HEADER    TRANSFERASE                             02-JUL-15   5CCV              
TITLE     CRYSTAL STRUCTURE OF FULL-LENGTH NS5 FROM DENGUE VIRUS TYPE 3         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RNA-DIRECTED RNA POLYMERASE NS5;                           
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: NON-STRUCTURAL PROTEIN 5;                                   
COMPND   5 EC: 2.1.1.56,2.1.1.57,2.7.7.48;                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DENGUE VIRUS TYPE 3;                            
SOURCE   3 ORGANISM_COMMON: DENV-3;                                             
SOURCE   4 ORGANISM_TAXID: 408870;                                              
SOURCE   5 STRAIN: PHILIPPINES/H87/1956;                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL                    
KEYWDS    METHYLTRANSFERASE, NONSTRUCTURAL PROTEIN, TRANSFERASE                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    V.J.KLEMA,K.H.CHOI                                                    
REVDAT   5   27-SEP-23 5CCV    1       REMARK                                   
REVDAT   4   23-MAR-22 5CCV    1       REMARK                                   
REVDAT   3   12-MAY-21 5CCV    1       JRNL   REMARK                            
REVDAT   2   01-JUN-16 5CCV    1       REMARK                                   
REVDAT   1   03-FEB-16 5CCV    0                                                
JRNL        AUTH   V.J.KLEMA,M.YE,A.HINDUPUR,T.TERAMOTO,K.GOTTIPATI,            
JRNL        AUTH 2 R.PADMANABHAN,K.H.CHOI                                       
JRNL        TITL   DENGUE VIRUS NONSTRUCTURAL PROTEIN 5 (NS5) ASSEMBLES INTO A  
JRNL        TITL 2 DIMER WITH A UNIQUE METHYLTRANSFERASE AND POLYMERASE         
JRNL        TITL 3 INTERFACE.                                                   
JRNL        REF    PLOS PATHOG.                  V.  12 05451 2016              
JRNL        REFN                   ESSN 1553-7374                               
JRNL        PMID   26895240                                                     
JRNL        DOI    10.1371/JOURNAL.PPAT.1005451                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 149621                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.274                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.340                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2004                            
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 49.2211 -  8.6619    1.00    11032   154  0.1555 0.1750        
REMARK   3     2  8.6619 -  6.8812    1.00    10718   141  0.1927 0.2127        
REMARK   3     3  6.8812 -  6.0131    1.00    10603   147  0.2217 0.2599        
REMARK   3     4  6.0131 -  5.4641    1.00    10601   142  0.2399 0.3525        
REMARK   3     5  5.4641 -  5.0729    1.00    10524   143  0.2315 0.2412        
REMARK   3     6  5.0729 -  4.7741    1.00    10504   144  0.2317 0.2608        
REMARK   3     7  4.7741 -  4.5351    1.00    10553   144  0.2397 0.2947        
REMARK   3     8  4.5351 -  4.3378    1.00    10453   140  0.2490 0.2734        
REMARK   3     9  4.3378 -  4.1709    1.00    10490   143  0.2649 0.2936        
REMARK   3    10  4.1709 -  4.0271    1.00    10463   140  0.2869 0.3721        
REMARK   3    11  4.0271 -  3.9012    1.00    10416   144  0.3097 0.3056        
REMARK   3    12  3.9012 -  3.7897    1.00    10475   138  0.3293 0.3796        
REMARK   3    13  3.7897 -  3.6900    1.00    10419   140  0.3523 0.4366        
REMARK   3    14  3.6900 -  3.6000    1.00    10366   144  0.3652 0.3993        
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)     : 0.600            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.490           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 100.5                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.002          53947                                  
REMARK   3   ANGLE     :  0.478          73136                                  
REMARK   3   CHIRALITY :  0.021           7854                                  
REMARK   3   PLANARITY :  0.002           9440                                  
REMARK   3   DIHEDRAL  :  9.727          19771                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):-115.4143  62.2044  39.5627              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9142 T22:   1.0036                                     
REMARK   3      T33:   0.8998 T12:   0.0592                                     
REMARK   3      T13:  -0.0504 T23:  -0.0643                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3400 L22:   0.1380                                     
REMARK   3      L33:   0.1970 L12:  -0.0476                                     
REMARK   3      L13:  -0.0977 L23:   0.0636                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0488 S12:   0.0700 S13:  -0.0423                       
REMARK   3      S21:  -0.0699 S22:  -0.0656 S23:   0.0799                       
REMARK   3      S31:   0.0097 S32:  -0.0846 S33:   0.0177                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5CCV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211377.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978720                           
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000 2.3.7                     
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 149778                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 16.40                              
REMARK 200  R MERGE                    (I) : 0.33000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.90300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.5.6                                          
REMARK 200 STARTING MODEL: PDB ENTRIES 3P97 AND 4HHJ                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M SUCCINIC ACID (PH 7.0), 0.1 M      
REMARK 280  HEPES (PH 7.0), 1% PEG MONOMETHYLETHER 2000, VAPOR DIFFUSION,       
REMARK 280  SITTING DROP, TEMPERATURE 290K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      320.45533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      160.22767            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      160.22767            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      320.45533            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14           
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 9                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 73510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 10                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 74500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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: 11                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 74230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 12                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 73640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 13                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 74260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 14                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 79220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     ASN A   405                                                      
REMARK 465     ALA A   406                                                      
REMARK 465     ALA A   407                                                      
REMARK 465     MET A   408                                                      
REMARK 465     GLY A   409                                                      
REMARK 465     ALA A   410                                                      
REMARK 465     VAL A   411                                                      
REMARK 465     PHE A   412                                                      
REMARK 465     THR A   413                                                      
REMARK 465     GLU A   414                                                      
REMARK 465     GLU A   415                                                      
REMARK 465     ASN A   416                                                      
REMARK 465     GLN A   417                                                      
REMARK 465     TRP A   418                                                      
REMARK 465     ASP A   419                                                      
REMARK 465     MET A   454                                                      
REMARK 465     GLY A   455                                                      
REMARK 465     LYS A   456                                                      
REMARK 465     ARG A   457                                                      
REMARK 465     GLU A   458                                                      
REMARK 465     LYS A   459                                                      
REMARK 465     LYS A   460                                                      
REMARK 465     LEU A   461                                                      
REMARK 465     GLY A   462                                                      
REMARK 465     GLU A   463                                                      
REMARK 465     PHE A   464                                                      
REMARK 465     GLY A   465                                                      
REMARK 465     LYS A   466                                                      
REMARK 465     ALA A   467                                                      
REMARK 465     LYS A   468                                                      
REMARK 465     GLY A   469                                                      
REMARK 465     SER A   470                                                      
REMARK 465     ARG A   471                                                      
REMARK 465     ALA A   472                                                      
REMARK 465     ILE A   473                                                      
REMARK 465     TRP A   474                                                      
REMARK 465     TYR A   475                                                      
REMARK 465     MET A   476                                                      
REMARK 465     TRP A   477                                                      
REMARK 465     ALA A   901                                                      
REMARK 465     ALA A   902                                                      
REMARK 465     ALA A   903                                                      
REMARK 465     LEU A   904                                                      
REMARK 465     GLU A   905                                                      
REMARK 465     HIS A   906                                                      
REMARK 465     HIS A   907                                                      
REMARK 465     HIS A   908                                                      
REMARK 465     HIS A   909                                                      
REMARK 465     HIS A   910                                                      
REMARK 465     HIS A   911                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     THR B   313                                                      
REMARK 465     GLY B   314                                                      
REMARK 465     SER B   315                                                      
REMARK 465     ALA B   316                                                      
REMARK 465     SER B   317                                                      
REMARK 465     MET B   454                                                      
REMARK 465     GLY B   455                                                      
REMARK 465     LYS B   456                                                      
REMARK 465     ARG B   457                                                      
REMARK 465     GLU B   458                                                      
REMARK 465     LYS B   459                                                      
REMARK 465     LYS B   460                                                      
REMARK 465     LEU B   461                                                      
REMARK 465     GLY B   462                                                      
REMARK 465     GLU B   463                                                      
REMARK 465     PHE B   464                                                      
REMARK 465     GLY B   465                                                      
REMARK 465     LYS B   466                                                      
REMARK 465     ALA B   467                                                      
REMARK 465     LYS B   468                                                      
REMARK 465     GLY B   469                                                      
REMARK 465     SER B   885                                                      
REMARK 465     MET B   886                                                      
REMARK 465     LYS B   887                                                      
REMARK 465     ARG B   888                                                      
REMARK 465     PHE B   889                                                      
REMARK 465     ARG B   890                                                      
REMARK 465     LYS B   891                                                      
REMARK 465     GLU B   892                                                      
REMARK 465     GLU B   893                                                      
REMARK 465     GLU B   894                                                      
REMARK 465     SER B   895                                                      
REMARK 465     GLU B   896                                                      
REMARK 465     GLY B   897                                                      
REMARK 465     ALA B   898                                                      
REMARK 465     ILE B   899                                                      
REMARK 465     TRP B   900                                                      
REMARK 465     ALA B   901                                                      
REMARK 465     ALA B   902                                                      
REMARK 465     ALA B   903                                                      
REMARK 465     LEU B   904                                                      
REMARK 465     GLU B   905                                                      
REMARK 465     HIS B   906                                                      
REMARK 465     HIS B   907                                                      
REMARK 465     HIS B   908                                                      
REMARK 465     HIS B   909                                                      
REMARK 465     HIS B   910                                                      
REMARK 465     HIS B   911                                                      
REMARK 465     GLY C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     GLY C     6                                                      
REMARK 465     THR C   245                                                      
REMARK 465     HIS C   246                                                      
REMARK 465     ARG C   247                                                      
REMARK 465     GLY C   455                                                      
REMARK 465     LYS C   456                                                      
REMARK 465     ARG C   457                                                      
REMARK 465     GLU C   458                                                      
REMARK 465     LYS C   459                                                      
REMARK 465     LYS C   460                                                      
REMARK 465     LEU C   461                                                      
REMARK 465     GLY C   462                                                      
REMARK 465     GLU C   463                                                      
REMARK 465     PHE C   464                                                      
REMARK 465     GLY C   465                                                      
REMARK 465     LYS C   466                                                      
REMARK 465     ALA C   467                                                      
REMARK 465     LYS C   468                                                      
REMARK 465     GLY C   469                                                      
REMARK 465     SER C   470                                                      
REMARK 465     ARG C   471                                                      
REMARK 465     SER C   885                                                      
REMARK 465     MET C   886                                                      
REMARK 465     LYS C   887                                                      
REMARK 465     ARG C   888                                                      
REMARK 465     PHE C   889                                                      
REMARK 465     ARG C   890                                                      
REMARK 465     LYS C   891                                                      
REMARK 465     GLU C   892                                                      
REMARK 465     GLU C   893                                                      
REMARK 465     GLU C   894                                                      
REMARK 465     SER C   895                                                      
REMARK 465     GLU C   896                                                      
REMARK 465     GLY C   897                                                      
REMARK 465     ALA C   898                                                      
REMARK 465     ILE C   899                                                      
REMARK 465     TRP C   900                                                      
REMARK 465     ALA C   901                                                      
REMARK 465     ALA C   902                                                      
REMARK 465     ALA C   903                                                      
REMARK 465     LEU C   904                                                      
REMARK 465     GLU C   905                                                      
REMARK 465     HIS C   906                                                      
REMARK 465     HIS C   907                                                      
REMARK 465     HIS C   908                                                      
REMARK 465     HIS C   909                                                      
REMARK 465     HIS C   910                                                      
REMARK 465     HIS C   911                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     GLN D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     ALA D   407                                                      
REMARK 465     MET D   408                                                      
REMARK 465     GLY D   409                                                      
REMARK 465     ALA D   410                                                      
REMARK 465     VAL D   411                                                      
REMARK 465     PHE D   412                                                      
REMARK 465     THR D   413                                                      
REMARK 465     GLU D   414                                                      
REMARK 465     GLU D   415                                                      
REMARK 465     ASN D   416                                                      
REMARK 465     GLN D   417                                                      
REMARK 465     TRP D   418                                                      
REMARK 465     ASP D   419                                                      
REMARK 465     MET D   454                                                      
REMARK 465     GLY D   455                                                      
REMARK 465     LYS D   456                                                      
REMARK 465     ARG D   457                                                      
REMARK 465     GLU D   458                                                      
REMARK 465     LYS D   459                                                      
REMARK 465     LYS D   460                                                      
REMARK 465     LEU D   461                                                      
REMARK 465     GLY D   462                                                      
REMARK 465     GLU D   463                                                      
REMARK 465     PHE D   464                                                      
REMARK 465     GLY D   465                                                      
REMARK 465     LYS D   466                                                      
REMARK 465     ALA D   467                                                      
REMARK 465     LYS D   468                                                      
REMARK 465     GLY D   469                                                      
REMARK 465     SER D   470                                                      
REMARK 465     ARG D   471                                                      
REMARK 465     ALA D   472                                                      
REMARK 465     ILE D   473                                                      
REMARK 465     TRP D   474                                                      
REMARK 465     ARG D   798                                                      
REMARK 465     THR D   799                                                      
REMARK 465     THR D   800                                                      
REMARK 465     ALA D   898                                                      
REMARK 465     ILE D   899                                                      
REMARK 465     TRP D   900                                                      
REMARK 465     ALA D   901                                                      
REMARK 465     ALA D   902                                                      
REMARK 465     ALA D   903                                                      
REMARK 465     LEU D   904                                                      
REMARK 465     GLU D   905                                                      
REMARK 465     HIS D   906                                                      
REMARK 465     HIS D   907                                                      
REMARK 465     HIS D   908                                                      
REMARK 465     HIS D   909                                                      
REMARK 465     HIS D   910                                                      
REMARK 465     HIS D   911                                                      
REMARK 465     GLY E     1                                                      
REMARK 465     THR E     2                                                      
REMARK 465     GLY E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     GLN E     5                                                      
REMARK 465     GLY E     6                                                      
REMARK 465     GLY E   455                                                      
REMARK 465     LYS E   456                                                      
REMARK 465     ARG E   457                                                      
REMARK 465     GLU E   458                                                      
REMARK 465     LYS E   459                                                      
REMARK 465     LYS E   460                                                      
REMARK 465     LEU E   461                                                      
REMARK 465     GLY E   462                                                      
REMARK 465     GLU E   463                                                      
REMARK 465     PHE E   464                                                      
REMARK 465     GLY E   465                                                      
REMARK 465     LYS E   466                                                      
REMARK 465     ALA E   467                                                      
REMARK 465     LYS E   468                                                      
REMARK 465     GLY E   469                                                      
REMARK 465     SER E   470                                                      
REMARK 465     ARG E   471                                                      
REMARK 465     ALA E   472                                                      
REMARK 465     MET E   883                                                      
REMARK 465     PRO E   884                                                      
REMARK 465     SER E   885                                                      
REMARK 465     MET E   886                                                      
REMARK 465     LYS E   887                                                      
REMARK 465     ARG E   888                                                      
REMARK 465     PHE E   889                                                      
REMARK 465     ARG E   890                                                      
REMARK 465     LYS E   891                                                      
REMARK 465     GLU E   892                                                      
REMARK 465     GLU E   893                                                      
REMARK 465     GLU E   894                                                      
REMARK 465     SER E   895                                                      
REMARK 465     GLU E   896                                                      
REMARK 465     GLY E   897                                                      
REMARK 465     ALA E   898                                                      
REMARK 465     ILE E   899                                                      
REMARK 465     TRP E   900                                                      
REMARK 465     ALA E   901                                                      
REMARK 465     ALA E   902                                                      
REMARK 465     ALA E   903                                                      
REMARK 465     LEU E   904                                                      
REMARK 465     GLU E   905                                                      
REMARK 465     HIS E   906                                                      
REMARK 465     HIS E   907                                                      
REMARK 465     HIS E   908                                                      
REMARK 465     HIS E   909                                                      
REMARK 465     HIS E   910                                                      
REMARK 465     HIS E   911                                                      
REMARK 465     GLY F     1                                                      
REMARK 465     THR F     2                                                      
REMARK 465     GLY F     3                                                      
REMARK 465     SER F     4                                                      
REMARK 465     GLN F     5                                                      
REMARK 465     GLY F     6                                                      
REMARK 465     ASN F   405                                                      
REMARK 465     ALA F   406                                                      
REMARK 465     ALA F   407                                                      
REMARK 465     MET F   408                                                      
REMARK 465     GLY F   409                                                      
REMARK 465     ALA F   410                                                      
REMARK 465     VAL F   411                                                      
REMARK 465     PHE F   412                                                      
REMARK 465     THR F   413                                                      
REMARK 465     GLU F   414                                                      
REMARK 465     GLU F   415                                                      
REMARK 465     ASN F   416                                                      
REMARK 465     GLN F   417                                                      
REMARK 465     TRP F   418                                                      
REMARK 465     ASP F   419                                                      
REMARK 465     MET F   454                                                      
REMARK 465     GLY F   455                                                      
REMARK 465     LYS F   456                                                      
REMARK 465     ARG F   457                                                      
REMARK 465     GLU F   458                                                      
REMARK 465     LYS F   459                                                      
REMARK 465     LYS F   460                                                      
REMARK 465     LEU F   461                                                      
REMARK 465     GLY F   462                                                      
REMARK 465     GLU F   463                                                      
REMARK 465     PHE F   464                                                      
REMARK 465     GLY F   465                                                      
REMARK 465     LYS F   466                                                      
REMARK 465     ALA F   467                                                      
REMARK 465     LYS F   468                                                      
REMARK 465     GLY F   469                                                      
REMARK 465     SER F   470                                                      
REMARK 465     ARG F   471                                                      
REMARK 465     ALA F   472                                                      
REMARK 465     ILE F   473                                                      
REMARK 465     TRP F   474                                                      
REMARK 465     TYR F   475                                                      
REMARK 465     TRP F   900                                                      
REMARK 465     ALA F   901                                                      
REMARK 465     ALA F   902                                                      
REMARK 465     ALA F   903                                                      
REMARK 465     LEU F   904                                                      
REMARK 465     GLU F   905                                                      
REMARK 465     HIS F   906                                                      
REMARK 465     HIS F   907                                                      
REMARK 465     HIS F   908                                                      
REMARK 465     HIS F   909                                                      
REMARK 465     HIS F   910                                                      
REMARK 465     HIS F   911                                                      
REMARK 465     GLY G     1                                                      
REMARK 465     THR G     2                                                      
REMARK 465     GLY G     3                                                      
REMARK 465     SER G     4                                                      
REMARK 465     GLN G     5                                                      
REMARK 465     GLY G     6                                                      
REMARK 465     GLU G     7                                                      
REMARK 465     THR G     8                                                      
REMARK 465     LEU G     9                                                      
REMARK 465     ASN G   405                                                      
REMARK 465     ALA G   406                                                      
REMARK 465     ALA G   407                                                      
REMARK 465     MET G   408                                                      
REMARK 465     GLY G   409                                                      
REMARK 465     ALA G   410                                                      
REMARK 465     VAL G   411                                                      
REMARK 465     PHE G   412                                                      
REMARK 465     THR G   413                                                      
REMARK 465     GLU G   414                                                      
REMARK 465     GLU G   415                                                      
REMARK 465     ASN G   416                                                      
REMARK 465     GLN G   417                                                      
REMARK 465     TRP G   418                                                      
REMARK 465     ASP G   419                                                      
REMARK 465     MET G   454                                                      
REMARK 465     GLY G   455                                                      
REMARK 465     LYS G   456                                                      
REMARK 465     ARG G   457                                                      
REMARK 465     GLU G   458                                                      
REMARK 465     LYS G   459                                                      
REMARK 465     LYS G   460                                                      
REMARK 465     LEU G   461                                                      
REMARK 465     GLY G   462                                                      
REMARK 465     GLU G   463                                                      
REMARK 465     PHE G   464                                                      
REMARK 465     GLY G   465                                                      
REMARK 465     LYS G   466                                                      
REMARK 465     ALA G   467                                                      
REMARK 465     LYS G   468                                                      
REMARK 465     GLY G   469                                                      
REMARK 465     SER G   470                                                      
REMARK 465     ARG G   471                                                      
REMARK 465     ALA G   472                                                      
REMARK 465     ILE G   473                                                      
REMARK 465     TRP G   474                                                      
REMARK 465     TYR G   475                                                      
REMARK 465     TRP G   900                                                      
REMARK 465     ALA G   901                                                      
REMARK 465     ALA G   902                                                      
REMARK 465     ALA G   903                                                      
REMARK 465     LEU G   904                                                      
REMARK 465     GLU G   905                                                      
REMARK 465     HIS G   906                                                      
REMARK 465     HIS G   907                                                      
REMARK 465     HIS G   908                                                      
REMARK 465     HIS G   909                                                      
REMARK 465     HIS G   910                                                      
REMARK 465     HIS G   911                                                      
REMARK 465     GLY H     1                                                      
REMARK 465     THR H     2                                                      
REMARK 465     GLY H     3                                                      
REMARK 465     SER H     4                                                      
REMARK 465     GLN H     5                                                      
REMARK 465     GLY H     6                                                      
REMARK 465     GLU H     7                                                      
REMARK 465     GLY H   148                                                      
REMARK 465     GLU H   149                                                      
REMARK 465     SER H   150                                                      
REMARK 465     GLY H   223                                                      
REMARK 465     THR H   224                                                      
REMARK 465     GLY H   225                                                      
REMARK 465     LYS H   311                                                      
REMARK 465     ALA H   312                                                      
REMARK 465     THR H   313                                                      
REMARK 465     GLY H   314                                                      
REMARK 465     SER H   315                                                      
REMARK 465     ALA H   316                                                      
REMARK 465     SER H   317                                                      
REMARK 465     SER H   318                                                      
REMARK 465     MET H   319                                                      
REMARK 465     ILE H   320                                                      
REMARK 465     MET H   340                                                      
REMARK 465     ALA H   341                                                      
REMARK 465     MET H   342                                                      
REMARK 465     THR H   343                                                      
REMARK 465     ASP H   344                                                      
REMARK 465     ARG H   403                                                      
REMARK 465     THR H   404                                                      
REMARK 465     ASN H   405                                                      
REMARK 465     ALA H   406                                                      
REMARK 465     ALA H   407                                                      
REMARK 465     MET H   408                                                      
REMARK 465     GLY H   409                                                      
REMARK 465     ALA H   410                                                      
REMARK 465     VAL H   411                                                      
REMARK 465     PHE H   412                                                      
REMARK 465     THR H   413                                                      
REMARK 465     GLU H   414                                                      
REMARK 465     GLU H   415                                                      
REMARK 465     ASN H   416                                                      
REMARK 465     GLN H   417                                                      
REMARK 465     TRP H   418                                                      
REMARK 465     ASP H   419                                                      
REMARK 465     VAL H   450                                                      
REMARK 465     TYR H   451                                                      
REMARK 465     ASN H   452                                                      
REMARK 465     MET H   453                                                      
REMARK 465     MET H   454                                                      
REMARK 465     GLY H   455                                                      
REMARK 465     LYS H   456                                                      
REMARK 465     ARG H   457                                                      
REMARK 465     GLU H   458                                                      
REMARK 465     LYS H   459                                                      
REMARK 465     LYS H   460                                                      
REMARK 465     LEU H   461                                                      
REMARK 465     GLY H   462                                                      
REMARK 465     GLU H   463                                                      
REMARK 465     PHE H   464                                                      
REMARK 465     GLY H   465                                                      
REMARK 465     LYS H   466                                                      
REMARK 465     ALA H   467                                                      
REMARK 465     LYS H   468                                                      
REMARK 465     GLY H   469                                                      
REMARK 465     SER H   470                                                      
REMARK 465     ARG H   471                                                      
REMARK 465     ALA H   472                                                      
REMARK 465     ILE H   473                                                      
REMARK 465     TRP H   474                                                      
REMARK 465     TYR H   475                                                      
REMARK 465     MET H   476                                                      
REMARK 465     TRP H   477                                                      
REMARK 465     LEU H   478                                                      
REMARK 465     GLN H   555                                                      
REMARK 465     MET H   556                                                      
REMARK 465     ALA H   738                                                      
REMARK 465     ARG H   739                                                      
REMARK 465     ILE H   740                                                      
REMARK 465     SER H   741                                                      
REMARK 465     GLN H   742                                                      
REMARK 465     GLY H   743                                                      
REMARK 465     ALA H   744                                                      
REMARK 465     GLY H   745                                                      
REMARK 465     VAL H   789                                                      
REMARK 465     PRO H   790                                                      
REMARK 465     VAL H   791                                                      
REMARK 465     HIS H   792                                                      
REMARK 465     TRP H   793                                                      
REMARK 465     VAL H   794                                                      
REMARK 465     PRO H   795                                                      
REMARK 465     THR H   796                                                      
REMARK 465     SER H   797                                                      
REMARK 465     ARG H   798                                                      
REMARK 465     THR H   799                                                      
REMARK 465     THR H   800                                                      
REMARK 465     HIS H   801                                                      
REMARK 465     GLN H   802                                                      
REMARK 465     TRP H   803                                                      
REMARK 465     MET H   804                                                      
REMARK 465     ILE H   874                                                      
REMARK 465     GLY H   875                                                      
REMARK 465     ASN H   876                                                      
REMARK 465     GLU H   877                                                      
REMARK 465     GLU H   878                                                      
REMARK 465     PHE H   879                                                      
REMARK 465     LEU H   880                                                      
REMARK 465     ASP H   881                                                      
REMARK 465     TYR H   882                                                      
REMARK 465     MET H   883                                                      
REMARK 465     PRO H   884                                                      
REMARK 465     SER H   885                                                      
REMARK 465     MET H   886                                                      
REMARK 465     LYS H   887                                                      
REMARK 465     ARG H   888                                                      
REMARK 465     PHE H   889                                                      
REMARK 465     ARG H   890                                                      
REMARK 465     LYS H   891                                                      
REMARK 465     GLU H   892                                                      
REMARK 465     GLU H   893                                                      
REMARK 465     GLU H   894                                                      
REMARK 465     SER H   895                                                      
REMARK 465     GLU H   896                                                      
REMARK 465     GLY H   897                                                      
REMARK 465     ALA H   898                                                      
REMARK 465     ILE H   899                                                      
REMARK 465     TRP H   900                                                      
REMARK 465     ALA H   901                                                      
REMARK 465     ALA H   902                                                      
REMARK 465     ALA H   903                                                      
REMARK 465     LEU H   904                                                      
REMARK 465     GLU H   905                                                      
REMARK 465     HIS H   906                                                      
REMARK 465     HIS H   907                                                      
REMARK 465     HIS H   908                                                      
REMARK 465     HIS H   909                                                      
REMARK 465     HIS H   910                                                      
REMARK 465     HIS H   911                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 890    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 891    CG   CD   CE   NZ                                   
REMARK 470     GLU A 892    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 893    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 894    CG   CD   OE1  OE2                                  
REMARK 470     SER A 895    OG                                                  
REMARK 470     TRP A 900    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 900    CZ3  CH2                                            
REMARK 470     GLU C  24    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 887    CG   CD   CE   NZ                                   
REMARK 470     ARG D 888    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 891    CG   CD   CE   NZ                                   
REMARK 470     GLU D 892    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 893    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 894    CG   CD   OE1  OE2                                  
REMARK 470     SER D 895    OG                                                  
REMARK 470     GLU D 896    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 481    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG F 888    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 891    CG   CD   CE   NZ                                   
REMARK 470     GLU F 892    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 893    CG   CD   OE1  OE2                                  
REMARK 470     GLU F 896    CG   CD   OE1  OE2                                  
REMARK 470     ILE F 899    CG1  CG2  CD1                                       
REMARK 470     ARG G 422    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G 888    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG G 890    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS G 891    CG   CD   CE   NZ                                   
REMARK 470     GLU G 893    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 894    CG   CD   OE1  OE2                                  
REMARK 470     SER G 895    OG                                                  
REMARK 470     ILE G 899    CG1  CG2  CD1                                       
REMARK 470     GLU H  11    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  12    CG   CD   CE   NZ                                   
REMARK 470     TRP H  13    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H  13    CZ3  CH2                                            
REMARK 470     LYS H  14    CG   CD   CE   NZ                                   
REMARK 470     LYS H  15    CG   CD   CE   NZ                                   
REMARK 470     LYS H  16    CG   CD   CE   NZ                                   
REMARK 470     LEU H  17    CG   CD1  CD2                                       
REMARK 470     GLN H  19    CG   CD   OE1  NE2                                  
REMARK 470     LEU H  20    CG   CD1  CD2                                       
REMARK 470     SER H  21    OG                                                  
REMARK 470     ARG H  22    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H  23    CG   CD   CE   NZ                                   
REMARK 470     GLU H  24    CG   CD   OE1  OE2                                  
REMARK 470     PHE H  25    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP H  26    CG   OD1  OD2                                       
REMARK 470     LEU H  27    CG   CD1  CD2                                       
REMARK 470     TYR H  28    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS H  29    CG   CD   CE   NZ                                   
REMARK 470     LYS H  30    CG   CD   CE   NZ                                   
REMARK 470     SER H  31    OG                                                  
REMARK 470     ILE H  33    CG1  CG2  CD1                                       
REMARK 470     THR H  34    OG1  CG2                                            
REMARK 470     GLU H  35    CG   CD   OE1  OE2                                  
REMARK 470     VAL H  36    CG1  CG2                                            
REMARK 470     ASP H  37    CG   OD1  OD2                                       
REMARK 470     THR H  39    OG1  CG2                                            
REMARK 470     GLU H  40    CG   CD   OE1  OE2                                  
REMARK 470     LYS H  42    CG   CD   CE   NZ                                   
REMARK 470     GLU H  43    CG   CD   OE1  OE2                                  
REMARK 470     LEU H  45    CG   CD1  CD2                                       
REMARK 470     LYS H  46    CG   CD   CE   NZ                                   
REMARK 470     ARG H  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE H  50    CG1  CG2  CD1                                       
REMARK 470     THR H  51    OG1  CG2                                            
REMARK 470     HIS H  52    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS H  53    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL H  55    CG1  CG2                                            
REMARK 470     SER H  56    OG                                                  
REMARK 470     ARG H  57    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER H  59    OG                                                  
REMARK 470     LYS H  61    CG   CD   CE   NZ                                   
REMARK 470     LEU H  62    CG   CD1  CD2                                       
REMARK 470     GLN H  63    CG   CD   OE1  NE2                                  
REMARK 470     TRP H  64    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H  64    CZ3  CH2                                            
REMARK 470     PHE H  65    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL H  66    CG1  CG2                                            
REMARK 470     GLU H  67    CG   CD   OE1  OE2                                  
REMARK 470     ARG H  68    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN H  69    CG   OD1  ND2                                       
REMARK 470     MET H  70    CG   SD   CE                                        
REMARK 470     VAL H  71    CG1  CG2                                            
REMARK 470     ILE H  72    CG1  CG2  CD1                                       
REMARK 470     GLU H  74    CG   CD   OE1  OE2                                  
REMARK 470     ARG H  76    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL H  77    CG1  CG2                                            
REMARK 470     ILE H  78    CG1  CG2  CD1                                       
REMARK 470     ASP H  79    CG   OD1  OD2                                       
REMARK 470     CYS H  82    SG                                                  
REMARK 470     ARG H  84    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP H  87    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H  87    CZ3  CH2                                            
REMARK 470     SER H  88    OG                                                  
REMARK 470     TYR H  89    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR H  90    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     CYS H  91    SG                                                  
REMARK 470     LEU H  94    CG   CD1  CD2                                       
REMARK 470     LYS H  95    CG   CD   CE   NZ                                   
REMARK 470     LYS H  96    CG   CD   CE   NZ                                   
REMARK 470     VAL H  97    CG1  CG2                                            
REMARK 470     THR H  98    OG1  CG2                                            
REMARK 470     VAL H 100    CG1  CG2                                            
REMARK 470     ARG H 101    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR H 104    OG1  CG2                                            
REMARK 470     LYS H 105    CG   CD   CE   NZ                                   
REMARK 470     HIS H 110    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU H 111    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 112    CG   CD   OE1  OE2                                  
REMARK 470     VAL H 114    CG1  CG2                                            
REMARK 470     SER H 117    OG                                                  
REMARK 470     THR H 118    OG1  CG2                                            
REMARK 470     TYR H 119    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN H 122    CG   OD1  ND2                                       
REMARK 470     ILE H 123    CG1  CG2  CD1                                       
REMARK 470     VAL H 124    CG1  CG2                                            
REMARK 470     LYS H 125    CG   CD   CE   NZ                                   
REMARK 470     LEU H 126    CG   CD1  CD2                                       
REMARK 470     MET H 127    CG   SD   CE                                        
REMARK 470     SER H 128    OG                                                  
REMARK 470     LYS H 130    CG   CD   CE   NZ                                   
REMARK 470     VAL H 132    CG1  CG2                                            
REMARK 470     PHE H 133    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TYR H 134    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU H 135    CG   CD1  CD2                                       
REMARK 470     GLU H 138    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 139    CG   CD   CE   NZ                                   
REMARK 470     CYS H 140    SG                                                  
REMARK 470     ASP H 141    CG   OD1  OD2                                       
REMARK 470     THR H 142    OG1  CG2                                            
REMARK 470     LEU H 143    CG   CD1  CD2                                       
REMARK 470     LEU H 144    CG   CD1  CD2                                       
REMARK 470     ILE H 147    CG1  CG2  CD1                                       
REMARK 470     SER H 151    OG                                                  
REMARK 470     SER H 153    OG                                                  
REMARK 470     VAL H 156    CG1  CG2                                            
REMARK 470     GLU H 157    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 158    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 160    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG H 163    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU H 165    CG   CD1  CD2                                       
REMARK 470     LYS H 166    CG   CD   CE   NZ                                   
REMARK 470     MET H 167    CG   SD   CE                                        
REMARK 470     GLU H 169    CG   CD   OE1  OE2                                  
REMARK 470     TRP H 171    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 171    CZ3  CH2                                            
REMARK 470     LEU H 172    CG   CD1  CD2                                       
REMARK 470     LYS H 173    CG   CD   CE   NZ                                   
REMARK 470     ASN H 175    CG   OD1  ND2                                       
REMARK 470     PHE H 177    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     CYS H 178    SG                                                  
REMARK 470     ILE H 179    CG1  CG2  CD1                                       
REMARK 470     LYS H 180    CG   CD   CE   NZ                                   
REMARK 470     VAL H 181    CG1  CG2                                            
REMARK 470     LEU H 182    CG   CD1  CD2                                       
REMARK 470     ASN H 183    CG   OD1  ND2                                       
REMARK 470     TYR H 185    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET H 186    CG   SD   CE                                        
REMARK 470     ILE H 190    CG1  CG2  CD1                                       
REMARK 470     GLU H 191    CG   CD   OE1  OE2                                  
REMARK 470     HIS H 192    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU H 193    CG   CD1  CD2                                       
REMARK 470     GLU H 194    CG   CD   OE1  OE2                                  
REMARK 470     LEU H 196    CG   CD1  CD2                                       
REMARK 470     GLN H 197    CG   CD   OE1  NE2                                  
REMARK 470     HIS H 200    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET H 203    CG   SD   CE                                        
REMARK 470     LEU H 204    CG   CD1  CD2                                       
REMARK 470     ARG H 206    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU H 209    CG   CD1  CD2                                       
REMARK 470     ARG H 211    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN H 212    CG   OD1  ND2                                       
REMARK 470     SER H 213    OG                                                  
REMARK 470     THR H 214    OG1  CG2                                            
REMARK 470     HIS H 215    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLU H 216    CG   CD   OE1  OE2                                  
REMARK 470     MET H 217    CG   SD   CE                                        
REMARK 470     TYR H 218    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE H 220    CG1  CG2  CD1                                       
REMARK 470     ASN H 222    CG   OD1  ND2                                       
REMARK 470     ASN H 226    CG   OD1  ND2                                       
REMARK 470     ILE H 227    CG1  CG2  CD1                                       
REMARK 470     SER H 230    OG                                                  
REMARK 470     ASN H 232    CG   OD1  ND2                                       
REMARK 470     MET H 233    CG   SD   CE                                        
REMARK 470     VAL H 234    CG1  CG2                                            
REMARK 470     ARG H 236    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU H 237    CG   CD1  CD2                                       
REMARK 470     LEU H 238    CG   CD1  CD2                                       
REMARK 470     LEU H 239    CG   CD1  CD2                                       
REMARK 470     ARG H 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR H 243    OG1  CG2                                            
REMARK 470     MET H 244    CG   SD   CE                                        
REMARK 470     THR H 245    OG1  CG2                                            
REMARK 470     HIS H 246    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG H 247    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H 252    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 254    CG   OD1  OD2                                       
REMARK 470     LEU H 257    CG   CD1  CD2                                       
REMARK 470     THR H 261    OG1  CG2                                            
REMARK 470     ARG H 262    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H 267    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 269    CG   CD   OE1  OE2                                  
REMARK 470     ASN H 272    CG   OD1  ND2                                       
REMARK 470     MET H 273    CG   SD   CE                                        
REMARK 470     ASP H 274    CG   OD1  OD2                                       
REMARK 470     VAL H 275    CG1  CG2                                            
REMARK 470     ILE H 276    CG1  CG2  CD1                                       
REMARK 470     GLU H 278    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 279    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE H 280    CG1  CG2  CD1                                       
REMARK 470     LYS H 281    CG   CD   CE   NZ                                   
REMARK 470     ARG H 282    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE H 283    CG1  CG2  CD1                                       
REMARK 470     LYS H 284    CG   CD   CE   NZ                                   
REMARK 470     GLU H 285    CG   CD   OE1  OE2                                  
REMARK 470     SER H 288    OG                                                  
REMARK 470     SER H 289    OG                                                  
REMARK 470     HIS H 292    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR H 293    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASN H 297    CG   OD1  ND2                                       
REMARK 470     TYR H 299    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS H 300    CG   CD   CE   NZ                                   
REMARK 470     THR H 301    OG1  CG2                                            
REMARK 470     TYR H 304    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     HIS H 305    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER H 307    OG                                                  
REMARK 470     TYR H 308    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL H 310    CG1  CG2                                            
REMARK 470     ASN H 321    CG   OD1  ND2                                       
REMARK 470     VAL H 324    CG1  CG2                                            
REMARK 470     LYS H 325    CG   CD   CE   NZ                                   
REMARK 470     LEU H 326    CG   CD1  CD2                                       
REMARK 470     LEU H 327    CG   CD1  CD2                                       
REMARK 470     THR H 328    OG1  CG2                                            
REMARK 470     LYS H 329    CG   CD   CE   NZ                                   
REMARK 470     ASP H 332    CG   OD1  OD2                                       
REMARK 470     VAL H 333    CG1  CG2                                            
REMARK 470     VAL H 334    CG1  CG2                                            
REMARK 470     MET H 336    CG   SD   CE                                        
REMARK 470     GLN H 339    CG   CD   OE1  NE2                                  
REMARK 470     GLN H 350    CG   CD   OE1  NE2                                  
REMARK 470     GLN H 351    CG   CD   OE1  NE2                                  
REMARK 470     ARG H 352    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL H 353    CG1  CG2                                            
REMARK 470     PHE H 354    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS H 355    CG   CD   CE   NZ                                   
REMARK 470     GLU H 356    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 357    CG   CD   CE   NZ                                   
REMARK 470     VAL H 358    CG1  CG2                                            
REMARK 470     ASP H 359    CG   OD1  OD2                                       
REMARK 470     THR H 360    OG1  CG2                                            
REMARK 470     ARG H 361    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR H 362    OG1  CG2                                            
REMARK 470     ARG H 364    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET H 366    CG   SD   CE                                        
REMARK 470     THR H 369    OG1  CG2                                            
REMARK 470     LYS H 371    CG   CD   CE   NZ                                   
REMARK 470     VAL H 372    CG1  CG2                                            
REMARK 470     MET H 373    CG   SD   CE                                        
REMARK 470     GLU H 374    CG   CD   OE1  OE2                                  
REMARK 470     ILE H 375    CG1  CG2  CD1                                       
REMARK 470     THR H 376    OG1  CG2                                            
REMARK 470     GLU H 378    CG   CD   OE1  OE2                                  
REMARK 470     LEU H 380    CG   CD1  CD2                                       
REMARK 470     THR H 383    OG1  CG2                                            
REMARK 470     LEU H 384    CG   CD1  CD2                                       
REMARK 470     ARG H 386    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H 388    CG   CD   CE   NZ                                   
REMARK 470     ARG H 389    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG H 391    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU H 392    CG   CD1  CD2                                       
REMARK 470     CYS H 393    SG                                                  
REMARK 470     THR H 394    OG1  CG2                                            
REMARK 470     GLU H 396    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 397    CG   CD   OE1  OE2                                  
REMARK 470     PHE H 398    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR H 399    OG1  CG2                                            
REMARK 470     LYS H 400    CG   CD   CE   NZ                                   
REMARK 470     LYS H 401    CG   CD   CE   NZ                                   
REMARK 470     VAL H 402    CG1  CG2                                            
REMARK 470     SER H 420    OG                                                  
REMARK 470     ARG H 422    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL H 425    CG1  CG2                                            
REMARK 470     GLU H 426    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 428    CG   CD   OE1  OE2                                  
REMARK 470     PHE H 430    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS H 432    CG   CD   CE   NZ                                   
REMARK 470     LEU H 433    CG   CD1  CD2                                       
REMARK 470     VAL H 434    CG1  CG2                                            
REMARK 470     ASP H 435    CG   OD1  OD2                                       
REMARK 470     ARG H 436    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H 439    CG   CD   OE1  OE2                                  
REMARK 470     LEU H 440    CG   CD1  CD2                                       
REMARK 470     LEU H 443    CG   CD1  CD2                                       
REMARK 470     LYS H 445    CG   CD   CE   NZ                                   
REMARK 470     SER H 448    OG                                                  
REMARK 470     ARG H 481    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR H 482    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU H 483    CG   CD1  CD2                                       
REMARK 470     GLU H 484    CG   CD   OE1  OE2                                  
REMARK 470     PHE H 485    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU H 486    CG   CD   OE1  OE2                                  
REMARK 470     LEU H 488    CG   CD1  CD2                                       
REMARK 470     LEU H 491    CG   CD1  CD2                                       
REMARK 470     ASN H 492    CG   OD1  ND2                                       
REMARK 470     TRP H 496    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 496    CZ3  CH2                                            
REMARK 470     SER H 498    OG                                                  
REMARK 470     ARG H 499    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN H 501    CG   OD1  ND2                                       
REMARK 470     SER H 502    OG                                                  
REMARK 470     TYR H 503    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER H 504    OG                                                  
REMARK 470     VAL H 506    CG1  CG2                                            
REMARK 470     GLU H 507    CG   CD   OE1  OE2                                  
REMARK 470     LEU H 511    CG   CD1  CD2                                       
REMARK 470     HIS H 512    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS H 513    CG   CD   CE   NZ                                   
REMARK 470     LEU H 514    CG   CD1  CD2                                       
REMARK 470     TYR H 516    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE H 517    CG1  CG2  CD1                                       
REMARK 470     ARG H 519    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP H 520    CG   OD1  OD2                                       
REMARK 470     ILE H 521    CG1  CG2  CD1                                       
REMARK 470     SER H 522    OG                                                  
REMARK 470     LYS H 523    CG   CD   CE   NZ                                   
REMARK 470     ILE H 524    CG1  CG2  CD1                                       
REMARK 470     MET H 529    CG   SD   CE                                        
REMARK 470     ASP H 532    CG   OD1  OD2                                       
REMARK 470     ASP H 533    CG   OD1  OD2                                       
REMARK 470     THR H 534    OG1  CG2                                            
REMARK 470     ASP H 538    CG   OD1  OD2                                       
REMARK 470     ARG H 540    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE H 541    CG1  CG2  CD1                                       
REMARK 470     THR H 542    OG1  CG2                                            
REMARK 470     GLU H 543    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 544    CG   OD1  OD2                                       
REMARK 470     ASP H 545    CG   OD1  OD2                                       
REMARK 470     LEU H 546    CG   CD1  CD2                                       
REMARK 470     ASN H 548    CG   OD1  ND2                                       
REMARK 470     GLU H 549    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 551    CG   CD   CE   NZ                                   
REMARK 470     ILE H 552    CG1  CG2  CD1                                       
REMARK 470     THR H 553    OG1  CG2                                            
REMARK 470     ASP H 557    CG   OD1  OD2                                       
REMARK 470     GLU H 559    CG   CD   OE1  OE2                                  
REMARK 470     ARG H 561    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN H 562    CG   CD   OE1  NE2                                  
REMARK 470     LEU H 563    CG   CD1  CD2                                       
REMARK 470     ILE H 567    CG1  CG2  CD1                                       
REMARK 470     PHE H 568    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS H 569    CG   CD   CE   NZ                                   
REMARK 470     LEU H 570    CG   CD1  CD2                                       
REMARK 470     THR H 571    OG1  CG2                                            
REMARK 470     TYR H 572    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN H 573    CG   CD   OE1  NE2                                  
REMARK 470     LYS H 575    CG   CD   CE   NZ                                   
REMARK 470     VAL H 576    CG1  CG2                                            
REMARK 470     VAL H 577    CG1  CG2                                            
REMARK 470     LYS H 578    CG   CD   CE   NZ                                   
REMARK 470     VAL H 579    CG1  CG2                                            
REMARK 470     GLN H 580    CG   CD   OE1  NE2                                  
REMARK 470     ARG H 581    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR H 583    OG1  CG2                                            
REMARK 470     LYS H 585    CG   CD   CE   NZ                                   
REMARK 470     THR H 587    OG1  CG2                                            
REMARK 470     VAL H 588    CG1  CG2                                            
REMARK 470     MET H 589    CG   SD   CE                                        
REMARK 470     ASP H 590    CG   OD1  OD2                                       
REMARK 470     ILE H 591    CG1  CG2  CD1                                       
REMARK 470     ILE H 592    CG1  CG2  CD1                                       
REMARK 470     SER H 593    OG                                                  
REMARK 470     ARG H 594    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H 595    CG   CD   CE   NZ                                   
REMARK 470     ASP H 596    CG   OD1  OD2                                       
REMARK 470     GLN H 597    CG   CD   OE1  NE2                                  
REMARK 470     SER H 600    OG                                                  
REMARK 470     GLN H 602    CG   CD   OE1  NE2                                  
REMARK 470     VAL H 603    CG1  CG2                                            
REMARK 470     THR H 605    OG1  CG2                                            
REMARK 470     THR H 610    OG1  CG2                                            
REMARK 470     PHE H 611    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR H 612    OG1  CG2                                            
REMARK 470     ASN H 613    CG   OD1  ND2                                       
REMARK 470     MET H 614    CG   SD   CE                                        
REMARK 470     GLU H 615    CG   CD   OE1  OE2                                  
REMARK 470     GLN H 617    CG   CD   OE1  NE2                                  
REMARK 470     LEU H 618    CG   CD1  CD2                                       
REMARK 470     ILE H 619    CG1  CG2  CD1                                       
REMARK 470     ARG H 620    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET H 622    CG   SD   CE                                        
REMARK 470     GLU H 623    CG   CD   OE1  OE2                                  
REMARK 470     VAL H 627    CG1  CG2                                            
REMARK 470     LEU H 628    CG   CD1  CD2                                       
REMARK 470     SER H 629    OG                                                  
REMARK 470     LYS H 630    CG   CD   CE   NZ                                   
REMARK 470     LEU H 633    CG   CD1  CD2                                       
REMARK 470     GLU H 634    CG   CD   OE1  OE2                                  
REMARK 470     ASN H 635    CG   OD1  ND2                                       
REMARK 470     HIS H 637    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU H 639    CG   CD1  CD2                                       
REMARK 470     GLU H 640    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 641    CG   CD   CE   NZ                                   
REMARK 470     LYS H 642    CG   CD   CE   NZ                                   
REMARK 470     ILE H 643    CG1  CG2  CD1                                       
REMARK 470     GLN H 645    CG   CD   OE1  NE2                                  
REMARK 470     GLU H 648    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 650    CG   CD   CE   NZ                                   
REMARK 470     LEU H 655    CG   CD1  CD2                                       
REMARK 470     LYS H 656    CG   CD   CE   NZ                                   
REMARK 470     ILE H 660    CG1  CG2  CD1                                       
REMARK 470     ASP H 664    CG   OD1  OD2                                       
REMARK 470     CYS H 665    SG                                                  
REMARK 470     VAL H 667    CG1  CG2                                            
REMARK 470     LYS H 668    CG   CD   CE   NZ                                   
REMARK 470     ILE H 670    CG1  CG2  CD1                                       
REMARK 470     LEU H 679    CG   CD1  CD2                                       
REMARK 470     LEU H 681    CG   CD1  CD2                                       
REMARK 470     ASN H 682    CG   OD1  ND2                                       
REMARK 470     LYS H 686    CG   CD   CE   NZ                                   
REMARK 470     VAL H 687    CG1  CG2                                            
REMARK 470     LYS H 689    CG   CD   CE   NZ                                   
REMARK 470     ASP H 690    CG   OD1  OD2                                       
REMARK 470     ILE H 691    CG1  CG2  CD1                                       
REMARK 470     GLN H 693    CG   CD   OE1  NE2                                  
REMARK 470     GLN H 695    CG   CD   OE1  NE2                                  
REMARK 470     SER H 697    OG                                                  
REMARK 470     LYS H 698    CG   CD   CE   NZ                                   
REMARK 470     GLN H 705    CG   CD   OE1  NE2                                  
REMARK 470     CYS H 709    SG                                                  
REMARK 470     SER H 710    OG                                                  
REMARK 470     PHE H 713    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU H 716    CG   CD1  CD2                                       
REMARK 470     ILE H 717    CG1  CG2  CD1                                       
REMARK 470     MET H 718    CG   SD   CE                                        
REMARK 470     LYS H 719    CG   CD   CE   NZ                                   
REMARK 470     ARG H 722    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H 723    CG   CD   CE   NZ                                   
REMARK 470     LEU H 724    CG   CD1  CD2                                       
REMARK 470     VAL H 725    CG1  CG2                                            
REMARK 470     GLN H 731    CG   CD   OE1  NE2                                  
REMARK 470     ASP H 732    CG   OD1  OD2                                       
REMARK 470     GLU H 733    CG   CD   OE1  OE2                                  
REMARK 470     LEU H 734    CG   CD1  CD2                                       
REMARK 470     ILE H 735    CG1  CG2  CD1                                       
REMARK 470     ARG H 737    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER H 747    OG                                                  
REMARK 470     GLU H 750    CG   CD   OE1  OE2                                  
REMARK 470     THR H 751    OG1  CG2                                            
REMARK 470     LEU H 754    CG   CD1  CD2                                       
REMARK 470     LYS H 756    CG   CD   CE   NZ                                   
REMARK 470     TYR H 758    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN H 760    CG   CD   OE1  NE2                                  
REMARK 470     MET H 761    CG   SD   CE                                        
REMARK 470     TRP H 762    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 762    CZ3  CH2                                            
REMARK 470     LEU H 764    CG   CD1  CD2                                       
REMARK 470     MET H 765    CG   SD   CE                                        
REMARK 470     HIS H 768    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG H 769    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG H 770    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU H 772    CG   CD1  CD2                                       
REMARK 470     ARG H 773    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU H 774    CG   CD1  CD2                                       
REMARK 470     SER H 776    OG                                                  
REMARK 470     ILE H 779    CG1  CG2  CD1                                       
REMARK 470     CYS H 780    SG                                                  
REMARK 470     THR H 805    N    OG1  CG2                                       
REMARK 470     THR H 806    OG1  CG2                                            
REMARK 470     GLU H 807    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 808    CG   OD1  OD2                                       
REMARK 470     MET H 809    CG   SD   CE                                        
REMARK 470     VAL H 812    CG1  CG2                                            
REMARK 470     TRP H 813    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 813    CZ3  CH2                                            
REMARK 470     ASN H 814    CG   OD1  ND2                                       
REMARK 470     ARG H 815    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL H 816    CG1  CG2                                            
REMARK 470     TRP H 817    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 817    CZ3  CH2                                            
REMARK 470     ILE H 818    CG1  CG2  CD1                                       
REMARK 470     GLU H 819    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 820    CG   OD1  OD2                                       
REMARK 470     ASN H 821    CG   OD1  ND2                                       
REMARK 470     MET H 824    CG   SD   CE                                        
REMARK 470     GLU H 825    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 826    CG   OD1  OD2                                       
REMARK 470     LYS H 827    CG   CD   CE   NZ                                   
REMARK 470     VAL H 830    CG1  CG2                                            
REMARK 470     THR H 831    OG1  CG2                                            
REMARK 470     THR H 832    OG1  CG2                                            
REMARK 470     TRP H 833    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 833    CZ3  CH2                                            
REMARK 470     GLU H 834    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 835    CG   OD1  OD2                                       
REMARK 470     VAL H 836    CG1  CG2                                            
REMARK 470     TYR H 838    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU H 839    CG   CD1  CD2                                       
REMARK 470     LYS H 841    CG   CD   CE   NZ                                   
REMARK 470     GLU H 843    CG   CD   OE1  OE2                                  
REMARK 470     ASP H 844    CG   OD1  OD2                                       
REMARK 470     GLN H 845    CG   CD   OE1  NE2                                  
REMARK 470     TRP H 846    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 846    CZ3  CH2                                            
REMARK 470     SER H 849    OG                                                  
REMARK 470     LEU H 850    CG   CD1  CD2                                       
REMARK 470     ILE H 851    CG1  CG2  CD1                                       
REMARK 470     LEU H 853    CG   CD1  CD2                                       
REMARK 470     THR H 854    OG1  CG2                                            
REMARK 470     SER H 855    OG                                                  
REMARK 470     ARG H 856    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR H 858    OG1  CG2                                            
REMARK 470     TRP H 859    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 859    CZ3  CH2                                            
REMARK 470     GLN H 861    CG   CD   OE1  NE2                                  
REMARK 470     ASN H 862    CG   OD1  ND2                                       
REMARK 470     ILE H 863    CG1  CG2  CD1                                       
REMARK 470     LEU H 864    CG   CD1  CD2                                       
REMARK 470     THR H 865    OG1  CG2                                            
REMARK 470     ILE H 867    CG1  CG2  CD1                                       
REMARK 470     GLN H 868    CG   CD   OE1  NE2                                  
REMARK 470     GLN H 869    CG   CD   OE1  NE2                                  
REMARK 470     VAL H 870    CG1  CG2                                            
REMARK 470     SER H 872    OG                                                  
REMARK 470     LEU H 873    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    SER G   420     N    ARG G   422              1.97            
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    HIS A  52      -17.41     65.15                                   
REMARK 500    THR A 328       49.55    -99.44                                   
REMARK 500    LYS A 357      -44.70   -130.76                                   
REMARK 500    TYR A 503      -37.33     63.43                                   
REMARK 500    ALA A 531       85.90   -150.88                                   
REMARK 500    ASP A 596     -146.25   -153.88                                   
REMARK 500    GLN A 597     -153.17     54.96                                   
REMARK 500    THR A 649      -62.06    -99.11                                   
REMARK 500    ARG A 792       60.20    -69.57                                   
REMARK 500    THR A 794       36.88   -153.43                                   
REMARK 500    MET A 804       48.82   -102.98                                   
REMARK 500    ILE A 818      -57.94   -123.97                                   
REMARK 500    PRO A 884        0.26    -68.72                                   
REMARK 500    SER A 895      -71.43    -91.66                                   
REMARK 500    ILE A 899      -71.76    -67.84                                   
REMARK 500    ILE B  33     -168.36    -78.74                                   
REMARK 500    THR B  51      -96.58   -105.27                                   
REMARK 500    ARG B 241       47.12   -109.29                                   
REMARK 500    THR B 328       50.84   -113.14                                   
REMARK 500    ASP B 344       71.61   -115.91                                   
REMARK 500    LYS B 357      -30.75   -140.21                                   
REMARK 500    ASN B 387      -51.13   -126.82                                   
REMARK 500    THR B 404     -105.27     58.11                                   
REMARK 500    ALA B 406     -133.59     54.89                                   
REMARK 500    GLU B 415      -40.81   -135.65                                   
REMARK 500    ARG B 471     -159.44    -75.90                                   
REMARK 500    TYR B 503      -30.74     63.94                                   
REMARK 500    PRO B 669     -179.52    -68.24                                   
REMARK 500    MET B 718     -171.06    -69.84                                   
REMARK 500    THR B 790      -84.54   -115.38                                   
REMARK 500    SER B 791     -128.71     53.83                                   
REMARK 500    ARG B 792       -5.90   -152.51                                   
REMARK 500    HIS B 801     -147.09    -92.36                                   
REMARK 500    MET B 804       49.79   -103.97                                   
REMARK 500    ILE B 818      -58.82   -121.70                                   
REMARK 500    SER C  31       86.32    -69.85                                   
REMARK 500    HIS C  52      -17.06     64.82                                   
REMARK 500    ARG C 262      -67.73   -137.05                                   
REMARK 500    HIS C 263      -60.88     72.59                                   
REMARK 500    VAL C 264      -20.66     91.20                                   
REMARK 500    HIS C 287       45.41    -99.35                                   
REMARK 500    GLU C 296       43.74   -107.74                                   
REMARK 500    THR C 328       54.40   -114.67                                   
REMARK 500    LYS C 357      -50.21   -130.90                                   
REMARK 500    PHE C 412     -153.57   -169.68                                   
REMARK 500    ASN C 416       30.77    -89.22                                   
REMARK 500    ASP C 419      -69.58    -95.60                                   
REMARK 500    TYR C 503      -37.90     64.24                                   
REMARK 500    THR C 790     -109.76   -120.79                                   
REMARK 500    SER C 791     -172.29     58.74                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     159 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 437   OE1                                                    
REMARK 620 2 HIS A 441   NE2 108.0                                              
REMARK 620 3 CYS A 446   SG  117.9 110.9                                        
REMARK 620 4 CYS A 449   SG  119.8 103.0  96.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 712   NE2                                                    
REMARK 620 2 HIS A 714   NE2 105.9                                              
REMARK 620 3 CYS A 728   SG   85.5 117.1                                        
REMARK 620 4 CYS A 847   SG  114.7 115.7 113.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 437   OE1                                                    
REMARK 620 2 HIS B 441   NE2  90.1                                              
REMARK 620 3 CYS B 446   SG  106.0 123.8                                        
REMARK 620 4 CYS B 449   SG  118.5 115.4 103.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 712   NE2                                                    
REMARK 620 2 HIS B 714   NE2 101.3                                              
REMARK 620 3 CYS B 728   SG   95.9 130.2                                        
REMARK 620 4 CYS B 847   SG   97.8 119.7 103.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 437   OE1                                                    
REMARK 620 2 HIS C 441   NE2  93.3                                              
REMARK 620 3 CYS C 446   SG   94.1 118.0                                        
REMARK 620 4 CYS C 449   SG  126.8 113.8 109.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 712   NE2                                                    
REMARK 620 2 HIS C 714   NE2 103.7                                              
REMARK 620 3 CYS C 728   SG   90.0 132.8                                        
REMARK 620 4 CYS C 847   SG  103.0 120.1  99.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 437   OE1                                                    
REMARK 620 2 HIS D 441   NE2 106.3                                              
REMARK 620 3 CYS D 446   SG  119.0 114.8                                        
REMARK 620 4 CYS D 449   SG  121.7  97.0  96.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 712   NE2                                                    
REMARK 620 2 HIS D 714   NE2 105.5                                              
REMARK 620 3 CYS D 728   SG   91.3 122.3                                        
REMARK 620 4 CYS D 847   SG  114.8 118.6 101.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 437   OE1                                                    
REMARK 620 2 HIS E 441   NE2  96.8                                              
REMARK 620 3 CYS E 446   SG  116.5 132.6                                        
REMARK 620 4 CYS E 449   SG  108.3 108.5  92.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E 712   NE2                                                    
REMARK 620 2 HIS E 714   NE2  96.7                                              
REMARK 620 3 CYS E 728   SG   98.4 114.7                                        
REMARK 620 4 CYS E 847   SG  122.4 108.0 115.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU F 437   OE1                                                    
REMARK 620 2 HIS F 441   NE2  86.3                                              
REMARK 620 3 CYS F 446   SG  110.6 115.0                                        
REMARK 620 4 CYS F 449   SG  125.6 111.4 107.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 712   NE2                                                    
REMARK 620 2 HIS F 714   NE2 103.6                                              
REMARK 620 3 CYS F 728   SG   95.4 128.5                                        
REMARK 620 4 CYS F 847   SG  112.9 115.9  98.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 437   OE1                                                    
REMARK 620 2 HIS G 441   NE2  96.5                                              
REMARK 620 3 CYS G 446   SG  112.3 121.4                                        
REMARK 620 4 CYS G 449   SG  125.9 103.6  98.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G 712   NE2                                                    
REMARK 620 2 HIS G 714   NE2 109.3                                              
REMARK 620 3 CYS G 728   SG   83.0 126.8                                        
REMARK 620 4 CYS G 847   SG  101.6 120.8 105.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H 441   NE2                                                    
REMARK 620 2 CYS H 446   SG   84.1                                              
REMARK 620 3 CYS H 449   SG  151.8 122.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H 712   NE2                                                    
REMARK 620 2 HIS H 714   NE2  91.5                                              
REMARK 620 3 CYS H 728   SG   78.6 148.7                                        
REMARK 620 4 CYS H 847   SG  104.0 110.6 100.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH C 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH D 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN E 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH E 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH F 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH G 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN H 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN H 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH H 1003                
DBREF  5CCV A    1   900  UNP    P27915   POLG_DEN3P    2491   3390             
DBREF  5CCV B    1   900  UNP    P27915   POLG_DEN3P    2491   3390             
DBREF  5CCV C    1   900  UNP    P27915   POLG_DEN3P    2491   3390             
DBREF  5CCV D    1   900  UNP    P27915   POLG_DEN3P    2491   3390             
DBREF  5CCV E    1   900  UNP    P27915   POLG_DEN3P    2491   3390             
DBREF  5CCV F    1   900  UNP    P27915   POLG_DEN3P    2491   3390             
DBREF  5CCV G    1   900  UNP    P27915   POLG_DEN3P    2491   3390             
DBREF  5CCV H    1   900  UNP    P27915   POLG_DEN3P    2491   3390             
SEQADV 5CCV ALA A  763  UNP  P27915    THR  3253 CONFLICT                       
SEQADV 5CCV     A       UNP  P27915    TRP  3285 DELETION                       
SEQADV 5CCV     A       UNP  P27915    SER  3286 DELETION                       
SEQADV 5CCV     A       UNP  P27915    ILE  3287 DELETION                       
SEQADV 5CCV     A       UNP  P27915    HIS  3288 DELETION                       
SEQADV 5CCV     A       UNP  P27915    ALA  3289 DELETION                       
SEQADV 5CCV     A       UNP  P27915    HIS  3290 DELETION                       
SEQADV 5CCV ALA A  901  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA A  902  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA A  903  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV LEU A  904  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV GLU A  905  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS A  906  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS A  907  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS A  908  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS A  909  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS A  910  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS A  911  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA B  763  UNP  P27915    THR  3253 CONFLICT                       
SEQADV 5CCV     B       UNP  P27915    TRP  3285 DELETION                       
SEQADV 5CCV     B       UNP  P27915    SER  3286 DELETION                       
SEQADV 5CCV     B       UNP  P27915    ILE  3287 DELETION                       
SEQADV 5CCV     B       UNP  P27915    HIS  3288 DELETION                       
SEQADV 5CCV     B       UNP  P27915    ALA  3289 DELETION                       
SEQADV 5CCV     B       UNP  P27915    HIS  3290 DELETION                       
SEQADV 5CCV ALA B  901  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA B  902  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA B  903  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV LEU B  904  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV GLU B  905  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS B  906  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS B  907  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS B  908  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS B  909  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS B  910  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS B  911  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA C  763  UNP  P27915    THR  3253 CONFLICT                       
SEQADV 5CCV     C       UNP  P27915    TRP  3285 DELETION                       
SEQADV 5CCV     C       UNP  P27915    SER  3286 DELETION                       
SEQADV 5CCV     C       UNP  P27915    ILE  3287 DELETION                       
SEQADV 5CCV     C       UNP  P27915    HIS  3288 DELETION                       
SEQADV 5CCV     C       UNP  P27915    ALA  3289 DELETION                       
SEQADV 5CCV     C       UNP  P27915    HIS  3290 DELETION                       
SEQADV 5CCV ALA C  901  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA C  902  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA C  903  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV LEU C  904  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV GLU C  905  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS C  906  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS C  907  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS C  908  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS C  909  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS C  910  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS C  911  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA D  763  UNP  P27915    THR  3253 CONFLICT                       
SEQADV 5CCV     D       UNP  P27915    TRP  3285 DELETION                       
SEQADV 5CCV     D       UNP  P27915    SER  3286 DELETION                       
SEQADV 5CCV     D       UNP  P27915    ILE  3287 DELETION                       
SEQADV 5CCV     D       UNP  P27915    HIS  3288 DELETION                       
SEQADV 5CCV     D       UNP  P27915    ALA  3289 DELETION                       
SEQADV 5CCV     D       UNP  P27915    HIS  3290 DELETION                       
SEQADV 5CCV ALA D  901  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA D  902  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA D  903  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV LEU D  904  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV GLU D  905  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS D  906  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS D  907  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS D  908  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS D  909  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS D  910  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS D  911  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA E  763  UNP  P27915    THR  3253 CONFLICT                       
SEQADV 5CCV     E       UNP  P27915    TRP  3285 DELETION                       
SEQADV 5CCV     E       UNP  P27915    SER  3286 DELETION                       
SEQADV 5CCV     E       UNP  P27915    ILE  3287 DELETION                       
SEQADV 5CCV     E       UNP  P27915    HIS  3288 DELETION                       
SEQADV 5CCV     E       UNP  P27915    ALA  3289 DELETION                       
SEQADV 5CCV     E       UNP  P27915    HIS  3290 DELETION                       
SEQADV 5CCV ALA E  901  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA E  902  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA E  903  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV LEU E  904  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV GLU E  905  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS E  906  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS E  907  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS E  908  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS E  909  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS E  910  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS E  911  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA F  763  UNP  P27915    THR  3253 CONFLICT                       
SEQADV 5CCV     F       UNP  P27915    TRP  3285 DELETION                       
SEQADV 5CCV     F       UNP  P27915    SER  3286 DELETION                       
SEQADV 5CCV     F       UNP  P27915    ILE  3287 DELETION                       
SEQADV 5CCV     F       UNP  P27915    HIS  3288 DELETION                       
SEQADV 5CCV     F       UNP  P27915    ALA  3289 DELETION                       
SEQADV 5CCV     F       UNP  P27915    HIS  3290 DELETION                       
SEQADV 5CCV ALA F  901  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA F  902  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA F  903  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV LEU F  904  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV GLU F  905  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS F  906  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS F  907  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS F  908  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS F  909  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS F  910  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS F  911  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA G  763  UNP  P27915    THR  3253 CONFLICT                       
SEQADV 5CCV     G       UNP  P27915    TRP  3285 DELETION                       
SEQADV 5CCV     G       UNP  P27915    SER  3286 DELETION                       
SEQADV 5CCV     G       UNP  P27915    ILE  3287 DELETION                       
SEQADV 5CCV     G       UNP  P27915    HIS  3288 DELETION                       
SEQADV 5CCV     G       UNP  P27915    ALA  3289 DELETION                       
SEQADV 5CCV     G       UNP  P27915    HIS  3290 DELETION                       
SEQADV 5CCV ALA G  901  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA G  902  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA G  903  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV LEU G  904  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV GLU G  905  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS G  906  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS G  907  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS G  908  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS G  909  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS G  910  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS G  911  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA H  763  UNP  P27915    THR  3253 CONFLICT                       
SEQADV 5CCV     H       UNP  P27915    TRP  3285 DELETION                       
SEQADV 5CCV     H       UNP  P27915    SER  3286 DELETION                       
SEQADV 5CCV     H       UNP  P27915    ILE  3287 DELETION                       
SEQADV 5CCV     H       UNP  P27915    HIS  3288 DELETION                       
SEQADV 5CCV     H       UNP  P27915    ALA  3289 DELETION                       
SEQADV 5CCV     H       UNP  P27915    HIS  3290 DELETION                       
SEQADV 5CCV ALA H  901  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA H  902  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV ALA H  903  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV LEU H  904  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV GLU H  905  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS H  906  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS H  907  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS H  908  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS H  909  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS H  910  UNP  P27915              EXPRESSION TAG                 
SEQADV 5CCV HIS H  911  UNP  P27915              EXPRESSION TAG                 
SEQRES   1 A  905  GLY THR GLY SER GLN GLY GLU THR LEU GLY GLU LYS TRP          
SEQRES   2 A  905  LYS LYS LYS LEU ASN GLN LEU SER ARG LYS GLU PHE ASP          
SEQRES   3 A  905  LEU TYR LYS LYS SER GLY ILE THR GLU VAL ASP ARG THR          
SEQRES   4 A  905  GLU ALA LYS GLU GLY LEU LYS ARG GLY GLU ILE THR HIS          
SEQRES   5 A  905  HIS ALA VAL SER ARG GLY SER ALA LYS LEU GLN TRP PHE          
SEQRES   6 A  905  VAL GLU ARG ASN MET VAL ILE PRO GLU GLY ARG VAL ILE          
SEQRES   7 A  905  ASP LEU GLY CYS GLY ARG GLY GLY TRP SER TYR TYR CYS          
SEQRES   8 A  905  ALA GLY LEU LYS LYS VAL THR GLU VAL ARG GLY TYR THR          
SEQRES   9 A  905  LYS GLY GLY PRO GLY HIS GLU GLU PRO VAL PRO MET SER          
SEQRES  10 A  905  THR TYR GLY TRP ASN ILE VAL LYS LEU MET SER GLY LYS          
SEQRES  11 A  905  ASP VAL PHE TYR LEU PRO PRO GLU LYS CYS ASP THR LEU          
SEQRES  12 A  905  LEU CYS ASP ILE GLY GLU SER SER PRO SER PRO THR VAL          
SEQRES  13 A  905  GLU GLU SER ARG THR ILE ARG VAL LEU LYS MET VAL GLU          
SEQRES  14 A  905  PRO TRP LEU LYS ASN ASN GLN PHE CYS ILE LYS VAL LEU          
SEQRES  15 A  905  ASN PRO TYR MET PRO THR VAL ILE GLU HIS LEU GLU ARG          
SEQRES  16 A  905  LEU GLN ARG LYS HIS GLY GLY MET LEU VAL ARG ASN PRO          
SEQRES  17 A  905  LEU SER ARG ASN SER THR HIS GLU MET TYR TRP ILE SER          
SEQRES  18 A  905  ASN GLY THR GLY ASN ILE VAL SER SER VAL ASN MET VAL          
SEQRES  19 A  905  SER ARG LEU LEU LEU ASN ARG PHE THR MET THR HIS ARG          
SEQRES  20 A  905  ARG PRO THR ILE GLU LYS ASP VAL ASP LEU GLY ALA GLY          
SEQRES  21 A  905  THR ARG HIS VAL ASN ALA GLU PRO GLU THR PRO ASN MET          
SEQRES  22 A  905  ASP VAL ILE GLY GLU ARG ILE LYS ARG ILE LYS GLU GLU          
SEQRES  23 A  905  HIS SER SER THR TRP HIS TYR ASP ASP GLU ASN PRO TYR          
SEQRES  24 A  905  LYS THR TRP ALA TYR HIS GLY SER TYR GLU VAL LYS ALA          
SEQRES  25 A  905  THR GLY SER ALA SER SER MET ILE ASN GLY VAL VAL LYS          
SEQRES  26 A  905  LEU LEU THR LYS PRO TRP ASP VAL VAL PRO MET VAL THR          
SEQRES  27 A  905  GLN MET ALA MET THR ASP THR THR PRO PHE GLY GLN GLN          
SEQRES  28 A  905  ARG VAL PHE LYS GLU LYS VAL ASP THR ARG THR PRO ARG          
SEQRES  29 A  905  PRO MET PRO GLY THR ARG LYS VAL MET GLU ILE THR ALA          
SEQRES  30 A  905  GLU TRP LEU TRP ARG THR LEU GLY ARG ASN LYS ARG PRO          
SEQRES  31 A  905  ARG LEU CYS THR ARG GLU GLU PHE THR LYS LYS VAL ARG          
SEQRES  32 A  905  THR ASN ALA ALA MET GLY ALA VAL PHE THR GLU GLU ASN          
SEQRES  33 A  905  GLN TRP ASP SER ALA ARG ALA ALA VAL GLU ASP GLU GLU          
SEQRES  34 A  905  PHE TRP LYS LEU VAL ASP ARG GLU ARG GLU LEU HIS LYS          
SEQRES  35 A  905  LEU GLY LYS CYS GLY SER CYS VAL TYR ASN MET MET GLY          
SEQRES  36 A  905  LYS ARG GLU LYS LYS LEU GLY GLU PHE GLY LYS ALA LYS          
SEQRES  37 A  905  GLY SER ARG ALA ILE TRP TYR MET TRP LEU GLY ALA ARG          
SEQRES  38 A  905  TYR LEU GLU PHE GLU ALA LEU GLY PHE LEU ASN GLU ASP          
SEQRES  39 A  905  HIS TRP PHE SER ARG GLU ASN SER TYR SER GLY VAL GLU          
SEQRES  40 A  905  GLY GLU GLY LEU HIS LYS LEU GLY TYR ILE LEU ARG ASP          
SEQRES  41 A  905  ILE SER LYS ILE PRO GLY GLY ALA MET TYR ALA ASP ASP          
SEQRES  42 A  905  THR ALA GLY TRP ASP THR ARG ILE THR GLU ASP ASP LEU          
SEQRES  43 A  905  HIS ASN GLU GLU LYS ILE THR GLN GLN MET ASP PRO GLU          
SEQRES  44 A  905  HIS ARG GLN LEU ALA ASN ALA ILE PHE LYS LEU THR TYR          
SEQRES  45 A  905  GLN ASN LYS VAL VAL LYS VAL GLN ARG PRO THR PRO LYS          
SEQRES  46 A  905  GLY THR VAL MET ASP ILE ILE SER ARG LYS ASP GLN ARG          
SEQRES  47 A  905  GLY SER GLY GLN VAL GLY THR TYR GLY LEU ASN THR PHE          
SEQRES  48 A  905  THR ASN MET GLU ALA GLN LEU ILE ARG GLN MET GLU GLY          
SEQRES  49 A  905  GLU GLY VAL LEU SER LYS ALA ASP LEU GLU ASN PRO HIS          
SEQRES  50 A  905  PRO LEU GLU LYS LYS ILE THR GLN TRP LEU GLU THR LYS          
SEQRES  51 A  905  GLY VAL GLU ARG LEU LYS ARG MET ALA ILE SER GLY ASP          
SEQRES  52 A  905  ASP CYS VAL VAL LYS PRO ILE ASP ASP ARG PHE ALA ASN          
SEQRES  53 A  905  ALA LEU LEU ALA LEU ASN ASP MET GLY LYS VAL ARG LYS          
SEQRES  54 A  905  ASP ILE PRO GLN TRP GLN PRO SER LYS GLY TRP HIS ASP          
SEQRES  55 A  905  TRP GLN GLN VAL PRO PHE CYS SER HIS HIS PHE HIS GLU          
SEQRES  56 A  905  LEU ILE MET LYS ASP GLY ARG LYS LEU VAL VAL PRO CYS          
SEQRES  57 A  905  ARG PRO GLN ASP GLU LEU ILE GLY ARG ALA ARG ILE SER          
SEQRES  58 A  905  GLN GLY ALA GLY TRP SER LEU ARG GLU THR ALA CYS LEU          
SEQRES  59 A  905  GLY LYS ALA TYR ALA GLN MET TRP ALA LEU MET TYR PHE          
SEQRES  60 A  905  HIS ARG ARG ASP LEU ARG LEU ALA SER ASN ALA ILE CYS          
SEQRES  61 A  905  SER ALA VAL PRO VAL HIS TRP VAL PRO THR SER ARG THR          
SEQRES  62 A  905  THR HIS GLN TRP MET THR THR GLU ASP MET LEU THR VAL          
SEQRES  63 A  905  TRP ASN ARG VAL TRP ILE GLU ASP ASN PRO TRP MET GLU          
SEQRES  64 A  905  ASP LYS THR PRO VAL THR THR TRP GLU ASP VAL PRO TYR          
SEQRES  65 A  905  LEU GLY LYS ARG GLU ASP GLN TRP CYS GLY SER LEU ILE          
SEQRES  66 A  905  GLY LEU THR SER ARG ALA THR TRP ALA GLN ASN ILE LEU          
SEQRES  67 A  905  THR ALA ILE GLN GLN VAL ARG SER LEU ILE GLY ASN GLU          
SEQRES  68 A  905  GLU PHE LEU ASP TYR MET PRO SER MET LYS ARG PHE ARG          
SEQRES  69 A  905  LYS GLU GLU GLU SER GLU GLY ALA ILE TRP ALA ALA ALA          
SEQRES  70 A  905  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  905  GLY THR GLY SER GLN GLY GLU THR LEU GLY GLU LYS TRP          
SEQRES   2 B  905  LYS LYS LYS LEU ASN GLN LEU SER ARG LYS GLU PHE ASP          
SEQRES   3 B  905  LEU TYR LYS LYS SER GLY ILE THR GLU VAL ASP ARG THR          
SEQRES   4 B  905  GLU ALA LYS GLU GLY LEU LYS ARG GLY GLU ILE THR HIS          
SEQRES   5 B  905  HIS ALA VAL SER ARG GLY SER ALA LYS LEU GLN TRP PHE          
SEQRES   6 B  905  VAL GLU ARG ASN MET VAL ILE PRO GLU GLY ARG VAL ILE          
SEQRES   7 B  905  ASP LEU GLY CYS GLY ARG GLY GLY TRP SER TYR TYR CYS          
SEQRES   8 B  905  ALA GLY LEU LYS LYS VAL THR GLU VAL ARG GLY TYR THR          
SEQRES   9 B  905  LYS GLY GLY PRO GLY HIS GLU GLU PRO VAL PRO MET SER          
SEQRES  10 B  905  THR TYR GLY TRP ASN ILE VAL LYS LEU MET SER GLY LYS          
SEQRES  11 B  905  ASP VAL PHE TYR LEU PRO PRO GLU LYS CYS ASP THR LEU          
SEQRES  12 B  905  LEU CYS ASP ILE GLY GLU SER SER PRO SER PRO THR VAL          
SEQRES  13 B  905  GLU GLU SER ARG THR ILE ARG VAL LEU LYS MET VAL GLU          
SEQRES  14 B  905  PRO TRP LEU LYS ASN ASN GLN PHE CYS ILE LYS VAL LEU          
SEQRES  15 B  905  ASN PRO TYR MET PRO THR VAL ILE GLU HIS LEU GLU ARG          
SEQRES  16 B  905  LEU GLN ARG LYS HIS GLY GLY MET LEU VAL ARG ASN PRO          
SEQRES  17 B  905  LEU SER ARG ASN SER THR HIS GLU MET TYR TRP ILE SER          
SEQRES  18 B  905  ASN GLY THR GLY ASN ILE VAL SER SER VAL ASN MET VAL          
SEQRES  19 B  905  SER ARG LEU LEU LEU ASN ARG PHE THR MET THR HIS ARG          
SEQRES  20 B  905  ARG PRO THR ILE GLU LYS ASP VAL ASP LEU GLY ALA GLY          
SEQRES  21 B  905  THR ARG HIS VAL ASN ALA GLU PRO GLU THR PRO ASN MET          
SEQRES  22 B  905  ASP VAL ILE GLY GLU ARG ILE LYS ARG ILE LYS GLU GLU          
SEQRES  23 B  905  HIS SER SER THR TRP HIS TYR ASP ASP GLU ASN PRO TYR          
SEQRES  24 B  905  LYS THR TRP ALA TYR HIS GLY SER TYR GLU VAL LYS ALA          
SEQRES  25 B  905  THR GLY SER ALA SER SER MET ILE ASN GLY VAL VAL LYS          
SEQRES  26 B  905  LEU LEU THR LYS PRO TRP ASP VAL VAL PRO MET VAL THR          
SEQRES  27 B  905  GLN MET ALA MET THR ASP THR THR PRO PHE GLY GLN GLN          
SEQRES  28 B  905  ARG VAL PHE LYS GLU LYS VAL ASP THR ARG THR PRO ARG          
SEQRES  29 B  905  PRO MET PRO GLY THR ARG LYS VAL MET GLU ILE THR ALA          
SEQRES  30 B  905  GLU TRP LEU TRP ARG THR LEU GLY ARG ASN LYS ARG PRO          
SEQRES  31 B  905  ARG LEU CYS THR ARG GLU GLU PHE THR LYS LYS VAL ARG          
SEQRES  32 B  905  THR ASN ALA ALA MET GLY ALA VAL PHE THR GLU GLU ASN          
SEQRES  33 B  905  GLN TRP ASP SER ALA ARG ALA ALA VAL GLU ASP GLU GLU          
SEQRES  34 B  905  PHE TRP LYS LEU VAL ASP ARG GLU ARG GLU LEU HIS LYS          
SEQRES  35 B  905  LEU GLY LYS CYS GLY SER CYS VAL TYR ASN MET MET GLY          
SEQRES  36 B  905  LYS ARG GLU LYS LYS LEU GLY GLU PHE GLY LYS ALA LYS          
SEQRES  37 B  905  GLY SER ARG ALA ILE TRP TYR MET TRP LEU GLY ALA ARG          
SEQRES  38 B  905  TYR LEU GLU PHE GLU ALA LEU GLY PHE LEU ASN GLU ASP          
SEQRES  39 B  905  HIS TRP PHE SER ARG GLU ASN SER TYR SER GLY VAL GLU          
SEQRES  40 B  905  GLY GLU GLY LEU HIS LYS LEU GLY TYR ILE LEU ARG ASP          
SEQRES  41 B  905  ILE SER LYS ILE PRO GLY GLY ALA MET TYR ALA ASP ASP          
SEQRES  42 B  905  THR ALA GLY TRP ASP THR ARG ILE THR GLU ASP ASP LEU          
SEQRES  43 B  905  HIS ASN GLU GLU LYS ILE THR GLN GLN MET ASP PRO GLU          
SEQRES  44 B  905  HIS ARG GLN LEU ALA ASN ALA ILE PHE LYS LEU THR TYR          
SEQRES  45 B  905  GLN ASN LYS VAL VAL LYS VAL GLN ARG PRO THR PRO LYS          
SEQRES  46 B  905  GLY THR VAL MET ASP ILE ILE SER ARG LYS ASP GLN ARG          
SEQRES  47 B  905  GLY SER GLY GLN VAL GLY THR TYR GLY LEU ASN THR PHE          
SEQRES  48 B  905  THR ASN MET GLU ALA GLN LEU ILE ARG GLN MET GLU GLY          
SEQRES  49 B  905  GLU GLY VAL LEU SER LYS ALA ASP LEU GLU ASN PRO HIS          
SEQRES  50 B  905  PRO LEU GLU LYS LYS ILE THR GLN TRP LEU GLU THR LYS          
SEQRES  51 B  905  GLY VAL GLU ARG LEU LYS ARG MET ALA ILE SER GLY ASP          
SEQRES  52 B  905  ASP CYS VAL VAL LYS PRO ILE ASP ASP ARG PHE ALA ASN          
SEQRES  53 B  905  ALA LEU LEU ALA LEU ASN ASP MET GLY LYS VAL ARG LYS          
SEQRES  54 B  905  ASP ILE PRO GLN TRP GLN PRO SER LYS GLY TRP HIS ASP          
SEQRES  55 B  905  TRP GLN GLN VAL PRO PHE CYS SER HIS HIS PHE HIS GLU          
SEQRES  56 B  905  LEU ILE MET LYS ASP GLY ARG LYS LEU VAL VAL PRO CYS          
SEQRES  57 B  905  ARG PRO GLN ASP GLU LEU ILE GLY ARG ALA ARG ILE SER          
SEQRES  58 B  905  GLN GLY ALA GLY TRP SER LEU ARG GLU THR ALA CYS LEU          
SEQRES  59 B  905  GLY LYS ALA TYR ALA GLN MET TRP ALA LEU MET TYR PHE          
SEQRES  60 B  905  HIS ARG ARG ASP LEU ARG LEU ALA SER ASN ALA ILE CYS          
SEQRES  61 B  905  SER ALA VAL PRO VAL HIS TRP VAL PRO THR SER ARG THR          
SEQRES  62 B  905  THR HIS GLN TRP MET THR THR GLU ASP MET LEU THR VAL          
SEQRES  63 B  905  TRP ASN ARG VAL TRP ILE GLU ASP ASN PRO TRP MET GLU          
SEQRES  64 B  905  ASP LYS THR PRO VAL THR THR TRP GLU ASP VAL PRO TYR          
SEQRES  65 B  905  LEU GLY LYS ARG GLU ASP GLN TRP CYS GLY SER LEU ILE          
SEQRES  66 B  905  GLY LEU THR SER ARG ALA THR TRP ALA GLN ASN ILE LEU          
SEQRES  67 B  905  THR ALA ILE GLN GLN VAL ARG SER LEU ILE GLY ASN GLU          
SEQRES  68 B  905  GLU PHE LEU ASP TYR MET PRO SER MET LYS ARG PHE ARG          
SEQRES  69 B  905  LYS GLU GLU GLU SER GLU GLY ALA ILE TRP ALA ALA ALA          
SEQRES  70 B  905  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  905  GLY THR GLY SER GLN GLY GLU THR LEU GLY GLU LYS TRP          
SEQRES   2 C  905  LYS LYS LYS LEU ASN GLN LEU SER ARG LYS GLU PHE ASP          
SEQRES   3 C  905  LEU TYR LYS LYS SER GLY ILE THR GLU VAL ASP ARG THR          
SEQRES   4 C  905  GLU ALA LYS GLU GLY LEU LYS ARG GLY GLU ILE THR HIS          
SEQRES   5 C  905  HIS ALA VAL SER ARG GLY SER ALA LYS LEU GLN TRP PHE          
SEQRES   6 C  905  VAL GLU ARG ASN MET VAL ILE PRO GLU GLY ARG VAL ILE          
SEQRES   7 C  905  ASP LEU GLY CYS GLY ARG GLY GLY TRP SER TYR TYR CYS          
SEQRES   8 C  905  ALA GLY LEU LYS LYS VAL THR GLU VAL ARG GLY TYR THR          
SEQRES   9 C  905  LYS GLY GLY PRO GLY HIS GLU GLU PRO VAL PRO MET SER          
SEQRES  10 C  905  THR TYR GLY TRP ASN ILE VAL LYS LEU MET SER GLY LYS          
SEQRES  11 C  905  ASP VAL PHE TYR LEU PRO PRO GLU LYS CYS ASP THR LEU          
SEQRES  12 C  905  LEU CYS ASP ILE GLY GLU SER SER PRO SER PRO THR VAL          
SEQRES  13 C  905  GLU GLU SER ARG THR ILE ARG VAL LEU LYS MET VAL GLU          
SEQRES  14 C  905  PRO TRP LEU LYS ASN ASN GLN PHE CYS ILE LYS VAL LEU          
SEQRES  15 C  905  ASN PRO TYR MET PRO THR VAL ILE GLU HIS LEU GLU ARG          
SEQRES  16 C  905  LEU GLN ARG LYS HIS GLY GLY MET LEU VAL ARG ASN PRO          
SEQRES  17 C  905  LEU SER ARG ASN SER THR HIS GLU MET TYR TRP ILE SER          
SEQRES  18 C  905  ASN GLY THR GLY ASN ILE VAL SER SER VAL ASN MET VAL          
SEQRES  19 C  905  SER ARG LEU LEU LEU ASN ARG PHE THR MET THR HIS ARG          
SEQRES  20 C  905  ARG PRO THR ILE GLU LYS ASP VAL ASP LEU GLY ALA GLY          
SEQRES  21 C  905  THR ARG HIS VAL ASN ALA GLU PRO GLU THR PRO ASN MET          
SEQRES  22 C  905  ASP VAL ILE GLY GLU ARG ILE LYS ARG ILE LYS GLU GLU          
SEQRES  23 C  905  HIS SER SER THR TRP HIS TYR ASP ASP GLU ASN PRO TYR          
SEQRES  24 C  905  LYS THR TRP ALA TYR HIS GLY SER TYR GLU VAL LYS ALA          
SEQRES  25 C  905  THR GLY SER ALA SER SER MET ILE ASN GLY VAL VAL LYS          
SEQRES  26 C  905  LEU LEU THR LYS PRO TRP ASP VAL VAL PRO MET VAL THR          
SEQRES  27 C  905  GLN MET ALA MET THR ASP THR THR PRO PHE GLY GLN GLN          
SEQRES  28 C  905  ARG VAL PHE LYS GLU LYS VAL ASP THR ARG THR PRO ARG          
SEQRES  29 C  905  PRO MET PRO GLY THR ARG LYS VAL MET GLU ILE THR ALA          
SEQRES  30 C  905  GLU TRP LEU TRP ARG THR LEU GLY ARG ASN LYS ARG PRO          
SEQRES  31 C  905  ARG LEU CYS THR ARG GLU GLU PHE THR LYS LYS VAL ARG          
SEQRES  32 C  905  THR ASN ALA ALA MET GLY ALA VAL PHE THR GLU GLU ASN          
SEQRES  33 C  905  GLN TRP ASP SER ALA ARG ALA ALA VAL GLU ASP GLU GLU          
SEQRES  34 C  905  PHE TRP LYS LEU VAL ASP ARG GLU ARG GLU LEU HIS LYS          
SEQRES  35 C  905  LEU GLY LYS CYS GLY SER CYS VAL TYR ASN MET MET GLY          
SEQRES  36 C  905  LYS ARG GLU LYS LYS LEU GLY GLU PHE GLY LYS ALA LYS          
SEQRES  37 C  905  GLY SER ARG ALA ILE TRP TYR MET TRP LEU GLY ALA ARG          
SEQRES  38 C  905  TYR LEU GLU PHE GLU ALA LEU GLY PHE LEU ASN GLU ASP          
SEQRES  39 C  905  HIS TRP PHE SER ARG GLU ASN SER TYR SER GLY VAL GLU          
SEQRES  40 C  905  GLY GLU GLY LEU HIS LYS LEU GLY TYR ILE LEU ARG ASP          
SEQRES  41 C  905  ILE SER LYS ILE PRO GLY GLY ALA MET TYR ALA ASP ASP          
SEQRES  42 C  905  THR ALA GLY TRP ASP THR ARG ILE THR GLU ASP ASP LEU          
SEQRES  43 C  905  HIS ASN GLU GLU LYS ILE THR GLN GLN MET ASP PRO GLU          
SEQRES  44 C  905  HIS ARG GLN LEU ALA ASN ALA ILE PHE LYS LEU THR TYR          
SEQRES  45 C  905  GLN ASN LYS VAL VAL LYS VAL GLN ARG PRO THR PRO LYS          
SEQRES  46 C  905  GLY THR VAL MET ASP ILE ILE SER ARG LYS ASP GLN ARG          
SEQRES  47 C  905  GLY SER GLY GLN VAL GLY THR TYR GLY LEU ASN THR PHE          
SEQRES  48 C  905  THR ASN MET GLU ALA GLN LEU ILE ARG GLN MET GLU GLY          
SEQRES  49 C  905  GLU GLY VAL LEU SER LYS ALA ASP LEU GLU ASN PRO HIS          
SEQRES  50 C  905  PRO LEU GLU LYS LYS ILE THR GLN TRP LEU GLU THR LYS          
SEQRES  51 C  905  GLY VAL GLU ARG LEU LYS ARG MET ALA ILE SER GLY ASP          
SEQRES  52 C  905  ASP CYS VAL VAL LYS PRO ILE ASP ASP ARG PHE ALA ASN          
SEQRES  53 C  905  ALA LEU LEU ALA LEU ASN ASP MET GLY LYS VAL ARG LYS          
SEQRES  54 C  905  ASP ILE PRO GLN TRP GLN PRO SER LYS GLY TRP HIS ASP          
SEQRES  55 C  905  TRP GLN GLN VAL PRO PHE CYS SER HIS HIS PHE HIS GLU          
SEQRES  56 C  905  LEU ILE MET LYS ASP GLY ARG LYS LEU VAL VAL PRO CYS          
SEQRES  57 C  905  ARG PRO GLN ASP GLU LEU ILE GLY ARG ALA ARG ILE SER          
SEQRES  58 C  905  GLN GLY ALA GLY TRP SER LEU ARG GLU THR ALA CYS LEU          
SEQRES  59 C  905  GLY LYS ALA TYR ALA GLN MET TRP ALA LEU MET TYR PHE          
SEQRES  60 C  905  HIS ARG ARG ASP LEU ARG LEU ALA SER ASN ALA ILE CYS          
SEQRES  61 C  905  SER ALA VAL PRO VAL HIS TRP VAL PRO THR SER ARG THR          
SEQRES  62 C  905  THR HIS GLN TRP MET THR THR GLU ASP MET LEU THR VAL          
SEQRES  63 C  905  TRP ASN ARG VAL TRP ILE GLU ASP ASN PRO TRP MET GLU          
SEQRES  64 C  905  ASP LYS THR PRO VAL THR THR TRP GLU ASP VAL PRO TYR          
SEQRES  65 C  905  LEU GLY LYS ARG GLU ASP GLN TRP CYS GLY SER LEU ILE          
SEQRES  66 C  905  GLY LEU THR SER ARG ALA THR TRP ALA GLN ASN ILE LEU          
SEQRES  67 C  905  THR ALA ILE GLN GLN VAL ARG SER LEU ILE GLY ASN GLU          
SEQRES  68 C  905  GLU PHE LEU ASP TYR MET PRO SER MET LYS ARG PHE ARG          
SEQRES  69 C  905  LYS GLU GLU GLU SER GLU GLY ALA ILE TRP ALA ALA ALA          
SEQRES  70 C  905  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 D  905  GLY THR GLY SER GLN GLY GLU THR LEU GLY GLU LYS TRP          
SEQRES   2 D  905  LYS LYS LYS LEU ASN GLN LEU SER ARG LYS GLU PHE ASP          
SEQRES   3 D  905  LEU TYR LYS LYS SER GLY ILE THR GLU VAL ASP ARG THR          
SEQRES   4 D  905  GLU ALA LYS GLU GLY LEU LYS ARG GLY GLU ILE THR HIS          
SEQRES   5 D  905  HIS ALA VAL SER ARG GLY SER ALA LYS LEU GLN TRP PHE          
SEQRES   6 D  905  VAL GLU ARG ASN MET VAL ILE PRO GLU GLY ARG VAL ILE          
SEQRES   7 D  905  ASP LEU GLY CYS GLY ARG GLY GLY TRP SER TYR TYR CYS          
SEQRES   8 D  905  ALA GLY LEU LYS LYS VAL THR GLU VAL ARG GLY TYR THR          
SEQRES   9 D  905  LYS GLY GLY PRO GLY HIS GLU GLU PRO VAL PRO MET SER          
SEQRES  10 D  905  THR TYR GLY TRP ASN ILE VAL LYS LEU MET SER GLY LYS          
SEQRES  11 D  905  ASP VAL PHE TYR LEU PRO PRO GLU LYS CYS ASP THR LEU          
SEQRES  12 D  905  LEU CYS ASP ILE GLY GLU SER SER PRO SER PRO THR VAL          
SEQRES  13 D  905  GLU GLU SER ARG THR ILE ARG VAL LEU LYS MET VAL GLU          
SEQRES  14 D  905  PRO TRP LEU LYS ASN ASN GLN PHE CYS ILE LYS VAL LEU          
SEQRES  15 D  905  ASN PRO TYR MET PRO THR VAL ILE GLU HIS LEU GLU ARG          
SEQRES  16 D  905  LEU GLN ARG LYS HIS GLY GLY MET LEU VAL ARG ASN PRO          
SEQRES  17 D  905  LEU SER ARG ASN SER THR HIS GLU MET TYR TRP ILE SER          
SEQRES  18 D  905  ASN GLY THR GLY ASN ILE VAL SER SER VAL ASN MET VAL          
SEQRES  19 D  905  SER ARG LEU LEU LEU ASN ARG PHE THR MET THR HIS ARG          
SEQRES  20 D  905  ARG PRO THR ILE GLU LYS ASP VAL ASP LEU GLY ALA GLY          
SEQRES  21 D  905  THR ARG HIS VAL ASN ALA GLU PRO GLU THR PRO ASN MET          
SEQRES  22 D  905  ASP VAL ILE GLY GLU ARG ILE LYS ARG ILE LYS GLU GLU          
SEQRES  23 D  905  HIS SER SER THR TRP HIS TYR ASP ASP GLU ASN PRO TYR          
SEQRES  24 D  905  LYS THR TRP ALA TYR HIS GLY SER TYR GLU VAL LYS ALA          
SEQRES  25 D  905  THR GLY SER ALA SER SER MET ILE ASN GLY VAL VAL LYS          
SEQRES  26 D  905  LEU LEU THR LYS PRO TRP ASP VAL VAL PRO MET VAL THR          
SEQRES  27 D  905  GLN MET ALA MET THR ASP THR THR PRO PHE GLY GLN GLN          
SEQRES  28 D  905  ARG VAL PHE LYS GLU LYS VAL ASP THR ARG THR PRO ARG          
SEQRES  29 D  905  PRO MET PRO GLY THR ARG LYS VAL MET GLU ILE THR ALA          
SEQRES  30 D  905  GLU TRP LEU TRP ARG THR LEU GLY ARG ASN LYS ARG PRO          
SEQRES  31 D  905  ARG LEU CYS THR ARG GLU GLU PHE THR LYS LYS VAL ARG          
SEQRES  32 D  905  THR ASN ALA ALA MET GLY ALA VAL PHE THR GLU GLU ASN          
SEQRES  33 D  905  GLN TRP ASP SER ALA ARG ALA ALA VAL GLU ASP GLU GLU          
SEQRES  34 D  905  PHE TRP LYS LEU VAL ASP ARG GLU ARG GLU LEU HIS LYS          
SEQRES  35 D  905  LEU GLY LYS CYS GLY SER CYS VAL TYR ASN MET MET GLY          
SEQRES  36 D  905  LYS ARG GLU LYS LYS LEU GLY GLU PHE GLY LYS ALA LYS          
SEQRES  37 D  905  GLY SER ARG ALA ILE TRP TYR MET TRP LEU GLY ALA ARG          
SEQRES  38 D  905  TYR LEU GLU PHE GLU ALA LEU GLY PHE LEU ASN GLU ASP          
SEQRES  39 D  905  HIS TRP PHE SER ARG GLU ASN SER TYR SER GLY VAL GLU          
SEQRES  40 D  905  GLY GLU GLY LEU HIS LYS LEU GLY TYR ILE LEU ARG ASP          
SEQRES  41 D  905  ILE SER LYS ILE PRO GLY GLY ALA MET TYR ALA ASP ASP          
SEQRES  42 D  905  THR ALA GLY TRP ASP THR ARG ILE THR GLU ASP ASP LEU          
SEQRES  43 D  905  HIS ASN GLU GLU LYS ILE THR GLN GLN MET ASP PRO GLU          
SEQRES  44 D  905  HIS ARG GLN LEU ALA ASN ALA ILE PHE LYS LEU THR TYR          
SEQRES  45 D  905  GLN ASN LYS VAL VAL LYS VAL GLN ARG PRO THR PRO LYS          
SEQRES  46 D  905  GLY THR VAL MET ASP ILE ILE SER ARG LYS ASP GLN ARG          
SEQRES  47 D  905  GLY SER GLY GLN VAL GLY THR TYR GLY LEU ASN THR PHE          
SEQRES  48 D  905  THR ASN MET GLU ALA GLN LEU ILE ARG GLN MET GLU GLY          
SEQRES  49 D  905  GLU GLY VAL LEU SER LYS ALA ASP LEU GLU ASN PRO HIS          
SEQRES  50 D  905  PRO LEU GLU LYS LYS ILE THR GLN TRP LEU GLU THR LYS          
SEQRES  51 D  905  GLY VAL GLU ARG LEU LYS ARG MET ALA ILE SER GLY ASP          
SEQRES  52 D  905  ASP CYS VAL VAL LYS PRO ILE ASP ASP ARG PHE ALA ASN          
SEQRES  53 D  905  ALA LEU LEU ALA LEU ASN ASP MET GLY LYS VAL ARG LYS          
SEQRES  54 D  905  ASP ILE PRO GLN TRP GLN PRO SER LYS GLY TRP HIS ASP          
SEQRES  55 D  905  TRP GLN GLN VAL PRO PHE CYS SER HIS HIS PHE HIS GLU          
SEQRES  56 D  905  LEU ILE MET LYS ASP GLY ARG LYS LEU VAL VAL PRO CYS          
SEQRES  57 D  905  ARG PRO GLN ASP GLU LEU ILE GLY ARG ALA ARG ILE SER          
SEQRES  58 D  905  GLN GLY ALA GLY TRP SER LEU ARG GLU THR ALA CYS LEU          
SEQRES  59 D  905  GLY LYS ALA TYR ALA GLN MET TRP ALA LEU MET TYR PHE          
SEQRES  60 D  905  HIS ARG ARG ASP LEU ARG LEU ALA SER ASN ALA ILE CYS          
SEQRES  61 D  905  SER ALA VAL PRO VAL HIS TRP VAL PRO THR SER ARG THR          
SEQRES  62 D  905  THR HIS GLN TRP MET THR THR GLU ASP MET LEU THR VAL          
SEQRES  63 D  905  TRP ASN ARG VAL TRP ILE GLU ASP ASN PRO TRP MET GLU          
SEQRES  64 D  905  ASP LYS THR PRO VAL THR THR TRP GLU ASP VAL PRO TYR          
SEQRES  65 D  905  LEU GLY LYS ARG GLU ASP GLN TRP CYS GLY SER LEU ILE          
SEQRES  66 D  905  GLY LEU THR SER ARG ALA THR TRP ALA GLN ASN ILE LEU          
SEQRES  67 D  905  THR ALA ILE GLN GLN VAL ARG SER LEU ILE GLY ASN GLU          
SEQRES  68 D  905  GLU PHE LEU ASP TYR MET PRO SER MET LYS ARG PHE ARG          
SEQRES  69 D  905  LYS GLU GLU GLU SER GLU GLY ALA ILE TRP ALA ALA ALA          
SEQRES  70 D  905  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 E  905  GLY THR GLY SER GLN GLY GLU THR LEU GLY GLU LYS TRP          
SEQRES   2 E  905  LYS LYS LYS LEU ASN GLN LEU SER ARG LYS GLU PHE ASP          
SEQRES   3 E  905  LEU TYR LYS LYS SER GLY ILE THR GLU VAL ASP ARG THR          
SEQRES   4 E  905  GLU ALA LYS GLU GLY LEU LYS ARG GLY GLU ILE THR HIS          
SEQRES   5 E  905  HIS ALA VAL SER ARG GLY SER ALA LYS LEU GLN TRP PHE          
SEQRES   6 E  905  VAL GLU ARG ASN MET VAL ILE PRO GLU GLY ARG VAL ILE          
SEQRES   7 E  905  ASP LEU GLY CYS GLY ARG GLY GLY TRP SER TYR TYR CYS          
SEQRES   8 E  905  ALA GLY LEU LYS LYS VAL THR GLU VAL ARG GLY TYR THR          
SEQRES   9 E  905  LYS GLY GLY PRO GLY HIS GLU GLU PRO VAL PRO MET SER          
SEQRES  10 E  905  THR TYR GLY TRP ASN ILE VAL LYS LEU MET SER GLY LYS          
SEQRES  11 E  905  ASP VAL PHE TYR LEU PRO PRO GLU LYS CYS ASP THR LEU          
SEQRES  12 E  905  LEU CYS ASP ILE GLY GLU SER SER PRO SER PRO THR VAL          
SEQRES  13 E  905  GLU GLU SER ARG THR ILE ARG VAL LEU LYS MET VAL GLU          
SEQRES  14 E  905  PRO TRP LEU LYS ASN ASN GLN PHE CYS ILE LYS VAL LEU          
SEQRES  15 E  905  ASN PRO TYR MET PRO THR VAL ILE GLU HIS LEU GLU ARG          
SEQRES  16 E  905  LEU GLN ARG LYS HIS GLY GLY MET LEU VAL ARG ASN PRO          
SEQRES  17 E  905  LEU SER ARG ASN SER THR HIS GLU MET TYR TRP ILE SER          
SEQRES  18 E  905  ASN GLY THR GLY ASN ILE VAL SER SER VAL ASN MET VAL          
SEQRES  19 E  905  SER ARG LEU LEU LEU ASN ARG PHE THR MET THR HIS ARG          
SEQRES  20 E  905  ARG PRO THR ILE GLU LYS ASP VAL ASP LEU GLY ALA GLY          
SEQRES  21 E  905  THR ARG HIS VAL ASN ALA GLU PRO GLU THR PRO ASN MET          
SEQRES  22 E  905  ASP VAL ILE GLY GLU ARG ILE LYS ARG ILE LYS GLU GLU          
SEQRES  23 E  905  HIS SER SER THR TRP HIS TYR ASP ASP GLU ASN PRO TYR          
SEQRES  24 E  905  LYS THR TRP ALA TYR HIS GLY SER TYR GLU VAL LYS ALA          
SEQRES  25 E  905  THR GLY SER ALA SER SER MET ILE ASN GLY VAL VAL LYS          
SEQRES  26 E  905  LEU LEU THR LYS PRO TRP ASP VAL VAL PRO MET VAL THR          
SEQRES  27 E  905  GLN MET ALA MET THR ASP THR THR PRO PHE GLY GLN GLN          
SEQRES  28 E  905  ARG VAL PHE LYS GLU LYS VAL ASP THR ARG THR PRO ARG          
SEQRES  29 E  905  PRO MET PRO GLY THR ARG LYS VAL MET GLU ILE THR ALA          
SEQRES  30 E  905  GLU TRP LEU TRP ARG THR LEU GLY ARG ASN LYS ARG PRO          
SEQRES  31 E  905  ARG LEU CYS THR ARG GLU GLU PHE THR LYS LYS VAL ARG          
SEQRES  32 E  905  THR ASN ALA ALA MET GLY ALA VAL PHE THR GLU GLU ASN          
SEQRES  33 E  905  GLN TRP ASP SER ALA ARG ALA ALA VAL GLU ASP GLU GLU          
SEQRES  34 E  905  PHE TRP LYS LEU VAL ASP ARG GLU ARG GLU LEU HIS LYS          
SEQRES  35 E  905  LEU GLY LYS CYS GLY SER CYS VAL TYR ASN MET MET GLY          
SEQRES  36 E  905  LYS ARG GLU LYS LYS LEU GLY GLU PHE GLY LYS ALA LYS          
SEQRES  37 E  905  GLY SER ARG ALA ILE TRP TYR MET TRP LEU GLY ALA ARG          
SEQRES  38 E  905  TYR LEU GLU PHE GLU ALA LEU GLY PHE LEU ASN GLU ASP          
SEQRES  39 E  905  HIS TRP PHE SER ARG GLU ASN SER TYR SER GLY VAL GLU          
SEQRES  40 E  905  GLY GLU GLY LEU HIS LYS LEU GLY TYR ILE LEU ARG ASP          
SEQRES  41 E  905  ILE SER LYS ILE PRO GLY GLY ALA MET TYR ALA ASP ASP          
SEQRES  42 E  905  THR ALA GLY TRP ASP THR ARG ILE THR GLU ASP ASP LEU          
SEQRES  43 E  905  HIS ASN GLU GLU LYS ILE THR GLN GLN MET ASP PRO GLU          
SEQRES  44 E  905  HIS ARG GLN LEU ALA ASN ALA ILE PHE LYS LEU THR TYR          
SEQRES  45 E  905  GLN ASN LYS VAL VAL LYS VAL GLN ARG PRO THR PRO LYS          
SEQRES  46 E  905  GLY THR VAL MET ASP ILE ILE SER ARG LYS ASP GLN ARG          
SEQRES  47 E  905  GLY SER GLY GLN VAL GLY THR TYR GLY LEU ASN THR PHE          
SEQRES  48 E  905  THR ASN MET GLU ALA GLN LEU ILE ARG GLN MET GLU GLY          
SEQRES  49 E  905  GLU GLY VAL LEU SER LYS ALA ASP LEU GLU ASN PRO HIS          
SEQRES  50 E  905  PRO LEU GLU LYS LYS ILE THR GLN TRP LEU GLU THR LYS          
SEQRES  51 E  905  GLY VAL GLU ARG LEU LYS ARG MET ALA ILE SER GLY ASP          
SEQRES  52 E  905  ASP CYS VAL VAL LYS PRO ILE ASP ASP ARG PHE ALA ASN          
SEQRES  53 E  905  ALA LEU LEU ALA LEU ASN ASP MET GLY LYS VAL ARG LYS          
SEQRES  54 E  905  ASP ILE PRO GLN TRP GLN PRO SER LYS GLY TRP HIS ASP          
SEQRES  55 E  905  TRP GLN GLN VAL PRO PHE CYS SER HIS HIS PHE HIS GLU          
SEQRES  56 E  905  LEU ILE MET LYS ASP GLY ARG LYS LEU VAL VAL PRO CYS          
SEQRES  57 E  905  ARG PRO GLN ASP GLU LEU ILE GLY ARG ALA ARG ILE SER          
SEQRES  58 E  905  GLN GLY ALA GLY TRP SER LEU ARG GLU THR ALA CYS LEU          
SEQRES  59 E  905  GLY LYS ALA TYR ALA GLN MET TRP ALA LEU MET TYR PHE          
SEQRES  60 E  905  HIS ARG ARG ASP LEU ARG LEU ALA SER ASN ALA ILE CYS          
SEQRES  61 E  905  SER ALA VAL PRO VAL HIS TRP VAL PRO THR SER ARG THR          
SEQRES  62 E  905  THR HIS GLN TRP MET THR THR GLU ASP MET LEU THR VAL          
SEQRES  63 E  905  TRP ASN ARG VAL TRP ILE GLU ASP ASN PRO TRP MET GLU          
SEQRES  64 E  905  ASP LYS THR PRO VAL THR THR TRP GLU ASP VAL PRO TYR          
SEQRES  65 E  905  LEU GLY LYS ARG GLU ASP GLN TRP CYS GLY SER LEU ILE          
SEQRES  66 E  905  GLY LEU THR SER ARG ALA THR TRP ALA GLN ASN ILE LEU          
SEQRES  67 E  905  THR ALA ILE GLN GLN VAL ARG SER LEU ILE GLY ASN GLU          
SEQRES  68 E  905  GLU PHE LEU ASP TYR MET PRO SER MET LYS ARG PHE ARG          
SEQRES  69 E  905  LYS GLU GLU GLU SER GLU GLY ALA ILE TRP ALA ALA ALA          
SEQRES  70 E  905  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 F  905  GLY THR GLY SER GLN GLY GLU THR LEU GLY GLU LYS TRP          
SEQRES   2 F  905  LYS LYS LYS LEU ASN GLN LEU SER ARG LYS GLU PHE ASP          
SEQRES   3 F  905  LEU TYR LYS LYS SER GLY ILE THR GLU VAL ASP ARG THR          
SEQRES   4 F  905  GLU ALA LYS GLU GLY LEU LYS ARG GLY GLU ILE THR HIS          
SEQRES   5 F  905  HIS ALA VAL SER ARG GLY SER ALA LYS LEU GLN TRP PHE          
SEQRES   6 F  905  VAL GLU ARG ASN MET VAL ILE PRO GLU GLY ARG VAL ILE          
SEQRES   7 F  905  ASP LEU GLY CYS GLY ARG GLY GLY TRP SER TYR TYR CYS          
SEQRES   8 F  905  ALA GLY LEU LYS LYS VAL THR GLU VAL ARG GLY TYR THR          
SEQRES   9 F  905  LYS GLY GLY PRO GLY HIS GLU GLU PRO VAL PRO MET SER          
SEQRES  10 F  905  THR TYR GLY TRP ASN ILE VAL LYS LEU MET SER GLY LYS          
SEQRES  11 F  905  ASP VAL PHE TYR LEU PRO PRO GLU LYS CYS ASP THR LEU          
SEQRES  12 F  905  LEU CYS ASP ILE GLY GLU SER SER PRO SER PRO THR VAL          
SEQRES  13 F  905  GLU GLU SER ARG THR ILE ARG VAL LEU LYS MET VAL GLU          
SEQRES  14 F  905  PRO TRP LEU LYS ASN ASN GLN PHE CYS ILE LYS VAL LEU          
SEQRES  15 F  905  ASN PRO TYR MET PRO THR VAL ILE GLU HIS LEU GLU ARG          
SEQRES  16 F  905  LEU GLN ARG LYS HIS GLY GLY MET LEU VAL ARG ASN PRO          
SEQRES  17 F  905  LEU SER ARG ASN SER THR HIS GLU MET TYR TRP ILE SER          
SEQRES  18 F  905  ASN GLY THR GLY ASN ILE VAL SER SER VAL ASN MET VAL          
SEQRES  19 F  905  SER ARG LEU LEU LEU ASN ARG PHE THR MET THR HIS ARG          
SEQRES  20 F  905  ARG PRO THR ILE GLU LYS ASP VAL ASP LEU GLY ALA GLY          
SEQRES  21 F  905  THR ARG HIS VAL ASN ALA GLU PRO GLU THR PRO ASN MET          
SEQRES  22 F  905  ASP VAL ILE GLY GLU ARG ILE LYS ARG ILE LYS GLU GLU          
SEQRES  23 F  905  HIS SER SER THR TRP HIS TYR ASP ASP GLU ASN PRO TYR          
SEQRES  24 F  905  LYS THR TRP ALA TYR HIS GLY SER TYR GLU VAL LYS ALA          
SEQRES  25 F  905  THR GLY SER ALA SER SER MET ILE ASN GLY VAL VAL LYS          
SEQRES  26 F  905  LEU LEU THR LYS PRO TRP ASP VAL VAL PRO MET VAL THR          
SEQRES  27 F  905  GLN MET ALA MET THR ASP THR THR PRO PHE GLY GLN GLN          
SEQRES  28 F  905  ARG VAL PHE LYS GLU LYS VAL ASP THR ARG THR PRO ARG          
SEQRES  29 F  905  PRO MET PRO GLY THR ARG LYS VAL MET GLU ILE THR ALA          
SEQRES  30 F  905  GLU TRP LEU TRP ARG THR LEU GLY ARG ASN LYS ARG PRO          
SEQRES  31 F  905  ARG LEU CYS THR ARG GLU GLU PHE THR LYS LYS VAL ARG          
SEQRES  32 F  905  THR ASN ALA ALA MET GLY ALA VAL PHE THR GLU GLU ASN          
SEQRES  33 F  905  GLN TRP ASP SER ALA ARG ALA ALA VAL GLU ASP GLU GLU          
SEQRES  34 F  905  PHE TRP LYS LEU VAL ASP ARG GLU ARG GLU LEU HIS LYS          
SEQRES  35 F  905  LEU GLY LYS CYS GLY SER CYS VAL TYR ASN MET MET GLY          
SEQRES  36 F  905  LYS ARG GLU LYS LYS LEU GLY GLU PHE GLY LYS ALA LYS          
SEQRES  37 F  905  GLY SER ARG ALA ILE TRP TYR MET TRP LEU GLY ALA ARG          
SEQRES  38 F  905  TYR LEU GLU PHE GLU ALA LEU GLY PHE LEU ASN GLU ASP          
SEQRES  39 F  905  HIS TRP PHE SER ARG GLU ASN SER TYR SER GLY VAL GLU          
SEQRES  40 F  905  GLY GLU GLY LEU HIS LYS LEU GLY TYR ILE LEU ARG ASP          
SEQRES  41 F  905  ILE SER LYS ILE PRO GLY GLY ALA MET TYR ALA ASP ASP          
SEQRES  42 F  905  THR ALA GLY TRP ASP THR ARG ILE THR GLU ASP ASP LEU          
SEQRES  43 F  905  HIS ASN GLU GLU LYS ILE THR GLN GLN MET ASP PRO GLU          
SEQRES  44 F  905  HIS ARG GLN LEU ALA ASN ALA ILE PHE LYS LEU THR TYR          
SEQRES  45 F  905  GLN ASN LYS VAL VAL LYS VAL GLN ARG PRO THR PRO LYS          
SEQRES  46 F  905  GLY THR VAL MET ASP ILE ILE SER ARG LYS ASP GLN ARG          
SEQRES  47 F  905  GLY SER GLY GLN VAL GLY THR TYR GLY LEU ASN THR PHE          
SEQRES  48 F  905  THR ASN MET GLU ALA GLN LEU ILE ARG GLN MET GLU GLY          
SEQRES  49 F  905  GLU GLY VAL LEU SER LYS ALA ASP LEU GLU ASN PRO HIS          
SEQRES  50 F  905  PRO LEU GLU LYS LYS ILE THR GLN TRP LEU GLU THR LYS          
SEQRES  51 F  905  GLY VAL GLU ARG LEU LYS ARG MET ALA ILE SER GLY ASP          
SEQRES  52 F  905  ASP CYS VAL VAL LYS PRO ILE ASP ASP ARG PHE ALA ASN          
SEQRES  53 F  905  ALA LEU LEU ALA LEU ASN ASP MET GLY LYS VAL ARG LYS          
SEQRES  54 F  905  ASP ILE PRO GLN TRP GLN PRO SER LYS GLY TRP HIS ASP          
SEQRES  55 F  905  TRP GLN GLN VAL PRO PHE CYS SER HIS HIS PHE HIS GLU          
SEQRES  56 F  905  LEU ILE MET LYS ASP GLY ARG LYS LEU VAL VAL PRO CYS          
SEQRES  57 F  905  ARG PRO GLN ASP GLU LEU ILE GLY ARG ALA ARG ILE SER          
SEQRES  58 F  905  GLN GLY ALA GLY TRP SER LEU ARG GLU THR ALA CYS LEU          
SEQRES  59 F  905  GLY LYS ALA TYR ALA GLN MET TRP ALA LEU MET TYR PHE          
SEQRES  60 F  905  HIS ARG ARG ASP LEU ARG LEU ALA SER ASN ALA ILE CYS          
SEQRES  61 F  905  SER ALA VAL PRO VAL HIS TRP VAL PRO THR SER ARG THR          
SEQRES  62 F  905  THR HIS GLN TRP MET THR THR GLU ASP MET LEU THR VAL          
SEQRES  63 F  905  TRP ASN ARG VAL TRP ILE GLU ASP ASN PRO TRP MET GLU          
SEQRES  64 F  905  ASP LYS THR PRO VAL THR THR TRP GLU ASP VAL PRO TYR          
SEQRES  65 F  905  LEU GLY LYS ARG GLU ASP GLN TRP CYS GLY SER LEU ILE          
SEQRES  66 F  905  GLY LEU THR SER ARG ALA THR TRP ALA GLN ASN ILE LEU          
SEQRES  67 F  905  THR ALA ILE GLN GLN VAL ARG SER LEU ILE GLY ASN GLU          
SEQRES  68 F  905  GLU PHE LEU ASP TYR MET PRO SER MET LYS ARG PHE ARG          
SEQRES  69 F  905  LYS GLU GLU GLU SER GLU GLY ALA ILE TRP ALA ALA ALA          
SEQRES  70 F  905  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 G  905  GLY THR GLY SER GLN GLY GLU THR LEU GLY GLU LYS TRP          
SEQRES   2 G  905  LYS LYS LYS LEU ASN GLN LEU SER ARG LYS GLU PHE ASP          
SEQRES   3 G  905  LEU TYR LYS LYS SER GLY ILE THR GLU VAL ASP ARG THR          
SEQRES   4 G  905  GLU ALA LYS GLU GLY LEU LYS ARG GLY GLU ILE THR HIS          
SEQRES   5 G  905  HIS ALA VAL SER ARG GLY SER ALA LYS LEU GLN TRP PHE          
SEQRES   6 G  905  VAL GLU ARG ASN MET VAL ILE PRO GLU GLY ARG VAL ILE          
SEQRES   7 G  905  ASP LEU GLY CYS GLY ARG GLY GLY TRP SER TYR TYR CYS          
SEQRES   8 G  905  ALA GLY LEU LYS LYS VAL THR GLU VAL ARG GLY TYR THR          
SEQRES   9 G  905  LYS GLY GLY PRO GLY HIS GLU GLU PRO VAL PRO MET SER          
SEQRES  10 G  905  THR TYR GLY TRP ASN ILE VAL LYS LEU MET SER GLY LYS          
SEQRES  11 G  905  ASP VAL PHE TYR LEU PRO PRO GLU LYS CYS ASP THR LEU          
SEQRES  12 G  905  LEU CYS ASP ILE GLY GLU SER SER PRO SER PRO THR VAL          
SEQRES  13 G  905  GLU GLU SER ARG THR ILE ARG VAL LEU LYS MET VAL GLU          
SEQRES  14 G  905  PRO TRP LEU LYS ASN ASN GLN PHE CYS ILE LYS VAL LEU          
SEQRES  15 G  905  ASN PRO TYR MET PRO THR VAL ILE GLU HIS LEU GLU ARG          
SEQRES  16 G  905  LEU GLN ARG LYS HIS GLY GLY MET LEU VAL ARG ASN PRO          
SEQRES  17 G  905  LEU SER ARG ASN SER THR HIS GLU MET TYR TRP ILE SER          
SEQRES  18 G  905  ASN GLY THR GLY ASN ILE VAL SER SER VAL ASN MET VAL          
SEQRES  19 G  905  SER ARG LEU LEU LEU ASN ARG PHE THR MET THR HIS ARG          
SEQRES  20 G  905  ARG PRO THR ILE GLU LYS ASP VAL ASP LEU GLY ALA GLY          
SEQRES  21 G  905  THR ARG HIS VAL ASN ALA GLU PRO GLU THR PRO ASN MET          
SEQRES  22 G  905  ASP VAL ILE GLY GLU ARG ILE LYS ARG ILE LYS GLU GLU          
SEQRES  23 G  905  HIS SER SER THR TRP HIS TYR ASP ASP GLU ASN PRO TYR          
SEQRES  24 G  905  LYS THR TRP ALA TYR HIS GLY SER TYR GLU VAL LYS ALA          
SEQRES  25 G  905  THR GLY SER ALA SER SER MET ILE ASN GLY VAL VAL LYS          
SEQRES  26 G  905  LEU LEU THR LYS PRO TRP ASP VAL VAL PRO MET VAL THR          
SEQRES  27 G  905  GLN MET ALA MET THR ASP THR THR PRO PHE GLY GLN GLN          
SEQRES  28 G  905  ARG VAL PHE LYS GLU LYS VAL ASP THR ARG THR PRO ARG          
SEQRES  29 G  905  PRO MET PRO GLY THR ARG LYS VAL MET GLU ILE THR ALA          
SEQRES  30 G  905  GLU TRP LEU TRP ARG THR LEU GLY ARG ASN LYS ARG PRO          
SEQRES  31 G  905  ARG LEU CYS THR ARG GLU GLU PHE THR LYS LYS VAL ARG          
SEQRES  32 G  905  THR ASN ALA ALA MET GLY ALA VAL PHE THR GLU GLU ASN          
SEQRES  33 G  905  GLN TRP ASP SER ALA ARG ALA ALA VAL GLU ASP GLU GLU          
SEQRES  34 G  905  PHE TRP LYS LEU VAL ASP ARG GLU ARG GLU LEU HIS LYS          
SEQRES  35 G  905  LEU GLY LYS CYS GLY SER CYS VAL TYR ASN MET MET GLY          
SEQRES  36 G  905  LYS ARG GLU LYS LYS LEU GLY GLU PHE GLY LYS ALA LYS          
SEQRES  37 G  905  GLY SER ARG ALA ILE TRP TYR MET TRP LEU GLY ALA ARG          
SEQRES  38 G  905  TYR LEU GLU PHE GLU ALA LEU GLY PHE LEU ASN GLU ASP          
SEQRES  39 G  905  HIS TRP PHE SER ARG GLU ASN SER TYR SER GLY VAL GLU          
SEQRES  40 G  905  GLY GLU GLY LEU HIS LYS LEU GLY TYR ILE LEU ARG ASP          
SEQRES  41 G  905  ILE SER LYS ILE PRO GLY GLY ALA MET TYR ALA ASP ASP          
SEQRES  42 G  905  THR ALA GLY TRP ASP THR ARG ILE THR GLU ASP ASP LEU          
SEQRES  43 G  905  HIS ASN GLU GLU LYS ILE THR GLN GLN MET ASP PRO GLU          
SEQRES  44 G  905  HIS ARG GLN LEU ALA ASN ALA ILE PHE LYS LEU THR TYR          
SEQRES  45 G  905  GLN ASN LYS VAL VAL LYS VAL GLN ARG PRO THR PRO LYS          
SEQRES  46 G  905  GLY THR VAL MET ASP ILE ILE SER ARG LYS ASP GLN ARG          
SEQRES  47 G  905  GLY SER GLY GLN VAL GLY THR TYR GLY LEU ASN THR PHE          
SEQRES  48 G  905  THR ASN MET GLU ALA GLN LEU ILE ARG GLN MET GLU GLY          
SEQRES  49 G  905  GLU GLY VAL LEU SER LYS ALA ASP LEU GLU ASN PRO HIS          
SEQRES  50 G  905  PRO LEU GLU LYS LYS ILE THR GLN TRP LEU GLU THR LYS          
SEQRES  51 G  905  GLY VAL GLU ARG LEU LYS ARG MET ALA ILE SER GLY ASP          
SEQRES  52 G  905  ASP CYS VAL VAL LYS PRO ILE ASP ASP ARG PHE ALA ASN          
SEQRES  53 G  905  ALA LEU LEU ALA LEU ASN ASP MET GLY LYS VAL ARG LYS          
SEQRES  54 G  905  ASP ILE PRO GLN TRP GLN PRO SER LYS GLY TRP HIS ASP          
SEQRES  55 G  905  TRP GLN GLN VAL PRO PHE CYS SER HIS HIS PHE HIS GLU          
SEQRES  56 G  905  LEU ILE MET LYS ASP GLY ARG LYS LEU VAL VAL PRO CYS          
SEQRES  57 G  905  ARG PRO GLN ASP GLU LEU ILE GLY ARG ALA ARG ILE SER          
SEQRES  58 G  905  GLN GLY ALA GLY TRP SER LEU ARG GLU THR ALA CYS LEU          
SEQRES  59 G  905  GLY LYS ALA TYR ALA GLN MET TRP ALA LEU MET TYR PHE          
SEQRES  60 G  905  HIS ARG ARG ASP LEU ARG LEU ALA SER ASN ALA ILE CYS          
SEQRES  61 G  905  SER ALA VAL PRO VAL HIS TRP VAL PRO THR SER ARG THR          
SEQRES  62 G  905  THR HIS GLN TRP MET THR THR GLU ASP MET LEU THR VAL          
SEQRES  63 G  905  TRP ASN ARG VAL TRP ILE GLU ASP ASN PRO TRP MET GLU          
SEQRES  64 G  905  ASP LYS THR PRO VAL THR THR TRP GLU ASP VAL PRO TYR          
SEQRES  65 G  905  LEU GLY LYS ARG GLU ASP GLN TRP CYS GLY SER LEU ILE          
SEQRES  66 G  905  GLY LEU THR SER ARG ALA THR TRP ALA GLN ASN ILE LEU          
SEQRES  67 G  905  THR ALA ILE GLN GLN VAL ARG SER LEU ILE GLY ASN GLU          
SEQRES  68 G  905  GLU PHE LEU ASP TYR MET PRO SER MET LYS ARG PHE ARG          
SEQRES  69 G  905  LYS GLU GLU GLU SER GLU GLY ALA ILE TRP ALA ALA ALA          
SEQRES  70 G  905  LEU GLU HIS HIS HIS HIS HIS HIS                              
SEQRES   1 H  905  GLY THR GLY SER GLN GLY GLU THR LEU GLY GLU LYS TRP          
SEQRES   2 H  905  LYS LYS LYS LEU ASN GLN LEU SER ARG LYS GLU PHE ASP          
SEQRES   3 H  905  LEU TYR LYS LYS SER GLY ILE THR GLU VAL ASP ARG THR          
SEQRES   4 H  905  GLU ALA LYS GLU GLY LEU LYS ARG GLY GLU ILE THR HIS          
SEQRES   5 H  905  HIS ALA VAL SER ARG GLY SER ALA LYS LEU GLN TRP PHE          
SEQRES   6 H  905  VAL GLU ARG ASN MET VAL ILE PRO GLU GLY ARG VAL ILE          
SEQRES   7 H  905  ASP LEU GLY CYS GLY ARG GLY GLY TRP SER TYR TYR CYS          
SEQRES   8 H  905  ALA GLY LEU LYS LYS VAL THR GLU VAL ARG GLY TYR THR          
SEQRES   9 H  905  LYS GLY GLY PRO GLY HIS GLU GLU PRO VAL PRO MET SER          
SEQRES  10 H  905  THR TYR GLY TRP ASN ILE VAL LYS LEU MET SER GLY LYS          
SEQRES  11 H  905  ASP VAL PHE TYR LEU PRO PRO GLU LYS CYS ASP THR LEU          
SEQRES  12 H  905  LEU CYS ASP ILE GLY GLU SER SER PRO SER PRO THR VAL          
SEQRES  13 H  905  GLU GLU SER ARG THR ILE ARG VAL LEU LYS MET VAL GLU          
SEQRES  14 H  905  PRO TRP LEU LYS ASN ASN GLN PHE CYS ILE LYS VAL LEU          
SEQRES  15 H  905  ASN PRO TYR MET PRO THR VAL ILE GLU HIS LEU GLU ARG          
SEQRES  16 H  905  LEU GLN ARG LYS HIS GLY GLY MET LEU VAL ARG ASN PRO          
SEQRES  17 H  905  LEU SER ARG ASN SER THR HIS GLU MET TYR TRP ILE SER          
SEQRES  18 H  905  ASN GLY THR GLY ASN ILE VAL SER SER VAL ASN MET VAL          
SEQRES  19 H  905  SER ARG LEU LEU LEU ASN ARG PHE THR MET THR HIS ARG          
SEQRES  20 H  905  ARG PRO THR ILE GLU LYS ASP VAL ASP LEU GLY ALA GLY          
SEQRES  21 H  905  THR ARG HIS VAL ASN ALA GLU PRO GLU THR PRO ASN MET          
SEQRES  22 H  905  ASP VAL ILE GLY GLU ARG ILE LYS ARG ILE LYS GLU GLU          
SEQRES  23 H  905  HIS SER SER THR TRP HIS TYR ASP ASP GLU ASN PRO TYR          
SEQRES  24 H  905  LYS THR TRP ALA TYR HIS GLY SER TYR GLU VAL LYS ALA          
SEQRES  25 H  905  THR GLY SER ALA SER SER MET ILE ASN GLY VAL VAL LYS          
SEQRES  26 H  905  LEU LEU THR LYS PRO TRP ASP VAL VAL PRO MET VAL THR          
SEQRES  27 H  905  GLN MET ALA MET THR ASP THR THR PRO PHE GLY GLN GLN          
SEQRES  28 H  905  ARG VAL PHE LYS GLU LYS VAL ASP THR ARG THR PRO ARG          
SEQRES  29 H  905  PRO MET PRO GLY THR ARG LYS VAL MET GLU ILE THR ALA          
SEQRES  30 H  905  GLU TRP LEU TRP ARG THR LEU GLY ARG ASN LYS ARG PRO          
SEQRES  31 H  905  ARG LEU CYS THR ARG GLU GLU PHE THR LYS LYS VAL ARG          
SEQRES  32 H  905  THR ASN ALA ALA MET GLY ALA VAL PHE THR GLU GLU ASN          
SEQRES  33 H  905  GLN TRP ASP SER ALA ARG ALA ALA VAL GLU ASP GLU GLU          
SEQRES  34 H  905  PHE TRP LYS LEU VAL ASP ARG GLU ARG GLU LEU HIS LYS          
SEQRES  35 H  905  LEU GLY LYS CYS GLY SER CYS VAL TYR ASN MET MET GLY          
SEQRES  36 H  905  LYS ARG GLU LYS LYS LEU GLY GLU PHE GLY LYS ALA LYS          
SEQRES  37 H  905  GLY SER ARG ALA ILE TRP TYR MET TRP LEU GLY ALA ARG          
SEQRES  38 H  905  TYR LEU GLU PHE GLU ALA LEU GLY PHE LEU ASN GLU ASP          
SEQRES  39 H  905  HIS TRP PHE SER ARG GLU ASN SER TYR SER GLY VAL GLU          
SEQRES  40 H  905  GLY GLU GLY LEU HIS LYS LEU GLY TYR ILE LEU ARG ASP          
SEQRES  41 H  905  ILE SER LYS ILE PRO GLY GLY ALA MET TYR ALA ASP ASP          
SEQRES  42 H  905  THR ALA GLY TRP ASP THR ARG ILE THR GLU ASP ASP LEU          
SEQRES  43 H  905  HIS ASN GLU GLU LYS ILE THR GLN GLN MET ASP PRO GLU          
SEQRES  44 H  905  HIS ARG GLN LEU ALA ASN ALA ILE PHE LYS LEU THR TYR          
SEQRES  45 H  905  GLN ASN LYS VAL VAL LYS VAL GLN ARG PRO THR PRO LYS          
SEQRES  46 H  905  GLY THR VAL MET ASP ILE ILE SER ARG LYS ASP GLN ARG          
SEQRES  47 H  905  GLY SER GLY GLN VAL GLY THR TYR GLY LEU ASN THR PHE          
SEQRES  48 H  905  THR ASN MET GLU ALA GLN LEU ILE ARG GLN MET GLU GLY          
SEQRES  49 H  905  GLU GLY VAL LEU SER LYS ALA ASP LEU GLU ASN PRO HIS          
SEQRES  50 H  905  PRO LEU GLU LYS LYS ILE THR GLN TRP LEU GLU THR LYS          
SEQRES  51 H  905  GLY VAL GLU ARG LEU LYS ARG MET ALA ILE SER GLY ASP          
SEQRES  52 H  905  ASP CYS VAL VAL LYS PRO ILE ASP ASP ARG PHE ALA ASN          
SEQRES  53 H  905  ALA LEU LEU ALA LEU ASN ASP MET GLY LYS VAL ARG LYS          
SEQRES  54 H  905  ASP ILE PRO GLN TRP GLN PRO SER LYS GLY TRP HIS ASP          
SEQRES  55 H  905  TRP GLN GLN VAL PRO PHE CYS SER HIS HIS PHE HIS GLU          
SEQRES  56 H  905  LEU ILE MET LYS ASP GLY ARG LYS LEU VAL VAL PRO CYS          
SEQRES  57 H  905  ARG PRO GLN ASP GLU LEU ILE GLY ARG ALA ARG ILE SER          
SEQRES  58 H  905  GLN GLY ALA GLY TRP SER LEU ARG GLU THR ALA CYS LEU          
SEQRES  59 H  905  GLY LYS ALA TYR ALA GLN MET TRP ALA LEU MET TYR PHE          
SEQRES  60 H  905  HIS ARG ARG ASP LEU ARG LEU ALA SER ASN ALA ILE CYS          
SEQRES  61 H  905  SER ALA VAL PRO VAL HIS TRP VAL PRO THR SER ARG THR          
SEQRES  62 H  905  THR HIS GLN TRP MET THR THR GLU ASP MET LEU THR VAL          
SEQRES  63 H  905  TRP ASN ARG VAL TRP ILE GLU ASP ASN PRO TRP MET GLU          
SEQRES  64 H  905  ASP LYS THR PRO VAL THR THR TRP GLU ASP VAL PRO TYR          
SEQRES  65 H  905  LEU GLY LYS ARG GLU ASP GLN TRP CYS GLY SER LEU ILE          
SEQRES  66 H  905  GLY LEU THR SER ARG ALA THR TRP ALA GLN ASN ILE LEU          
SEQRES  67 H  905  THR ALA ILE GLN GLN VAL ARG SER LEU ILE GLY ASN GLU          
SEQRES  68 H  905  GLU PHE LEU ASP TYR MET PRO SER MET LYS ARG PHE ARG          
SEQRES  69 H  905  LYS GLU GLU GLU SER GLU GLY ALA ILE TRP ALA ALA ALA          
SEQRES  70 H  905  LEU GLU HIS HIS HIS HIS HIS HIS                              
HET     ZN  A1001       1                                                       
HET     ZN  A1002       1                                                       
HET    SAH  A1003      26                                                       
HET     ZN  B1001       1                                                       
HET     ZN  B1002       1                                                       
HET    SAH  B1003      26                                                       
HET     ZN  C1001       1                                                       
HET     ZN  C1002       1                                                       
HET    SAH  C1003      26                                                       
HET     ZN  D1001       1                                                       
HET     ZN  D1002       1                                                       
HET    SAH  D1003      26                                                       
HET     ZN  E1001       1                                                       
HET     ZN  E1002       1                                                       
HET    SAH  E1003      26                                                       
HET     ZN  F1001       1                                                       
HET     ZN  F1002       1                                                       
HET    SAH  F1003      26                                                       
HET     ZN  G1001       1                                                       
HET     ZN  G1002       1                                                       
HET    SAH  G1003      26                                                       
HET     ZN  H1001       1                                                       
HET     ZN  H1002       1                                                       
HET    SAH  H1003      26                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
FORMUL   9   ZN    16(ZN 2+)                                                    
FORMUL  11  SAH    8(C14 H20 N6 O5 S)                                           
HELIX    1 AA1 THR A    8  LEU A   20  1                                  13    
HELIX    2 AA2 SER A   21  LYS A   30  1                                  10    
HELIX    3 AA3 ARG A   38  GLY A   48  1                                  11    
HELIX    4 AA4 ARG A   57  GLU A   67  1                                  11    
HELIX    5 AA5 GLY A   85  GLY A   93  1                                   9    
HELIX    6 AA6 GLY A  120  ASN A  122  5                                   3    
HELIX    7 AA7 ASP A  131  LEU A  135  5                                   5    
HELIX    8 AA8 SER A  153  GLU A  169  1                                  17    
HELIX    9 AA9 MET A  186  GLY A  201  1                                  16    
HELIX   10 AB1 ASN A  226  ARG A  241  1                                  16    
HELIX   11 AB2 ILE A  276  HIS A  287  1                                  12    
HELIX   12 AB3 ASN A  321  LEU A  326  1                                   6    
HELIX   13 AB4 THR A  328  VAL A  333  5                                   6    
HELIX   14 AB5 VAL A  334  MET A  340  1                                   7    
HELIX   15 AB6 THR A  346  LYS A  357  1                                  12    
HELIX   16 AB7 MET A  366  GLY A  385  1                                  20    
HELIX   17 AB8 THR A  394  THR A  404  1                                  11    
HELIX   18 AB9 ASP A  427  LEU A  443  1                                  17    
HELIX   19 AC1 GLY A  479  GLY A  489  1                                  11    
HELIX   20 AC2 GLY A  489  ASP A  494  1                                   6    
HELIX   21 AC3 SER A  498  TYR A  503  1                                   6    
HELIX   22 AC4 GLY A  510  LYS A  523  1                                  14    
HELIX   23 AC5 GLY A  536  ILE A  541  5                                   6    
HELIX   24 AC6 THR A  542  GLU A  550  1                                   9    
HELIX   25 AC7 LYS A  551  MET A  556  5                                   6    
HELIX   26 AC8 ASP A  557  THR A  571  1                                  15    
HELIX   27 AC9 GLY A  604  GLY A  626  1                                  23    
HELIX   28 AD1 SER A  629  ASN A  635  1                                   7    
HELIX   29 AD2 GLU A  640  LYS A  650  1                                  11    
HELIX   30 AD3 LYS A  650  ARG A  657  1                                   8    
HELIX   31 AD4 ASP A  671  ALA A  677  5                                   7    
HELIX   32 AD5 LEU A  678  MET A  684  1                                   7    
HELIX   33 AD6 ASP A  702  VAL A  706  5                                   5    
HELIX   34 AD7 PRO A  730  ARG A  739  1                                  10    
HELIX   35 AD8 SER A  747  TYR A  766  1                                  20    
HELIX   36 AD9 ARG A  769  VAL A  783  1                                  15    
HELIX   37 AE1 ASP A  808  ILE A  818  1                                  11    
HELIX   38 AE2 GLY A  840  CYS A  847  1                                   8    
HELIX   39 AE3 LEU A  853  ASN A  862  1                                  10    
HELIX   40 AE4 ASN A  862  GLY A  875  1                                  14    
HELIX   41 AE5 TYR A  882  SER A  885  5                                   4    
HELIX   42 AE6 MET A  886  SER A  895  1                                  10    
HELIX   43 AE7 SER A  895  TRP A  900  1                                   6    
HELIX   44 AE8 THR B    8  LEU B   20  1                                  13    
HELIX   45 AE9 SER B   21  LYS B   29  1                                   9    
HELIX   46 AF1 ARG B   38  GLY B   48  1                                  11    
HELIX   47 AF2 ARG B   57  GLU B   67  1                                  11    
HELIX   48 AF3 GLY B   85  GLY B   93  1                                   9    
HELIX   49 AF4 GLY B  120  ASN B  122  5                                   3    
HELIX   50 AF5 ASP B  131  LEU B  135  5                                   5    
HELIX   51 AF6 SER B  153  LYS B  166  1                                  14    
HELIX   52 AF7 MET B  186  GLY B  201  1                                  16    
HELIX   53 AF8 ASN B  226  ASN B  240  1                                  15    
HELIX   54 AF9 ASN B  272  HIS B  287  1                                  16    
HELIX   55 AG1 ASN B  321  THR B  328  1                                   8    
HELIX   56 AG2 LYS B  329  VAL B  333  5                                   5    
HELIX   57 AG3 VAL B  334  MET B  340  1                                   7    
HELIX   58 AG4 THR B  346  LYS B  355  1                                  10    
HELIX   59 AG5 MET B  366  GLY B  385  1                                  20    
HELIX   60 AG6 THR B  394  VAL B  402  1                                   9    
HELIX   61 AG7 SER B  420  ASP B  427  1                                   8    
HELIX   62 AG8 ASP B  427  LEU B  443  1                                  17    
HELIX   63 AG9 TRP B  477  GLY B  489  1                                  13    
HELIX   64 AH1 GLY B  489  ASP B  494  1                                   6    
HELIX   65 AH2 SER B  498  TYR B  503  1                                   6    
HELIX   66 AH3 GLY B  510  ILE B  524  1                                  15    
HELIX   67 AH4 GLY B  536  ARG B  540  5                                   5    
HELIX   68 AH5 THR B  542  GLU B  550  1                                   9    
HELIX   69 AH6 LYS B  551  MET B  556  5                                   6    
HELIX   70 AH7 ASP B  557  THR B  571  1                                  15    
HELIX   71 AH8 GLY B  604  GLU B  625  1                                  22    
HELIX   72 AH9 SER B  629  ASN B  635  1                                   7    
HELIX   73 AI1 LEU B  639  LYS B  650  1                                  12    
HELIX   74 AI2 LYS B  650  LYS B  656  1                                   7    
HELIX   75 AI3 ASP B  671  ASN B  676  5                                   6    
HELIX   76 AI4 LEU B  678  MET B  684  1                                   7    
HELIX   77 AI5 ASP B  702  VAL B  706  5                                   5    
HELIX   78 AI6 PRO B  730  ARG B  739  1                                  10    
HELIX   79 AI7 SER B  747  MET B  765  1                                  19    
HELIX   80 AI8 ARG B  769  VAL B  783  1                                  15    
HELIX   81 AI9 ASP B  808  ILE B  818  1                                  11    
HELIX   82 AJ1 THR B  832  VAL B  836  5                                   5    
HELIX   83 AJ2 GLY B  840  CYS B  847  1                                   8    
HELIX   84 AJ3 LEU B  853  ASN B  862  1                                  10    
HELIX   85 AJ4 ASN B  862  GLY B  875  1                                  14    
HELIX   86 AJ5 THR C    8  GLN C   19  1                                  12    
HELIX   87 AJ6 GLU C   24  LYS C   29  1                                   6    
HELIX   88 AJ7 ARG C   38  GLY C   48  1                                  11    
HELIX   89 AJ8 ARG C   57  GLU C   67  1                                  11    
HELIX   90 AJ9 GLY C   85  GLY C   93  1                                   9    
HELIX   91 AK1 GLY C  120  ASN C  122  5                                   3    
HELIX   92 AK2 ASP C  131  LEU C  135  5                                   5    
HELIX   93 AK3 SER C  153  GLU C  169  1                                  17    
HELIX   94 AK4 MET C  186  HIS C  200  1                                  15    
HELIX   95 AK5 ASN C  226  ARG C  241  1                                  16    
HELIX   96 AK6 ASN C  272  HIS C  287  1                                  16    
HELIX   97 AK7 ASN C  321  LEU C  326  1                                   6    
HELIX   98 AK8 LYS C  329  VAL C  333  5                                   5    
HELIX   99 AK9 VAL C  334  MET C  340  1                                   7    
HELIX  100 AL1 THR C  346  LYS C  357  1                                  12    
HELIX  101 AL2 MET C  366  GLY C  385  1                                  20    
HELIX  102 AL3 THR C  394  VAL C  402  1                                   9    
HELIX  103 AL4 SER C  420  ASP C  427  1                                   8    
HELIX  104 AL5 ASP C  427  LYS C  442  1                                  16    
HELIX  105 AL6 TRP C  477  GLY C  489  1                                  13    
HELIX  106 AL7 GLY C  489  ASP C  494  1                                   6    
HELIX  107 AL8 SER C  498  TYR C  503  1                                   6    
HELIX  108 AL9 GLY C  510  ILE C  524  1                                  15    
HELIX  109 AM1 GLY C  536  ILE C  541  1                                   6    
HELIX  110 AM2 THR C  542  GLU C  550  1                                   9    
HELIX  111 AM3 LYS C  551  MET C  556  5                                   6    
HELIX  112 AM4 ASP C  557  TYR C  572  1                                  16    
HELIX  113 AM5 GLY C  604  GLU C  625  1                                  22    
HELIX  114 AM6 SER C  629  ASN C  635  1                                   7    
HELIX  115 AM7 LEU C  639  ARG C  657  1                                  19    
HELIX  116 AM8 ASP C  671  ALA C  677  5                                   7    
HELIX  117 AM9 LEU C  678  MET C  684  1                                   7    
HELIX  118 AN1 ASP C  702  VAL C  706  5                                   5    
HELIX  119 AN2 PRO C  730  ARG C  739  1                                  10    
HELIX  120 AN3 SER C  747  MET C  765  1                                  19    
HELIX  121 AN4 ARG C  769  VAL C  783  1                                  15    
HELIX  122 AN5 ASP C  808  ILE C  818  1                                  11    
HELIX  123 AN6 THR C  832  VAL C  836  5                                   5    
HELIX  124 AN7 GLY C  840  CYS C  847  1                                   8    
HELIX  125 AN8 LEU C  853  ASN C  862  1                                  10    
HELIX  126 AN9 ASN C  862  GLY C  875  1                                  14    
HELIX  127 AO1 THR D    8  LEU D   17  1                                  10    
HELIX  128 AO2 SER D   21  LYS D   30  1                                  10    
HELIX  129 AO3 ARG D   38  ARG D   47  1                                  10    
HELIX  130 AO4 ARG D   57  GLU D   67  1                                  11    
HELIX  131 AO5 GLY D   85  ALA D   92  1                                   8    
HELIX  132 AO6 GLY D  120  ASN D  122  5                                   3    
HELIX  133 AO7 ASP D  131  LEU D  135  5                                   5    
HELIX  134 AO8 SER D  153  GLU D  169  1                                  17    
HELIX  135 AO9 MET D  186  GLY D  201  1                                  16    
HELIX  136 AP1 ASN D  226  ARG D  241  1                                  16    
HELIX  137 AP2 HIS D  263  GLU D  267  5                                   5    
HELIX  138 AP3 ILE D  276  HIS D  287  1                                  12    
HELIX  139 AP4 ASN D  321  THR D  328  1                                   8    
HELIX  140 AP5 LYS D  329  VAL D  333  5                                   5    
HELIX  141 AP6 VAL D  334  MET D  340  1                                   7    
HELIX  142 AP7 THR D  346  LYS D  357  1                                  12    
HELIX  143 AP8 MET D  366  GLY D  385  1                                  20    
HELIX  144 AP9 THR D  394  ALA D  406  1                                  13    
HELIX  145 AQ1 ALA D  421  ASP D  427  1                                   7    
HELIX  146 AQ2 ASP D  427  LYS D  442  1                                  16    
HELIX  147 AQ3 MET D  476  GLY D  489  1                                  14    
HELIX  148 AQ4 GLY D  489  ASP D  494  1                                   6    
HELIX  149 AQ5 SER D  498  TYR D  503  1                                   6    
HELIX  150 AQ6 GLY D  510  ILE D  524  1                                  15    
HELIX  151 AQ7 GLY D  536  ILE D  541  1                                   6    
HELIX  152 AQ8 THR D  542  GLU D  550  1                                   9    
HELIX  153 AQ9 LYS D  551  MET D  556  5                                   6    
HELIX  154 AR1 ASP D  557  TYR D  572  1                                  16    
HELIX  155 AR2 GLY D  604  GLY D  626  1                                  23    
HELIX  156 AR3 GLU D  640  LYS D  650  1                                  11    
HELIX  157 AR4 LYS D  650  LYS D  656  1                                   7    
HELIX  158 AR5 ASP D  671  ALA D  675  5                                   5    
HELIX  159 AR6 LEU D  678  MET D  684  1                                   7    
HELIX  160 AR7 ASP D  702  VAL D  706  5                                   5    
HELIX  161 AR8 PRO D  730  ARG D  739  1                                  10    
HELIX  162 AR9 SER D  747  MET D  765  1                                  19    
HELIX  163 AS1 ARG D  769  VAL D  783  1                                  15    
HELIX  164 AS2 ASP D  808  ILE D  818  1                                  11    
HELIX  165 AS3 GLY D  840  CYS D  847  1                                   8    
HELIX  166 AS4 LEU D  853  ASN D  862  1                                  10    
HELIX  167 AS5 ASN D  862  GLY D  875  1                                  14    
HELIX  168 AS6 TYR D  882  MET D  886  5                                   5    
HELIX  169 AS7 LYS D  887  GLU D  896  1                                  10    
HELIX  170 AS8 THR E    8  LEU E   20  1                                  13    
HELIX  171 AS9 SER E   21  LYS E   30  1                                  10    
HELIX  172 AT1 ARG E   38  GLY E   48  1                                  11    
HELIX  173 AT2 ARG E   57  GLU E   67  1                                  11    
HELIX  174 AT3 GLY E   85  GLY E   93  1                                   9    
HELIX  175 AT4 GLY E  120  ASN E  122  5                                   3    
HELIX  176 AT5 ASP E  131  LEU E  135  5                                   5    
HELIX  177 AT6 SER E  153  GLU E  169  1                                  17    
HELIX  178 AT7 MET E  186  HIS E  200  1                                  15    
HELIX  179 AT8 ASN E  226  MET E  244  1                                  19    
HELIX  180 AT9 HIS E  263  GLU E  267  5                                   5    
HELIX  181 AU1 ILE E  276  HIS E  287  1                                  12    
HELIX  182 AU2 ASN E  321  THR E  328  1                                   8    
HELIX  183 AU3 LYS E  329  VAL E  333  5                                   5    
HELIX  184 AU4 VAL E  334  MET E  340  1                                   7    
HELIX  185 AU5 THR E  346  LYS E  357  1                                  12    
HELIX  186 AU6 MET E  366  GLY E  385  1                                  20    
HELIX  187 AU7 THR E  394  VAL E  402  1                                   9    
HELIX  188 AU8 THR E  413  TRP E  418  5                                   6    
HELIX  189 AU9 SER E  420  VAL E  425  1                                   6    
HELIX  190 AV1 ASP E  427  LEU E  443  1                                  17    
HELIX  191 AV2 TRP E  477  GLY E  489  1                                  13    
HELIX  192 AV3 GLY E  489  ASP E  494  1                                   6    
HELIX  193 AV4 GLY E  510  HIS E  512  5                                   3    
HELIX  194 AV5 LYS E  513  LYS E  523  1                                  11    
HELIX  195 AV6 GLY E  536  ARG E  540  5                                   5    
HELIX  196 AV7 THR E  542  GLU E  550  1                                   9    
HELIX  197 AV8 LYS E  551  MET E  556  5                                   6    
HELIX  198 AV9 ASP E  557  TYR E  572  1                                  16    
HELIX  199 AW1 GLY E  604  GLU E  625  1                                  22    
HELIX  200 AW2 SER E  629  ASN E  635  1                                   7    
HELIX  201 AW3 LEU E  639  LYS E  650  1                                  12    
HELIX  202 AW4 LYS E  650  LYS E  656  1                                   7    
HELIX  203 AW5 ASP E  672  ALA E  677  1                                   6    
HELIX  204 AW6 LEU E  678  MET E  684  1                                   7    
HELIX  205 AW7 ASP E  702  VAL E  706  5                                   5    
HELIX  206 AW8 PRO E  730  ARG E  739  1                                  10    
HELIX  207 AW9 SER E  747  ALA E  763  1                                  17    
HELIX  208 AX1 ARG E  769  VAL E  783  1                                  15    
HELIX  209 AX2 ASP E  808  ILE E  818  1                                  11    
HELIX  210 AX3 GLY E  840  CYS E  847  1                                   8    
HELIX  211 AX4 LEU E  853  ALA E  860  1                                   8    
HELIX  212 AX5 ASN E  862  GLY E  875  1                                  14    
HELIX  213 AX6 THR F    8  LEU F   20  1                                  13    
HELIX  214 AX7 SER F   21  LYS F   29  1                                   9    
HELIX  215 AX8 GLU F   40  GLY F   48  1                                   9    
HELIX  216 AX9 ARG F   57  ARG F   68  1                                  12    
HELIX  217 AY1 GLY F   85  GLY F   93  1                                   9    
HELIX  218 AY2 GLY F  120  ASN F  122  5                                   3    
HELIX  219 AY3 ASP F  131  LEU F  135  5                                   5    
HELIX  220 AY4 SER F  153  GLU F  169  1                                  17    
HELIX  221 AY5 MET F  186  GLY F  201  1                                  16    
HELIX  222 AY6 ASN F  226  MET F  244  1                                  19    
HELIX  223 AY7 ASN F  272  HIS F  287  1                                  16    
HELIX  224 AY8 ASN F  321  THR F  328  1                                   8    
HELIX  225 AY9 LYS F  329  VAL F  333  5                                   5    
HELIX  226 AZ1 VAL F  334  MET F  340  1                                   7    
HELIX  227 AZ2 THR F  346  LYS F  357  1                                  12    
HELIX  228 AZ3 MET F  366  GLY F  385  1                                  20    
HELIX  229 AZ4 THR F  394  THR F  404  1                                  11    
HELIX  230 AZ5 ALA F  421  VAL F  425  1                                   5    
HELIX  231 AZ6 ASP F  427  LEU F  443  1                                  17    
HELIX  232 AZ7 TRP F  477  GLY F  489  1                                  13    
HELIX  233 AZ8 GLY F  489  ASP F  494  1                                   6    
HELIX  234 AZ9 SER F  498  TYR F  503  1                                   6    
HELIX  235 BA1 GLY F  510  ILE F  524  1                                  15    
HELIX  236 BA2 GLY F  536  ARG F  540  5                                   5    
HELIX  237 BA3 THR F  542  GLU F  550  1                                   9    
HELIX  238 BA4 LYS F  551  MET F  556  5                                   6    
HELIX  239 BA5 ASP F  557  THR F  571  1                                  15    
HELIX  240 BA6 GLY F  604  GLY F  626  1                                  23    
HELIX  241 BA7 SER F  629  ASN F  635  1                                   7    
HELIX  242 BA8 LEU F  639  LYS F  650  1                                  12    
HELIX  243 BA9 LYS F  650  LYS F  656  1                                   7    
HELIX  244 BB1 ASP F  671  ALA F  677  5                                   7    
HELIX  245 BB2 LEU F  678  MET F  684  1                                   7    
HELIX  246 BB3 ASP F  702  VAL F  706  5                                   5    
HELIX  247 BB4 PRO F  730  ARG F  739  1                                  10    
HELIX  248 BB5 SER F  747  MET F  765  1                                  19    
HELIX  249 BB6 ARG F  769  VAL F  783  1                                  15    
HELIX  250 BB7 ASP F  808  ILE F  818  1                                  11    
HELIX  251 BB8 GLY F  840  CYS F  847  1                                   8    
HELIX  252 BB9 LEU F  853  ASN F  862  1                                  10    
HELIX  253 BC1 ASN F  862  GLY F  875  1                                  14    
HELIX  254 BC2 TYR F  882  MET F  886  5                                   5    
HELIX  255 BC3 ARG F  890  GLU F  896  1                                   7    
HELIX  256 BC4 LYS G   12  LEU G   20  1                                   9    
HELIX  257 BC5 SER G   21  LYS G   29  1                                   9    
HELIX  258 BC6 ARG G   38  GLY G   48  1                                  11    
HELIX  259 BC7 ARG G   57  GLU G   67  1                                  11    
HELIX  260 BC8 GLY G   85  GLY G   93  1                                   9    
HELIX  261 BC9 GLY G  120  ASN G  122  5                                   3    
HELIX  262 BD1 ASP G  131  LEU G  135  5                                   5    
HELIX  263 BD2 SER G  153  GLU G  169  1                                  17    
HELIX  264 BD3 PRO G  170  LEU G  172  5                                   3    
HELIX  265 BD4 MET G  186  GLY G  201  1                                  16    
HELIX  266 BD5 ASN G  226  ARG G  241  1                                  16    
HELIX  267 BD6 HIS G  263  GLU G  267  5                                   5    
HELIX  268 BD7 ILE G  276  HIS G  287  1                                  12    
HELIX  269 BD8 ASN G  321  THR G  328  1                                   8    
HELIX  270 BD9 LYS G  329  VAL G  333  5                                   5    
HELIX  271 BE1 VAL G  334  MET G  340  1                                   7    
HELIX  272 BE2 THR G  346  LYS G  357  1                                  12    
HELIX  273 BE3 MET G  366  GLY G  385  1                                  20    
HELIX  274 BE4 THR G  394  THR G  404  1                                  11    
HELIX  275 BE5 ARG G  422  ASP G  427  1                                   6    
HELIX  276 BE6 ASP G  427  LYS G  442  1                                  16    
HELIX  277 BE7 TRP G  477  GLY G  489  1                                  13    
HELIX  278 BE8 GLY G  489  ASP G  494  1                                   6    
HELIX  279 BE9 SER G  498  TYR G  503  1                                   6    
HELIX  280 BF1 GLY G  510  LYS G  523  1                                  14    
HELIX  281 BF2 GLY G  536  ILE G  541  5                                   6    
HELIX  282 BF3 THR G  542  GLU G  550  1                                   9    
HELIX  283 BF4 LYS G  551  MET G  556  5                                   6    
HELIX  284 BF5 ASP G  557  THR G  571  1                                  15    
HELIX  285 BF6 GLY G  604  GLU G  625  1                                  22    
HELIX  286 BF7 SER G  629  ASN G  635  1                                   7    
HELIX  287 BF8 GLU G  640  LYS G  650  1                                  11    
HELIX  288 BF9 LYS G  650  ARG G  657  1                                   8    
HELIX  289 BG1 ASP G  671  ASN G  676  5                                   6    
HELIX  290 BG2 LEU G  678  MET G  684  1                                   7    
HELIX  291 BG3 ASP G  702  VAL G  706  5                                   5    
HELIX  292 BG4 PRO G  730  ARG G  739  1                                  10    
HELIX  293 BG5 SER G  747  MET G  765  1                                  19    
HELIX  294 BG6 ARG G  769  VAL G  783  1                                  15    
HELIX  295 BG7 ASP G  808  ILE G  818  1                                  11    
HELIX  296 BG8 GLY G  840  CYS G  847  1                                   8    
HELIX  297 BG9 LEU G  853  ASN G  862  1                                  10    
HELIX  298 BH1 ASN G  862  GLY G  875  1                                  14    
HELIX  299 BH2 MET G  886  GLY G  897  1                                  12    
HELIX  300 BH3 GLY H   10  LEU H   17  1                                   8    
HELIX  301 BH4 SER H   21  TYR H   28  1                                   8    
HELIX  302 BH5 ARG H   38  LYS H   46  1                                   9    
HELIX  303 BH6 ARG H   57  ARG H   68  1                                  12    
HELIX  304 BH7 GLY H   85  ALA H   92  1                                   8    
HELIX  305 BH8 GLY H  120  ASN H  122  5                                   3    
HELIX  306 BH9 SER H  153  GLU H  169  1                                  17    
HELIX  307 BI1 PRO H  170  LEU H  172  5                                   3    
HELIX  308 BI2 MET H  186  ARG H  195  1                                  10    
HELIX  309 BI3 ILE H  227  MET H  244  1                                  18    
HELIX  310 BI4 HIS H  263  GLU H  267  5                                   5    
HELIX  311 BI5 ILE H  276  HIS H  287  1                                  12    
HELIX  312 BI6 VAL H  323  THR H  328  1                                   6    
HELIX  313 BI7 LYS H  329  VAL H  334  5                                   6    
HELIX  314 BI8 THR H  346  LYS H  355  1                                  10    
HELIX  315 BI9 MET H  366  GLY H  385  1                                  20    
HELIX  316 BJ1 THR H  394  THR H  399  1                                   6    
HELIX  317 BJ2 ALA H  421  ASP H  427  1                                   7    
HELIX  318 BJ3 GLU H  429  GLY H  444  1                                  16    
HELIX  319 BJ4 ALA H  480  GLU H  486  1                                   7    
HELIX  320 BJ5 LYS H  513  SER H  522  1                                  10    
HELIX  321 BJ6 GLY H  536  ILE H  541  1                                   6    
HELIX  322 BJ7 THR H  542  GLU H  550  1                                   9    
HELIX  323 BJ8 LYS H  551  GLN H  554  5                                   4    
HELIX  324 BJ9 PRO H  558  LEU H  570  1                                  13    
HELIX  325 BK1 GLY H  604  GLU H  625  1                                  22    
HELIX  326 BK2 SER H  629  ASN H  635  1                                   7    
HELIX  327 BK3 LEU H  639  LYS H  650  1                                  12    
HELIX  328 BK4 LYS H  650  LYS H  656  1                                   7    
HELIX  329 BK5 ASP H  671  ALA H  675  5                                   5    
HELIX  330 BK6 LEU H  678  MET H  684  1                                   7    
HELIX  331 BK7 ASP H  702  VAL H  706  5                                   5    
HELIX  332 BK8 PRO H  730  ILE H  735  1                                   6    
HELIX  333 BK9 LEU H  748  MET H  765  1                                  18    
HELIX  334 BL1 ARG H  769  ALA H  782  1                                  14    
HELIX  335 BL2 ASP H  808  TRP H  817  1                                  10    
HELIX  336 BL3 THR H  832  VAL H  836  5                                   5    
HELIX  337 BL4 GLY H  840  CYS H  847  1                                   8    
HELIX  338 BL5 LEU H  853  ASN H  862  1                                  10    
HELIX  339 BL6 ASN H  862  VAL H  870  1                                   9    
SHEET    1 AA1 2 THR A  34  VAL A  36  0                                        
SHEET    2 AA1 2 THR A 250  GLU A 252  1  O  THR A 250   N  GLU A  35           
SHEET    1 AA2 7 VAL A 124  SER A 128  0                                        
SHEET    2 AA2 7 VAL A  97  THR A 104  1  N  GLY A 102   O  LYS A 125           
SHEET    3 AA2 7 GLY A  75  LEU A  80  1  N  VAL A  77   O  ARG A 101           
SHEET    4 AA2 7 THR A 142  CYS A 145  1  O  LEU A 144   N  ILE A  78           
SHEET    5 AA2 7 GLN A 176  VAL A 181  1  O  GLN A 176   N  LEU A 143           
SHEET    6 AA2 7 MET A 217  ILE A 220 -1  O  MET A 217   N  VAL A 181           
SHEET    7 AA2 7 MET A 203  VAL A 205 -1  N  VAL A 205   O  TYR A 218           
SHEET    1 AA3 4 ALA A 303  VAL A 310  0                                        
SHEET    2 AA3 4 GLY A 586  ARG A 594 -1  O  THR A 587   N  VAL A 310           
SHEET    3 AA3 4 LYS A 575  THR A 583 -1  N  THR A 583   O  GLY A 586           
SHEET    4 AA3 4 TYR A 451  ASN A 452  1  N  TYR A 451   O  VAL A 576           
SHEET    1 AA4 2 MET A 658  SER A 661  0                                        
SHEET    2 AA4 2 ASP A 664  VAL A 667 -1  O  ASP A 664   N  SER A 661           
SHEET    1 AA5 2 HIS A 712  ILE A 717  0                                        
SHEET    2 AA5 2 LYS A 723  CYS A 728 -1  O  CYS A 728   N  HIS A 712           
SHEET    1 AA6 2 THR B  34  VAL B  36  0                                        
SHEET    2 AA6 2 THR B 250  GLU B 252  1  O  THR B 250   N  GLU B  35           
SHEET    1 AA7 7 VAL B 124  SER B 128  0                                        
SHEET    2 AA7 7 VAL B  97  THR B 104  1  N  VAL B 100   O  LYS B 125           
SHEET    3 AA7 7 GLY B  75  LEU B  80  1  N  VAL B  77   O  ARG B 101           
SHEET    4 AA7 7 THR B 142  CYS B 145  1  O  LEU B 144   N  LEU B  80           
SHEET    5 AA7 7 GLN B 176  VAL B 181  1  O  LYS B 180   N  CYS B 145           
SHEET    6 AA7 7 MET B 217  ILE B 220 -1  O  MET B 217   N  VAL B 181           
SHEET    7 AA7 7 MET B 203  VAL B 205 -1  N  VAL B 205   O  TYR B 218           
SHEET    1 AA8 4 ALA B 303  GLU B 309  0                                        
SHEET    2 AA8 4 THR B 587  ARG B 594 -1  O  ILE B 591   N  HIS B 305           
SHEET    3 AA8 4 LYS B 575  PRO B 582 -1  N  ARG B 581   O  VAL B 588           
SHEET    4 AA8 4 TYR B 451  ASN B 452  1  N  TYR B 451   O  VAL B 576           
SHEET    1 AA9 2 MET B 319  ILE B 320  0                                        
SHEET    2 AA9 2 ILE B 740  SER B 741 -1  O  SER B 741   N  MET B 319           
SHEET    1 AB1 2 MET B 658  SER B 661  0                                        
SHEET    2 AB1 2 ASP B 664  VAL B 667 -1  O  ASP B 664   N  SER B 661           
SHEET    1 AB2 2 HIS B 712  ILE B 717  0                                        
SHEET    2 AB2 2 LYS B 723  CYS B 728 -1  O  LEU B 724   N  LEU B 716           
SHEET    1 AB3 2 THR C  34  VAL C  36  0                                        
SHEET    2 AB3 2 THR C 250  GLU C 252  1  O  THR C 250   N  GLU C  35           
SHEET    1 AB4 7 VAL C 124  MET C 127  0                                        
SHEET    2 AB4 7 VAL C  97  TYR C 103  1  N  GLY C 102   O  LYS C 125           
SHEET    3 AB4 7 GLY C  75  LEU C  80  1  N  VAL C  77   O  ARG C 101           
SHEET    4 AB4 7 THR C 142  CYS C 145  1  O  LEU C 144   N  ILE C  78           
SHEET    5 AB4 7 GLN C 176  VAL C 181  1  O  LYS C 180   N  CYS C 145           
SHEET    6 AB4 7 MET C 217  ILE C 220 -1  O  MET C 217   N  VAL C 181           
SHEET    7 AB4 7 MET C 203  VAL C 205 -1  N  VAL C 205   O  TYR C 218           
SHEET    1 AB5 5 TRP C 291  HIS C 292  0                                        
SHEET    2 AB5 5 GLY C 306  GLU C 309 -1  O  SER C 307   N  HIS C 292           
SHEET    3 AB5 5 THR C 587  ARG C 594 -1  O  MET C 589   N  TYR C 308           
SHEET    4 AB5 5 LYS C 575  PRO C 582 -1  N  ARG C 581   O  VAL C 588           
SHEET    5 AB5 5 TYR C 451  ASN C 452  1  N  TYR C 451   O  VAL C 576           
SHEET    1 AB6 2 MET C 319  ILE C 320  0                                        
SHEET    2 AB6 2 ILE C 740  SER C 741 -1  O  SER C 741   N  MET C 319           
SHEET    1 AB7 2 MET C 658  SER C 661  0                                        
SHEET    2 AB7 2 ASP C 664  VAL C 667 -1  O  ASP C 664   N  SER C 661           
SHEET    1 AB8 2 HIS C 712  ILE C 717  0                                        
SHEET    2 AB8 2 LYS C 723  CYS C 728 -1  O  LEU C 724   N  LEU C 716           
SHEET    1 AB9 2 THR D  34  VAL D  36  0                                        
SHEET    2 AB9 2 THR D 250  GLU D 252  1  O  THR D 250   N  GLU D  35           
SHEET    1 AC1 7 VAL D 124  MET D 127  0                                        
SHEET    2 AC1 7 VAL D  97  TYR D 103  1  N  GLY D 102   O  MET D 127           
SHEET    3 AC1 7 GLY D  75  LEU D  80  1  N  VAL D  77   O  ARG D 101           
SHEET    4 AC1 7 THR D 142  CYS D 145  1  O  LEU D 144   N  ILE D  78           
SHEET    5 AC1 7 GLN D 176  VAL D 181  1  O  LYS D 180   N  CYS D 145           
SHEET    6 AC1 7 MET D 217  ILE D 220 -1  O  MET D 217   N  VAL D 181           
SHEET    7 AC1 7 MET D 203  VAL D 205 -1  N  VAL D 205   O  TYR D 218           
SHEET    1 AC2 4 GLY D 306  GLU D 309  0                                        
SHEET    2 AC2 4 GLY D 586  ARG D 594 -1  O  MET D 589   N  TYR D 308           
SHEET    3 AC2 4 LYS D 575  THR D 583 -1  N  THR D 583   O  GLY D 586           
SHEET    4 AC2 4 VAL D 450  ASN D 452  1  N  TYR D 451   O  VAL D 576           
SHEET    1 AC3 2 MET D 658  SER D 661  0                                        
SHEET    2 AC3 2 ASP D 664  VAL D 667 -1  O  ASP D 664   N  SER D 661           
SHEET    1 AC4 2 HIS D 712  ILE D 717  0                                        
SHEET    2 AC4 2 LYS D 723  CYS D 728 -1  O  LEU D 724   N  LEU D 716           
SHEET    1 AC5 2 THR E  34  VAL E  36  0                                        
SHEET    2 AC5 2 THR E 250  GLU E 252  1  O  THR E 250   N  GLU E  35           
SHEET    1 AC6 7 VAL E 124  MET E 127  0                                        
SHEET    2 AC6 7 VAL E  97  TYR E 103  1  N  GLY E 102   O  LYS E 125           
SHEET    3 AC6 7 GLY E  75  LEU E  80  1  N  VAL E  77   O  ARG E 101           
SHEET    4 AC6 7 THR E 142  CYS E 145  1  O  LEU E 144   N  LEU E  80           
SHEET    5 AC6 7 GLN E 176  VAL E 181  1  O  LYS E 180   N  CYS E 145           
SHEET    6 AC6 7 MET E 217  ILE E 220 -1  O  MET E 217   N  VAL E 181           
SHEET    7 AC6 7 MET E 203  VAL E 205 -1  N  VAL E 205   O  TYR E 218           
SHEET    1 AC7 3 ALA E 303  VAL E 310  0                                        
SHEET    2 AC7 3 GLY E 586  ARG E 594 -1  O  MET E 589   N  TYR E 308           
SHEET    3 AC7 3 LYS E 575  THR E 583 -1  N  THR E 583   O  GLY E 586           
SHEET    1 AC8 2 MET E 658  SER E 661  0                                        
SHEET    2 AC8 2 ASP E 664  VAL E 667 -1  O  ASP E 664   N  SER E 661           
SHEET    1 AC9 2 HIS E 712  ILE E 717  0                                        
SHEET    2 AC9 2 LYS E 723  CYS E 728 -1  O  LEU E 724   N  LEU E 716           
SHEET    1 AD1 2 THR F  34  VAL F  36  0                                        
SHEET    2 AD1 2 THR F 250  GLU F 252  1  O  GLU F 252   N  GLU F  35           
SHEET    1 AD2 7 VAL F 124  MET F 127  0                                        
SHEET    2 AD2 7 VAL F  97  TYR F 103  1  N  GLY F 102   O  LYS F 125           
SHEET    3 AD2 7 GLY F  75  LEU F  80  1  N  VAL F  77   O  GLU F  99           
SHEET    4 AD2 7 THR F 142  CYS F 145  1  O  LEU F 144   N  ILE F  78           
SHEET    5 AD2 7 GLN F 176  VAL F 181  1  O  GLN F 176   N  LEU F 143           
SHEET    6 AD2 7 MET F 217  ILE F 220 -1  O  MET F 217   N  VAL F 181           
SHEET    7 AD2 7 MET F 203  VAL F 205 -1  N  VAL F 205   O  TYR F 218           
SHEET    1 AD3 4 ALA F 303  GLU F 309  0                                        
SHEET    2 AD3 4 THR F 587  ARG F 594 -1  O  MET F 589   N  TYR F 308           
SHEET    3 AD3 4 LYS F 575  PRO F 582 -1  N  ARG F 581   O  VAL F 588           
SHEET    4 AD3 4 TYR F 451  ASN F 452  1  N  TYR F 451   O  LYS F 578           
SHEET    1 AD4 2 MET F 658  SER F 661  0                                        
SHEET    2 AD4 2 ASP F 664  VAL F 667 -1  O  VAL F 666   N  ALA F 659           
SHEET    1 AD5 2 HIS F 712  ILE F 717  0                                        
SHEET    2 AD5 2 LYS F 723  CYS F 728 -1  O  LEU F 724   N  LEU F 716           
SHEET    1 AD6 2 THR G  34  VAL G  36  0                                        
SHEET    2 AD6 2 THR G 250  GLU G 252  1  O  GLU G 252   N  GLU G  35           
SHEET    1 AD7 7 VAL G 124  MET G 127  0                                        
SHEET    2 AD7 7 VAL G  97  TYR G 103  1  N  GLY G 102   O  LYS G 125           
SHEET    3 AD7 7 GLY G  75  LEU G  80  1  N  ASP G  79   O  ARG G 101           
SHEET    4 AD7 7 THR G 142  CYS G 145  1  O  LEU G 144   N  LEU G  80           
SHEET    5 AD7 7 GLN G 176  VAL G 181  1  O  GLN G 176   N  LEU G 143           
SHEET    6 AD7 7 MET G 217  ILE G 220 -1  O  MET G 217   N  VAL G 181           
SHEET    7 AD7 7 MET G 203  VAL G 205 -1  N  VAL G 205   O  TYR G 218           
SHEET    1 AD8 4 ALA G 303  GLU G 309  0                                        
SHEET    2 AD8 4 THR G 587  ARG G 594 -1  O  MET G 589   N  TYR G 308           
SHEET    3 AD8 4 LYS G 575  PRO G 582 -1  N  VAL G 579   O  ASP G 590           
SHEET    4 AD8 4 TYR G 451  ASN G 452  1  N  TYR G 451   O  VAL G 576           
SHEET    1 AD9 2 MET G 658  SER G 661  0                                        
SHEET    2 AD9 2 ASP G 664  VAL G 667 -1  O  ASP G 664   N  SER G 661           
SHEET    1 AE1 2 HIS G 712  ILE G 717  0                                        
SHEET    2 AE1 2 LYS G 723  CYS G 728 -1  O  LEU G 724   N  LEU G 716           
SHEET    1 AE2 2 THR H  34  VAL H  36  0                                        
SHEET    2 AE2 2 THR H 250  GLU H 252  1  O  GLU H 252   N  GLU H  35           
SHEET    1 AE3 7 VAL H 124  MET H 127  0                                        
SHEET    2 AE3 7 VAL H  97  TYR H 103  1  N  GLY H 102   O  MET H 127           
SHEET    3 AE3 7 GLY H  75  LEU H  80  1  N  VAL H  77   O  GLU H  99           
SHEET    4 AE3 7 THR H 142  CYS H 145  1  O  LEU H 144   N  ILE H  78           
SHEET    5 AE3 7 GLN H 176  VAL H 181  1  O  GLN H 176   N  LEU H 143           
SHEET    6 AE3 7 MET H 217  ILE H 220 -1  O  TRP H 219   N  ILE H 179           
SHEET    7 AE3 7 MET H 203  VAL H 205 -1  N  VAL H 205   O  TYR H 218           
SHEET    1 AE4 3 ALA H 303  GLU H 309  0                                        
SHEET    2 AE4 3 THR H 587  ARG H 594 -1  O  MET H 589   N  TYR H 308           
SHEET    3 AE4 3 LYS H 575  PRO H 582 -1  N  ARG H 581   O  VAL H 588           
SHEET    1 AE5 2 MET H 658  SER H 661  0                                        
SHEET    2 AE5 2 ASP H 664  VAL H 667 -1  O  ASP H 664   N  SER H 661           
SHEET    1 AE6 2 HIS H 712  ILE H 717  0                                        
SHEET    2 AE6 2 LYS H 723  CYS H 728 -1  O  CYS H 728   N  HIS H 712           
LINK         OE1 GLU A 437                ZN    ZN A1002     1555   1555  2.07  
LINK         NE2 HIS A 441                ZN    ZN A1002     1555   1555  2.14  
LINK         SG  CYS A 446                ZN    ZN A1002     1555   1555  2.40  
LINK         SG  CYS A 449                ZN    ZN A1002     1555   1555  2.39  
LINK         NE2 HIS A 712                ZN    ZN A1001     1555   1555  2.00  
LINK         NE2 HIS A 714                ZN    ZN A1001     1555   1555  2.15  
LINK         SG  CYS A 728                ZN    ZN A1001     1555   1555  2.28  
LINK         SG  CYS A 847                ZN    ZN A1001     1555   1555  2.36  
LINK         OE1 GLU B 437                ZN    ZN B1001     1555   1555  2.04  
LINK         NE2 HIS B 441                ZN    ZN B1001     1555   1555  2.18  
LINK         SG  CYS B 446                ZN    ZN B1001     1555   1555  2.33  
LINK         SG  CYS B 449                ZN    ZN B1001     1555   1555  2.25  
LINK         NE2 HIS B 712                ZN    ZN B1002     1555   1555  1.97  
LINK         NE2 HIS B 714                ZN    ZN B1002     1555   1555  2.09  
LINK         SG  CYS B 728                ZN    ZN B1002     1555   1555  2.24  
LINK         SG  CYS B 847                ZN    ZN B1002     1555   1555  2.35  
LINK         OE1 GLU C 437                ZN    ZN C1001     1555   1555  2.10  
LINK         NE2 HIS C 441                ZN    ZN C1001     1555   1555  2.08  
LINK         SG  CYS C 446                ZN    ZN C1001     1555   1555  2.24  
LINK         SG  CYS C 449                ZN    ZN C1001     1555   1555  2.21  
LINK         NE2 HIS C 712                ZN    ZN C1002     1555   1555  2.07  
LINK         NE2 HIS C 714                ZN    ZN C1002     1555   1555  2.06  
LINK         SG  CYS C 728                ZN    ZN C1002     1555   1555  2.23  
LINK         SG  CYS C 847                ZN    ZN C1002     1555   1555  2.38  
LINK         OE1 GLU D 437                ZN    ZN D1001     1555   1555  2.11  
LINK         NE2 HIS D 441                ZN    ZN D1001     1555   1555  2.05  
LINK         SG  CYS D 446                ZN    ZN D1001     1555   1555  2.35  
LINK         SG  CYS D 449                ZN    ZN D1001     1555   1555  2.30  
LINK         NE2 HIS D 712                ZN    ZN D1002     1555   1555  1.99  
LINK         NE2 HIS D 714                ZN    ZN D1002     1555   1555  2.13  
LINK         SG  CYS D 728                ZN    ZN D1002     1555   1555  2.26  
LINK         SG  CYS D 847                ZN    ZN D1002     1555   1555  2.39  
LINK         OE1 GLU E 437                ZN    ZN E1001     1555   1555  2.10  
LINK         NE2 HIS E 441                ZN    ZN E1001     1555   1555  2.04  
LINK         SG  CYS E 446                ZN    ZN E1001     1555   1555  2.41  
LINK         SG  CYS E 449                ZN    ZN E1001     1555   1555  2.34  
LINK         NE2 HIS E 712                ZN    ZN E1002     1555   1555  2.09  
LINK         NE2 HIS E 714                ZN    ZN E1002     1555   1555  2.09  
LINK         SG  CYS E 728                ZN    ZN E1002     1555   1555  2.38  
LINK         SG  CYS E 847                ZN    ZN E1002     1555   1555  2.42  
LINK         OE1 GLU F 437                ZN    ZN F1002     1555   1555  2.19  
LINK         NE2 HIS F 441                ZN    ZN F1002     1555   1555  2.10  
LINK         SG  CYS F 446                ZN    ZN F1002     1555   1555  2.27  
LINK         SG  CYS F 449                ZN    ZN F1002     1555   1555  2.24  
LINK         NE2 HIS F 712                ZN    ZN F1001     1555   1555  1.93  
LINK         NE2 HIS F 714                ZN    ZN F1001     1555   1555  2.07  
LINK         SG  CYS F 728                ZN    ZN F1001     1555   1555  2.18  
LINK         SG  CYS F 847                ZN    ZN F1001     1555   1555  2.45  
LINK         OE1 GLU G 437                ZN    ZN G1001     1555   1555  2.01  
LINK         NE2 HIS G 441                ZN    ZN G1001     1555   1555  2.06  
LINK         SG  CYS G 446                ZN    ZN G1001     1555   1555  2.32  
LINK         SG  CYS G 449                ZN    ZN G1001     1555   1555  2.26  
LINK         NE2 HIS G 712                ZN    ZN G1002     1555   1555  2.13  
LINK         NE2 HIS G 714                ZN    ZN G1002     1555   1555  2.06  
LINK         SG  CYS G 728                ZN    ZN G1002     1555   1555  2.25  
LINK         SG  CYS G 847                ZN    ZN G1002     1555   1555  2.34  
LINK         NE2 HIS H 441                ZN    ZN H1002     1555   1555  2.31  
LINK         SG  CYS H 446                ZN    ZN H1002     1555   1555  2.44  
LINK         SG  CYS H 449                ZN    ZN H1002     1555   1555  2.51  
LINK         NE2 HIS H 712                ZN    ZN H1001     1555   1555  2.36  
LINK         NE2 HIS H 714                ZN    ZN H1001     1555   1555  2.19  
LINK         SG  CYS H 728                ZN    ZN H1001     1555   1555  2.40  
LINK         SG  CYS H 847                ZN    ZN H1001     1555   1555  2.38  
SITE     1 AC1  4 HIS A 712  HIS A 714  CYS A 728  CYS A 847                    
SITE     1 AC2  5 GLU A 437  HIS A 441  CYS A 446  GLY A 447                    
SITE     2 AC2  5 CYS A 449                                                     
SITE     1 AC3 17 SER A  56  GLY A  58  GLY A  81  CYS A  82                    
SITE     2 AC3 17 GLY A  83  ARG A  84  GLY A  85  GLY A  86                    
SITE     3 AC3 17 TRP A  87  THR A 104  LYS A 105  HIS A 110                    
SITE     4 AC3 17 LYS A 130  ASP A 131  VAL A 132  PHE A 133                    
SITE     5 AC3 17 ASP A 146                                                     
SITE     1 AC4  4 GLU B 437  HIS B 441  CYS B 446  CYS B 449                    
SITE     1 AC5  4 HIS B 712  HIS B 714  CYS B 728  CYS B 847                    
SITE     1 AC6 15 SER B  56  GLY B  58  GLY B  81  CYS B  82                    
SITE     2 AC6 15 GLY B  83  GLY B  86  TRP B  87  LYS B 105                    
SITE     3 AC6 15 HIS B 110  GLU B 111  LYS B 130  ASP B 131                    
SITE     4 AC6 15 VAL B 132  PHE B 133  ASP B 146                               
SITE     1 AC7  4 GLU C 437  HIS C 441  CYS C 446  CYS C 449                    
SITE     1 AC8  4 HIS C 712  HIS C 714  CYS C 728  CYS C 847                    
SITE     1 AC9 15 SER C  56  GLY C  58  GLY C  81  CYS C  82                    
SITE     2 AC9 15 GLY C  83  GLY C  86  TRP C  87  THR C 104                    
SITE     3 AC9 15 LYS C 105  HIS C 110  GLU C 111  LYS C 130                    
SITE     4 AC9 15 ASP C 131  VAL C 132  ASP C 146                               
SITE     1 AD1  5 GLU D 437  HIS D 441  CYS D 446  GLY D 447                    
SITE     2 AD1  5 CYS D 449                                                     
SITE     1 AD2  4 HIS D 712  HIS D 714  CYS D 728  CYS D 847                    
SITE     1 AD3 16 SER D  56  GLY D  58  GLY D  81  CYS D  82                    
SITE     2 AD3 16 GLY D  83  GLY D  86  TRP D  87  THR D 104                    
SITE     3 AD3 16 LYS D 105  HIS D 110  GLU D 111  LYS D 130                    
SITE     4 AD3 16 ASP D 131  VAL D 132  PHE D 133  ASP D 146                    
SITE     1 AD4  5 GLU E 437  HIS E 441  CYS E 446  GLY E 447                    
SITE     2 AD4  5 CYS E 449                                                     
SITE     1 AD5  4 HIS E 712  HIS E 714  CYS E 728  CYS E 847                    
SITE     1 AD6 14 SER E  56  GLY E  58  GLY E  81  CYS E  82                    
SITE     2 AD6 14 GLY E  83  GLY E  86  TRP E  87  LYS E 105                    
SITE     3 AD6 14 HIS E 110  LYS E 130  ASP E 131  VAL E 132                    
SITE     4 AD6 14 PHE E 133  ASP E 146                                          
SITE     1 AD7  4 HIS F 712  HIS F 714  CYS F 728  CYS F 847                    
SITE     1 AD8  4 GLU F 437  HIS F 441  CYS F 446  CYS F 449                    
SITE     1 AD9 15 SER F  56  GLY F  58  GLY F  81  CYS F  82                    
SITE     2 AD9 15 GLY F  83  GLY F  86  TRP F  87  THR F 104                    
SITE     3 AD9 15 LYS F 105  HIS F 110  LYS F 130  ASP F 131                    
SITE     4 AD9 15 VAL F 132  PHE F 133  ASP F 146                               
SITE     1 AE1  4 GLU G 437  HIS G 441  CYS G 446  CYS G 449                    
SITE     1 AE2  4 HIS G 712  HIS G 714  CYS G 728  CYS G 847                    
SITE     1 AE3 18 SER G  56  GLY G  58  GLY G  81  CYS G  82                    
SITE     2 AE3 18 GLY G  83  GLY G  85  GLY G  86  TRP G  87                    
SITE     3 AE3 18 THR G 104  LYS G 105  HIS G 110  GLU G 111                    
SITE     4 AE3 18 LYS G 130  ASP G 131  VAL G 132  PHE G 133                    
SITE     5 AE3 18 ASP G 146  ILE G 147                                          
SITE     1 AE4  4 HIS H 712  HIS H 714  CYS H 728  CYS H 847                    
SITE     1 AE5  4 GLU H 437  HIS H 441  CYS H 446  CYS H 449                    
SITE     1 AE6 14 SER H  56  GLY H  81  CYS H  82  GLY H  83                    
SITE     2 AE6 14 GLY H  86  TRP H  87  THR H 104  LYS H 105                    
SITE     3 AE6 14 HIS H 110  GLU H 111  LYS H 130  ASP H 131                    
SITE     4 AE6 14 VAL H 132  ASP H 146                                          
CRYST1  215.314  215.314  480.683  90.00  90.00 120.00 P 32 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      0.004644  0.002681  0.000000        0.00000                         
SCALE2      0.000000  0.005363  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002080        0.00000