.620 111.347  1.00            
ATOM    460  OE1 GLN B   4     -25.025  -2.166 110.527  1.00            
ATOM    461  NE2 GLN B   4     -27.014  -2.066 111.566  1.00            
ATOM    462  N   ILE B   5     -21.529  -6.124 113.239  1.00            
ATOM    463  CA  ILE B   5     -20.461  -6.011 114.228  1.00            
ATOM    464  C   ILE B   5     -19.431  -4.987 113.770  1.00            
ATOM    465  O   ILE B   5     -18.926  -5.048 112.650  1.00            
ATOM    466  CB  ILE B   5     -19.747  -7.362 114.487  1.00            
ATOM    467  CG1 ILE B   5     -20.746  -8.427 114.934  1.00            
ATOM    468  CG2 ILE B   5     -18.712  -7.222 115.588  1.00            
ATOM    469  CD1 ILE B   5     -21.239  -9.300 113.833  1.00            
ATOM    470  N   HIS B   6     -19.097  -4.067 114.657  1.00            
ATOM    471  CA  HIS B   6     -18.175  -3.010 114.365  1.00            
ATOM    472  C   HIS B   6     -16.889  -3.189 115.082  1.00            
ATOM    473  O   HIS B   6     -16.842  -3.213 116.255  1.00            
ATOM    474  CB  HIS B   6     -18.755  -1.682 114.760  1.00            
ATOM    475  CG  HIS B   6     -20.104  -1.401 114.200  1.00            
ATOM    476  ND1 HIS B   6     -20.296  -0.870 112.953  1.00            
ATOM    477  CD2 HIS B   6     -21.328  -1.525 114.743  1.00            
ATOM    478  CE1 HIS B   6     -21.580  -0.712 112.743  1.00            
ATOM    479  NE2 HIS B   6     -22.226  -1.087 113.818  1.00            
ATOM    480  N   ILE B   7     -15.828  -3.297 114.336  1.00            
ATOM    481  CA  ILE B   7     -14.520  -3.625 114.897  1.00            
ATOM    482  C   ILE B   7     -13.425  -2.723 114.346  1.00            
ATOM    483  O   ILE B   7     -13.594  -2.081 113.313  1.00            
ATOM    484  CB  ILE B   7     -14.144  -5.099 114.623  1.00            
ATOM    485  CG1 ILE B   7     -13.971  -5.349 113.119  1.00            
ATOM    486  CG2 ILE B   7     -15.212  -6.016 115.188  1.00            
ATOM    487  CD1 ILE B   7     -13.442  -6.725 112.781  1.00            
ATOM    488  N   LEU B   8     -12.303  -2.670 115.055  1.00            
ATOM    489  CA  LEU B   8     -11.144  -1.925 114.590  1.00            
ATOM    490  C   LEU B   8     -10.455  -2.704 113.474  1.00            
ATOM    491  O   LEU B   8     -10.333  -3.927 113.551  1.00            
ATOM    492  CB  LEU B   8     -10.177  -1.679 115.749  1.00            
ATOM    493  CG  LEU B   8     -10.669  -0.716 116.836  1.00            
ATOM    494  CD1 LEU B   8      -9.639  -0.609 117.954  1.00            
ATOM    495  CD2 LEU B   8     -11.030   0.660 116.290  1.00            
ATOM    496  N   GLU B   9      -9.996  -2.005 112.440  1.00            
ATOM    497  CA  GLU B   9      -9.343  -2.679 111.324  1.00            
ATOM    498  C   GLU B   9      -7.944  -3.087 111.751  1.00            
ATOM    499  O   GLU B   9      -7.395  -2.538 112.708  1.00            
ATOM    500  CB  GLU B   9      -9.278  -1.791 110.077  1.00            
ATOM    501  CG  GLU B   9      -8.421  -0.548 110.220  1.00            
ATOM    502  CD  GLU B   9      -8.422   0.302 108.963  1.00            
ATOM    503  OE1 GLU B   9      -9.424   0.262 108.216  1.00            
ATOM    504  OE2 GLU B   9      -7.420   1.008 108.718  1.00            
ATOM    505  N   GLY B  10      -7.381  -4.061 111.045  1.00            
ATOM    506  CA  GLY B  10      -6.036  -4.521 111.318  1.00            
ATOM    507  C   GLY B  10      -5.968  -6.030 111.423  1.00            
ATOM    508  O   GLY B  10      -4.881  -6.611 111.438  1.00            
ATOM    509  N   ARG B  11      -7.128  -6.673 111.495  1.00            
ATOM    510  CA  ARG B  11      -7.165  -8.114 111.670  1.00            
ATOM    511  C   ARG B  11      -7.041  -8.864 110.361  1.00            
ATOM    512  O   ARG B  11      -7.259  -8.325 109.279  1.00            
ATOM    513  CB  ARG B  11      -8.448  -8.546 112.380  1.00            
ATOM    514  CG  ARG B  11      -8.493  -8.094 113.808  1.00            
ATOM    515  CD  ARG B  11      -9.607  -8.755 114.575  1.00            
ATOM    516  NE  ARG B  11      -9.330  -8.671 116.002  1.00            
ATOM    517  CZ  ARG B  11      -9.607  -7.618 116.761  1.00            
ATOM    518  NH1 ARG B  11     -10.191  -6.546 116.237  1.00            
ATOM    519  NH2 ARG B  11      -9.301  -7.643 118.051  1.00            
ATOM    520  N   SER B  12      -6.675 -10.129 110.494  1.00            
ATOM    521  CA  SER B  12      -6.511 -11.015 109.361  1.00            
ATOM    522  C   SER B  12      -7.869 -11.482 108.866  1.00            
ATOM    523  O   SER B  12      -8.864 -11.344 109.561  1.00            
ATOM    524  CB  SER B  12      -5.664 -12.215 109.773  1.00            
ATOM    525  OG  SER B  12      -6.422 -13.076 110.607  1.00            
ATOM    526  N   ASP B  13      -7.904 -12.013 107.649  1.00            
ATOM    527  CA  ASP B  13      -9.124 -12.590 107.094  1.00            
ATOM    528  C   ASP B  13      -9.481 -13.841 107.893  1.00            
ATOM    529  O   ASP B  13     -10.631 -14.287 107.898  1.00            
ATOM    530  CB  ASP B  13      -8.968 -12.924 105.606  1.00            
ATOM    531  CG  ASP B  13      -9.136 -11.707 104.701  1.00            
ATOM    532  OD1 ASP B  13      -9.480 -10.612 105.199  1.00            
ATOM    533  OD2 ASP B  13      -8.930 -11.854 103.476  1.00            
ATOM    534  N   GLU B  14      -8.483 -14.410 108.566  1.00            
ATOM    535  CA  GLU B  14      -8.677 -15.657 109.307  1.00            
ATOM    536  C   GLU B  14      -9.680 -15.524 110.440  1.00            
ATOM    537  O   GLU B  14     -10.608 -16.320 110.569  1.00            
ATOM    538  CB  GLU B  14      -7.355 -16.116 109.944  1.00            
ATOM    539  CG  GLU B  14      -6.599 -17.203 109.200  1.00            
ATOM    540  CD  GLU B  14      -5.365 -16.684 108.469  1.00            
ATOM    541  OE1 GLU B  14      -5.229 -15.455 108.290  1.00            
ATOM    542  OE2 GLU B  14      -4.565 -17.520 107.999  1.00            
ATOM    543  N   GLN B  15      -9.481 -14.502 111.258  1.00            
ATOM    544  CA  GLN B  15     -10.340 -14.248 112.407  1.00            
ATOM    545  C   GLN B  15     -11.731 -13.753 112.043  1.00            
ATOM    546  O   GLN B  15     -12.713 -14.141 112.673  1.00            
ATOM    547  CB  GLN B  15      -9.682 -13.238 113.349  1.00            
ATOM    548  CG  GLN B  15      -8.173 -13.376 113.460  1.00            
ATOM    549  CD  GLN B  15      -7.562 -12.355 114.393  1.00            
ATOM    550  OE1 GLN B  15      -8.008 -12.188 115.529  1.00            
ATOM    551  NE2 GLN B  15      -6.539 -11.656 113.913  1.00            
ATOM    552  N   LYS B  16     -11.820 -12.910 111.018  1.00            
ATOM    553  CA  LYS B  16     -13.073 -12.228 110.746  1.00            
ATOM    554  C   LYS B  16     -14.133 -13.180 110.195  1.00            
ATOM    555  O   LYS B  16     -15.323 -12.951 110.402  1.00            
ATOM    556  CB  LYS B  16     -12.843 -11.065 109.769  1.00            
ATOM    557  CG  LYS B  16     -11.878 -10.018 110.334  1.00            
ATOM    558  CD  LYS B  16     -11.764  -8.731 109.511  1.00            
ATOM    559  CE  LYS B  16     -10.773  -8.818 108.353  1.00            
ATOM    560  NZ  LYS B  16     -10.649  -7.491 107.678  1.00            
ATOM    561  N   GLU B  17     -13.724 -14.243 109.505  1.00            
ATOM    562  CA  GLU B  17     -14.697 -15.235 109.052  1.00            
ATOM    563  C   GLU B  17     -15.088 -16.154 110.216  1.00            
ATOM    564  O   GLU B  17     -16.218 -16.639 110.274  1.00            
ATOM    565  CB  GLU B  17     -14.198 -16.033 107.836  1.00            
ATOM    566  CG  GLU B  17     -13.729 -17.459 108.077  1.00            
ATOM    567  CD  GLU B  17     -13.524 -18.209 106.768  1.00            
ATOM    568  OE1 GLU B  17     -12.448 -18.080 106.146  1.00            
ATOM    569  OE2 GLU B  17     -14.467 -18.920 106.351  1.00            
ATOM    570  N   THR B  18     -14.154 -16.401 111.133  1.00            
ATOM    571  CA  THR B  18     -14.458 -17.190 112.328  1.00            
ATOM    572  C   THR B  18     -15.499 -16.445 113.151  1.00            
ATOM    573  O   THR B  18     -16.403 -17.051 113.720  1.00            
ATOM    574  CB  THR B  18     -13.202 -17.455 113.191  1.00            
ATOM    575  OG1 THR B  18     -12.276 -18.265 112.458  1.00            
ATOM    576  CG2 THR B  18     -13.567 -18.171 114.496  1.00            
ATOM    577  N   LEU B  19     -15.361 -15.125 113.196  1.00            
ATOM    578  CA  LEU B  19     -16.293 -14.265 113.909  1.00            
ATOM    579  C   LEU B  19     -17.702 -14.480 113.372  1.00            
ATOM    580  O   LEU B  19     -18.648 -14.667 114.137  1.00            
ATOM    581  CB  LEU B  19     -15.875 -12.801 113.768  1.00            
ATOM    582  CG  LEU B  19     -16.763 -11.744 114.422  1.00            
ATOM    583  CD1 LEU B  19     -16.627 -11.780 115.930  1.00            
ATOM    584  CD2 LEU B  19     -16.386 -10.374 113.885  1.00            
ATOM    585  N   ILE B  20     -17.827 -14.435 112.050  1.00            
ATOM    586  CA  ILE B  20     -19.104 -14.643 111.377  1.00            
ATOM    587  C   ILE B  20     -19.687 -15.993 111.777  1.00            
ATOM    588  O   ILE B  20     -20.887 -16.115 112.026  1.00            
ATOM    589  CB  ILE B  20     -18.938 -14.567 109.846  1.00            
ATOM    590  CG1 ILE B  20     -18.592 -13.133 109.439  1.00            
ATOM    591  CG2 ILE B  20     -20.204 -15.047 109.127  1.00            
ATOM    592  CD1 ILE B  20     -18.257 -12.957 107.970  1.00            
ATOM    593  N   ARG B  21     -18.827 -17.003 111.815  1.00            
ATOM    594  CA  ARG B  21     -19.237 -18.361 112.158  1.00            
ATOM    595  C   ARG B  21     -19.632 -18.470 113.632  1.00            
ATOM    596  O   ARG B  21     -20.657 -19.061 113.963  1.00            
ATOM    597  CB  ARG B  21     -18.119 -19.357 111.814  1.00            
ATOM    598  CG  ARG B  21     -18.453 -20.798 112.168  1.00            
ATOM    599  CD  ARG B  21     -17.382 -21.796 111.713  1.00            
ATOM    600  NE  ARG B  21     -17.162 -21.761 110.266  1.00            
ATOM    601  CZ  ARG B  21     -16.076 -21.300 109.646  1.00            
ATOM    602  NH1 ARG B  21     -15.034 -20.810 110.310  1.00            
ATOM    603  NH2 ARG B  21     -16.036 -21.347 108.323  1.00            
ATOM    604  N   GLU B  22     -18.802 -17.912 114.507  1.00            
ATOM    605  CA  GLU B  22     -19.022 -17.985 115.945  1.00            
ATOM    606  C   GLU B  22     -20.243 -17.187 116.399  1.00            
ATOM    607  O   GLU B  22     -20.979 -17.616 117.284  1.00            
ATOM    608  CB  GLU B  22     -17.781 -17.474 116.675  1.00            
ATOM    609  CG  GLU B  22     -17.480 -18.171 117.988  1.00            
ATOM    610  CD  GLU B  22     -16.650 -19.431 117.808  1.00            
ATOM    611  OE1 GLU B  22     -17.220 -20.473 117.414  1.00            
ATOM    612  OE2 GLU B  22     -15.425 -19.378 118.058  1.00            
ATOM    613  N   VAL B  23     -20.431 -16.011 115.809  1.00            
ATOM    614  CA  VAL B  23     -21.553 -15.150 116.158  1.00            
ATOM    615  C   VAL B  23     -22.881 -15.697 115.637  1.00            
ATOM    616  O   VAL B  23     -23.891 -15.653 116.339  1.00            
ATOM    617  CB  VAL B  23     -21.339 -13.725 115.614  1.00            
ATOM    618  CG1 VAL B  23     -22.630 -12.913 115.676  1.00            
ATOM    619  CG2 VAL B  23     -20.244 -13.023 116.398  1.00            
ATOM    620  N   SER B  24     -22.871 -16.223 114.415  1.00            
ATOM    621  CA  SER B  24     -24.080 -16.767 113.801  1.00            
ATOM    622  C   SER B  24     -24.647 -17.905 114.635  1.00            
ATOM    623  O   SER B  24     -25.859 -18.015 114.825  1.00            
ATOM    624  CB  SER B  24     -23.792 -17.250 112.379  1.00            
ATOM    625  OG  SER B  24     -23.331 -16.184 111.567  1.00            
ATOM    626  N   GLU B  25     -23.752 -18.750 115.127  1.00            
ATOM    627  CA  GLU B  25     -24.120 -19.864 115.985  1.00            
ATOM    628  C   GLU B  25     -24.754 -19.411 117.303  1.00            
ATOM    629  O   GLU B  25     -25.750 -19.985 117.744  1.00            
ATOM    630  CB  GLU B  25     -22.873 -20.718 116.238  1.00            
ATOM    631  CG  GLU B  25     -23.077 -21.907 117.160  1.00            
ATOM    632  CD  GLU B  25     -23.064 -21.519 118.634  1.00            
ATOM    633  OE1 GLU B  25     -22.485 -20.463 118.978  1.00            
ATOM    634  OE2 GLU B  25     -23.635 -22.269 119.445  1.00            
ATOM    635  N   ALA B  26     -24.178 -18.389 117.928  1.00            
ATOM    636  CA  ALA B  26     -24.690 -17.881 119.198  1.00            
ATOM    637  C   ALA B  26     -26.107 -17.338 119.053  1.00            
ATOM    638  O   ALA B  26     -26.940 -17.500 119.947  1.00            
ATOM    639  CB  ALA B  26     -23.773 -16.815 119.743  1.00            
ATOM    640  N   ILE B  27     -26.378 -16.689 117.925  1.00            
ATOM    641  CA  ILE B  27     -27.706 -16.146 117.671  1.00            
ATOM    642  C   ILE B  27     -28.688 -17.296 117.479  1.00            
ATOM    643  O   ILE B  27     -29.797 -17.268 118.016  1.00            
ATOM    644  CB  ILE B  27     -27.720 -15.214 116.438  1.00            
ATOM    645  CG1 ILE B  27     -26.829 -13.994 116.695  1.00            
ATOM    646  CG2 ILE B  27     -29.143 -14.762 116.119  1.00            
ATOM    647  CD1 ILE B  27     -26.643 -13.083 115.494  1.00            
ATOM    648  N   SER B  28     -28.280 -18.306 116.715  1.00            
ATOM    649  CA  SER B  28     -29.138 -19.457 116.454  1.00            
ATOM    650  C   SER B  28     -29.542 -20.202 117.727  1.00            
ATOM    651  O   SER B  28     -30.708 -20.556 117.889  1.00            
ATOM    652  CB  SER B  28     -28.441 -20.427 115.500  1.00            
ATOM    653  OG  SER B  28     -29.309 -21.485 115.127  1.00            
ATOM    654  N   ARG B  29     -28.597 -20.426 118.637  1.00            
ATOM    655  CA  ARG B  29     -28.923 -21.105 119.892  1.00            
ATOM    656  C   ARG B  29     -29.816 -20.250 120.773  1.00            
ATOM    657  O   ARG B  29     -30.849 -20.708 121.261  1.00            
ATOM    658  CB  ARG B  29     -27.681 -21.464 120.709  1.00            
ATOM    659  CG  ARG B  29     -27.055 -22.800 120.383  1.00            
ATOM    660  CD  ARG B  29     -26.004 -23.150 121.422  1.00            
ATOM    661  NE  ARG B  29     -24.822 -22.296 121.344  1.00            
ATOM    662  CZ  ARG B  29     -24.536 -21.322 122.207  1.00            
ATOM    663  NH1 ARG B  29     -25.334 -21.054 123.237  1.00            
ATOM    664  NH2 ARG B  29     -23.436 -20.607 122.040  1.00            
ATOM    665  N   SER B  30     -29.389 -19.009 120.988  1.00            
ATOM    666  CA  SER B  30     -30.042 -18.120 121.939  1.00            
ATOM    667  C   SER B  30     -31.504 -17.868 121.593  1.00            
ATOM    668  O   SER B  30     -32.345 -17.782 122.486  1.00            
ATOM    669  CB  SER B  30     -29.296 -16.785 122.007  1.00            
ATOM    670  OG  SER B  30     -27.955 -16.966 122.424  1.00            
ATOM    671  N   LEU B  31     -31.803 -17.766 120.301  1.00            
ATOM    672  CA  LEU B  31     -33.141 -17.402 119.850  1.00            
ATOM    673  C   LEU B  31     -33.893 -18.549 119.174  1.00            
ATOM    674  O   LEU B  31     -34.947 -18.327 118.579  1.00            
ATOM    675  CB  LEU B  31     -33.050 -16.220 118.883  1.00            
ATOM    676  CG  LEU B  31     -32.207 -15.028 119.337  1.00            
ATOM    677  CD1 LEU B  31     -32.231 -13.936 118.278  1.00            
ATOM    678  CD2 LEU B  31     -32.699 -14.493 120.672  1.00            
ATOM    679  N   ASP B  32     -33.378 -19.769 119.317  1.00            
ATOM    680  CA  ASP B  32     -33.921 -20.943 118.630  1.00            
ATOM    681  C   ASP B  32     -34.331 -20.608 117.199  1.00            
ATOM    682  O   ASP B  32     -35.441 -20.929 116.767  1.00            
ATOM    683  CB  ASP B  32     -35.121 -21.511 119.395  1.00            
ATOM    684  CG  ASP B  32     -35.543 -22.889 118.893  1.00            
ATOM    685  OD1 ASP B  32     -34.865 -23.443 118.001  1.00            
ATOM    686  OD2 ASP B  32     -36.564 -23.412 119.391  1.00            
ATOM    687  N   ALA B  33     -33.430 -19.947 116.480  1.00            
ATOM    688  CA  ALA B  33     -33.683 -19.553 115.105  1.00            
ATOM    689  C   ALA B  33     -32.834 -20.422 114.189  1.00            
ATOM    690  O   ALA B  33     -31.706 -20.764 114.541  1.00            
ATOM    691  CB  ALA B  33     -33.362 -18.081 114.901  1.00            
ATOM    692  N   PRO B  34     -33.369 -20.789 113.012  1.00            
ATOM    693  CA  PRO B  34     -32.564 -21.564 112.063  1.00            
ATOM    694  C   PRO B  34     -31.324 -20.795 111.617  1.00            
ATOM    695  O   PRO B  34     -31.419 -19.615 111.280  1.00            
ATOM    696  CB  PRO B  34     -33.528 -21.814 110.897  1.00            
ATOM    697  CG  PRO B  34     -34.577 -20.766 111.032  1.00            
ATOM    698  CD  PRO B  34     -34.730 -20.549 112.501  1.00            
ATOM    699  N   LEU B  35     -30.178 -21.466 111.627  1.00            
ATOM    700  CA  LEU B  35     -28.901 -20.843 111.296  1.00            
ATOM    701  C   LEU B  35     -28.934 -20.178 109.925  1.00            
ATOM    702  O   LEU B  35     -28.298 -19.146 109.710  1.00            
ATOM    703  CB  LEU B  35     -27.783 -21.887 111.336  1.00            
ATOM    704  CG  LEU B  35     -26.353 -21.394 111.096  1.00            
ATOM    705  CD1 LEU B  35     -25.878 -20.494 112.229  1.00            
ATOM    706  CD2 LEU B  35     -25.417 -22.578 110.907  1.00            
ATOM    707  N   THR B  36     -29.674 -20.776 108.999  1.00            
ATOM    708  CA  THR B  36     -29.705 -20.302 107.620  1.00            
ATOM    709  C   THR B  36     -30.370 -18.932 107.467  1.00            
ATOM    710  O   THR B  36     -30.280 -18.315 106.405  1.00            
ATOM    711  CB  THR B  36     -30.443 -21.309 106.720  1.00            
ATOM    712  OG1 THR B  36     -31.755 -21.549 107.246  1.00            
ATOM    713  CG2 THR B  36     -29.679 -22.623 106.653  1.00            
ATOM    714  N   SER B  37     -31.030 -18.459 108.521  1.00            
ATOM    715  CA  SER B  37     -31.686 -17.152 108.499  1.00            
ATOM    716  C   SER B  37     -30.826 -16.056 109.137  1.00            
ATOM    717  O   SER B  37     -31.162 -14.874 109.058  1.00            
ATOM    718  CB  SER B  37     -33.039 -17.223 109.214  1.00            
ATOM    719  OG  SER B  37     -32.879 -17.555 110.582  1.00            
ATOM    720  N   VAL B  38     -29.717 -16.447 109.762  1.00            
ATOM    721  CA  VAL B  38     -28.859 -15.502 110.483  1.00            
ATOM    722  C   VAL B  38     -27.879 -14.773 109.563  1.00            
ATOM    723  O   VAL B  38     -27.164 -15.402 108.787  1.00            
ATOM    724  CB  VAL B  38     -28.064 -16.213 111.599  1.00            
ATOM    725  CG1 VAL B  38     -27.203 -15.213 112.358  1.00            
ATOM    726  CG2 VAL B  38     -29.004 -16.941 112.550  1.00            
ATOM    727  N   ARG B  39     -27.844 -13.445 109.673  1.00            
ATOM    728  CA  ARG B  39     -26.943 -12.638 108.865  1.00            
ATOM    729  C   ARG B  39     -25.937 -11.911 109.739  1.00            
ATOM    730  O   ARG B  39     -26.262 -11.426 110.813  1.00            
ATOM    731  CB  ARG B  39     -27.735 -11.625 108.028  1.00            
ATOM    732  CG  ARG B  39     -28.772 -12.296 107.174  1.00            
ATOM    733  CD  ARG B  39     -28.392 -12.292 105.720  1.00            
ATOM    734  NE  ARG B  39     -29.254 -13.226 105.002  1.00            
ATOM    735  CZ  ARG B  39     -30.123 -12.932 104.040  1.00            
ATOM    736  NH1 ARG B  39     -30.304 -11.687 103.609  1.00            
ATOM    737  NH2 ARG B  39     -30.820 -13.917 103.497  1.00            
ATOM    738  N   VAL B  40     -24.697 -11.875 109.266  1.00            
ATOM    739  CA  VAL B  40     -23.633 -11.160 109.944  1.00            
ATOM    740  C   VAL B  40     -22.936 -10.275 108.924  1.00            
ATOM    741  O   VAL B  40     -22.574 -10.731 107.841  1.00            
ATOM    742  CB  VAL B  40     -22.623 -12.120 110.597  1.00            
ATOM    743  CG1 VAL B  40     -21.520 -11.338 111.266  1.00            
ATOM    744  CG2 VAL B  40     -23.328 -13.015 111.607  1.00            
ATOM    745  N   ILE B  41     -22.767  -9.004 109.272  1.00            
ATOM    746  CA  ILE B  41     -22.022  -8.076 108.434  1.00            
ATOM    747  C   ILE B  41     -20.998  -7.342 109.291  1.00            
ATOM    748  O   ILE B  41     -21.335  -6.750 110.313  1.00            
ATOM    749  CB  ILE B  41     -22.958  -7.081 107.713  1.00            
ATOM    750  CG1 ILE B  41     -23.981  -6.491 108.685  1.00            
ATOM    751  CG2 ILE B  41     -23.669  -7.786 106.566  1.00            
ATOM    752  CD1 ILE B  41     -24.910  -5.449 108.069  1.00            
ATOM    753  N   ILE B  42     -19.743  -7.390 108.861  1.00            
ATOM    754  CA  ILE B  42     -18.652  -6.771 109.600  1.00            
ATOM    755  C   ILE B  42     -18.289  -5.430 108.983  1.00            
ATOM    756  O   ILE B  42     -18.154  -5.316 107.766  1.00            
ATOM    757  CB  ILE B  42     -17.417  -7.694 109.623  1.00            
ATOM    758  CG1 ILE B  42     -17.785  -9.036 110.267  1.00            
ATOM    759  CG2 ILE B  42     -16.256  -7.028 110.360  1.00            
ATOM    760  CD1 ILE B  42     -16.691 -10.083 110.200  1.00            
ATOM    761  N   THR B  43     -18.129  -4.421 109.834  1.00            
ATOM    762  CA  THR B  43     -17.662  -3.108 109.408  1.00            
ATOM    763  C   THR B  43     -16.411  -2.729 110.193  1.00            
ATOM    764  O   THR B  43     -16.432  -2.674 111.424  1.00            
ATOM    765  CB  THR B  43     -18.744  -2.028 109.602  1.00            
ATOM    766  OG1 THR B  43     -19.977  -2.472 109.023  1.00            
ATOM    767  CG2 THR B  43     -18.323  -0.721 108.943  1.00            
ATOM    768  N   GLU B  44     -15.322  -2.480 109.471  1.00            
ATOM    769  CA  GLU B  44     -14.049  -2.120 110.086  1.00            
ATOM    770  C   GLU B  44     -13.833  -0.613 110.150  1.00            
ATOM    771  O   GLU B  44     -14.272   0.121 109.265  1.00            
ATOM    772  CB  GLU B  44     -12.897  -2.768 109.326  1.00            
ATOM    773  CG  GLU B  44     -12.835  -4.269 109.484  1.00            
ATOM    774  CD  GLU B  44     -11.576  -4.855 108.890  1.00            
ATOM    775  OE1 GLU B  44     -11.354  -4.670 107.675  1.00            
ATOM    776  OE2 GLU B  44     -10.805  -5.493 109.641  1.00            
ATOM    777  N   TYR B  45     -13.107  -0.168 111.151  1.00            
ATOM    778  CA  TYR B  45     -12.835   1.237 111.312  1.00            
ATOM    779  C   TYR B  45     -11.381   1.522 111.482  1.00            
ATOM    780  O   TYR B  45     -10.726   0.861 112.224  1.00            
ATOM    781  CB  TYR B  45     -13.614   1.798 112.491  1.00            
ATOM    782  CG  TYR B  45     -15.076   1.774 112.266  1.00            
ATOM    783  CD1 TYR B  45     -15.731   2.832 111.723  1.00            
ATOM    784  CD2 TYR B  45     -15.800   0.689 112.591  1.00            
ATOM    785  CE1 TYR B  45     -17.072   2.795 111.526  1.00            
ATOM    786  CE2 TYR B  45     -17.133   0.644 112.380  1.00            
ATOM    787  CZ  TYR B  45     -17.759   1.698 111.863  1.00            
ATOM    788  OH  TYR B  45     -19.082   1.610 111.669  1.00            
ATOM    789  N   ALA B  46     -10.915   2.531 110.767  1.00            
ATOM    790  CA  ALA B  46      -9.539   3.023 110.771  1.00            
ATOM    791  C   ALA B  46      -9.201   3.817 112.031  1.00            
ATOM    792  O   ALA B  46     -10.094   4.257 112.755  1.00            
ATOM    793  CB  ALA B  46      -9.292   3.874 109.536  1.00            
ATOM    794  N   LYS B  47      -7.904   3.973 112.289  1.00            
ATOM    795  CA  LYS B  47      -7.415   4.624 113.502  1.00            
ATOM    796  C   LYS B  47      -8.084   5.970 113.764  1.00            
ATOM    797  O   LYS B  47      -8.400   6.299 114.906  1.00            
ATOM    798  CB  LYS B  47      -5.901   4.857 113.400  1.00            
ATOM    799  CG  LYS B  47      -5.020   3.877 114.165  1.00            
ATOM    800  CD  LYS B  47      -4.827   2.568 113.410  1.00            
ATOM    801  CE  LYS B  47      -3.372   2.108 113.436  1.00            
ATOM    802  NZ  LYS B  47      -2.987   1.480 114.733  1.00            
ATOM    803  N   GLY B  48      -8.295   6.742 112.702  1.00            
ATOM    804  CA  GLY B  48      -8.897   8.058 112.819  1.00            
ATOM    805  C   GLY B  48     -10.414   8.074 112.792  1.00            
ATOM    806  O   GLY B  48     -11.014   9.146 112.710  1.00            
ATOM    807  N   HIS B  49     -11.035   6.900 112.869  1.00            
ATOM    808  CA  HIS B  49     -12.489   6.799 112.767  1.00            
ATOM    809  C   HIS B  49     -13.143   6.159 113.993  1.00            
ATOM    810  O   HIS B  49     -14.323   5.820 113.952  1.00            
ATOM    811  CB  HIS B  49     -12.860   6.007 111.509  1.00            
ATOM    812  CG  HIS B  49     -12.555   6.729 110.233  1.00            
ATOM    813  ND1 HIS B  49     -12.537   6.100 109.006  1.00            
ATOM    814  CD2 HIS B  49     -12.238   8.024 109.996  1.00            
ATOM    815  CE1 HIS B  49     -12.233   6.979 108.068  1.00            
ATOM    816  NE2 HIS B  49     -12.045   8.154 108.641  1.00            
ATOM    817  N   ALA B  50     -12.381   5.976 115.069  1.00            
ATOM    818  CA  ALA B  50     -12.916   5.366 116.286  1.00            
ATOM    819  C   ALA B  50     -12.526   6.162 117.531  1.00            
ATOM    820  O   ALA B  50     -11.359   6.510 117.711  1.00            
ATOM    821  CB  ALA B  50     -12.429   3.929 116.407  1.00            
ATOM    822  N   GLY B  51     -13.510   6.433 118.388  1.00            
ATOM    823  CA  GLY B  51     -13.293   7.174 119.623  1.00            
ATOM    824  C   GLY B  51     -13.735   6.440 120.880  1.00            
ATOM    825  O   GLY B  51     -14.703   5.683 120.846  1.00            
ATOM    826  N   ILE B  52     -13.008   6.651 121.978  1.00            
ATOM    827  CA  ILE B  52     -13.373   6.105 123.292  1.00            
ATOM    828  C   ILE B  52     -13.040   7.110 124.400  1.00            
ATOM    829  O   ILE B  52     -12.038   6.957 125.099  1.00            
ATOM    830  CB  ILE B  52     -12.661   4.770 123.608  1.00            
ATOM    831  CG1 ILE B  52     -12.939   3.743 122.508  1.00            
ATOM    832  CG2 ILE B  52     -13.114   4.236 124.986  1.00            
ATOM    833  CD1 ILE B  52     -12.371   2.358 122.784  1.00            
ATOM    834  N   GLY B  53     -13.832   8.169 124.519  1.00            
ATOM    835  CA  GLY B  53     -13.611   9.159 125.559  1.00            
ATOM    836  C   GLY B  53     -13.212  10.485 124.954  1.00            
ATOM    837  O   GLY B  53     -12.700  11.366 125.643  1.00            
ATOM    838  N   GLY B  54     -13.435  10.609 123.652  1.00            
ATOM    839  CA  GLY B  54     -13.036  11.787 122.907  1.00            
ATOM    840  C   GLY B  54     -11.658  11.615 122.297  1.00            
ATOM    841  O   GLY B  54     -11.192  12.473 121.545  1.00            
ATOM    842  N   GLU B  55     -11.005  10.503 122.629  1.00            
ATOM    843  CA  GLU B  55      -9.672  10.182 122.116  1.00            
ATOM    844  C   GLU B  55      -9.691   8.980 121.180  1.00            
ATOM    845  O   GLU B  55     -10.579   8.133 121.265  1.00            
ATOM    846  CB  GLU B  55      -8.706   9.931 123.270  1.00            
ATOM    847  CG  GLU B  55      -8.417  11.178 124.082  1.00            
ATOM    848  CD  GLU B  55      -7.421  10.939 125.195  1.00            
ATOM    849  OE1 GLU B  55      -7.698  10.092 126.071  1.00            
ATOM    850  OE2 GLU B  55      -6.359  11.598 125.189  1.00            
ATOM    851  N   LEU B  56      -8.706   8.909 120.289  1.00            
ATOM    852  CA  LEU B  56      -8.681   7.867 119.274  1.00            
ATOM    853  C   LEU B  56      -8.442   6.519 119.948  1.00            
ATOM    854  O   LEU B  56      -7.963   6.465 121.080  1.00            
ATOM    855  CB  LEU B  56      -7.580   8.161 118.250  1.00            
ATOM    856  CG  LEU B  56      -7.763   9.384 117.344  1.00            
ATOM    857  CD1 LEU B  56      -6.549   9.579 116.444  1.00            
ATOM    858  CD2 LEU B  56      -9.015   9.239 116.493  1.00            
ATOM    859  N   ALA B  57      -8.757   5.437 119.242  1.00            
ATOM    860  CA  ALA B  57      -8.605   4.090 119.786  1.00            
ATOM    861  C   ALA B  57      -7.381   3.391 119.205  1.00            
ATOM    862  O   ALA B  57      -6.451   4.041 118.730  1.00            
ATOM    863  CB  ALA B  57      -9.863   3.275 119.528  1.00            
TER     864      ALA B  57                                                      
ATOM    865  N   PRO C   1     -23.011   5.426 125.973  1.00            
ATOM    866  CA  PRO C   1     -23.673   5.851 124.735  1.00            
ATOM    867  C   PRO C   1     -22.772   5.707 123.509  1.00            
ATOM    868  O   PRO C   1     -21.564   5.922 123.602  1.00            
ATOM    869  CB  PRO C   1     -24.022   7.320 124.995  1.00            
ATOM    870  CG  PRO C   1     -23.152   7.763 126.107  1.00            
ATOM    871  CD  PRO C   1     -22.632   6.561 126.832  1.00            
ATOM    872  N   ILE C   2     -23.372   5.341 122.379  1.00            
ATOM    873  CA  ILE C   2     -22.639   5.091 121.142  1.00            
ATOM    874  C   ILE C   2     -23.195   5.954 120.015  1.00            
ATOM    875  O   ILE C   2     -24.390   5.929 119.729  1.00            
ATOM    876  CB  ILE C   2     -22.715   3.599 120.750  1.00            
ATOM    877  CG1 ILE C   2     -22.004   2.745 121.802  1.00            
ATOM    878  CG2 ILE C   2     -22.084   3.354 119.382  1.00            
ATOM    879  CD1 ILE C   2     -22.434   1.293 121.812  1.00            
ATOM    880  N   ALA C   3     -22.308   6.708 119.374  1.00            
ATOM    881  CA  ALA C   3     -22.676   7.587 118.269  1.00            
ATOM    882  C   ALA C   3     -22.076   7.104 116.956  1.00            
ATOM    883  O   ALA C   3     -20.869   6.880 116.862  1.00            
ATOM    884  CB  ALA C   3     -22.229   9.013 118.560  1.00            
ATOM    885  N   GLN C   4     -22.932   6.941 115.950  1.00            
ATOM    886  CA  GLN C   4     -22.493   6.594 114.603  1.00            
ATOM    887  C   GLN C   4     -22.674   7.783 113.674  1.00            
ATOM    888  O   GLN C   4     -23.809   8.173 113.398  1.00            
ATOM    889  CB  GLN C   4     -23.299   5.418 114.046  1.00            
ATOM    890  CG  GLN C   4     -23.448   4.231 114.970  1.00            
ATOM    891  CD  GLN C   4     -24.192   3.088 114.303  1.00            
ATOM    892  OE1 GLN C   4     -25.220   2.624 114.798  1.00            
ATOM    893  NE2 GLN C   4     -23.667   2.624 113.173  1.00            
ATOM    894  N   ILE C   5     -21.576   8.355 113.188  1.00            
ATOM    895  CA  ILE C   5     -21.665   9.504 112.291  1.00            
ATOM    896  C   ILE C   5     -21.317   9.111 110.862  1.00            
ATOM    897  O   ILE C   5     -20.251   8.562 110.586  1.00            
ATOM    898  CB  ILE C   5     -20.768  10.662 112.755  1.00            
ATOM    899  CG1 ILE C   5     -21.218  11.137 114.134  1.00            
ATOM    900  CG2 ILE C   5     -20.934  11.855 111.841  1.00            
ATOM    901  CD1 ILE C   5     -20.485  10.522 115.265  1.00            
ATOM    902  N   HIS C   6     -22.247   9.423 109.965  1.00            
ATOM    903  CA  HIS C   6     -22.154   9.091 108.550  1.00            
ATOM    904  C   HIS C   6     -21.857  10.382 107.796  1.00            
ATOM    905  O   HIS C   6     -22.669  11.308 107.823  1.00            
ATOM    906  CB  HIS C   6     -23.466   8.474 108.061  1.00            
ATOM    907  CG  HIS C   6     -23.920   7.289 108.869  1.00            
ATOM    908  ND1 HIS C   6     -23.453   6.021 108.657  1.00            
ATOM    909  CD2 HIS C   6     -24.819   7.215 109.883  1.00            
ATOM    910  CE1 HIS C   6     -24.044   5.192 109.518  1.00            
ATOM    911  NE2 HIS C   6     -24.864   5.885 110.259  1.00            
ATOM    912  N   ILE C   7     -20.707  10.455 107.130  1.00            
ATOM    913  CA  ILE C   7     -20.289  11.690 106.467  1.00            
ATOM    914  C   ILE C   7     -19.781  11.425 105.058  1.00            
ATOM    915  O   ILE C   7     -19.397  10.307 104.728  1.00            
ATOM    916  CB  ILE C   7     -19.193  12.416 107.281  1.00            
ATOM    917  CG1 ILE C   7     -17.906  11.585 107.331  1.00            
ATOM    918  CG2 ILE C   7     -19.695  12.686 108.677  1.00            
ATOM    919  CD1 ILE C   7     -16.742  12.295 107.993  1.00            
ATOM    920  N   LEU C   8     -19.772  12.467 104.238  1.00            
ATOM    921  CA  LEU C   8     -19.211  12.381 102.903  1.00            
ATOM    922  C   LEU C   8     -17.694  12.374 102.955  1.00            
ATOM    923  O   LEU C   8     -17.089  13.116 103.723  1.00            
ATOM    924  CB  LEU C   8     -19.719  13.550 102.058  1.00            
ATOM    925  CG  LEU C   8     -21.182  13.425 101.625  1.00            
ATOM    926  CD1 LEU C   8     -21.667  14.657 100.892  1.00            
ATOM    927  CD2 LEU C   8     -21.346  12.210 100.733  1.00            
ATOM    928  N   GLU C   9     -17.078  11.542 102.123  1.00            
ATOM    929  CA  GLU C   9     -15.625  11.457 102.110  1.00            
ATOM    930  C   GLU C   9     -15.075  12.685 101.407  1.00            
ATOM    931  O   GLU C   9     -15.789  13.349 100.657  1.00            
ATOM    932  CB  GLU C   9     -15.126  10.190 101.411  1.00            
ATOM    933  CG  GLU C   9     -15.433  10.113  99.922  1.00            
ATOM    934  CD  GLU C   9     -14.908   8.835  99.290  1.00            
ATOM    935  OE1 GLU C   9     -14.797   7.813 100.004  1.00            
ATOM    936  OE2 GLU C   9     -14.603   8.852  98.078  1.00            
ATOM    937  N   GLY C  10     -13.815  12.999 101.683  1.00            
ATOM    938  CA  GLY C  10     -13.143  14.106 101.035  1.00            
ATOM    939  C   GLY C  10     -12.489  15.027 102.038  1.00            
ATOM    940  O   GLY C  10     -11.680  15.878 101.678  1.00            
ATOM    941  N   ARG C  11     -12.849  14.861 103.304  1.00            
ATOM    942  CA  ARG C  11     -12.341  15.737 104.344  1.00            
ATOM    943  C   ARG C  11     -11.012  15.203 104.866  1.00            
ATOM    944  O   ARG C  11     -10.702  14.022 104.709  1.00            
ATOM    945  CB  ARG C  11     -13.370  15.877 105.467  1.00            
ATOM    946  CG  ARG C  11     -14.648  16.561 104.986  1.00            
ATOM    947  CD  ARG C  11     -15.577  16.952 106.116  1.00            
ATOM    948  NE  ARG C  11     -16.965  16.575 105.838  1.00            
ATOM    949  CZ  ARG C  11     -17.967  17.429 105.623  1.00            
ATOM    950  NH1 ARG C  11     -17.765  18.743 105.621  1.00            
ATOM    951  NH2 ARG C  11     -19.186  16.962 105.387  1.00            
ATOM    952  N   SER C  12     -10.233  16.078 105.491  1.00            
ATOM    953  CA  SER C  12      -8.915  15.716 106.002  1.00            
ATOM    954  C   SER C  12      -9.011  14.940 107.312  1.00            
ATOM    955  O   SER C  12     -10.062  14.909 107.951  1.00            
ATOM    956  CB  SER C  12      -8.066  16.974 106.194  1.00            
ATOM    957  OG  SER C  12      -8.501  17.718 107.321  1.00            
ATOM    958  N   ASP C  13      -7.905  14.311 107.701  1.00            
ATOM    959  CA  ASP C  13      -7.842  13.560 108.952  1.00            
ATOM    960  C   ASP C  13      -7.955  14.478 110.165  1.00            
ATOM    961  O   ASP C  13      -8.381  14.048 111.238  1.00            
ATOM    962  CB  ASP C  13      -6.540  12.756 109.028  1.00            
ATOM    963  CG  ASP C  13      -6.601  11.460 108.238  1.00            
ATOM    964  OD1 ASP C  13      -7.683  11.114 107.714  1.00            
ATOM    965  OD2 ASP C  13      -5.559  10.776 108.150  1.00            
ATOM    966  N   GLU C  14      -7.554  15.733 109.995  1.00            
ATOM    967  CA  GLU C  14      -7.585  16.699 111.084  1.00            
ATOM    968  C   GLU C  14      -9.020  17.033 111.503  1.00            
ATOM    969  O   GLU C  14      -9.318  17.104 112.696  1.00            
ATOM    970  CB  GLU C  14      -6.821  17.963 110.674  1.00            
ATOM    971  CG  GLU C  14      -6.501  18.921 111.813  1.00            
ATOM    972  CD  GLU C  14      -5.730  20.139 111.338  1.00            
ATOM    973  OE1 GLU C  14      -5.627  20.331 110.107  1.00            
ATOM    974  OE2 GLU C  14      -5.226  20.900 112.192  1.00            
ATOM    975  N   GLN C  15      -9.901  17.239 110.529  1.00            
ATOM    976  CA  GLN C  15     -11.304  17.534 110.812  1.00            
ATOM    977  C   GLN C  15     -12.050  16.382 111.467  1.00            
ATOM    978  O   GLN C  15     -12.879  16.596 112.351  1.00            
ATOM    979  CB  GLN C  15     -12.029  17.917 109.527  1.00            
ATOM    980  CG  GLN C  15     -11.750  19.310 109.025  1.00            
ATOM    981  CD  GLN C  15     -12.449  19.574 107.710  1.00            
ATOM    982  OE1 GLN C  15     -11.932  19.239 106.644  1.00            
ATOM    983  NE2 GLN C  15     -13.657  20.122 107.781  1.00            
ATOM    984  N   LYS C  16     -11.756  15.164 111.031  1.00            
ATOM    985  CA  LYS C  16     -12.497  13.997 111.495  1.00            
ATOM    986  C   LYS C  16     -12.150  13.606 112.934  1.00            
ATOM    987  O   LYS C  16     -12.972  13.018 113.640  1.00            
ATOM    988  CB  LYS C  16     -12.231  12.821 110.555  1.00            
ATOM    989  CG  LYS C  16     -12.816  13.042 109.169  1.00            
ATOM    990  CD  LYS C  16     -12.665  11.827 108.276  1.00            
ATOM    991  CE  LYS C  16     -11.313  11.803 107.580  1.00            
ATOM    992  NZ  LYS C  16     -11.190  10.638 106.663  1.00            
ATOM    993  N   GLU C  17     -10.936  13.933 113.367  1.00            
ATOM    994  CA  GLU C  17     -10.518  13.666 114.742  1.00            
ATOM    995  C   GLU C  17     -11.132  14.664 115.723  1.00            
ATOM    996  O   GLU C  17     -11.474  14.309 116.852  1.00            
ATOM    997  CB  GLU C  17      -8.994  13.700 114.857  1.00            
ATOM    998  CG  GLU C  17      -8.477  13.269 116.221  1.00            
ATOM    999  CD  GLU C  17      -6.963  13.219 116.288  1.00            
ATOM   1000  OE1 GLU C  17      -6.313  13.285 115.222  1.00            
ATOM   1001  OE2 GLU C  17      -6.422  13.104 117.408  1.00            
ATOM   1002  N   THR C  18     -11.277  15.909 115.278  1.00            
ATOM   1003  CA  THR C  18     -11.900  16.954 116.085  1.00            
ATOM   1004  C   THR C  18     -13.358  16.603 116.327  1.00            
ATOM   1005  O   THR C  18     -13.903  16.852 117.402  1.00            
ATOM   1006  CB  THR C  18     -11.810  18.335 115.402  1.00            
ATOM   1007  OG1 THR C  18     -10.437  18.707 115.239  1.00            
ATOM   1008  CG2 THR C  18     -12.534  19.405 116.221  1.00            
ATOM   1009  N   LEU C  19     -13.982  16.030 115.306  1.00            
ATOM   1010  CA  LEU C  19     -15.379  15.639 115.372  1.00            
ATOM   1011  C   LEU C  19     -15.587  14.670 116.534  1.00            
ATOM   1012  O   LEU C  19     -16.496  14.850 117.344  1.00            
ATOM   1013  CB  LEU C  19     -15.817  15.014 114.048  1.00            
ATOM   1014  CG  LEU C  19     -17.275  14.571 113.962  1.00            
ATOM   1015  CD1 LEU C  19     -18.165  15.794 113.876  1.00            
ATOM   1016  CD2 LEU C  19     -17.491  13.670 112.757  1.00            
ATOM   1017  N   ILE C  20     -14.740  13.648 116.606  1.00            
ATOM   1018  CA  ILE C  20     -14.814  12.654 117.672  1.00            
ATOM   1019  C   ILE C  20     -14.731  13.322 119.036  1.00            
ATOM   1020  O   ILE C  20     -15.479  12.984 119.952  1.00            
ATOM   1021  CB  ILE C  20     -13.679  11.610 117.554  1.00            
ATOM   1022  CG1 ILE C  20     -13.878  10.757 116.298  1.00            
ATOM   1023  CG2 ILE C  20     -13.603  10.730 118.814  1.00            
ATOM   1024  CD1 ILE C  20     -12.745   9.791 116.011  1.00            
ATOM   1025  N   ARG C  21     -13.817  14.274 119.166  1.00            
ATOM   1026  CA  ARG C  21     -13.601  14.934 120.443  1.00            
ATOM   1027  C   ARG C  21     -14.811  15.796 120.798  1.00            
ATOM   1028  O   ARG C  21     -15.329  15.723 121.912  1.00            
ATOM   1029  CB  ARG C  21     -12.320  15.779 120.398  1.00            
ATOM   1030  CG  ARG C  21     -11.971  16.472 121.712  1.00            
ATOM   1031  CD  ARG C  21     -12.317  17.950 121.681  1.00            
ATOM   1032  NE  ARG C  21     -11.381  18.715 120.859  1.00            
ATOM   1033  CZ  ARG C  21     -11.629  19.923 120.360  1.00            
ATOM   1034  NH1 ARG C  21     -12.796  20.516 120.585  1.00            
ATOM   1035  NH2 ARG C  21     -10.712  20.538 119.626  1.00            
ATOM   1036  N   GLU C  22     -15.259  16.613 119.849  1.00            
ATOM   1037  CA  GLU C  22     -16.366  17.531 120.100  1.00            
ATOM   1038  C   GLU C  22     -17.724  16.844 120.258  1.00            
ATOM   1039  O   GLU C  22     -18.528  17.251 121.097  1.00            
ATOM   1040  CB  GLU C  22     -16.452  18.576 118.988  1.00            
ATOM   1041  CG  GLU C  22     -15.353  19.619 119.071  1.00            
ATOM   1042  CD  GLU C  22     -15.597  20.813 118.171  1.00            
ATOM   1043  OE1 GLU C  22     -16.753  21.278 118.094  1.00            
ATOM   1044  OE2 GLU C  22     -14.627  21.290 117.546  1.00            
ATOM   1045  N   VAL C  23     -17.987  15.812 119.461  1.00            
ATOM   1046  CA  VAL C  23     -19.268  15.115 119.540  1.00            
ATOM   1047  C   VAL C  23     -19.327  14.366 120.864  1.00            
ATOM   1048  O   VAL C  23     -20.370  14.311 121.513  1.00            
ATOM   1049  CB  VAL C  23     -19.475  14.130 118.366  1.00            
ATOM   1050  CG1 VAL C  23     -20.676  13.212 118.628  1.00            
ATOM   1051  CG2 VAL C  23     -19.697  14.886 117.074  1.00            
ATOM   1052  N   SER C  24     -18.195  13.796 121.260  1.00            
ATOM   1053  CA  SER C  24     -18.098  13.071 122.520  1.00            
ATOM   1054  C   SER C  24     -18.413  13.968 123.711  1.00            
ATOM   1055  O   SER C  24     -19.103  13.561 124.647  1.00            
ATOM   1056  CB  SER C  24     -16.698  12.478 122.686  1.00            
ATOM   1057  OG  SER C  24     -16.391  11.576 121.638  1.00            
ATOM   1058  N   GLU C  25     -17.891  15.190 123.670  1.00            
ATOM   1059  CA  GLU C  25     -18.091  16.153 124.744  1.00            
ATOM   1060  C   GLU C  25     -19.572  16.534 124.835  1.00            
ATOM   1061  O   GLU C  25     -20.129  16.636 125.929  1.00            
ATOM   1062  CB  GLU C  25     -17.216  17.391 124.512  1.00            
ATOM   1063  CG  GLU C  25     -17.155  18.364 125.686  1.00            
ATOM   1064  CD  GLU C  25     -18.373  19.249 125.837  1.00            
ATOM   1065  OE1 GLU C  25     -19.085  19.491 124.840  1.00            
ATOM   1066  OE2 GLU C  25     -18.628  19.697 126.977  1.00            
ATOM   1067  N   ALA C  26     -20.197  16.743 123.675  1.00            
ATOM   1068  CA  ALA C  26     -21.608  17.135 123.601  1.00            
ATOM   1069  C   ALA C  26     -22.518  16.080 124.212  1.00            
ATOM   1070  O   ALA C  26     -23.494  16.401 124.893  1.00            
ATOM   1071  CB  ALA C  26     -22.010  17.390 122.155  1.00            
ATOM   1072  N   ILE C  27     -22.186  14.818 123.970  1.00            
ATOM   1073  CA  ILE C  27     -22.953  13.708 124.513  1.00            
ATOM   1074  C   ILE C  27     -22.771  13.662 126.023  1.00            
ATOM   1075  O   ILE C  27     -23.733  13.465 126.765  1.00            
ATOM   1076  CB  ILE C  27     -22.533  12.367 123.871  1.00            
ATOM   1077  CG1 ILE C  27     -22.882  12.381 122.380  1.00            
ATOM   1078  CG2 ILE C  27     -23.234  11.198 124.551  1.00            
ATOM   1079  CD1 ILE C  27     -22.369  11.193 121.595  1.00            
ATOM   1080  N   SER C  28     -21.534  13.839 126.473  1.00            
ATOM   1081  CA  SER C  28     -21.233  13.812 127.898  1.00            
ATOM   1082  C   SER C  28     -21.986  14.893 128.679  1.00            
ATOM   1083  O   SER C  28     -22.528  14.620 129.750  1.00            
ATOM   1084  CB  SER C  28     -19.728  13.970 128.115  1.00            
ATOM   1085  OG  SER C  28     -19.391  13.810 129.480  1.00            
ATOM   1086  N   ARG C  29     -22.033  16.112 128.146  1.00            
ATOM   1087  CA  ARG C  29     -22.767  17.190 128.807  1.00            
ATOM   1088  C   ARG C  29     -24.267  16.967 128.809  1.00            
ATOM   1089  O   ARG C  29     -24.920  17.064 129.848  1.00            
ATOM   1090  CB  ARG C  29     -22.529  18.542 128.148  1.00            
ATOM   1091  CG  ARG C  29     -21.374  19.365 128.665  1.00            
ATOM   1092  CD  ARG C  29     -21.493  20.700 127.983  1.00            
ATOM   1093  NE  ARG C  29     -21.163  20.601 126.567  1.00            
ATOM   1094  CZ  ARG C  29     -21.937  21.039 125.578  1.00            
ATOM   1095  NH1 ARG C  29     -23.141  21.544 125.827  1.00            
ATOM   1096  NH2 ARG C  29     -21.534  20.909 124.324  1.00            
ATOM   1097  N   SER C  30     -24.806  16.694 127.624  1.00            
ATOM   1098  CA  SER C  30     -26.247  16.635 127.426  1.00            
ATOM   1099  C   SER C  30     -26.893  15.596 128.329  1.00            
ATOM   1100  O   SER C  30     -27.998  15.803 128.824  1.00            
ATOM   1101  CB  SER C  30     -26.567  16.322 125.960  1.00            
ATOM   1102  OG  SER C  30     -26.045  17.316 125.097  1.00            
ATOM   1103  N   LEU C  31     -26.194  14.488 128.550  1.00            
ATOM   1104  CA  LEU C  31     -26.751  13.368 129.297  1.00            
ATOM   1105  C   LEU C  31     -26.100  13.174 130.666  1.00            
ATOM   1106  O   LEU C  31     -26.349  12.166 131.327  1.00            
ATOM   1107  CB  LEU C  31     -26.596  12.090 128.474  1.00            
ATOM   1108  CG  LEU C  31     -27.040  12.194 127.013  1.00            
ATOM   1109  CD1 LEU C  31     -26.853  10.864 126.305  1.00            
ATOM   1110  CD2 LEU C  31     -28.484  12.663 126.912  1.00            
ATOM   1111  N   ASP C  32     -25.325  14.164 131.104  1.00            
ATOM   1112  CA  ASP C  32     -24.531  14.070 132.334  1.00            
ATOM   1113  C   ASP C  32     -23.913  12.680 132.477  1.00            
ATOM   1114  O   ASP C  32     -24.032  12.038 133.523  1.00            
ATOM   1115  CB  ASP C  32     -25.387  14.392 133.564  1.00            
ATOM   1116  CG  ASP C  32     -24.555  14.595 134.824  1.00            
ATOM   1117  OD1 ASP C  32     -23.309  14.561 134.736  1.00            
ATOM   1118  OD2 ASP C  32     -25.151  14.782 135.908  1.00            
ATOM   1119  N   ALA C  33     -23.277  12.218 131.405  1.00            
ATOM   1120  CA  ALA C  33     -22.663  10.899 131.373  1.00            
ATOM   1121  C   ALA C  33     -21.146  11.035 131.397  1.00            
ATOM   1122  O   ALA C  33     -20.606  11.984 130.831  1.00            
ATOM   1123  CB  ALA C  33     -23.110  10.136 130.133  1.00            
ATOM   1124  N   PRO C  34     -20.449  10.094 132.056  1.00            
ATOM   1125  CA  PRO C  34     -18.982  10.142 132.044  1.00            
ATOM   1126  C   PRO C  34     -18.425  10.035 130.629  1.00            
ATOM   1127  O   PRO C  34     -18.852   9.176 129.858  1.00            
ATOM   1128  CB  PRO C  34     -18.577   8.934 132.897  1.00            
ATOM   1129  CG  PRO C  34     -19.763   8.037 132.887  1.00            
ATOM   1130  CD  PRO C  34     -20.946   8.952 132.841  1.00            
ATOM   1131  N   LEU C  35     -17.485  10.913 130.299  1.00            
ATOM   1132  CA  LEU C  35     -16.926  10.983 128.955  1.00            
ATOM   1133  C   LEU C  35     -16.327   9.657 128.491  1.00            
ATOM   1134  O   LEU C  35     -16.460   9.290 127.326  1.00            
ATOM   1135  CB  LEU C  35     -15.856  12.073 128.902  1.00            
ATOM   1136  CG  LEU C  35     -15.229  12.369 127.538  1.00            
ATOM   1137  CD1 LEU C  35     -16.253  12.983 126.599  1.00            
ATOM   1138  CD2 LEU C  35     -14.022  13.281 127.697  1.00            
ATOM   1139  N   THR C  36     -15.694   8.930 129.407  1.00            
ATOM   1140  CA  THR C  36     -14.986   7.699 129.054  1.00            
ATOM   1141  C   THR C  36     -15.907   6.565 128.603  1.00            
ATOM   1142  O   THR C  36     -15.433   5.545 128.102  1.00            
ATOM   1143  CB  THR C  36     -14.124   7.189 130.231  1.00            
ATOM   1144  OG1 THR C  36     -14.936   7.054 131.405  1.00            
ATOM   1145  CG2 THR C  36     -12.984   8.156 130.523  1.00            
ATOM   1146  N   SER C  37     -17.215   6.744 128.762  1.00            
ATOM   1147  CA  SER C  37     -18.174   5.729 128.334  1.00            
ATOM   1148  C   SER C  37     -18.676   6.039 126.927  1.00            
ATOM   1149  O   SER C  37     -19.369   5.226 126.313  1.00            
ATOM   1150  CB  SER C  37     -19.355   5.650 129.303  1.00            
ATOM   1151  OG  SER C  37     -20.077   6.870 129.332  1.00            
ATOM   1152  N   VAL C  38     -18.314   7.214 126.418  1.00            
ATOM   1153  CA  VAL C  38     -18.773   7.658 125.108  1.00            
ATOM   1154  C   VAL C  38     -17.899   7.113 123.984  1.00            
ATOM   1155  O   VAL C  38     -16.677   7.260 124.004  1.00            
ATOM   1156  CB  VAL C  38     -18.795   9.198 125.018  1.00            
ATOM   1157  CG1 VAL C  38     -19.325   9.651 123.662  1.00            
ATOM   1158  CG2 VAL C  38     -19.634   9.784 126.145  1.00            
ATOM   1159  N   ARG C  39     -18.545   6.486 123.006  1.00            
ATOM   1160  CA  ARG C  39     -17.865   5.982 121.818  1.00            
ATOM   1161  C   ARG C  39     -18.380   6.629 120.543  1.00            
ATOM   1162  O   ARG C  39     -19.579   6.859 120.387  1.00            
ATOM   1163  CB  ARG C  39     -18.008   4.465 121.709  1.00            
ATOM   1164  CG  ARG C  39     -17.131   3.692 122.674  1.00            
ATOM   1165  CD  ARG C  39     -17.544   2.237 122.764  1.00            
ATOM   1166  NE  ARG C  39     -16.582   1.456 123.534  1.00            
ATOM   1167  CZ  ARG C  39     -16.473   1.485 124.859  1.00            
ATOM   1168  NH1 ARG C  39     -17.276   2.253 125.586  1.00            
ATOM   1169  NH2 ARG C  39     -15.557   0.738 125.460  1.00            
ATOM   1170  N   VAL C  40     -17.452   6.925 119.639  1.00            
ATOM   1171  CA  VAL C  40     -17.783   7.488 118.340  1.00            
ATOM   1172  C   VAL C  40     -17.104   6.680 117.248  1.00            
ATOM   1173  O   VAL C  40     -15.920   6.365 117.336  1.00            
ATOM   1174  CB  VAL C  40     -17.353   8.968 118.209  1.00            
ATOM   1175  CG1 VAL C  40     -17.648   9.488 116.805  1.00            
ATOM   1176  CG2 VAL C  40     -18.045   9.827 119.252  1.00            
ATOM   1177  N   ILE C  41     -17.879   6.338 116.228  1.00            
ATOM   1178  CA  ILE C  41     -17.358   5.679 115.043  1.00            
ATOM   1179  C   ILE C  41     -17.816   6.441 113.812  1.00            
ATOM   1180  O   ILE C  41     -19.006   6.682 113.615  1.00            
ATOM   1181  CB  ILE C  41     -17.787   4.198 114.967  1.00            
ATOM   1182  CG1 ILE C  41     -19.223   4.038 115.480  1.00            
ATOM   1183  CG2 ILE C  41     -16.891   3.354 115.852  1.00            
ATOM   1184  CD1 ILE C  41     -19.788   2.629 115.369  1.00            
ATOM   1185  N   ILE C  42     -16.843   6.807 112.984  1.00            
ATOM   1186  CA  ILE C  42     -17.093   7.584 111.782  1.00            
ATOM   1187  C   ILE C  42     -17.145   6.657 110.580  1.00            
ATOM   1188  O   ILE C  42     -16.303   5.773 110.431  1.00            
ATOM   1189  CB  ILE C  42     -15.998   8.655 111.567  1.00            
ATOM   1190  CG1 ILE C  42     -15.934   9.599 112.772  1.00            
ATOM   1191  CG2 ILE C  42     -16.248   9.434 110.272  1.00            
ATOM   1192  CD1 ILE C  42     -14.784  10.589 112.725  1.00            
ATOM   1193  N   THR C  43     -18.146   6.865 109.734  1.00            
ATOM   1194  CA  THR C  43     -18.264   6.141 108.476  1.00            
ATOM   1195  C   THR C  43     -18.333   7.120 107.316  1.00            
ATOM   1196  O   THR C  43     -19.228   7.964 107.259  1.00            
ATOM   1197  CB  THR C  43     -19.511   5.239 108.460  1.00            
ATOM   1198  OG1 THR C  43     -19.533   4.435 109.646  1.00            
ATOM   1199  CG2 THR C  43     -19.507   4.332 107.239  1.00            
ATOM   1200  N   GLU C  44     -17.378   7.005 106.399  1.00            
ATOM   1201  CA  GLU C  44     -17.331   7.868 105.228  1.00            
ATOM   1202  C   GLU C  44     -17.994   7.183 104.043  1.00            
ATOM   1203  O   GLU C  44     -17.941   5.960 103.911  1.00            
ATOM   1204  CB  GLU C  44     -15.896   8.252 104.884  1.00            
ATOM   1205  CG  GLU C  44     -15.259   9.174 105.902  1.00            
ATOM   1206  CD  GLU C  44     -13.926   9.717 105.435  1.00            
ATOM   1207  OE1 GLU C  44     -13.017   8.910 105.154  1.00            
ATOM   1208  OE2 GLU C  44     -13.790  10.956 105.342  1.00            
ATOM   1209  N   TYR C  45     -18.627   7.982 103.192  1.00            
ATOM   1210  CA  TYR C  45     -19.300   7.473 102.006  1.00            
ATOM   1211  C   TYR C  45     -18.771   8.129 100.745  1.00            
ATOM   1212  O   TYR C  45     -18.628   9.351 100.680  1.00            
ATOM   1213  CB  TYR C  45     -20.806   7.688 102.130  1.00            
ATOM   1214  CG  TYR C  45     -21.385   6.895 103.270  1.00            
ATOM   1215  CD1 TYR C  45     -21.357   7.391 104.565  1.00            
ATOM   1216  CD2 TYR C  45     -21.934   5.636 103.060  1.00            
ATOM   1217  CE1 TYR C  45     -21.870   6.664 105.618  1.00            
ATOM   1218  CE2 TYR C  45     -22.452   4.900 104.111  1.00            
ATOM   1219  CZ  TYR C  45     -22.416   5.421 105.388  1.00            
ATOM   1220  OH  TYR C  45     -22.928   4.700 106.440  1.00            
ATOM   1221  N   ALA C  46     -18.489   7.308  99.739  1.00            
ATOM   1222  CA  ALA C  46     -18.031   7.831  98.469  1.00            
ATOM   1223  C   ALA C  46     -19.196   8.568  97.842  1.00            
ATOM   1224  O   ALA C  46     -20.353   8.266  98.129  1.00            
ATOM   1225  CB  ALA C  46     -17.532   6.707  97.567  1.00            
ATOM   1226  N   LYS C  47     -18.882   9.546  97.000  1.00            
ATOM   1227  CA  LYS C  47     -19.898  10.407  96.408  1.00            
ATOM   1228  C   LYS C  47     -20.984   9.579  95.726  1.00            
ATOM   1229  O   LYS C  47     -22.157   9.947  95.750  1.00            
ATOM   1230  CB  LYS C  47     -19.262  11.388  95.423  1.00            
ATOM   1231  CG  LYS C  47     -18.361  12.430  96.083  1.00            
ATOM   1232  CD  LYS C  47     -17.681  13.290  95.040  1.00            
ATOM   1233  CE  LYS C  47     -18.684  14.227  94.387  1.00            
ATOM   1234  NZ  LYS C  47     -18.017  15.307  93.614  1.00            
ATOM   1235  N   GLY C  48     -20.591   8.457  95.129  1.00            
ATOM   1236  CA  GLY C  48     -21.537   7.601  94.436  1.00            
ATOM   1237  C   GLY C  48     -22.299   6.670  95.366  1.00            
ATOM   1238  O   GLY C  48     -23.014   5.782  94.902  1.00            
ATOM   1239  N   HIS C  49     -22.161   6.883  96.675  1.00            
ATOM   1240  CA  HIS C  49     -22.823   6.048  97.681  1.00            
ATOM   1241  C   HIS C  49     -23.733   6.858  98.605  1.00            
ATOM   1242  O   HIS C  49     -24.224   6.334  99.604  1.00            
ATOM   1243  CB  HIS C  49     -21.788   5.298  98.529  1.00            
ATOM   1244  CG  HIS C  49     -21.077   4.204  97.798  1.00            
ATOM   1245  ND1 HIS C  49     -19.932   3.610  98.280  1.00            
ATOM   1246  CD2 HIS C  49     -21.350   3.592  96.619  1.00            
ATOM   1247  CE1 HIS C  49     -19.529   2.679  97.434  1.00            
ATOM   1248  NE2 HIS C  49     -20.372   2.649  96.418  1.00            
ATOM   1249  N   ALA C  50     -23.952   8.129  98.278  1.00            
ATOM   1250  CA  ALA C  50     -24.787   9.007  99.100  1.00            
ATOM   1251  C   ALA C  50     -25.785   9.787  98.245  1.00            
ATOM   1252  O   ALA C  50     -25.425  10.326  97.197  1.00            
ATOM   1253  CB  ALA C  50     -23.919   9.960  99.897  1.00            
ATOM   1254  N   GLY C  51     -27.038   9.828  98.697  1.00            
ATOM   1255  CA  GLY C  51     -28.115  10.515  97.991  1.00            
ATOM   1256  C   GLY C  51     -28.864  11.604  98.754  1.00            
ATOM   1257  O   GLY C  51     -28.993  11.532  99.976  1.00            
ATOM   1258  N   ILE C  52     -29.334  12.620  98.023  1.00            
ATOM   1259  CA  ILE C  52     -30.177  13.695  98.568  1.00            
ATOM   1260  C   ILE C  52     -31.264  14.034  97.564  1.00            
ATOM   1261  O   ILE C  52     -31.150  15.018  96.832  1.00            
ATOM   1262  CB  ILE C  52     -29.410  14.998  98.873  1.00            
ATOM   1263  CG1 ILE C  52     -28.312  14.764  99.874  1.00            
ATOM   1264  CG2 ILE C  52     -30.296  16.067  99.482  1.00            
ATOM   1265  CD1 ILE C  52     -27.015  14.620  99.193  1.00            
ATOM   1266  N   GLY C  53     -32.267  13.174  97.451  1.00            
ATOM   1267  CA  GLY C  53     -33.382  13.445  96.563  1.00            
ATOM   1268  C   GLY C  53     -33.390  12.484  95.399  1.00            
ATOM   1269  O   GLY C  53     -34.069  12.712  94.401  1.00            
ATOM   1270  N   GLY C  54     -32.618  11.412  95.534  1.00            
ATOM   1271  CA  GLY C  54     -32.455  10.450  94.466  1.00            
ATOM   1272  C   GLY C  54     -31.243  10.778  93.609  1.00            
ATOM   1273  O   GLY C  54     -30.896  10.024  92.697  1.00            
ATOM   1274  N   GLU C  55     -30.602  11.908  93.906  1.00            
ATOM   1275  CA  GLU C  55     -29.411  12.363  93.188  1.00            
ATOM   1276  C   GLU C  55     -28.172  12.258  94.057  1.00            
ATOM   1277  O   GLU C  55     -28.261  12.322  95.282  1.00            
ATOM   1278  CB  GLU C  55     -29.574  13.814  92.731  1.00            
ATOM   1279  CG  GLU C  55     -30.616  14.043  91.647  1.00            
ATOM   1280  CD  GLU C  55     -30.412  13.159  90.431  1.00            
ATOM   1281  OE1 GLU C  55     -29.244  12.929  90.048  1.00            
ATOM   1282  OE2 GLU C  55     -31.419  12.702  89.852  1.00            
ATOM   1283  N   LEU C  56     -27.015  12.097  93.425  1.00            
ATOM   1284  CA  LEU C  56     -25.782  11.911  94.170  1.00            
ATOM   1285  C   LEU C  56     -25.417  13.212  94.862  1.00            
ATOM   1286  O   LEU C  56     -25.956  14.272  94.543  1.00            
ATOM   1287  CB  LEU C  56     -24.644  11.467  93.248  1.00            
ATOM   1288  CG  LEU C  56     -24.724  10.070  92.631  1.00            
ATOM   1289  CD1 LEU C  56     -23.534   9.819  91.721  1.00            
ATOM   1290  CD2 LEU C  56     -24.791   9.024  93.729  1.00            
ATOM   1291  N   ALA C  57     -24.499  13.117  95.815  1.00            
ATOM   1292  CA  ALA C  57     -24.059  14.275  96.581  1.00            
ATOM   1293  C   ALA C  57     -22.696  14.773  96.102  1.00            
ATOM   1294  O   ALA C  57     -21.723  14.019  96.063  1.00            
ATOM   1295  CB  ALA C  57     -24.008  13.931  98.050  1.00            
TER    1296      ALA C  57                                                      
ATOM   1297  N   PRO D   1     -24.437  15.256 106.647  1.00            
ATOM   1298  CA  PRO D   1     -23.966  14.353 107.703  1.00            
ATOM   1299  C   PRO D   1     -25.118  13.821 108.553  1.00            
ATOM   1300  O   PRO D   1     -26.042  14.571 108.869  1.00            
ATOM   1301  CB  PRO D   1     -23.030  15.233 108.538  1.00            
ATOM   1302  CG  PRO D   1     -23.404  16.643 108.223  1.00            
ATOM   1303  CD  PRO D   1     -24.167  16.673 106.938  1.00            
ATOM   1304  N   ILE D   2     -25.050  12.545 108.922  1.00            
ATOM   1305  CA  ILE D   2     -26.112  11.901 109.690  1.00            
ATOM   1306  C   ILE D   2     -25.526  11.233 110.924  1.00            
ATOM   1307  O   ILE D   2     -24.590  10.441 110.819  1.00            
ATOM   1308  CB  ILE D   2     -26.866  10.844 108.861  1.00            
ATOM   1309  CG1 ILE D   2     -27.517  11.480 107.634  1.00            
ATOM   1310  CG2 ILE D   2     -27.910  10.124 109.718  1.00            
ATOM   1311  CD1 ILE D   2     -27.833  10.487 106.539  1.00            
ATOM   1312  N   ALA D   3     -26.079  11.554 112.088  1.00            
ATOM   1313  CA  ALA D   3     -25.638  10.945 113.335  1.00            
ATOM   1314  C   ALA D   3     -26.741  10.075 113.926  1.00            
ATOM   1315  O   ALA D   3     -27.858  10.535 114.139  1.00            
ATOM   1316  CB  ALA D   3     -25.214  12.016 114.326  1.00            
ATOM   1317  N   GLN D   4     -26.414   8.812 114.181  1.00            
ATOM   1318  CA  GLN D   4     -27.313   7.902 114.879  1.00            
ATOM   1319  C   GLN D   4     -26.726   7.661 116.258  1.00            
ATOM   1320  O   GLN D   4     -25.666   7.051 116.389  1.00            
ATOM   1321  CB  GLN D   4     -27.478   6.584 114.118  1.00            
ATOM   1322  CG  GLN D   4     -28.643   5.730 114.603  1.00            
ATOM   1323  CD  GLN D   4     -28.835   4.468 113.775  1.00            
ATOM   1324  OE1 GLN D   4     -28.177   4.277 112.747  1.00            
ATOM   1325  NE2 GLN D   4     -29.748   3.604 114.216  1.00            
ATOM   1326  N   ILE D   5     -27.418   8.146 117.282  1.00            
ATOM   1327  CA  ILE D   5     -26.919   8.053 118.647  1.00            
ATOM   1328  C   ILE D   5     -27.689   7.014 119.447  1.00            
ATOM   1329  O   ILE D   5     -28.915   7.048 119.524  1.00            
ATOM   1330  CB  ILE D   5     -26.999   9.414 119.365  1.00            
ATOM   1331  CG1 ILE D   5     -26.350  10.499 118.500  1.00            
ATOM   1332  CG2 ILE D   5     -26.318   9.333 120.726  1.00            
ATOM   1333  CD1 ILE D   5     -26.527  11.892 119.023  1.00            
ATOM   1334  N   HIS D   6     -26.935   6.097 120.044  1.00            
ATOM   1335  CA  HIS D   6     -27.481   4.989 120.813  1.00            
ATOM   1336  C   HIS D   6     -27.267   5.219 122.301  1.00            
ATOM   1337  O   HIS D   6     -26.132   5.304 122.764  1.00            
ATOM   1338  CB  HIS D   6     -26.822   3.678 120.385  1.00            
ATOM   1339  CG  HIS D   6     -26.968   3.375 118.926  1.00            
ATOM   1340  ND1 HIS D   6     -28.089   2.769 118.397  1.00            
ATOM   1341  CD2 HIS D   6     -26.132   3.592 117.885  1.00            
ATOM   1342  CE1 HIS D   6     -27.935   2.627 117.093  1.00            
ATOM   1343  NE2 HIS D   6     -26.756   3.117 116.757  1.00            
ATOM   1344  N   ILE D   7     -28.364   5.331 123.045  1.00            
ATOM   1345  CA  ILE D   7     -28.298   5.630 124.474  1.00            
ATOM   1346  C   ILE D   7     -29.231   4.720 125.272  1.00            
ATOM   1347  O   ILE D   7     -30.172   4.149 124.719  1.00            
ATOM   1348  CB  ILE D   7     -28.657   7.107 124.753  1.00            
ATOM   1349  CG1 ILE D   7     -30.135   7.380 124.452  1.00            
ATOM   1350  CG2 ILE D   7     -27.761   8.028 123.933  1.00            
ATOM   1351  CD1 ILE D   7     -30.601   8.763 124.845  1.00            
ATOM   1352  N   LEU D   8     -28.968   4.589 126.568  1.00            
ATOM   1353  CA  LEU D   8     -29.845   3.825 127.443  1.00            
ATOM   1354  C   LEU D   8     -31.079   4.668 127.723  1.00            
ATOM   1355  O   LEU D   8     -30.985   5.881 127.834  1.00            
ATOM   1356  CB  LEU D   8     -29.162   3.461 128.760  1.00            
ATOM   1357  CG  LEU D   8     -27.909   2.588 128.718  1.00            
ATOM   1358  CD1 LEU D   8     -27.446   2.378 130.161  1.00            
ATOM   1359  CD2 LEU D   8     -28.147   1.281 127.966  1.00            
ATOM   1360  N   GLU D   9     -32.241   4.034 127.818  1.00            
ATOM   1361  CA  GLU D   9     -33.462   4.779 128.087  1.00            
ATOM   1362  C   GLU D   9     -33.455   5.235 129.543  1.00            
ATOM   1363  O   GLU D   9     -32.754   4.663 130.384  1.00            
ATOM   1364  CB  GLU D   9     -34.700   3.933 127.788  1.00            
ATOM   1365  CG  GLU D   9     -34.848   2.704 128.658  1.00            
ATOM   1366  CD  GLU D   9     -36.072   1.887 128.287  1.00            
ATOM   1367  OE1 GLU D   9     -36.480   1.940 127.106  1.00            
ATOM   1368  OE2 GLU D   9     -36.625   1.190 129.168  1.00            
ATOM   1369  N   GLY D  10     -34.232   6.275 129.830  1.00            
ATOM   1370  CA  GLY D  10     -34.349   6.806 131.174  1.00            
ATOM   1371  C   GLY D  10     -34.235   8.318 131.276  1.00            
ATOM   1372  O   GLY D  10     -34.596   8.882 132.306  1.00            
ATOM   1373  N   ARG D  11     -33.761   8.987 130.225  1.00            
ATOM   1374  CA  ARG D  11     -33.643  10.445 130.280  1.00            
ATOM   1375  C   ARG D  11     -34.945  11.124 129.906  1.00            
ATOM   1376  O   ARG D  11     -35.837  10.532 129.298  1.00            
ATOM   1377  CB  ARG D  11     -32.545  11.006 129.361  1.00            
ATOM   1378  CG  ARG D  11     -31.120  10.719 129.779  1.00            
ATOM   1379  CD  ARG D  11     -30.689   9.311 129.454  1.00            
ATOM   1380  NE  ARG D  11     -29.306   9.075 129.859  1.00            
ATOM   1381  CZ  ARG D  11     -28.538   8.100 129.383  1.00            
ATOM   1382  NH1 ARG D  11     -29.033   7.209 128.536  1.00            
ATOM   1383  NH2 ARG D  11     -27.289   7.977 129.811  1.00            
ATOM   1384  N   SER D  12     -35.028  12.387 130.293  1.00            
ATOM   1385  CA  SER D  12     -36.181  13.212 130.017  1.00            
ATOM   1386  C   SER D  12     -36.122  13.674 128.563  1.00            
ATOM   1387  O   SER D  12     -35.087  13.544 127.910  1.00            
ATOM   1388  CB  SER D  12     -36.201  14.403 130.966  1.00            
ATOM   1389  OG  SER D  12     -35.231  15.359 130.578  1.00            
ATOM   1390  N   ASP D  13     -37.227  14.203 128.051  1.00            
ATOM   1391  CA  ASP D  13     -37.254  14.721 126.689  1.00            
ATOM   1392  C   ASP D  13     -36.338  15.934 126.556  1.00            
ATOM   1393  O   ASP D  13     -35.802  16.209 125.483  1.00            
ATOM   1394  CB  ASP D  13     -38.681  15.097 126.284  1.00            
ATOM   1395  CG  ASP D  13     -39.506  13.897 125.845  1.00            
ATOM   1396  OD1 ASP D  13     -38.949  12.784 125.742  1.00            
ATOM   1397  OD2 ASP D  13     -40.721  14.069 125.601  1.00            
ATOM   1398  N   GLU D  14     -36.139  16.639 127.664  1.00            
ATOM   1399  CA  GLU D  14     -35.328  17.852 127.675  1.00            
ATOM   1400  C   GLU D  14     -33.862  17.537 127.404  1.00            
ATOM   1401  O   GLU D  14     -33.207  18.220 126.618  1.00            
ATOM   1402  CB  GLU D  14     -35.462  18.575 129.019  1.00            
ATOM   1403  CG  GLU D  14     -36.871  19.058 129.354  1.00            
ATOM   1404  CD  GLU D  14     -37.789  17.948 129.845  1.00            
ATOM   1405  OE1 GLU D  14     -37.423  16.764 129.715  1.00            
ATOM   1406  OE2 GLU D  14     -38.876  18.260 130.376  1.00            
ATOM   1407  N   GLN D  15     -33.358  16.486 128.041  1.00            
ATOM   1408  CA  GLN D  15     -31.968  16.082 127.874  1.00            
ATOM   1409  C   GLN D  15     -31.716  15.649 126.436  1.00            
ATOM   1410  O   GLN D  15     -30.668  15.940 125.859  1.00            
ATOM   1411  CB  GLN D  15     -31.627  14.950 128.840  1.00            
ATOM   1412  CG  GLN D  15     -31.515  15.387 130.280  1.00            
ATOM   1413  CD  GLN D  15     -31.235  14.230 131.209  1.00            
ATOM   1414  OE1 GLN D  15     -32.144  13.483 131.581  1.00            
ATOM   1415  NE2 GLN D  15     -29.965  14.037 131.546  1.00            
ATOM   1416  N   LYS D  16     -32.689  14.949 125.865  1.00            
ATOM   1417  CA  LYS D  16     -32.591  14.453 124.498  1.00            
ATOM   1418  C   LYS D  16     -32.745  15.583 123.485  1.00            
ATOM   1419  O   LYS D  16     -32.234  15.504 122.368  1.00            
ATOM   1420  CB  LYS D  16     -33.643  13.372 124.266  1.00            
ATOM   1421  CG  LYS D  16     -33.299  12.051 124.934  1.00            
ATOM   1422  CD  LYS D  16     -34.346  10.995 124.653  1.00            
ATOM   1423  CE  LYS D  16     -35.438  11.055 125.705  1.00            
ATOM   1424  NZ  LYS D  16     -36.491  10.029 125.514  1.00            
ATOM   1425  N   GLU D  17     -33.447  16.638 123.882  1.00            
ATOM   1426  CA  GLU D  17     -33.581  17.812 123.033  1.00            
ATOM   1427  C   GLU D  17     -32.259  18.569 123.050  1.00            
ATOM   1428  O   GLU D  17     -31.829  19.128 122.039  1.00            
ATOM   1429  CB  GLU D  17     -34.722  18.704 123.520  1.00            
ATOM   1430  CG  GLU D  17     -35.034  19.880 122.609  1.00            
ATOM   1431  CD  GLU D  17     -36.226  20.688 123.089  1.00            
ATOM   1432  OE1 GLU D  17     -36.955  20.209 123.985  1.00            
ATOM   1433  OE2 GLU D  17     -36.433  21.805 122.571  1.00            
ATOM   1434  N   THR D  18     -31.617  18.568 124.215  1.00            
ATOM   1435  CA  THR D  18     -30.302  19.168 124.379  1.00            
ATOM   1436  C   THR D  18     -29.250  18.378 123.606  1.00            
ATOM   1437  O   THR D  18     -28.364  18.958 122.977  1.00            
ATOM   1438  CB  THR D  18     -29.909  19.239 125.874  1.00            
ATOM   1439  OG1 THR D  18     -30.825  20.091 126.571  1.00            
ATOM   1440  CG2 THR D  18     -28.493  19.774 126.055  1.00            
ATOM   1441  N   LEU D  19     -29.359  17.054 123.660  1.00            
ATOM   1442  CA  LEU D  19     -28.422  16.173 122.973  1.00            
ATOM   1443  C   LEU D  19     -28.441  16.449 121.475  1.00            
ATOM   1444  O   LEU D  19     -27.394  16.644 120.854  1.00            
ATOM   1445  CB  LEU D  19     -28.755  14.706 123.259  1.00            
ATOM   1446  CG  LEU D  19     -27.859  13.655 122.598  1.00            
ATOM   1447  CD1 LEU D  19     -26.493  13.631 123.256  1.00            
ATOM   1448  CD2 LEU D  19     -28.503  12.280 122.680  1.00            
ATOM   1449  N   ILE D  20     -29.640  16.459 120.903  1.00            
ATOM   1450  CA  ILE D  20     -29.820  16.720 119.479  1.00            
ATOM   1451  C   ILE D  20     -29.230  18.064 119.066  1.00            
ATOM   1452  O   ILE D  20     -28.566  18.160 118.035  1.00            
ATOM   1453  CB  ILE D  20     -31.316  16.659 119.097  1.00            
ATOM   1454  CG1 ILE D  20     -31.779  15.203 119.145  1.00            
ATOM   1455  CG2 ILE D  20     -31.555  17.225 117.699  1.00            
ATOM   1456  CD1 ILE D  20     -33.263  14.992 118.938  1.00            
ATOM   1457  N   ARG D  21     -29.465  19.098 119.864  1.00            
ATOM   1458  CA  ARG D  21     -28.977  20.426 119.514  1.00            
ATOM   1459  C   ARG D  21     -27.457  20.499 119.611  1.00            
ATOM   1460  O   ARG D  21     -26.784  20.952 118.685  1.00            
ATOM   1461  CB  ARG D  21     -29.579  21.491 120.429  1.00            
ATOM   1462  CG  ARG D  21     -29.138  22.911 120.075  1.00            
ATOM   1463  CD  ARG D  21     -29.746  23.952 120.995  1.00            
ATOM   1464  NE  ARG D  21     -30.863  23.424 121.779  1.00            
ATOM   1465  CZ  ARG D  21     -30.817  23.149 123.082  1.00            
ATOM   1466  NH1 ARG D  21     -29.695  23.313 123.779  1.00            
ATOM   1467  NH2 ARG D  21     -31.897  22.677 123.690  1.00            
ATOM   1468  N   GLU D  22     -26.927  20.037 120.739  1.00            
ATOM   1469  CA  GLU D  22     -25.503  20.159 121.030  1.00            
ATOM   1470  C   GLU D  22     -24.650  19.286 120.110  1.00            
ATOM   1471  O   GLU D  22     -23.566  19.694 119.694  1.00            
ATOM   1472  CB  GLU D  22     -25.234  19.811 122.497  1.00            
ATOM   1473  CG  GLU D  22     -25.769  20.863 123.466  1.00            
ATOM   1474  CD  GLU D  22     -25.164  22.237 123.248  1.00            
ATOM   1475  OE1 GLU D  22     -23.936  22.391 123.416  1.00            
ATOM   1476  OE2 GLU D  22     -25.921  23.158 122.874  1.00            
ATOM   1477  N   VAL D  23     -25.127  18.085 119.800  1.00            
ATOM   1478  CA  VAL D  23     -24.388  17.201 118.907  1.00            
ATOM   1479  C   VAL D  23     -24.422  17.767 117.495  1.00            
ATOM   1480  O   VAL D  23     -23.418  17.750 116.784  1.00            
ATOM   1481  CB  VAL D  23     -24.967  15.765 118.898  1.00            
ATOM   1482  CG1 VAL D  23     -24.452  14.970 117.688  1.00            
ATOM   1483  CG2 VAL D  23     -24.636  15.048 120.188  1.00            
ATOM   1484  N   SER D  24     -25.584  18.281 117.106  1.00            
ATOM   1485  CA  SER D  24     -25.765  18.867 115.785  1.00            
ATOM   1486  C   SER D  24     -24.834  20.053 115.576  1.00            
ATOM   1487  O   SER D  24     -24.251  20.215 114.503  1.00            
ATOM   1488  CB  SER D  24     -27.215  19.304 115.591  1.00            
ATOM   1489  OG  SER D  24     -28.094  18.201 115.711  1.00            
ATOM   1490  N   GLU D  25     -24.702  20.882 116.606  1.00            
ATOM   1491  CA  GLU D  25     -23.838  22.052 116.539  1.00            
ATOM   1492  C   GLU D  25     -22.382  21.634 116.360  1.00            
ATOM   1493  O   GLU D  25     -21.664  22.186 115.527  1.00            
ATOM   1494  CB  GLU D  25     -23.978  22.893 117.810  1.00            
ATOM   1495  CG  GLU D  25     -25.212  23.789 117.859  1.00            
ATOM   1496  CD  GLU D  25     -25.204  24.882 116.810  1.00            
ATOM   1497  OE1 GLU D  25     -24.140  25.126 116.201  1.00            
ATOM   1498  OE2 GLU D  25     -26.266  25.505 116.600  1.00            
ATOM   1499  N   ALA D  26     -21.965  20.635 117.132  1.00            
ATOM   1500  CA  ALA D  26     -20.590  20.147 117.105  1.00            
ATOM   1501  C   ALA D  26     -20.199  19.596 115.738  1.00            
ATOM   1502  O   ALA D  26     -19.073  19.794 115.286  1.00            
ATOM   1503  CB  ALA D  26     -20.391  19.081 118.175  1.00            
ATOM   1504  N   ILE D  27     -21.127  18.910 115.080  1.00            
ATOM   1505  CA  ILE D  27     -20.858  18.355 113.759  1.00            
ATOM   1506  C   ILE D  27     -20.705  19.477 112.746  1.00            
ATOM   1507  O   ILE D  27     -19.764  19.484 111.951  1.00            
ATOM   1508  CB  ILE D  27     -21.988  17.407 113.303  1.00            
ATOM   1509  CG1 ILE D  27     -22.065  16.197 114.235  1.00            
ATOM   1510  CG2 ILE D  27     -21.763  16.949 111.858  1.00            
ATOM   1511  CD1 ILE D  27     -23.253  15.290 113.981  1.00            
ATOM   1512  N   SER D  28     -21.633  20.426 112.789  1.00            
ATOM   1513  CA  SER D  28     -21.608  21.570 111.890  1.00            
ATOM   1514  C   SER D  28     -20.326  22.362 112.100  1.00            
ATOM   1515  O   SER D  28     -19.680  22.806 111.153  1.00            
ATOM   1516  CB  SER D  28     -22.826  22.462 112.132  1.00            
ATOM   1517  OG  SER D  28     -22.900  23.505 111.177  1.00            
ATOM   1518  N   ARG D  29     -19.972  22.518 113.368  1.00            
ATOM   1519  CA  ARG D  29     -18.779  23.242 113.780  1.00            
ATOM   1520  C   ARG D  29     -17.502  22.495 113.369  1.00            
ATOM   1521  O   ARG D  29     -16.618  23.075 112.742  1.00            
ATOM   1522  CB  ARG D  29     -18.876  23.488 115.290  1.00            
ATOM   1523  CG  ARG D  29     -17.984  24.557 115.892  1.00            
ATOM   1524  CD  ARG D  29     -18.403  24.719 117.346  1.00            
ATOM   1525  NE  ARG D  29     -18.153  23.546 118.184  1.00            
ATOM   1526  CZ  ARG D  29     -19.026  23.024 119.047  1.00            
ATOM   1527  NH1 ARG D  29     -20.268  23.491 119.137  1.00            
ATOM   1528  NH2 ARG D  29     -18.675  21.975 119.778  1.00            
ATOM   1529  N   SER D  30     -17.410  21.214 113.721  1.00            
ATOM   1530  CA  SER D  30     -16.208  20.413 113.460  1.00            
ATOM   1531  C   SER D  30     -15.873  20.229 111.976  1.00            
ATOM   1532  O   SER D  30     -14.701  20.211 111.604  1.00            
ATOM   1533  CB  SER D  30     -16.340  19.029 114.100  1.00            
ATOM   1534  OG  SER D  30     -16.477  19.124 115.506  1.00            
ATOM   1535  N   LEU D  31     -16.898  20.101 111.136  1.00            
ATOM   1536  CA  LEU D  31     -16.709  19.768 109.723  1.00            
ATOM   1537  C   LEU D  31     -16.952  20.962 108.810  1.00            
ATOM   1538  O   LEU D  31     -17.015  20.806 107.590  1.00            
ATOM   1539  CB  LEU D  31     -17.661  18.634 109.317  1.00            
ATOM   1540  CG  LEU D  31     -17.708  17.377 110.185  1.00            
ATOM   1541  CD1 LEU D  31     -18.729  16.393 109.638  1.00            
ATOM   1542  CD2 LEU D  31     -16.336  16.726 110.240  1.00            
ATOM   1543  N   ASP D  32     -17.018  22.150 109.407  1.00            
ATOM   1544  CA  ASP D  32     -17.383  23.376 108.699  1.00            
ATOM   1545  C   ASP D  32     -18.509  23.063 107.719  1.00            
ATOM   1546  O   ASP D  32     -18.463  23.442 106.548  1.00            
ATOM   1547  CB  ASP D  32     -16.173  23.964 107.967  1.00            
ATOM   1548  CG  ASP D  32     -16.413  25.384 107.478  1.00            
ATOM   1549  OD1 ASP D  32     -17.491  25.946 107.768  1.00            
ATOM   1550  OD2 ASP D  32     -15.518  25.939 106.804  1.00            
ATOM   1551  N   ALA D  33     -19.517  22.362 108.232  1.00            
ATOM   1552  CA  ALA D  33     -20.652  21.910 107.441  1.00            
ATOM   1553  C   ALA D  33     -21.888  22.717 107.803  1.00            
ATOM   1554  O   ALA D  33     -22.047  23.115 108.955  1.00            
ATOM   1555  CB  ALA D  33     -20.902  20.427 107.674  1.00            
ATOM   1556  N   PRO D  34     -22.769  22.968 106.821  1.00            
ATOM   1557  CA  PRO D  34     -23.996  23.698 107.154  1.00            
ATOM   1558  C   PRO D  34     -24.834  22.977 108.205  1.00            
ATOM   1559  O   PRO D  34     -25.099  21.782 108.070  1.00            
ATOM   1560  CB  PRO D  34     -24.737  23.756 105.816  1.00            
ATOM   1561  CG  PRO D  34     -23.657  23.698 104.798  1.00            
ATOM   1562  CD  PRO D  34     -22.627  22.773 105.368  1.00            
ATOM   1563  N   LEU D  35     -25.234  23.705 109.242  1.00            
ATOM   1564  CA  LEU D  35     -26.009  23.124 110.332  1.00            
ATOM   1565  C   LEU D  35     -27.310  22.515 109.822  1.00            
ATOM   1566  O   LEU D  35     -27.743  21.464 110.289  1.00            
ATOM   1567  CB  LEU D  35     -26.308  24.183 111.394  1.00            
ATOM   1568  CG  LEU D  35     -27.063  23.691 112.631  1.00            
ATOM   1569  CD1 LEU D  35     -26.221  22.709 113.436  1.00            
ATOM   1570  CD2 LEU D  35     -27.484  24.868 113.496  1.00            
ATOM   1571  N   THR D  36     -27.907  23.172 108.835  1.00            
ATOM   1572  CA  THR D  36     -29.211  22.775 108.323  1.00            
ATOM   1573  C   THR D  36     -29.177  21.432 107.589  1.00            
ATOM   1574  O   THR D  36     -30.225  20.853 107.295  1.00            
ATOM   1575  CB  THR D  36     -29.762  23.849 107.365  1.00            
ATOM   1576  OG1 THR D  36     -28.824  24.075 106.306  1.00            
ATOM   1577  CG2 THR D  36     -30.003  25.153 108.111  1.00            
ATOM   1578  N   SER D  37     -27.975  20.933 107.315  1.00            
ATOM   1579  CA  SER D  37     -27.810  19.658 106.623  1.00            
ATOM   1580  C   SER D  37     -27.596  18.522 107.617  1.00            
ATOM   1581  O   SER D  37     -27.594  17.352 107.238  1.00            
ATOM   1582  CB  SER D  37     -26.634  19.717 105.644  1.00            
ATOM   1583  OG  SER D  37     -25.406  19.935 106.319  1.00            
ATOM   1584  N   VAL D  38     -27.429  18.871 108.890  1.00            
ATOM   1585  CA  VAL D  38     -27.149  17.879 109.921  1.00            
ATOM   1586  C   VAL D  38     -28.416  17.208 110.425  1.00            
ATOM   1587  O   VAL D  38     -29.367  17.880 110.829  1.00            
ATOM   1588  CB  VAL D  38     -26.426  18.517 111.135  1.00            
ATOM   1589  CG1 VAL D  38     -26.125  17.469 112.202  1.00            
ATOM   1590  CG2 VAL D  38     -25.156  19.224 110.701  1.00            
ATOM   1591  N   ARG D  39     -28.422  15.878 110.396  1.00            
ATOM   1592  CA  ARG D  39     -29.517  15.106 110.974  1.00            
ATOM   1593  C   ARG D  39     -29.023  14.210 112.089  1.00            
ATOM   1594  O   ARG D  39     -27.960  13.594 111.997  1.00            
ATOM   1595  CB  ARG D  39     -30.249  14.272 109.923  1.00            
ATOM   1596  CG  ARG D  39     -31.138  15.133 109.063  1.00            
ATOM   1597  CD  ARG D  39     -31.680  14.442 107.829  1.00            
ATOM   1598  NE  ARG D  39     -32.609  15.333 107.145  1.00            
ATOM   1599  CZ  ARG D  39     -32.235  16.400 106.443  1.00            
ATOM   1600  NH1 ARG D  39     -30.950  16.717 106.330  1.00            
ATOM   1601  NH2 ARG D  39     -33.148  17.162 105.857  1.00            
ATOM   1602  N   VAL D  40     -29.823  14.158 113.145  1.00            
ATOM   1603  CA  VAL D  40     -29.546  13.336 114.302  1.00            
ATOM   1604  C   VAL D  40     -30.788  12.522 114.613  1.00            
ATOM   1605  O   VAL D  40     -31.895  13.058 114.642  1.00            
ATOM   1606  CB  VAL D  40     -29.153  14.187 115.523  1.00            
ATOM   1607  CG1 VAL D  40     -28.946  13.303 116.751  1.00            
ATOM   1608  CG2 VAL D  40     -27.908  15.008 115.221  1.00            
ATOM   1609  N   ILE D  41     -30.605  11.225 114.833  1.00            
ATOM   1610  CA  ILE D  41     -31.709  10.371 115.234  1.00            
ATOM   1611  C   ILE D  41     -31.277   9.592 116.474  1.00            
ATOM   1612  O   ILE D  41     -30.203   8.989 116.503  1.00            
ATOM   1613  CB  ILE D  41     -32.151   9.414 114.101  1.00            
ATOM   1614  CG1 ILE D  41     -30.970   8.614 113.543  1.00            
ATOM   1615  CG2 ILE D  41     -32.868  10.206 113.015  1.00            
ATOM   1616  CD1 ILE D  41     -31.365   7.599 112.479  1.00            
ATOM   1617  N   ILE D  42     -32.114   9.632 117.505  1.00            
ATOM   1618  CA  ILE D  42     -31.817   8.976 118.770  1.00            
ATOM   1619  C   ILE D  42     -32.503   7.626 118.844  1.00            
ATOM   1620  O   ILE D  42     -33.671   7.494 118.482  1.00            
ATOM   1621  CB  ILE D  42     -32.284   9.818 119.979  1.00            
ATOM   1622  CG1 ILE D  42     -31.646  11.209 119.955  1.00            
ATOM   1623  CG2 ILE D  42     -31.982   9.084 121.294  1.00            
ATOM   1624  CD1 ILE D  42     -32.185  12.132 121.023  1.00            
ATOM   1625  N   THR D  43     -31.765   6.627 119.314  1.00            
ATOM   1626  CA  THR D  43     -32.329   5.313 119.581  1.00            
ATOM   1627  C   THR D  43     -32.089   4.952 121.040  1.00            
ATOM   1628  O   THR D  43     -30.945   4.885 121.492  1.00            
ATOM   1629  CB  THR D  43     -31.717   4.236 118.671  1.00            
ATOM   1630  OG1 THR D  43     -31.791   4.667 117.306  1.00            
ATOM   1631  CG2 THR D  43     -32.465   2.923 118.821  1.00            
ATOM   1632  N   GLU D  44     -33.176   4.719 121.771  1.00            
ATOM   1633  CA  GLU D  44     -33.088   4.362 123.180  1.00            
ATOM   1634  C   GLU D  44     -33.109   2.853 123.334  1.00            
ATOM   1635  O   GLU D  44     -33.787   2.154 122.580  1.00            
ATOM   1636  CB  GLU D  44     -34.238   4.977 123.977  1.00            
ATOM   1637  CG  GLU D  44     -34.176   6.483 124.104  1.00            
ATOM   1638  CD  GLU D  44     -35.214   7.013 125.068  1.00            
ATOM   1639  OE1 GLU D  44     -36.417   6.771 124.836  1.00            
ATOM   1640  OE2 GLU D  44     -34.828   7.667 126.060  1.00            
ATOM   1641  N   TYR D  45     -32.362   2.358 124.316  1.00            
ATOM   1642  CA  TYR D  45     -32.315   0.930 124.589  1.00            
ATOM   1643  C   TYR D  45     -32.676   0.627 126.029  1.00            
ATOM   1644  O   TYR D  45     -32.140   1.229 126.958  1.00            
ATOM   1645  CB  TYR D  45     -30.931   0.390 124.250  1.00            
ATOM   1646  CG  TYR D  45     -30.650   0.527 122.782  1.00            
ATOM   1647  CD1 TYR D  45     -31.243  -0.329 121.864  1.00            
ATOM   1648  CD2 TYR D  45     -29.821   1.530 122.306  1.00            
ATOM   1649  CE1 TYR D  45     -31.006  -0.199 120.510  1.00            
ATOM   1650  CE2 TYR D  45     -29.575   1.666 120.955  1.00            
ATOM   1651  CZ  TYR D  45     -30.170   0.803 120.062  1.00            
ATOM   1652  OH  TYR D  45     -29.919   0.941 118.718  1.00            
ATOM   1653  N   ALA D  46     -33.580  -0.329 126.203  1.00            
ATOM   1654  CA  ALA D  46     -33.979  -0.750 127.531  1.00            
ATOM   1655  C   ALA D  46     -32.844  -1.506 128.191  1.00            
ATOM   1656  O   ALA D  46     -31.969  -2.063 127.529  1.00            
ATOM   1657  CB  ALA D  46     -35.224  -1.605 127.477  1.00            
ATOM   1658  N   LYS D  47     -32.881  -1.502 129.514  1.00            
ATOM   1659  CA  LYS D  47     -31.839  -2.078 130.342  1.00            
ATOM   1660  C   LYS D  47     -31.499  -3.525 129.964  1.00            
ATOM   1661  O   LYS D  47     -30.344  -3.937 130.062  1.00            
ATOM   1662  CB  LYS D  47     -32.278  -1.988 131.797  1.00            
ATOM   1663  CG  LYS D  47     -32.307  -0.567 132.338  1.00            
ATOM   1664  CD  LYS D  47     -33.395  -0.410 133.380  1.00            
ATOM   1665  CE  LYS D  47     -33.114  -1.298 134.585  1.00            
ATOM   1666  NZ  LYS D  47     -33.908  -0.920 135.783  1.00            
ATOM   1667  N   GLY D  48     -32.510  -4.295 129.568  1.00            
ATOM   1668  CA  GLY D  48     -32.319  -5.683 129.175  1.00            
ATOM   1669  C   GLY D  48     -31.906  -5.869 127.723  1.00            
ATOM   1670  O   GLY D  48     -31.912  -6.991 127.216  1.00            
ATOM   1671  N   HIS D  49     -31.550  -4.773 127.055  1.00            
ATOM   1672  CA  HIS D  49     -31.174  -4.800 125.640  1.00            
ATOM   1673  C   HIS D  49     -29.754  -4.288 125.395  1.00            
ATOM   1674  O   HIS D  49     -29.365  -4.058 124.252  1.00            
ATOM   1675  CB  HIS D  49     -32.163  -3.972 124.810  1.00            
ATOM   1676  CG  HIS D  49     -33.514  -4.603 124.668  1.00            
ATOM   1677  ND1 HIS D  49     -34.615  -3.910 124.215  1.00            
ATOM   1678  CD2 HIS D  49     -33.938  -5.866 124.912  1.00            
ATOM   1679  CE1 HIS D  49     -35.661  -4.718 124.186  1.00            
ATOM   1680  NE2 HIS D  49     -35.275  -5.910 124.606  1.00            
ATOM   1681  N   ALA D  50     -28.987  -4.108 126.467  1.00            
ATOM   1682  CA  ALA D  50     -27.626  -3.587 126.363  1.00            
ATOM   1683  C   ALA D  50     -26.652  -4.436 127.178  1.00            
ATOM   1684  O   ALA D  50     -26.944  -4.802 128.317  1.00            
ATOM   1685  CB  ALA D  50     -27.582  -2.139 126.821  1.00            
ATOM   1686  N   GLY D  51     -25.498  -4.744 126.585  1.00            
ATOM   1687  CA  GLY D  51     -24.479  -5.557 127.233  1.00            
ATOM   1688  C   GLY D  51     -23.114  -4.900 127.399  1.00            
ATOM   1689  O   GLY D  51     -22.695  -4.089 126.573  1.00            
ATOM   1690  N   ILE D  52     -22.431  -5.257 128.487  1.00            
ATOM   1691  CA  ILE D  52     -21.066  -4.801 128.775  1.00            
ATOM   1692  C   ILE D  52     -20.244  -5.940 129.369  1.00            
ATOM   1693  O   ILE D  52     -20.044  -6.001 130.582  1.00            
ATOM   1694  CB  ILE D  52     -21.018  -3.607 129.759  1.00            
ATOM   1695  CG1 ILE D  52     -21.762  -2.399 129.199  1.00            
ATOM   1696  CG2 ILE D  52     -19.568  -3.180 130.040  1.00            
ATOM   1697  CD1 ILE D  52     -23.162  -2.253 129.725  1.00            
ATOM   1698  N   GLY D  53     -19.848  -6.890 128.533  1.00            
ATOM   1699  CA  GLY D  53     -19.031  -7.998 128.990  1.00            
ATOM   1700  C   GLY D  53     -19.843  -9.266 128.919  1.00            
ATOM   1701  O   GLY D  53     -19.492 -10.278 129.519  1.00            
ATOM   1702  N   GLY D  54     -20.955  -9.186 128.199  1.00            
ATOM   1703  CA  GLY D  54     -21.903 -10.277 128.109  1.00            
ATOM   1704  C   GLY D  54     -22.982 -10.143 129.172  1.00            
ATOM   1705  O   GLY D  54     -23.950 -10.902 129.176  1.00            
ATOM   1706  N   GLU D  55     -22.813  -9.174 130.072  1.00            
ATOM   1707  CA  GLU D  55     -23.782  -8.910 131.137  1.00            
ATOM   1708  C   GLU D  55     -24.494  -7.567 130.975  1.00            
ATOM   1709  O   GLU D  55     -23.979  -6.651 130.337  1.00            
ATOM   1710  CB  GLU D  55     -23.113  -8.960 132.511  1.00            
ATOM   1711  CG  GLU D  55     -22.635 -10.343 132.914  1.00            
ATOM   1712  CD  GLU D  55     -22.065 -10.371 134.319  1.00            
ATOM   1713  OE1 GLU D  55     -20.829 -10.468 134.464  1.00            
ATOM   1714  OE2 GLU D  55     -22.862 -10.301 135.281  1.00            
ATOM   1715  N   LEU D  56     -25.682  -7.466 131.566  1.00            
ATOM   1716  CA  LEU D  56     -26.524  -6.283 131.433  1.00            
ATOM   1717  C   LEU D  56     -25.949  -5.059 132.120  1.00            
ATOM   1718  O   LEU D  56     -25.001  -5.146 132.904  1.00            
ATOM   1719  CB  LEU D  56     -27.926  -6.551 131.987  1.00            
ATOM   1720  CG  LEU D  56     -28.822  -7.456 131.140  1.00            
ATOM   1721  CD1 LEU D  56     -28.333  -8.867 131.088  1.00            
ATOM   1722  CD2 LEU D  56     -30.241  -7.437 131.677  1.00            
ATOM   1723  N   ALA D  57     -26.558  -3.918 131.817  1.00            
ATOM   1724  CA  ALA D  57     -26.118  -2.630 132.326  1.00            
ATOM   1725  C   ALA D  57     -26.975  -2.188 133.507  1.00            
ATOM   1726  O   ALA D  57     -28.187  -2.404 133.522  1.00            
ATOM   1727  CB  ALA D  57     -26.175  -1.597 131.217  1.00            
TER    1728      ALA D  57                                                      
ATOM   1729  N   PRO E   1     -36.715  11.107 106.245  1.00            
ATOM   1730  CA  PRO E   1     -36.535   9.665 106.034  1.00            
ATOM   1731  C   PRO E   1     -35.142   9.316 105.512  1.00            
ATOM   1732  O   PRO E   1     -34.621   9.994 104.626  1.00            
ATOM   1733  CB  PRO E   1     -37.612   9.319 104.998  1.00            
ATOM   1734  CG  PRO E   1     -38.009  10.610 104.364  1.00            
ATOM   1735  CD  PRO E   1     -37.590  11.737 105.244  1.00            
ATOM   1736  N   ILE E   2     -34.560   8.259 106.070  1.00            
ATOM   1737  CA  ILE E   2     -33.202   7.830 105.737  1.00            
ATOM   1738  C   ILE E   2     -33.125   6.329 105.468  1.00            
ATOM   1739  O   ILE E   2     -33.582   5.529 106.282  1.00            
ATOM   1740  CB  ILE E   2     -32.213   8.208 106.858  1.00            
ATOM   1741  CG1 ILE E   2     -32.118   9.728 106.974  1.00            
ATOM   1742  CG2 ILE E   2     -30.824   7.634 106.584  1.00            
ATOM   1743  CD1 ILE E   2     -31.604  10.212 108.304  1.00            
ATOM   1744  N   ALA E   3     -32.539   5.953 104.334  1.00            
ATOM   1745  CA  ALA E   3     -32.359   4.544 103.995  1.00            
ATOM   1746  C   ALA E   3     -30.877   4.185 104.025  1.00            
ATOM   1747  O   ALA E   3     -30.059   4.818 103.359  1.00            
ATOM   1748  CB  ALA E   3     -32.949   4.240 102.630  1.00            
ATOM   1749  N   GLN E   4     -30.546   3.167 104.812  1.00            
ATOM   1750  CA  GLN E   4     -29.195   2.631 104.857  1.00            
ATOM   1751  C   GLN E   4     -29.225   1.259 104.199  1.00            
ATOM   1752  O   GLN E   4     -29.812   0.321 104.740  1.00            
ATOM   1753  CB  GLN E   4     -28.700   2.541 106.303  1.00            
ATOM   1754  CG  GLN E   4     -27.199   2.347 106.454  1.00            
ATOM   1755  CD  GLN E   4     -26.760   2.357 107.910  1.00            
ATOM   1756  OE1 GLN E   4     -27.557   2.633 108.813  1.00            
ATOM   1757  NE2 GLN E   4     -25.482   2.078 108.143  1.00            
ATOM   1758  N   ILE E   5     -28.588   1.143 103.038  1.00            
ATOM   1759  CA  ILE E   5     -28.620  -0.100 102.283  1.00            
ATOM   1760  C   ILE E   5     -27.277  -0.811 102.365  1.00            
ATOM   1761  O   ILE E   5     -26.234  -0.246 102.034  1.00            
ATOM   1762  CB  ILE E   5     -28.989   0.150 100.803  1.00            
ATOM   1763  CG1 ILE E   5     -30.262   0.998 100.711  1.00            
ATOM   1764  CG2 ILE E   5     -29.182  -1.171 100.073  1.00            
ATOM   1765  CD1 ILE E   5     -30.608   1.448  99.315  1.00            
ATOM   1766  N   HIS E   6     -27.327  -2.065 102.803  1.00            
ATOM   1767  CA  HIS E   6     -26.139  -2.887 102.988  1.00            
ATOM   1768  C   HIS E   6     -26.087  -3.940 101.893  1.00            
ATOM   1769  O   HIS E   6     -26.967  -4.795 101.812  1.00            
ATOM   1770  CB  HIS E   6     -26.158  -3.550 104.367  1.00            
ATOM   1771  CG  HIS E   6     -26.276  -2.580 105.503  1.00            
ATOM   1772  ND1 HIS E   6     -25.190  -1.925 106.041  1.00            
ATOM   1773  CD2 HIS E   6     -27.356  -2.157 106.201  1.00            
ATOM   1774  CE1 HIS E   6     -25.596  -1.140 107.023  1.00            
ATOM   1775  NE2 HIS E   6     -26.904  -1.262 107.142  1.00            
ATOM   1776  N   ILE E   7     -25.056  -3.879 101.057  1.00            
ATOM   1777  CA  ILE E   7     -24.944  -4.781  99.917  1.00            
ATOM   1778  C   ILE E   7     -23.534  -5.346  99.810  1.00            
ATOM   1779  O   ILE E   7     -22.592  -4.778 100.349  1.00            
ATOM   1780  CB  ILE E   7     -25.313  -4.052  98.603  1.00            
ATOM   1781  CG1 ILE E   7     -24.309  -2.932  98.301  1.00            
ATOM   1782  CG2 ILE E   7     -26.712  -3.471  98.707  1.00            
ATOM   1783  CD1 ILE E   7     -24.509  -2.264  96.960  1.00            
ATOM   1784  N   LEU E   8     -23.394  -6.482  99.137  1.00            
ATOM   1785  CA  LEU E   8     -22.072  -7.019  98.840  1.00            
ATOM   1786  C   LEU E   8     -21.454  -6.267  97.669  1.00            
ATOM   1787  O   LEU E   8     -22.146  -5.906  96.718  1.00            
ATOM   1788  CB  LEU E   8     -22.131  -8.523  98.565  1.00            
ATOM   1789  CG  LEU E   8     -22.291  -9.397  99.817  1.00            
ATOM   1790  CD1 LEU E   8     -23.436  -8.961 100.734  1.00            
ATOM   1791  CD2 LEU E   8     -22.442 -10.857  99.434  1.00            
ATOM   1792  N   GLU E   9     -20.148  -6.037  97.744  1.00            
ATOM   1793  CA  GLU E   9     -19.447  -5.287  96.712  1.00            
ATOM   1794  C   GLU E   9     -19.279  -6.109  95.447  1.00            
ATOM   1795  O   GLU E   9     -19.357  -7.337  95.475  1.00            
ATOM   1796  CB  GLU E   9     -18.066  -4.842  97.200  1.00            
ATOM   1797  CG  GLU E   9     -17.110  -5.990  97.488  1.00            
ATOM   1798  CD  GLU E   9     -15.757  -5.512  97.977  1.00            
ATOM   1799  OE1 GLU E   9     -15.692  -4.422  98.587  1.00            
ATOM   1800  OE2 GLU E   9     -14.756  -6.224  97.746  1.00            
ATOM   1801  N   GLY E  10     -19.060  -5.410  94.340  1.00            
ATOM   1802  CA  GLY E  10     -18.801  -6.042  93.061  1.00            
ATOM   1803  C   GLY E  10     -19.638  -5.486  91.931  1.00            
ATOM   1804  O   GLY E  10     -19.369  -5.750  90.762  1.00            
ATOM   1805  N   ARG E  11     -20.667  -4.727  92.281  1.00            
ATOM   1806  CA  ARG E  11     -21.571  -4.161  91.291  1.00            
ATOM   1807  C   ARG E  11     -21.037  -2.807  90.816  1.00            
ATOM   1808  O   ARG E  11     -20.234  -2.172  91.502  1.00            
ATOM   1809  CB  ARG E  11     -22.966  -4.065  91.894  1.00            
ATOM   1810  CG  ARG E  11     -23.500  -5.458  92.186  1.00            
ATOM   1811  CD  ARG E  11     -24.915  -5.480  92.673  1.00            
ATOM   1812  NE  ARG E  11     -24.901  -5.869  94.082  1.00            
ATOM   1813  CZ  ARG E  11     -25.312  -7.035  94.572  1.00            
ATOM   1814  NH1 ARG E  11     -25.787  -7.990  93.781  1.00            
ATOM   1815  NH2 ARG E  11     -25.231  -7.246  95.878  1.00            
ATOM   1816  N   SER E  12     -21.491  -2.370  89.646  1.00            
ATOM   1817  CA  SER E  12     -21.012  -1.132  89.041  1.00            
ATOM   1818  C   SER E  12     -21.634   0.120  89.655  1.00            
ATOM   1819  O   SER E  12     -22.633   0.045  90.368  1.00            
ATOM   1820  CB  SER E  12     -21.282  -1.164  87.535  1.00            
ATOM   1821  OG  SER E  12     -22.659  -0.978  87.256  1.00            
ATOM   1822  N   ASP E  13     -21.030   1.272  89.367  1.00            
ATOM   1823  CA  ASP E  13     -21.527   2.557  89.863  1.00            
ATOM   1824  C   ASP E  13     -22.871   2.955  89.267  1.00            
ATOM   1825  O   ASP E  13     -23.638   3.679  89.899  1.00            
ATOM   1826  CB  ASP E  13     -20.507   3.662  89.577  1.00            
ATOM   1827  CG  ASP E  13     -19.382   3.708  90.600  1.00            
ATOM   1828  OD1 ASP E  13     -19.431   2.958  91.602  1.00            
ATOM   1829  OD2 ASP E  13     -18.441   4.508  90.402  1.00            
ATOM   1830  N   GLU E  14     -23.148   2.506  88.050  1.00            
ATOM   1831  CA  GLU E  14     -24.410   2.834  87.400  1.00            
ATOM   1832  C   GLU E  14     -25.553   2.132  88.134  1.00            
ATOM   1833  O   GLU E  14     -26.625   2.707  88.315  1.00            
ATOM   1834  CB  GLU E  14     -24.369   2.482  85.908  1.00            
ATOM   1835  CG  GLU E  14     -25.519   3.096  85.118  1.00            
ATOM   1836  CD  GLU E  14     -25.448   2.821  83.625  1.00            
ATOM   1837  OE1 GLU E  14     -24.614   1.990  83.205  1.00            
ATOM   1838  OE2 GLU E  14     -26.235   3.443  82.875  1.00            
ATOM   1839  N   GLN E  15     -25.324   0.890  88.545  1.00            
ATOM   1840  CA  GLN E  15     -26.329   0.140  89.287  1.00            
ATOM   1841  C   GLN E  15     -26.628   0.802  90.630  1.00            
ATOM   1842  O   GLN E  15     -27.782   0.877  91.047  1.00            
ATOM   1843  CB  GLN E  15     -25.844  -1.288  89.526  1.00            
ATOM   1844  CG  GLN E  15     -25.845  -2.180  88.305  1.00            
ATOM   1845  CD  GLN E  15     -25.288  -3.551  88.616  1.00            
ATOM   1846  OE1 GLN E  15     -24.072  -3.742  88.660  1.00            
ATOM   1847  NE2 GLN E  15     -26.171  -4.495  88.907  1.00            
ATOM   1848  N   LYS E  16     -25.585   1.277  91.306  1.00            
ATOM   1849  CA  LYS E  16     -25.745   1.890  92.620  1.00            
ATOM   1850  C   LYS E  16     -26.327   3.295  92.483  1.00            
ATOM   1851  O   LYS E  16     -26.975   3.801  93.400  1.00            
ATOM   1852  CB  LYS E  16     -24.411   1.937  93.357  1.00            
ATOM   1853  CG  LYS E  16     -23.900   0.560  93.748  1.00            
ATOM   1854  CD  LYS E  16     -22.638   0.659  94.578  1.00            
ATOM   1855  CE  LYS E  16     -21.420   0.856  93.690  1.00            
ATOM   1856  NZ  LYS E  16     -20.191   0.206  94.199  1.00            
ATOM   1857  N   GLU E  17     -26.092   3.919  91.332  1.00            
ATOM   1858  CA  GLU E  17     -26.665   5.227  91.042  1.00            
ATOM   1859  C   GLU E  17     -28.146   5.053  90.781  1.00            
ATOM   1860  O   GLU E  17     -28.960   5.901  91.142  1.00            
ATOM   1861  CB  GLU E  17     -25.998   5.878  89.827  1.00            
ATOM   1862  CG  GLU E  17     -26.497   7.293  89.538  1.00            
ATOM   1863  CD  GLU E  17     -25.773   7.955  88.377  1.00            
ATOM   1864  OE1 GLU E  17     -24.721   7.435  87.947  1.00            
ATOM   1865  OE2 GLU E  17     -26.268   8.993  87.887  1.00            
ATOM   1866  N   THR E  18     -28.487   3.938  90.147  1.00            
ATOM   1867  CA  THR E  18     -29.876   3.611  89.920  1.00            
ATOM   1868  C   THR E  18     -30.536   3.334  91.259  1.00            
ATOM   1869  O   THR E  18     -31.586   3.896  91.566  1.00            
ATOM   1870  CB  THR E  18     -30.012   2.374  88.991  1.00            
ATOM   1871  OG1 THR E  18     -29.450   2.670  87.708  1.00            
ATOM   1872  CG2 THR E  18     -31.463   1.952  88.814  1.00            
ATOM   1873  N   LEU E  19     -29.843   2.579  92.106  1.00            
ATOM   1874  CA  LEU E  19     -30.394   2.164  93.389  1.00            
ATOM   1875  C   LEU E  19     -30.824   3.350  94.248  1.00            
ATOM   1876  O   LEU E  19     -31.959   3.398  94.717  1.00            
ATOM   1877  CB  LEU E  19     -29.367   1.326  94.152  1.00            
ATOM   1878  CG  LEU E  19     -29.798   0.786  95.515  1.00            
ATOM   1879  CD1 LEU E  19     -30.782  -0.354  95.332  1.00            
ATOM   1880  CD2 LEU E  19     -28.585   0.340  96.306  1.00            
ATOM   1881  N   ILE E  20     -29.922   4.306  94.440  1.00            
ATOM   1882  CA  ILE E  20     -30.214   5.483  95.252  1.00            
ATOM   1883  C   ILE E  20     -31.415   6.260  94.733  1.00            
ATOM   1884  O   ILE E  20     -32.291   6.643  95.509  1.00            
ATOM   1885  CB  ILE E  20     -28.996   6.420  95.313  1.00            
ATOM   1886  CG1 ILE E  20     -27.877   5.746  96.108  1.00            
ATOM   1887  CG2 ILE E  20     -29.371   7.772  95.932  1.00            
ATOM   1888  CD1 ILE E  20     -26.569   6.511  96.133  1.00            
ATOM   1889  N   ARG E  21     -31.465   6.466  93.422  1.00            
ATOM   1890  CA  ARG E  21     -32.552   7.221  92.813  1.00            
ATOM   1891  C   ARG E  21     -33.827   6.439  92.936  1.00            
ATOM   1892  O   ARG E  21     -34.864   6.963  93.335  1.00            
ATOM   1893  CB  ARG E  21     -32.292   7.494  91.332  1.00            
ATOM   1894  CG  ARG E  21     -33.437   8.235  90.630  1.00            
ATOM   1895  CD  ARG E  21     -33.090   8.563  89.186  1.00            
ATOM   1896  NE  ARG E  21     -31.877   9.376  89.098  1.00            
ATOM   1897  CZ  ARG E  21     -30.692   8.947  88.663  1.00            
ATOM   1898  NH1 ARG E  21     -30.518   7.688  88.275  1.00            
ATOM   1899  NH2 ARG E  21     -29.665   9.785  88.633  1.00            
ATOM   1900  N   GLU E  22     -33.725   5.166  92.586  1.00            
ATOM   1901  CA  GLU E  22     -34.904   4.343  92.495  1.00            
ATOM   1902  C   GLU E  22     -35.504   4.085  93.883  1.00            
ATOM   1903  O   GLU E  22     -36.722   4.067  94.040  1.00            
ATOM   1904  CB  GLU E  22     -34.586   3.007  91.815  1.00            
ATOM   1905  CG  GLU E  22     -34.190   3.073  90.333  1.00            
ATOM   1906  CD  GLU E  22     -35.204   3.800  89.459  1.00            
ATOM   1907  OE1 GLU E  22     -36.420   3.665  89.731  1.00            
ATOM   1908  OE2 GLU E  22     -34.791   4.487  88.490  1.00            
ATOM   1909  N   VAL E  23     -34.644   3.846  94.872  1.00            
ATOM   1910  CA  VAL E  23     -35.081   3.591  96.247  1.00            
ATOM   1911  C   VAL E  23     -35.615   4.860  96.894  1.00            
ATOM   1912  O   VAL E  23     -36.579   4.811  97.654  1.00            
ATOM   1913  CB  VAL E  23     -33.928   2.998  97.110  1.00            
ATOM   1914  CG1 VAL E  23     -34.200   3.150  98.612  1.00            
ATOM   1915  CG2 VAL E  23     -33.682   1.537  96.751  1.00            
ATOM   1916  N   SER E  24     -34.978   5.989  96.604  1.00            
ATOM   1917  CA  SER E  24     -35.411   7.267  97.159  1.00            
ATOM   1918  C   SER E  24     -36.846   7.591  96.750  1.00            
ATOM   1919  O   SER E  24     -37.645   8.059  97.562  1.00            
ATOM   1920  CB  SER E  24     -34.480   8.397  96.707  1.00            
ATOM   1921  OG  SER E  24     -33.148   8.185  97.144  1.00            
ATOM   1922  N   GLU E  25     -37.166   7.342  95.486  1.00            
ATOM   1923  CA  GLU E  25     -38.505   7.591  94.966  1.00            
ATOM   1924  C   GLU E  25     -39.559   6.697  95.643  1.00            
ATOM   1925  O   GLU E  25     -40.664   7.157  95.943  1.00            
ATOM   1926  CB  GLU E  25     -38.507   7.412  93.441  1.00            
ATOM   1927  CG  GLU E  25     -37.998   8.657  92.702  1.00            
ATOM   1928  CD  GLU E  25     -37.671   8.408  91.238  1.00            
ATOM   1929  OE1 GLU E  25     -38.076   7.356  90.700  1.00            
ATOM   1930  OE2 GLU E  25     -37.008   9.274  90.623  1.00            
ATOM   1931  N   ALA E  26     -39.215   5.428  95.862  1.00            
ATOM   1932  CA  ALA E  26     -40.120   4.464  96.484  1.00            
ATOM   1933  C   ALA E  26     -40.494   4.885  97.909  1.00            
ATOM   1934  O   ALA E  26     -41.625   4.685  98.348  1.00            
ATOM   1935  CB  ALA E  26     -39.498   3.078  96.499  1.00            
ATOM   1936  N   ILE E  27     -39.537   5.435  98.647  1.00            
ATOM   1937  CA  ILE E  27     -39.814   5.883 100.000  1.00            
ATOM   1938  C   ILE E  27     -40.728   7.110  99.973  1.00            
ATOM   1939  O   ILE E  27     -41.690   7.195 100.735  1.00            
ATOM   1940  CB  ILE E  27     -38.523   6.197 100.754  1.00            
ATOM   1941  CG1 ILE E  27     -37.668   4.930 100.849  1.00            
ATOM   1942  CG2 ILE E  27     -38.855   6.754 102.127  1.00            
ATOM   1943  CD1 ILE E  27     -36.313   5.161 101.432  1.00            
ATOM   1944  N   SER E  28     -40.430   8.042  99.073  1.00            
ATOM   1945  CA  SER E  28     -41.184   9.287  98.947  1.00            
ATOM   1946  C   SER E  28     -42.667   9.068  98.667  1.00            
ATOM   1947  O   SER E  28     -43.529   9.739  99.237  1.00            
ATOM   1948  CB  SER E  28     -40.582  10.133  97.822  1.00            
ATOM   1949  OG  SER E  28     -41.196  11.402  97.756  1.00            
ATOM   1950  N   ARG E  29     -42.943   8.130  97.773  1.00            
ATOM   1951  CA  ARG E  29     -44.298   7.764  97.381  1.00            
ATOM   1952  C   ARG E  29     -45.039   7.121  98.537  1.00            
ATOM   1953  O   ARG E  29     -46.144   7.518  98.910  1.00            
ATOM   1954  CB  ARG E  29     -44.232   6.763  96.239  1.00            
ATOM   1955  CG  ARG E  29     -44.077   7.358  94.880  1.00            
ATOM   1956  CD  ARG E  29     -43.918   6.234  93.877  1.00            
ATOM   1957  NE  ARG E  29     -42.582   5.617  93.964  1.00            
ATOM   1958  CZ  ARG E  29     -42.248   4.466  93.379  1.00            
ATOM   1959  NH1 ARG E  29     -43.164   3.805  92.681  1.00            
ATOM   1960  NH2 ARG E  29     -41.013   3.975  93.490  1.00            
ATOM   1961  N   SER E  30     -44.384   6.105  99.089  1.00            
ATOM   1962  CA  SER E  30     -44.958   5.231 100.098  1.00            
ATOM   1963  C   SER E  30     -45.382   6.028 101.316  1.00            
ATOM   1964  O   SER E  30     -46.377   5.701 101.958  1.00            
ATOM   1965  CB  SER E  30     -43.940   4.157 100.485  1.00            
ATOM   1966  OG  SER E  30     -43.577   3.389  99.352  1.00            
ATOM   1967  N   LEU E  31     -44.608   7.061 101.634  1.00            
ATOM   1968  CA  LEU E  31     -44.847   7.852 102.827  1.00            
ATOM   1969  C   LEU E  31     -45.341   9.250 102.443  1.00            
ATOM   1970  O   LEU E  31     -45.431  10.137 103.294  1.00            
ATOM   1971  CB  LEU E  31     -43.564   7.944 103.649  1.00            
ATOM   1972  CG  LEU E  31     -42.822   6.618 103.840  1.00            
ATOM   1973  CD1 LEU E  31     -41.595   6.836 104.712  1.00            
ATOM   1974  CD2 LEU E  31     -43.714   5.521 104.403  1.00            
ATOM   1975  N   ASP E  32     -45.694   9.412 101.166  1.00            
ATOM   1976  CA  ASP E  32     -46.089  10.699 100.585  1.00            
ATOM   1977  C   ASP E  32     -45.249  11.851 101.143  1.00            
ATOM   1978  O   ASP E  32     -45.783  12.870 101.584  1.00            
ATOM   1979  CB  ASP E  32     -47.578  10.967 100.822  1.00            
ATOM   1980  CG  ASP E  32     -48.108  12.125  99.981  1.00            
ATOM   1981  OD1 ASP E  32     -47.343  12.674  99.156  1.00            
ATOM   1982  OD2 ASP E  32     -49.295  12.485 100.144  1.00            
ATOM   1983  N   ALA E  33     -43.934  11.662 101.129  1.00            
ATOM   1984  CA  ALA E  33     -42.988  12.647 101.640  1.00            
ATOM   1985  C   ALA E  33     -42.255  13.284 100.467  1.00            
ATOM   1986  O   ALA E  33     -42.053  12.632  99.448  1.00            
ATOM   1987  CB  ALA E  33     -42.003  12.001 102.599  1.00            
ATOM   1988  N   PRO E  34     -41.877  14.567 100.589  1.00            
ATOM   1989  CA  PRO E  34     -41.114  15.164  99.488  1.00            
ATOM   1990  C   PRO E  34     -39.808  14.419  99.228  1.00            
ATOM   1991  O   PRO E  34     -39.070  14.118 100.167  1.00            
ATOM   1992  CB  PRO E  34     -40.850  16.595  99.975  1.00            
ATOM   1993  CG  PRO E  34     -41.012  16.536 101.459  1.00            
ATOM   1994  CD  PRO E  34     -42.081  15.518 101.694  1.00            
ATOM   1995  N   LEU E  35     -39.545  14.114  97.961  1.00            
ATOM   1996  CA  LEU E  35     -38.357  13.364  97.573  1.00            
ATOM   1997  C   LEU E  35     -37.082  14.031  98.050  1.00            
ATOM   1998  O   LEU E  35     -36.135  13.364  98.456  1.00            
ATOM   1999  CB  LEU E  35     -38.299  13.217  96.055  1.00            
ATOM   2000  CG  LEU E  35     -37.120  12.414  95.502  1.00            
ATOM   2001  CD1 LEU E  35     -37.208  10.946  95.889  1.00            
ATOM   2002  CD2 LEU E  35     -37.040  12.588  93.994  1.00            
ATOM   2003  N   THR E  36     -37.080  15.356  98.024  1.00            
ATOM   2004  CA  THR E  36     -35.882  16.125  98.329  1.00            
ATOM   2005  C   THR E  36     -35.450  15.968  99.792  1.00            
ATOM   2006  O   THR E  36     -34.365  16.413 100.169  1.00            
ATOM   2007  CB  THR E  36     -36.091  17.626  97.990  1.00            
ATOM   2008  OG1 THR E  36     -34.966  18.390  98.444  1.00            
ATOM   2009  CG2 THR E  36     -37.373  18.177  98.621  1.00            
ATOM   2010  N   SER E  37     -36.295  15.341 100.610  1.00            
ATOM   2011  CA  SER E  37     -35.962  15.087 102.012  1.00            
ATOM   2012  C   SER E  37     -35.423  13.667 102.218  1.00            
ATOM   2013  O   SER E  37     -34.932  13.333 103.298  1.00            
ATOM   2014  CB  SER E  37     -37.185  15.300 102.907  1.00            
ATOM   2015  OG  SER E  37     -38.219  14.384 102.593  1.00            
ATOM   2016  N   VAL E  38     -35.508  12.838 101.182  1.00            
ATOM   2017  CA  VAL E  38     -35.083  11.445 101.282  1.00            
ATOM   2018  C   VAL E  38     -33.589  11.337 101.063  1.00            
ATOM   2019  O   VAL E  38     -33.055  11.836 100.071  1.00            
ATOM   2020  CB  VAL E  38     -35.809  10.548 100.264  1.00            
ATOM   2021  CG1 VAL E  38     -35.357   9.096 100.403  1.00            
ATOM   2022  CG2 VAL E  38     -37.313  10.667 100.429  1.00            
ATOM   2023  N   ARG E  39     -32.918  10.684 102.002  1.00            
ATOM   2024  CA  ARG E  39     -31.488  10.490 101.897  1.00            
ATOM   2025  C   ARG E  39     -31.148   8.997 101.899  1.00            
ATOM   2026  O   ARG E  39     -31.758   8.224 102.636  1.00            
ATOM   2027  CB  ARG E  39     -30.795  11.221 103.036  1.00            
ATOM   2028  CG  ARG E  39     -30.960  12.737 102.961  1.00            
ATOM   2029  CD  ARG E  39     -30.460  13.371 104.219  1.00            
ATOM   2030  NE  ARG E  39     -29.010  13.429 104.113  1.00            
ATOM   2031  CZ  ARG E  39     -28.195  13.978 105.004  1.00            
ATOM   2032  NH1 ARG E  39     -28.681  14.600 106.067  1.00            
ATOM   2033  NH2 ARG E  39     -26.884  13.930 104.799  1.00            
ATOM   2034  N   VAL E  40     -30.177   8.602 101.078  1.00            
ATOM   2035  CA  VAL E  40     -29.763   7.203 100.976  1.00            
ATOM   2036  C   VAL E  40     -28.254   7.045 101.103  1.00            
ATOM   2037  O   VAL E  40     -27.491   7.793 100.495  1.00            
ATOM   2038  CB  VAL E  40     -30.213   6.590  99.639  1.00            
ATOM   2039  CG1 VAL E  40     -29.759   5.140  99.526  1.00            
ATOM   2040  CG2 VAL E  40     -31.718   6.680  99.499  1.00            
ATOM   2041  N   ILE E  41     -27.836   6.071 101.905  1.00            
ATOM   2042  CA  ILE E  41     -26.424   5.735 102.046  1.00            
ATOM   2043  C   ILE E  41     -26.182   4.240 101.847  1.00            
ATOM   2044  O   ILE E  41     -26.820   3.400 102.480  1.00            
ATOM   2045  CB  ILE E  41     -25.875   6.180 103.420  1.00            
ATOM   2046  CG1 ILE E  41     -26.876   5.841 104.532  1.00            
ATOM   2047  CG2 ILE E  41     -25.623   7.678 103.414  1.00            
ATOM   2048  CD1 ILE E  41     -26.394   6.167 105.940  1.00            
ATOM   2049  N   ILE E  42     -25.252   3.932 100.947  1.00            
ATOM   2050  CA  ILE E  42     -24.890   2.557 100.614  1.00            
ATOM   2051  C   ILE E  42     -23.611   2.149 101.332  1.00            
ATOM   2052  O   ILE E  42     -22.647   2.914 101.385  1.00            
ATOM   2053  CB  ILE E  42     -24.690   2.376  99.091  1.00            
ATOM   2054  CG1 ILE E  42     -25.980   2.717  98.340  1.00            
ATOM   2055  CG2 ILE E  42     -24.243   0.946  98.768  1.00            
ATOM   2056  CD1 ILE E  42     -25.833   2.718  96.826  1.00            
ATOM   2057  N   THR E  43     -23.614   0.943 101.890  1.00            
ATOM   2058  CA  THR E  43     -22.417   0.358 102.482  1.00            
ATOM   2059  C   THR E  43     -22.127  -0.982 101.812  1.00            
ATOM   2060  O   THR E  43     -22.962  -1.888 101.844  1.00            
ATOM   2061  CB  THR E  43     -22.574   0.163 104.003  1.00            
ATOM   2062  OG1 THR E  43     -23.034   1.384 104.598  1.00            
ATOM   2063  CG2 THR E  43     -21.253  -0.234 104.638  1.00            
ATOM   2064  N   GLU E  44     -20.946  -1.106 101.209  1.00            
ATOM   2065  CA  GLU E  44     -20.561  -2.342 100.530  1.00            
ATOM   2066  C   GLU E  44     -19.755  -3.242 101.461  1.00            
ATOM   2067  O   GLU E  44     -19.000  -2.755 102.303  1.00            
ATOM   2068  CB  GLU E  44     -19.754  -2.051  99.263  1.00            
ATOM   2069  CG  GLU E  44     -20.553  -1.403  98.144  1.00            
ATOM   2070  CD  GLU E  44     -19.781  -1.344  96.839  1.00            
ATOM   2071  OE1 GLU E  44     -18.688  -0.741  96.812  1.00            
ATOM   2072  OE2 GLU E  44     -20.272  -1.905  95.835  1.00            
ATOM   2073  N   TYR E  45     -19.926  -4.553 101.310  1.00            
ATOM   2074  CA  TYR E  45     -19.206  -5.520 102.136  1.00            
ATOM   2075  C   TYR E  45     -18.409  -6.519 101.292  1.00            
ATOM   2076  O   TYR E  45     -18.925  -7.101 100.336  1.00            
ATOM   2077  CB  TYR E  45     -20.193  -6.254 103.046  1.00            
ATOM   2078  CG  TYR E  45     -20.888  -5.326 104.018  1.00            
ATOM   2079  CD1 TYR E  45     -22.032  -4.635 103.642  1.00            
ATOM   2080  CD2 TYR E  45     -20.399  -5.129 105.302  1.00            
ATOM   2081  CE1 TYR E  45     -22.672  -3.779 104.515  1.00            
ATOM   2082  CE2 TYR E  45     -21.035  -4.271 106.186  1.00            
ATOM   2083  CZ  TYR E  45     -22.171  -3.599 105.785  1.00            
ATOM   2084  OH  TYR E  45     -22.816  -2.745 106.651  1.00            
ATOM   2085  N   ALA E  46     -17.147  -6.704 101.670  1.00            
ATOM   2086  CA  ALA E  46     -16.240  -7.652 101.025  1.00            
ATOM   2087  C   ALA E  46     -16.632  -9.094 101.334  1.00            
ATOM   2088  O   ALA E  46     -17.394  -9.346 102.267  1.00            
ATOM   2089  CB  ALA E  46     -14.812  -7.387 101.452  1.00            
ATOM   2090  N   LYS E  47     -16.130 -10.028 100.526  1.00            
ATOM   2091  CA  LYS E  47     -16.516 -11.437 100.619  1.00            
ATOM   2092  C   LYS E  47     -16.403 -11.976 102.042  1.00            
ATOM   2093  O   LYS E  47     -17.271 -12.712 102.511  1.00            
ATOM   2094  CB  LYS E  47     -15.609 -12.300  99.732  1.00            
ATOM   2095  CG  LYS E  47     -15.688 -12.051  98.233  1.00            
ATOM   2096  CD  LYS E  47     -14.644 -12.899  97.504  1.00            
ATOM   2097  CE  LYS E  47     -14.686 -12.695  95.999  1.00            
ATOM   2098  NZ  LYS E  47     -13.835 -13.683  95.276  1.00            
ATOM   2099  N   GLY E  48     -15.328 -11.590 102.723  1.00            
ATOM   2100  CA  GLY E  48     -15.055 -12.054 104.070  1.00            
ATOM   2101  C   GLY E  48     -15.715 -11.262 105.181  1.00            
ATOM   2102  O   GLY E  48     -15.394 -11.462 106.354  1.00            
ATOM   2103  N   HIS E  49     -16.637 -10.372 104.823  1.00            
ATOM   2104  CA  HIS E  49     -17.296  -9.513 105.804  1.00            
ATOM   2105  C   HIS E  49     -18.807  -9.710 105.826  1.00            
ATOM   2106  O   HIS E  49     -19.524  -8.947 106.469  1.00            
ATOM   2107  CB  HIS E  49     -16.958  -8.046 105.522  1.00            
ATOM   2108  CG  HIS E  49     -15.542  -7.686 105.843  1.00            
ATOM   2109  ND1 HIS E  49     -14.943  -6.529 105.392  1.00            
ATOM   2110  CD2 HIS E  49     -14.606  -8.328 106.584  1.00            
ATOM   2111  CE1 HIS E  49     -13.700  -6.477 105.834  1.00            
ATOM   2112  NE2 HIS E  49     -13.471  -7.557 106.560  1.00            
ATOM   2113  N   ALA E  50     -19.284 -10.733 105.122  1.00            
ATOM   2114  CA  ALA E  50     -20.710 -11.033 105.079  1.00            
ATOM   2115  C   ALA E  50     -20.954 -12.527 105.283  1.00            
ATOM   2116  O   ALA E  50     -20.307 -13.366 104.659  1.00            
ATOM   2117  CB  ALA E  50     -21.309 -10.567 103.765  1.00            
ATOM   2118  N   GLY E  51     -21.903 -12.833 106.163  1.00            
ATOM   2119  CA  GLY E  51     -22.289 -14.195 106.498  1.00            
ATOM   2120  C   GLY E  51     -23.766 -14.394 106.219  1.00            
ATOM   2121  O   GLY E  51     -24.522 -13.425 106.266  1.00            
ATOM   2122  N   ILE E  52     -24.188 -15.624 105.921  1.00            
ATOM   2123  CA  ILE E  52     -25.610 -15.886 105.684  1.00            
ATOM   2124  C   ILE E  52     -26.083 -17.146 106.407  1.00            
ATOM   2125  O   ILE E  52     -27.234 -17.228 106.835  1.00            
ATOM   2126  CB  ILE E  52     -25.928 -16.071 104.174  1.00            
ATOM   2127  CG1 ILE E  52     -25.303 -14.958 103.320  1.00            
ATOM   2128  CG2 ILE E  52     -27.448 -16.265 103.950  1.00            
ATOM   2129  CD1 ILE E  52     -26.179 -13.757 103.105  1.00            
ATOM   2130  N   GLY E  53     -25.203 -18.132 106.522  1.00            
ATOM   2131  CA  GLY E  53     -25.520 -19.373 107.208  1.00            
ATOM   2132  C   GLY E  53     -24.401 -19.716 108.168  1.00            
ATOM   2133  O   GLY E  53     -24.283 -20.850 108.629  1.00            
ATOM   2134  N   GLY E  54     -23.580 -18.715 108.466  1.00            
ATOM   2135  CA  GLY E  54     -22.370 -18.908 109.240  1.00            
ATOM   2136  C   GLY E  54     -21.230 -19.113 108.259  1.00            
ATOM   2137  O   GLY E  54     -20.062 -19.192 108.639  1.00            
ATOM   2138  N   GLU E  55     -21.595 -19.187 106.981  1.00            
ATOM   2139  CA  GLU E  55     -20.659 -19.335 105.874  1.00            
ATOM   2140  C   GLU E  55     -20.633 -18.041 105.085  1.00            
ATOM   2141  O   GLU E  55     -21.596 -17.274 105.117  1.00            
ATOM   2142  CB  GLU E  55     -21.048 -20.498 104.966  1.00            
ATOM   2143  CG  GLU E  55     -20.883 -21.864 105.600  1.00            
ATOM   2144  CD  GLU E  55     -21.248 -22.988 104.652  1.00            
ATOM   2145  OE1 GLU E  55     -21.605 -22.696 103.491  1.00            
ATOM   2146  OE2 GLU E  55     -21.165 -24.163 105.064  1.00            
ATOM   2147  N   LEU E  56     -19.533 -17.789 104.385  1.00            
ATOM   2148  CA  LEU E  56     -19.366 -16.514 103.711  1.00            
ATOM   2149  C   LEU E  56     -20.366 -16.417 102.566  1.00            
ATOM   2150  O   LEU E  56     -20.919 -17.427 102.125  1.00            
ATOM   2151  CB  LEU E  56     -17.935 -16.379 103.187  1.00            
ATOM   2152  CG  LEU E  56     -16.826 -16.292 104.241  1.00            
ATOM   2153  CD1 LEU E  56     -15.460 -16.199 103.578  1.00            
ATOM   2154  CD2 LEU E  56     -17.046 -15.118 105.182  1.00            
ATOM   2155  N   ALA E  57     -20.587 -15.198 102.087  1.00            
ATOM   2156  CA  ALA E  57     -21.542 -14.949 101.016  1.00            
ATOM   2157  C   ALA E  57     -20.834 -14.708  99.688  1.00            
ATOM   2158  O   ALA E  57     -20.392 -13.594  99.408  1.00            
ATOM   2159  CB  ALA E  57     -22.426 -13.773 101.373  1.00            
TER    2160      ALA E  57                                                      
ATOM   2161  N   PRO F   1     -29.032  -8.620 100.491  1.00            
ATOM   2162  CA  PRO F   1     -28.916  -7.205 100.856  1.00            
ATOM   2163  C   PRO F   1     -29.904  -6.799 101.948  1.00            
ATOM   2164  O   PRO F   1     -31.019  -7.318 102.006  1.00            
ATOM   2165  CB  PRO F   1     -29.202  -6.464  99.547  1.00            
ATOM   2166  CG  PRO F   1     -29.913  -7.424  98.674  1.00            
ATOM   2167  CD  PRO F   1     -29.676  -8.816  99.180  1.00            
ATOM   2168  N   ILE F   2     -29.477  -5.877 102.805  1.00            
ATOM   2169  CA  ILE F   2     -30.266  -5.437 103.946  1.00            
ATOM   2170  C   ILE F   2     -30.483  -3.936 103.886  1.00            
ATOM   2171  O   ILE F   2     -29.534  -3.165 103.758  1.00            
ATOM   2172  CB  ILE F   2     -29.571  -5.783 105.279  1.00            
ATOM   2173  CG1 ILE F   2     -29.407  -7.294 105.421  1.00            
ATOM   2174  CG2 ILE F   2     -30.338  -5.207 106.473  1.00            
ATOM   2175  CD1 ILE F   2     -27.965  -7.734 105.461  1.00            
ATOM   2176  N   ALA F   3     -31.746  -3.535 103.969  1.00            
ATOM   2177  CA  ALA F   3     -32.104  -2.127 103.981  1.00            
ATOM   2178  C   ALA F   3     -32.679  -1.774 105.342  1.00            
ATOM   2179  O   ALA F   3     -33.627  -2.404 105.813  1.00            
ATOM   2180  CB  ALA F   3     -33.105  -1.813 102.880  1.00            
ATOM   2181  N   GLN F   4     -32.083  -0.771 105.975  1.00            
ATOM   2182  CA  GLN F   4     -32.604  -0.229 107.215  1.00            
ATOM   2183  C   GLN F   4     -33.145   1.162 106.940  1.00            
ATOM   2184  O   GLN F   4     -32.385   2.080 106.632  1.00            
ATOM   2185  CB  GLN F   4     -31.520  -0.200 108.296  1.00            
ATOM   2186  CG  GLN F   4     -32.057   0.039 109.699  1.00            
ATOM   2187  CD  GLN F   4     -30.980  -0.058 110.763  1.00            
ATOM   2188  OE1 GLN F   4     -29.842  -0.446 110.482  1.00            
ATOM   2189  NE2 GLN F   4     -31.337   0.287 111.998  1.00            
ATOM   2190  N   ILE F   5     -34.461   1.309 107.053  1.00            
ATOM   2191  CA  ILE F   5     -35.122   2.580 106.779  1.00            
ATOM   2192  C   ILE F   5     -35.539   3.263 108.066  1.00            
ATOM   2193  O   ILE F   5     -36.230   2.689 108.905  1.00            
ATOM   2194  CB  ILE F   5     -36.359   2.408 105.868  1.00            
ATOM   2195  CG1 ILE F   5     -35.941   1.862 104.506  1.00            
ATOM   2196  CG2 ILE F   5     -37.000   3.740 105.577  1.00            
ATOM   2197  CD1 ILE F   5     -36.065   0.391 104.369  1.00            
ATOM   2198  N   HIS F   6     -35.099   4.510 108.191  1.00            
ATOM   2199  CA  HIS F   6     -35.343   5.325 109.367  1.00            
ATOM   2200  C   HIS F   6     -36.384   6.374 108.998  1.00            
ATOM   2201  O   HIS F   6     -36.139   7.201 108.123  1.00            
ATOM   2202  CB  HIS F   6     -34.048   5.994 109.833  1.00            
ATOM   2203  CG  HIS F   6     -32.916   5.034 110.058  1.00            
ATOM   2204  ND1 HIS F   6     -32.771   4.312 111.217  1.00            
ATOM   2205  CD2 HIS F   6     -31.864   4.706 109.270  1.00            
ATOM   2206  CE1 HIS F   6     -31.681   3.562 111.133  1.00            
ATOM   2207  NE2 HIS F   6     -31.117   3.784 109.965  1.00            
ATOM   2208  N   ILE F   7     -37.538   6.340 109.656  1.00            
ATOM   2209  CA  ILE F   7     -38.641   7.236 109.313  1.00            
ATOM   2210  C   ILE F   7     -39.272   7.895 110.529  1.00            
ATOM   2211  O   ILE F   7     -39.097   7.443 111.659  1.00            
ATOM   2212  CB  ILE F   7     -39.759   6.493 108.536  1.00            
ATOM   2213  CG1 ILE F   7     -40.408   5.412 109.410  1.00            
ATOM   2214  CG2 ILE F   7     -39.193   5.868 107.287  1.00            
ATOM   2215  CD1 ILE F   7     -41.621   4.753 108.783  1.00            
ATOM   2216  N   LEU F   8     -40.006   8.975 110.280  1.00            
ATOM   2217  CA  LEU F   8     -40.789   9.615 111.323  1.00            
ATOM   2218  C   LEU F   8     -41.988   8.753 111.666  1.00            
ATOM   2219  O   LEU F   8     -42.614   8.144 110.798  1.00            
ATOM   2220  CB  LEU F   8     -41.261  11.005 110.893  1.00            
ATOM   2221  CG  LEU F   8     -40.408  12.223 111.251  1.00            
ATOM   2222  CD1 LEU F   8     -40.733  12.639 112.680  1.00            
ATOM   2223  CD2 LEU F   8     -38.919  11.967 111.097  1.00            
ATOM   2224  N   GLU F   9     -42.283   8.695 112.955  1.00            
ATOM   2225  CA  GLU F   9     -43.383   7.895 113.464  1.00            
ATOM   2226  C   GLU F   9     -44.714   8.598 113.197  1.00            
ATOM   2227  O   GLU F   9     -44.752   9.819 113.057  1.00            
ATOM   2228  CB  GLU F   9     -43.136   7.633 114.958  1.00            
ATOM   2229  CG  GLU F   9     -44.316   7.714 115.891  1.00            
ATOM   2230  CD  GLU F   9     -43.905   7.409 117.324  1.00            
ATOM   2231  OE1 GLU F   9     -43.043   6.526 117.522  1.00            
ATOM   2232  OE2 GLU F   9     -44.425   8.065 118.248  1.00            
ATOM   2233  N   GLY F  10     -45.797   7.826 113.110  1.00            
ATOM   2234  CA  GLY F  10     -47.123   8.390 112.906  1.00            
ATOM   2235  C   GLY F  10     -47.909   7.776 111.760  1.00            
ATOM   2236  O   GLY F  10     -49.105   8.025 111.611  1.00            
ATOM   2237  N   ARG F  11     -47.229   6.989 110.936  1.00            
ATOM   2238  CA  ARG F  11     -47.824   6.412 109.735  1.00            
ATOM   2239  C   ARG F  11     -48.552   5.092 110.001  1.00            
ATOM   2240  O   ARG F  11     -48.306   4.429 111.010  1.00            
ATOM   2241  CB  ARG F  11     -46.718   6.252 108.693  1.00            
ATOM   2242  CG  ARG F  11     -46.227   7.619 108.227  1.00            
ATOM   2243  CD  ARG F  11     -45.211   7.566 107.117  1.00            
ATOM   2244  NE  ARG F  11     -43.921   8.071 107.596  1.00            
ATOM   2245  CZ  ARG F  11     -43.371   9.229 107.231  1.00            
ATOM   2246  NH1 ARG F  11     -43.978  10.030 106.361  1.00            
ATOM   2247  NH2 ARG F  11     -42.198   9.593 107.736  1.00            
ATOM   2248  N   SER F  12     -49.446   4.719 109.088  1.00            
ATOM   2249  CA  SER F  12     -50.256   3.515 109.249  1.00            
ATOM   2250  C   SER F  12     -49.468   2.253 108.934  1.00            
ATOM   2251  O   SER F  12     -48.400   2.315 108.325  1.00            
ATOM   2252  CB  SER F  12     -51.488   3.582 108.341  1.00            
ATOM   2253  OG  SER F  12     -51.137   3.362 106.985  1.00            
ATOM   2254  N   ASP F  13     -50.001   1.108 109.354  1.00            
ATOM   2255  CA  ASP F  13     -49.380  -0.177 109.054  1.00            
ATOM   2256  C   ASP F  13     -49.471  -0.448 107.556  1.00            
ATOM   2257  O   ASP F  13     -48.633  -1.149 106.989  1.00            
ATOM   2258  CB  ASP F  13     -50.038  -1.309 109.846  1.00            
ATOM   2259  CG  ASP F  13     -49.534  -1.396 111.278  1.00            
ATOM   2260  OD1 ASP F  13     -48.602  -0.649 111.643  1.00            
ATOM   2261  OD2 ASP F  13     -50.070  -2.224 112.044  1.00            
ATOM   2262  N   GLU F  14     -50.488   0.123 106.918  1.00            
ATOM   2263  CA  GLU F  14     -50.700  -0.062 105.489  1.00            
ATOM   2264  C   GLU F  14     -49.577   0.589 104.692  1.00            
ATOM   2265  O   GLU F  14     -49.021  -0.013 103.773  1.00            
ATOM   2266  CB  GLU F  14     -52.042   0.539 105.065  1.00            
ATOM   2267  CG  GLU F  14     -52.519   0.089 103.687  1.00            
ATOM   2268  CD  GLU F  14     -53.838   0.726 103.279  1.00            
ATOM   2269  OE1 GLU F  14     -54.293   1.665 103.969  1.00            
ATOM   2270  OE2 GLU F  14     -54.408   0.297 102.255  1.00            
ATOM   2271  N   GLN F  15     -49.223   1.809 105.081  1.00            
ATOM   2272  CA  GLN F  15     -48.183   2.571 104.397  1.00            
ATOM   2273  C   GLN F  15     -46.820   1.908 104.529  1.00            
ATOM   2274  O   GLN F  15     -46.040   1.867 103.578  1.00            
ATOM   2275  CB  GLN F  15     -48.112   3.992 104.957  1.00            
ATOM   2276  CG  GLN F  15     -49.265   4.886 104.559  1.00            
ATOM   2277  CD  GLN F  15     -49.170   6.266 105.181  1.00            
ATOM   2278  OE1 GLN F  15     -49.668   6.497 106.284  1.00            
ATOM   2279  NE2 GLN F  15     -48.524   7.192 104.477  1.00            
ATOM   2280  N   LYS F  16     -46.542   1.392 105.718  1.00            
ATOM   2281  CA  LYS F  16     -45.260   0.766 106.005  1.00            
ATOM   2282  C   LYS F  16     -45.131  -0.603 105.352  1.00            
ATOM   2283  O   LYS F  16     -44.030  -1.046 105.034  1.00            
ATOM   2284  CB  LYS F  16     -45.078   0.650 107.515  1.00            
ATOM   2285  CG  LYS F  16     -44.774   1.971 108.192  1.00            
ATOM   2286  CD  LYS F  16     -44.579   1.788 109.683  1.00            
ATOM   2287  CE  LYS F  16     -45.919   1.897 110.399  1.00            
ATOM   2288  NZ  LYS F  16     -45.820   1.758 111.871  1.00            
ATOM   2289  N   GLU F  17     -46.260  -1.266 105.140  1.00            
ATOM   2290  CA  GLU F  17     -46.261  -2.550 104.456  1.00            
ATOM   2291  C   GLU F  17     -46.045  -2.287 102.968  1.00            
ATOM   2292  O   GLU F  17     -45.398  -3.069 102.272  1.00            
ATOM   2293  CB  GLU F  17     -47.564  -3.307 104.725  1.00            
ATOM   2294  CG  GLU F  17     -47.589  -4.734 104.193  1.00            
ATOM   2295  CD  GLU F  17     -48.849  -5.483 104.593  1.00            
ATOM   2296  OE1 GLU F  17     -49.583  -4.988 105.477  1.00            
ATOM   2297  OE2 GLU F  17     -49.103  -6.570 104.033  1.00            
ATOM   2298  N   THR F  18     -46.593  -1.171 102.493  1.00            
ATOM   2299  CA  THR F  18     -46.377  -0.720 101.123  1.00            
ATOM   2300  C   THR F  18     -44.918  -0.320 100.937  1.00            
ATOM   2301  O   THR F  18     -44.309  -0.612  99.910  1.00            
ATOM   2302  CB  THR F  18     -47.288   0.482 100.772  1.00            
ATOM   2303  OG1 THR F  18     -48.662   0.084 100.839  1.00            
ATOM   2304  CG2 THR F  18     -46.987   1.017  99.376  1.00            
ATOM   2305  N   LEU F  19     -44.371   0.345 101.949  1.00            
ATOM   2306  CA  LEU F  19     -42.984   0.798 101.937  1.00            
ATOM   2307  C   LEU F  19     -42.019  -0.370 101.760  1.00            
ATOM   2308  O   LEU F  19     -41.132  -0.331 100.907  1.00            
ATOM   2309  CB  LEU F  19     -42.677   1.561 103.230  1.00            
ATOM   2310  CG  LEU F  19     -41.261   2.097 103.459  1.00            
ATOM   2311  CD1 LEU F  19     -40.953   3.282 102.567  1.00            
ATOM   2312  CD2 LEU F  19     -41.105   2.491 104.920  1.00            
ATOM   2313  N   ILE F  20     -42.195  -1.402 102.580  1.00            
ATOM   2314  CA  ILE F  20     -41.345  -2.588 102.532  1.00            
ATOM   2315  C   ILE F  20     -41.336  -3.268 101.171  1.00            
ATOM   2316  O   ILE F  20     -40.275  -3.602 100.644  1.00            
ATOM   2317  CB  ILE F  20     -41.799  -3.618 103.586  1.00            
ATOM   2318  CG1 ILE F  20     -41.494  -3.092 104.989  1.00            
ATOM   2319  CG2 ILE F  20     -41.115  -4.973 103.362  1.00            
ATOM   2320  CD1 ILE F  20     -42.038  -3.948 106.107  1.00            
ATOM   2321  N   ARG F  21     -42.516  -3.463 100.597  1.00            
ATOM   2322  CA  ARG F  21     -42.622  -4.152  99.317  1.00            
ATOM   2323  C   ARG F  21     -42.037  -3.294  98.201  1.00            
ATOM   2324  O   ARG F  21     -41.268  -3.784  97.376  1.00            
ATOM   2325  CB  ARG F  21     -44.074  -4.534  99.022  1.00            
ATOM   2326  CG  ARG F  21     -44.269  -5.229  97.688  1.00            
ATOM   2327  CD  ARG F  21     -45.716  -5.667  97.484  1.00            
ATOM   2328  NE  ARG F  21     -46.228  -6.680  98.431  1.00            
ATOM   2329  CZ  ARG F  21     -47.069  -6.483  99.460  1.00            
ATOM   2330  NH1 ARG F  21     -47.463  -5.260  99.787  1.00            
ATOM   2331  NH2 ARG F  21     -47.480  -7.534 100.187  1.00            
ATOM   2332  N   GLU F  22     -42.385  -2.013  98.176  1.00            
ATOM   2333  CA  GLU F  22     -41.917  -1.149  97.102  1.00            
ATOM   2334  C   GLU F  22     -40.396  -0.959  97.157  1.00            
ATOM   2335  O   GLU F  22     -39.727  -0.952  96.127  1.00            
ATOM   2336  CB  GLU F  22     -42.614   0.210  97.158  1.00            
ATOM   2337  CG  GLU F  22     -43.604   0.396  96.034  1.00            
ATOM   2338  CD  GLU F  22     -44.102   1.823  95.909  1.00            
ATOM   2339  OE1 GLU F  22     -43.612   2.545  95.019  1.00            
ATOM   2340  OE2 GLU F  22     -44.997   2.219  96.685  1.00            
ATOM   2341  N   VAL F  23     -39.852  -0.817  98.363  1.00            
ATOM   2342  CA  VAL F  23     -38.407  -0.620  98.526  1.00            
ATOM   2343  C   VAL F  23     -37.628  -1.900  98.203  1.00            
ATOM   2344  O   VAL F  23     -36.568  -1.844  97.575  1.00            
ATOM   2345  CB  VAL F  23     -38.054  -0.127  99.963  1.00            
ATOM   2346  CG1 VAL F  23     -36.557  -0.296 100.268  1.00            
ATOM   2347  CG2 VAL F  23     -38.465   1.329 100.151  1.00            
ATOM   2348  N   SER F  24     -38.157  -3.049  98.619  1.00            
ATOM   2349  CA  SER F  24     -37.504  -4.333  98.341  1.00            
ATOM   2350  C   SER F  24     -37.401  -4.615  96.848  1.00            
ATOM   2351  O   SER F  24     -36.346  -5.023  96.355  1.00            
ATOM   2352  CB  SER F  24     -38.248  -5.496  99.016  1.00            
ATOM   2353  OG  SER F  24     -38.271  -5.387 100.434  1.00            
ATOM   2354  N   GLU F  25     -38.493  -4.370  96.134  1.00            
ATOM   2355  CA  GLU F  25     -38.529  -4.551  94.685  1.00            
ATOM   2356  C   GLU F  25     -37.561  -3.607  93.971  1.00            
ATOM   2357  O   GLU F  25     -36.904  -4.011  93.013  1.00            
ATOM   2358  CB  GLU F  25     -39.971  -4.421  94.177  1.00            
ATOM   2359  CG  GLU F  25     -40.619  -5.802  94.037  1.00            
ATOM   2360  CD  GLU F  25     -42.134  -5.796  93.914  1.00            
ATOM   2361  OE1 GLU F  25     -42.729  -6.894  93.970  1.00            
ATOM   2362  OE2 GLU F  25     -42.730  -4.713  93.742  1.00            
ATOM   2363  N   ALA F  26     -37.467  -2.364  94.430  1.00            
ATOM   2364  CA  ALA F  26     -36.534  -1.406  93.840  1.00            
ATOM   2365  C   ALA F  26     -35.087  -1.882  93.979  1.00            
ATOM   2366  O   ALA F  26     -34.289  -1.729  93.058  1.00            
ATOM   2367  CB  ALA F  26     -36.705  -0.023  94.489  1.00            
ATOM   2368  N   ILE F  27     -34.756  -2.471  95.128  1.00            
ATOM   2369  CA  ILE F  27     -33.401  -2.984  95.368  1.00            
ATOM   2370  C   ILE F  27     -33.133  -4.214  94.513  1.00            
ATOM   2371  O   ILE F  27     -32.080  -4.327  93.890  1.00            
ATOM   2372  CB  ILE F  27     -33.155  -3.345  96.864  1.00            
ATOM   2373  CG1 ILE F  27     -33.263  -2.098  97.745  1.00            
ATOM   2374  CG2 ILE F  27     -31.772  -3.999  97.048  1.00            
ATOM   2375  CD1 ILE F  27     -33.190  -2.371  99.238  1.00            
ATOM   2376  N   SER F  28     -34.094  -5.132  94.493  1.00            
ATOM   2377  CA  SER F  28     -33.987  -6.351  93.702  1.00            
ATOM   2378  C   SER F  28     -33.841  -5.988  92.228  1.00            
ATOM   2379  O   SER F  28     -33.044  -6.576  91.492  1.00            
ATOM   2380  CB  SER F  28     -35.210  -7.238  93.925  1.00            
ATOM   2381  OG  SER F  28     -35.054  -8.498  93.298  1.00            
ATOM   2382  N   ARG F  29     -34.600  -4.974  91.834  1.00            
ATOM   2383  CA  ARG F  29     -34.586  -4.430  90.486  1.00            
ATOM   2384  C   ARG F  29     -33.232  -3.824  90.127  1.00            
ATOM   2385  O   ARG F  29     -32.614  -4.220  89.139  1.00            
ATOM   2386  CB  ARG F  29     -35.686  -3.373  90.395  1.00            
ATOM   2387  CG  ARG F  29     -35.777  -2.625  89.081  1.00            
ATOM   2388  CD  ARG F  29     -36.863  -1.548  89.113  1.00            
ATOM   2389  NE  ARG F  29     -36.549  -0.628  90.207  1.00            
ATOM   2390  CZ  ARG F  29     -37.409   0.170  90.844  1.00            
ATOM   2391  NH1 ARG F  29     -38.656   0.286  90.439  1.00            
ATOM   2392  NH2 ARG F  29     -36.984   0.914  91.843  1.00            
ATOM   2393  N   SER F  30     -32.755  -2.907  90.965  1.00            
ATOM   2394  CA  SER F  30     -31.539  -2.146  90.682  1.00            
ATOM   2395  C   SER F  30     -30.303  -3.033  90.561  1.00            
ATOM   2396  O   SER F  30     -29.422  -2.775  89.741  1.00            
ATOM   2397  CB  SER F  30     -31.302  -1.090  91.772  1.00            
ATOM   2398  OG  SER F  30     -32.375  -0.163  91.853  1.00            
ATOM   2399  N   LEU F  31     -30.251  -4.084  91.372  1.00            
ATOM   2400  CA  LEU F  31     -29.054  -4.914  91.470  1.00            
ATOM   2401  C   LEU F  31     -29.202  -6.305  90.893  1.00            
ATOM   2402  O   LEU F  31     -28.306  -7.136  91.048  1.00            
ATOM   2403  CB  LEU F  31     -28.670  -5.060  92.933  1.00            
ATOM   2404  CG  LEU F  31     -28.664  -3.750  93.708  1.00            
ATOM   2405  CD1 LEU F  31     -28.300  -4.016  95.151  1.00            
ATOM   2406  CD2 LEU F  31     -27.711  -2.745  93.073  1.00            
ATOM   2407  N   ASP F  32     -30.297  -6.536  90.184  1.00            
ATOM   2408  CA  ASP F  32     -30.588  -7.856  89.659  1.00            
ATOM   2409  C   ASP F  32     -30.269  -8.950  90.695  1.00            
ATOM   2410  O   ASP F  32     -29.570  -9.926  90.406  1.00            
ATOM   2411  CB  ASP F  32     -29.779  -8.051  88.380  1.00            
ATOM   2412  CG  ASP F  32     -30.225  -9.248  87.571  1.00            
ATOM   2413  OD1 ASP F  32     -31.216  -9.907  87.954  1.00            
ATOM   2414  OD2 ASP F  32     -29.571  -9.533  86.546  1.00            
ATOM   2415  N   ALA F  33     -30.764  -8.734  91.913  1.00            
ATOM   2416  CA  ALA F  33     -30.603  -9.648  93.043  1.00            
ATOM   2417  C   ALA F  33     -31.963 -10.286  93.313  1.00            
ATOM   2418  O   ALA F  33     -32.990  -9.650  93.076  1.00            
ATOM   2419  CB  ALA F  33     -30.097  -8.913  94.275  1.00            
ATOM   2420  N   PRO F  34     -31.987 -11.542  93.792  1.00            
ATOM   2421  CA  PRO F  34     -33.288 -12.153  94.095  1.00            
ATOM   2422  C   PRO F  34     -34.108 -11.378  95.119  1.00            
ATOM   2423  O   PRO F  34     -33.572 -10.975  96.150  1.00            
ATOM   2424  CB  PRO F  34     -32.907 -13.518  94.672  1.00            
ATOM   2425  CG  PRO F  34     -31.602 -13.828  94.066  1.00            
ATOM   2426  CD  PRO F  34     -30.886 -12.504  93.975  1.00            
ATOM   2427  N   LEU F  35     -35.385 -11.159  94.820  1.00            
ATOM   2428  CA  LEU F  35     -36.262 -10.422  95.718  1.00            
ATOM   2429  C   LEU F  35     -36.276 -11.141  97.061  1.00            
ATOM   2430  O   LEU F  35     -36.276 -10.518  98.118  1.00            
ATOM   2431  CB  LEU F  35     -37.679 -10.339  95.146  1.00            
ATOM   2432  CG  LEU F  35     -38.706  -9.490  95.898  1.00            
ATOM   2433  CD1 LEU F  35     -38.360  -8.008  95.791  1.00            
ATOM   2434  CD2 LEU F  35     -40.112  -9.773  95.392  1.00            
ATOM   2435  N   THR F  36     -36.249 -12.470  96.994  1.00            
ATOM   2436  CA  THR F  36     -36.352 -13.317  98.176  1.00            
ATOM   2437  C   THR F  36     -35.123 -13.208  99.079  1.00            
ATOM   2438  O   THR F  36     -35.134 -13.697 100.210  1.00            
ATOM   2439  CB  THR F  36     -36.552 -14.800  97.783  1.00            
ATOM   2440  OG1 THR F  36     -36.501 -15.625  98.954  1.00            
ATOM   2441  CG2 THR F  36     -35.482 -15.259  96.792  1.00            
ATOM   2442  N   SER F  37     -34.072 -12.562  98.582  1.00            
ATOM   2443  CA  SER F  37     -32.854 -12.371  99.361  1.00            
ATOM   2444  C   SER F  37     -32.887 -11.004 100.032  1.00            
ATOM   2445  O   SER F  37     -32.038 -10.690 100.868  1.00            
ATOM   2446  CB  SER F  37     -31.609 -12.491  98.476  1.00            
ATOM   2447  OG  SER F  37     -31.581 -11.474  97.490  1.00            
ATOM   2448  N   VAL F  38     -33.875 -10.196  99.665  1.00            
ATOM   2449  CA  VAL F  38     -33.978  -8.838 100.174  1.00            
ATOM   2450  C   VAL F  38     -34.668  -8.761 101.538  1.00            
ATOM   2451  O   VAL F  38     -35.765  -9.294 101.726  1.00            
ATOM   2452  CB  VAL F  38     -34.744  -7.932  99.174  1.00            
ATOM   2453  CG1 VAL F  38     -34.796  -6.496  99.677  1.00            
ATOM   2454  CG2 VAL F  38     -34.096  -7.984  97.800  1.00            
ATOM   2455  N   ARG F  39     -33.999  -8.097 102.477  1.00            
ATOM   2456  CA  ARG F  39     -34.554  -7.794 103.789  1.00            
ATOM   2457  C   ARG F  39     -34.668  -6.305 104.016  1.00            
ATOM   2458  O   ARG F  39     -33.797  -5.531 103.645  1.00            
ATOM   2459  CB  ARG F  39     -33.728  -8.416 104.919  1.00            
ATOM   2460  CG  ARG F  39     -34.033  -9.875 105.184  1.00            
ATOM   2461  CD  ARG F  39     -32.792 -10.720 105.219  1.00            
ATOM   2462  NE  ARG F  39     -33.086 -12.079 105.674  1.00            
ATOM   2463  CZ  ARG F  39     -33.699 -13.001 104.936  1.00            
ATOM   2464  NH1 ARG F  39     -34.083 -12.703 103.700  1.00            
ATOM   2465  NH2 ARG F  39     -33.937 -14.213 105.423  1.00            
ATOM   2466  N   VAL F  40     -35.779  -5.932 104.638  1.00            
ATOM   2467  CA  VAL F  40     -36.059  -4.552 104.988  1.00            
ATOM   2468  C   VAL F  40     -36.470  -4.500 106.446  1.00            
ATOM   2469  O   VAL F  40     -37.295  -5.296 106.891  1.00            
ATOM   2470  CB  VAL F  40     -37.169  -3.951 104.105  1.00            
ATOM   2471  CG1 VAL F  40     -37.453  -2.530 104.522  1.00            
ATOM   2472  CG2 VAL F  40     -36.764  -4.003 102.643  1.00            
ATOM   2473  N   ILE F  41     -35.877  -3.575 107.192  1.00            
ATOM   2474  CA  ILE F  41     -36.266  -3.359 108.577  1.00            
ATOM   2475  C   ILE F  41     -36.535  -1.877 108.809  1.00            
ATOM   2476  O   ILE F  41     -35.707  -1.023 108.492  1.00            
ATOM   2477  CB  ILE F  41     -35.192  -3.869 109.566  1.00            
ATOM   2478  CG1 ILE F  41     -33.795  -3.383 109.167  1.00            
ATOM   2479  CG2 ILE F  41     -35.229  -5.392 109.624  1.00            
ATOM   2480  CD1 ILE F  41     -32.702  -3.777 110.146  1.00            
ATOM   2481  N   ILE F  42     -37.710  -1.585 109.357  1.00            
ATOM   2482  CA  ILE F  42     -38.124  -0.214 109.626  1.00            
ATOM   2483  C   ILE F  42     -37.901   0.139 111.084  1.00            
ATOM   2484  O   ILE F  42     -38.218  -0.641 111.981  1.00            
ATOM   2485  CB  ILE F  42     -39.614   0.018 109.282  1.00            
ATOM   2486  CG1 ILE F  42     -39.869  -0.244 107.795  1.00            
ATOM   2487  CG2 ILE F  42     -40.031   1.444 109.649  1.00            
ATOM   2488  CD1 ILE F  42     -41.335  -0.188 107.394  1.00            
ATOM   2489  N   THR F  43     -37.345   1.325 111.305  1.00            
ATOM   2490  CA  THR F  43     -37.202   1.890 112.639  1.00            
ATOM   2491  C   THR F  43     -37.885   3.257 112.679  1.00            
ATOM   2492  O   THR F  43     -37.518   4.162 111.932  1.00            
ATOM   2493  CB  THR F  43     -35.719   2.013 113.035  1.00            
ATOM   2494  OG1 THR F  43     -35.071   0.749 112.836  1.00            
ATOM   2495  CG2 THR F  43     -35.577   2.421 114.492  1.00            
ATOM   2496  N   GLU F  44     -38.876   3.397 113.556  1.00            
ATOM   2497  CA  GLU F  44     -39.631   4.642 113.681  1.00            
ATOM   2498  C   GLU F  44     -39.076   5.534 114.784  1.00            
ATOM   2499  O   GLU F  44     -38.604   5.040 115.810  1.00            
ATOM   2500  CB  GLU F  44     -41.106   4.344 113.951  1.00            
ATOM   2501  CG  GLU F  44     -41.844   3.723 112.780  1.00            
ATOM   2502  CD  GLU F  44     -43.336   3.626 113.029  1.00            
ATOM   2503  OE1 GLU F  44     -43.732   2.968 114.014  1.00            
ATOM   2504  OE2 GLU F  44     -44.115   4.215 112.248  1.00            
ATOM   2505  N   TYR F  45     -39.143   6.847 114.570  1.00            
ATOM   2506  CA  TYR F  45     -38.651   7.811 115.551  1.00            
ATOM   2507  C   TYR F  45     -39.705   8.831 115.982  1.00            
ATOM   2508  O   TYR F  45     -40.355   9.467 115.152  1.00            
ATOM   2509  CB  TYR F  45     -37.430   8.533 114.980  1.00            
ATOM   2510  CG  TYR F  45     -36.268   7.601 114.727  1.00            
ATOM   2511  CD1 TYR F  45     -36.121   6.958 113.503  1.00            
ATOM   2512  CD2 TYR F  45     -35.326   7.349 115.715  1.00            
ATOM   2513  CE1 TYR F  45     -35.063   6.098 113.270  1.00            
ATOM   2514  CE2 TYR F  45     -34.266   6.492 115.489  1.00            
ATOM   2515  CZ  TYR F  45     -34.141   5.871 114.268  1.00            
ATOM   2516  OH  TYR F  45     -33.085   5.019 114.055  1.00            
ATOM   2517  N   ALA F  46     -39.833   8.988 117.296  1.00            
ATOM   2518  CA  ALA F  46     -40.745   9.948 117.921  1.00            
ATOM   2519  C   ALA F  46     -40.256  11.383 117.736  1.00            
ATOM   2520  O   ALA F  46     -39.088  11.605 117.419  1.00            
ATOM   2521  CB  ALA F  46     -40.919   9.623 119.398  1.00            
ATOM   2522  N   LYS F  47     -41.165  12.343 117.915  1.00            
ATOM   2523  CA  LYS F  47     -40.897  13.755 117.640  1.00            
ATOM   2524  C   LYS F  47     -39.606  14.203 118.305  1.00            
ATOM   2525  O   LYS F  47     -38.798  14.923 117.714  1.00            
ATOM   2526  CB  LYS F  47     -42.023  14.634 118.196  1.00            
ATOM   2527  CG  LYS F  47     -43.421  14.427 117.628  1.00            
ATOM   2528  CD  LYS F  47     -44.407  15.305 118.407  1.00            
ATOM   2529  CE  LYS F  47     -45.842  15.130 117.950  1.00            
ATOM   2530  NZ  LYS F  47     -46.333  13.780 118.346  1.00            
ATOM   2531  N   GLY F  48     -39.414  13.740 119.536  1.00            
ATOM   2532  CA  GLY F  48     -38.267  14.118 120.340  1.00            
ATOM   2533  C   GLY F  48     -36.994  13.317 120.146  1.00            
ATOM   2534  O   GLY F  48     -36.044  13.483 120.916  1.00            
ATOM   2535  N   HIS F  49     -36.954  12.463 119.126  1.00            
ATOM   2536  CA  HIS F  49     -35.783  11.620 118.886  1.00            
ATOM   2537  C   HIS F  49     -35.157  11.868 117.520  1.00            
ATOM   2538  O   HIS F  49     -34.249  11.145 117.118  1.00            
ATOM   2539  CB  HIS F  49     -36.161  10.140 119.002  1.00            
ATOM   2540  CG  HIS F  49     -36.460   9.694 120.398  1.00            
ATOM   2541  ND1 HIS F  49     -37.093   8.504 120.678  1.00            
ATOM   2542  CD2 HIS F  49     -36.209  10.277 121.596  1.00            
ATOM   2543  CE1 HIS F  49     -37.221   8.370 121.986  1.00            
ATOM   2544  NE2 HIS F  49     -36.692   9.433 122.564  1.00            
ATOM   2545  N   ALA F  50     -35.635  12.888 116.814  1.00            
ATOM   2546  CA  ALA F  50     -35.114  13.210 115.490  1.00            
ATOM   2547  C   ALA F  50     -34.874  14.708 115.346  1.00            
ATOM   2548  O   ALA F  50     -35.722  15.520 115.722  1.00            
ATOM   2549  CB  ALA F  50     -36.064  12.717 114.416  1.00            
ATOM   2550  N   GLY F  51     -33.709  15.061 114.810  1.00            
ATOM   2551  CA  GLY F  51     -33.338  16.449 114.603  1.00            
ATOM   2552  C   GLY F  51     -32.960  16.837 113.182  1.00            
ATOM   2553  O   GLY F  51     -32.443  16.022 112.419  1.00            
ATOM   2554  N   ILE F  52     -33.242  18.089 112.830  1.00            
ATOM   2555  CA  ILE F  52     -32.776  18.674 111.576  1.00            
ATOM   2556  C   ILE F  52     -32.333  20.078 111.947  1.00            
ATOM   2557  O   ILE F  52     -33.133  20.878 112.429  1.00            
ATOM   2558  CB  ILE F  52     -33.844  18.759 110.453  1.00            
ATOM   2559  CG1 ILE F  52     -34.492  17.405 110.176  1.00            
ATOM   2560  CG2 ILE F  52     -33.230  19.341 109.177  1.00            
ATOM   2561  CD1 ILE F  52     -35.833  17.252 110.841  1.00            
ATOM   2562  N   GLY F  53     -31.056  20.371 111.744  1.00            
ATOM   2563  CA  GLY F  53     -30.522  21.677 112.076  1.00            
ATOM   2564  C   GLY F  53     -30.366  21.877 113.574  1.00            
ATOM   2565  O   GLY F  53     -30.164  23.001 114.032  1.00            
ATOM   2566  N   GLY F  54     -30.459  20.789 114.337  1.00            
ATOM   2567  CA  GLY F  54     -30.371  20.857 115.788  1.00            
ATOM   2568  C   GLY F  54     -31.726  21.020 116.460  1.00            
ATOM   2569  O   GLY F  54     -31.835  20.991 117.687  1.00            
ATOM   2570  N   GLU F  55     -32.763  21.164 115.642  1.00            
ATOM   2571  CA  GLU F  55     -34.121  21.399 116.116  1.00            
ATOM   2572  C   GLU F  55     -34.959  20.151 115.890  1.00            
ATOM   2573  O   GLU F  55     -34.674  19.378 114.982  1.00            
ATOM   2574  CB  GLU F  55     -34.718  22.594 115.376  1.00            
ATOM   2575  CG  GLU F  55     -34.001  23.889 115.689  1.00            
ATOM   2576  CD  GLU F  55     -34.608  25.082 114.986  1.00            
ATOM   2577  OE1 GLU F  55     -35.658  24.918 114.326  1.00            
ATOM   2578  OE2 GLU F  55     -34.015  26.180 115.061  1.00            
ATOM   2579  N   LEU F  56     -36.003  19.952 116.689  1.00            
ATOM   2580  CA  LEU F  56     -36.761  18.709 116.602  1.00            
ATOM   2581  C   LEU F  56     -37.508  18.622 115.269  1.00            
ATOM   2582  O   LEU F  56     -37.671  19.626 114.573  1.00            
ATOM   2583  CB  LEU F  56     -37.770  18.601 117.746  1.00            
ATOM   2584  CG  LEU F  56     -37.248  18.484 119.179  1.00            
ATOM   2585  CD1 LEU F  56     -38.429  18.378 120.135  1.00            
ATOM   2586  CD2 LEU F  56     -36.290  17.318 119.360  1.00            
ATOM   2587  N   ALA F  57     -37.968  17.419 114.929  1.00            
ATOM   2588  CA  ALA F  57     -38.681  17.181 113.672  1.00            
ATOM   2589  C   ALA F  57     -40.183  17.057 113.905  1.00            
ATOM   2590  O   ALA F  57     -40.906  18.051 113.927  1.00            
ATOM   2591  CB  ALA F  57     -38.143  15.935 112.990  1.00            
TER    2592      ALA F  57                                                      
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

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