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Database: PDB
Entry: 3N7U
LinkDB: 3N7U
Original site: 3N7U 
HEADER    OXIDOREDUCTASE                          27-MAY-10   3N7U              
TITLE     NAD-DEPENDENT FORMATE DEHYDROGENASE FROM HIGHER-PLANT ARABIDOPSIS     
TITLE    2 THALIANA IN COMPLEX WITH NAD AND AZIDE                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FORMATE DEHYDROGENASE;                                     
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 SYNONYM: NAD-DEPENDENT FORMATE DEHYDROGENASE, FDH;                   
COMPND   5 EC: 1.2.1.2;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;                        
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 GENE: AT5G14780, FDH, FDH1, T9L3_80;                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: P1ARAFDH                                  
KEYWDS    HOMODIMER, HOLO-FORM, OXIDOREDUCTASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.G.SHABALIN,K.M.POLYAKOV,A.E.SEROV,O.E.SKIRGELLO,E.G.SADYKHOV,       
AUTHOR   2 P.V.DOROVATOVSKIY,V.I.TISHKOV,V.O.POPOV                              
REVDAT   1   09-JUN-10 3N7U    0                                                
JRNL        AUTH   I.G.SHABALIN,K.M.POLYAKOV,O.E.SKIRGELLO,V.I.TISHKOV,         
JRNL        AUTH 2 V.O.POPOV                                                    
JRNL        TITL   STRUCTURES OF THE APO AND HOLO FORMS OF NAD-DEPENDENT        
JRNL        TITL 2 FORMATE DEHYDROGENASE FROM THE HIGHER-PLANT ARABIDOPSIS      
JRNL        TITL 3 THALIANA                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0070                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 421051                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 22264                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 30332                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1518                         
REMARK   3   BIN FREE R VALUE                    : 0.3490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 32868                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 723                                     
REMARK   3   SOLVENT ATOMS            : 3745                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.09                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.61000                                              
REMARK   3    B22 (A**2) : -1.28000                                             
REMARK   3    B33 (A**2) : 0.67000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.097         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.551         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 34285 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 46483 ; 1.639 ; 1.993       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  4200 ; 6.457 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1500 ;34.465 ;24.720       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5882 ;14.434 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   180 ;17.014 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  5112 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 25668 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 20904 ; 0.807 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 33636 ; 1.419 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13381 ; 2.415 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 12847 ; 3.742 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES REFINED INDIVIDUALLY             
REMARK   4                                                                      
REMARK   4 3N7U COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059489.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : KURCHATOV SNC                      
REMARK 200  BEAMLINE                       : K4.4                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 428654                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.990                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9300                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION (2ML): 14 MG/ML FDH,    
REMARK 280  0.1M NA2HPO4, PH 7.0, 10 MM EDTA, 5MM SODIUM AZIDE, 5MM NAD.        
REMARK 280  RESERVOIR SOLUTION (2ML): 0.1M BIS-TRIS, PH 5.5, 2.1M AMMONIUM      
REMARK 280  SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      114.81000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      108.84000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      114.81000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000      108.84000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 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: 2                                                       
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: 10230 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -71.0 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: 3                                                       
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: 9740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 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: 4                                                       
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: 10080 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26190 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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
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: 10170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
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: 10290 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 26180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -78.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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    ASN A  40     -127.83     53.37                                   
REMARK 500    ASN A 178       84.10   -150.91                                   
REMARK 500    ASN A 254       41.94   -145.07                                   
REMARK 500    ALA A 283      -83.76    -89.86                                   
REMARK 500    PRO A 331     -179.15    -67.36                                   
REMARK 500    ASN B  40     -120.76     43.18                                   
REMARK 500    ASP B 128       93.85    -69.86                                   
REMARK 500    ASN B 178       89.95   -150.34                                   
REMARK 500    ALA B 199       58.99   -140.33                                   
REMARK 500    ASN B 254       39.17   -144.49                                   
REMARK 500    ALA B 283      -85.80    -88.16                                   
REMARK 500    ASN C  40     -126.19     48.87                                   
REMARK 500    ASN C 178       83.95   -154.00                                   
REMARK 500    ASN C 254       44.98   -142.10                                   
REMARK 500    ALA C 283      -81.48    -87.55                                   
REMARK 500    PRO C 331     -177.82    -64.80                                   
REMARK 500    ASN D  40     -121.00     50.21                                   
REMARK 500    ASN D 146       20.66   -140.09                                   
REMARK 500    ASN D 178       86.60   -151.10                                   
REMARK 500    GLU D 190      127.06    -38.98                                   
REMARK 500    ALA D 199       53.88   -143.68                                   
REMARK 500    ASN D 254       40.28   -143.13                                   
REMARK 500    ALA D 283      -84.83    -86.37                                   
REMARK 500    PRO D 331     -175.23    -64.48                                   
REMARK 500    ASN E  40     -130.84     54.14                                   
REMARK 500    GLU E 190      128.14    -38.19                                   
REMARK 500    ASN E 254       38.60   -145.94                                   
REMARK 500    ALA E 283      -92.89    -93.47                                   
REMARK 500    ASN F  40     -129.32     49.72                                   
REMARK 500    ASP F 128       91.89    -69.79                                   
REMARK 500    ASN F 146       21.24   -142.23                                   
REMARK 500    GLU F 190      125.85    -39.08                                   
REMARK 500    ALA F 283      -87.65    -84.48                                   
REMARK 500    LYS F 317      -37.45    -35.76                                   
REMARK 500    ASN G  40     -126.34     49.44                                   
REMARK 500    ASP G 128       94.89    -69.48                                   
REMARK 500    ASN G 254       45.14   -142.81                                   
REMARK 500    ALA G 283      -88.75    -86.40                                   
REMARK 500    ASN H  40     -129.14     44.61                                   
REMARK 500    ASN H 254       39.20   -144.92                                   
REMARK 500    ALA H 283      -85.92    -80.86                                   
REMARK 500    ASN I  40     -129.82     52.34                                   
REMARK 500    HIS I  99       71.79   -155.13                                   
REMARK 500    HIS I 126        3.80    -69.49                                   
REMARK 500    ASP I 128       88.60    -68.61                                   
REMARK 500    LYS I 174        4.10    -66.35                                   
REMARK 500    ASN I 254       41.68   -142.96                                   
REMARK 500    ALA I 283      -87.04    -82.98                                   
REMARK 500    LYS I 317      -33.27    -39.18                                   
REMARK 500    ASN J  40     -124.37     45.31                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      67 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR H 363        22.2      L          L   OUTSIDE RANGE           
REMARK 500    TYR I 344        25.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU K  41        20.5      L          L   OUTSIDE RANGE           
REMARK 500    TYR K 344        24.6      L          L   OUTSIDE RANGE           
REMARK 500    MET L 264        24.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 16                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 17                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 11                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 18                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 22                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 25                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD E 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI E 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 379                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD F 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI F 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 20                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 26                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD G 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI G 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD H 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI H 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 12                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 27                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD I 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI I 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL I 13                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL I 19                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL I 23                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD J 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI J 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD K 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI K 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 K 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL K 14                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL K 15                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL K 24                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD L 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI L 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL L 21                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2FSS   RELATED DB: PDB                                   
REMARK 900 FDH FROM CANDIDA BOIDINII IN APO-FORM                                
REMARK 900 RELATED ID: 2GSD   RELATED DB: PDB                                   
REMARK 900 FDH FROM MORAXELLA SP.C-1 IN HOLO-FORM                               
REMARK 900 RELATED ID: 2NAC   RELATED DB: PDB                                   
REMARK 900 FDH FROM PDEUDOMONAS SP.101 IN APO-FORM                              
REMARK 900 RELATED ID: 2NAD   RELATED DB: PDB                                   
REMARK 900 FDH FROM PDEUDOMONAS SP.101 IN HOLO-FORM                             
REMARK 900 RELATED ID: 3FN4   RELATED DB: PDB                                   
REMARK 900 FDH FROM MORAXELLA SP.C-1 IN APO-FORM IN CLOSED CONFORMATION         
DBREF  3N7U A   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
DBREF  3N7U B   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
DBREF  3N7U C   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
DBREF  3N7U D   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
DBREF  3N7U E   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
DBREF  3N7U F   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
DBREF  3N7U G   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
DBREF  3N7U H   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
DBREF  3N7U I   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
DBREF  3N7U J   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
DBREF  3N7U K   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
DBREF  3N7U L   28   378  UNP    Q9S7E4   FDH_ARATH       34    384             
SEQRES   1 A  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 A  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 A  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 A  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 A  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 A  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 A  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 A  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 A  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 A  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 A  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 A  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 A  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 A  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 A  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 A  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 A  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 A  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 A  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 A  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 A  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 A  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 A  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 A  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 A  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 A  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 A  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
SEQRES   1 B  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 B  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 B  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 B  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 B  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 B  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 B  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 B  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 B  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 B  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 B  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 B  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 B  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 B  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 B  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 B  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 B  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 B  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 B  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 B  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 B  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 B  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 B  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 B  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 B  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 B  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 B  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
SEQRES   1 C  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 C  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 C  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 C  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 C  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 C  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 C  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 C  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 C  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 C  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 C  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 C  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 C  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 C  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 C  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 C  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 C  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 C  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 C  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 C  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 C  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 C  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 C  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 C  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 C  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 C  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 C  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
SEQRES   1 D  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 D  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 D  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 D  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 D  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 D  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 D  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 D  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 D  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 D  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 D  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 D  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 D  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 D  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 D  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 D  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 D  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 D  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 D  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 D  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 D  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 D  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 D  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 D  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 D  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 D  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 D  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
SEQRES   1 E  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 E  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 E  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 E  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 E  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 E  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 E  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 E  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 E  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 E  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 E  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 E  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 E  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 E  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 E  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 E  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 E  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 E  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 E  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 E  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 E  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 E  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 E  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 E  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 E  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 E  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 E  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
SEQRES   1 F  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 F  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 F  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 F  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 F  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 F  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 F  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 F  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 F  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 F  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 F  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 F  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 F  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 F  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 F  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 F  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 F  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 F  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 F  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 F  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 F  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 F  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 F  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 F  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 F  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 F  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 F  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
SEQRES   1 G  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 G  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 G  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 G  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 G  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 G  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 G  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 G  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 G  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 G  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 G  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 G  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 G  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 G  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 G  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 G  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 G  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 G  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 G  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 G  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 G  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 G  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 G  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 G  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 G  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 G  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 G  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
SEQRES   1 H  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 H  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 H  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 H  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 H  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 H  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 H  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 H  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 H  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 H  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 H  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 H  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 H  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 H  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 H  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 H  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 H  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 H  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 H  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 H  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 H  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 H  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 H  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 H  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 H  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 H  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 H  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
SEQRES   1 I  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 I  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 I  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 I  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 I  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 I  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 I  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 I  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 I  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 I  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 I  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 I  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 I  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 I  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 I  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 I  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 I  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 I  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 I  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 I  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 I  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 I  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 I  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 I  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 I  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 I  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 I  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
SEQRES   1 J  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 J  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 J  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 J  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 J  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 J  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 J  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 J  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 J  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 J  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 J  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 J  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 J  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 J  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 J  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 J  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 J  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 J  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 J  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 J  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 J  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 J  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 J  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 J  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 J  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 J  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 J  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
SEQRES   1 K  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 K  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 K  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 K  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 K  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 K  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 K  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 K  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 K  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 K  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 K  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 K  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 K  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 K  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 K  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 K  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 K  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 K  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 K  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 K  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 K  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 K  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 K  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 K  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 K  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 K  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 K  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
SEQRES   1 L  351  ASP SER LYS LYS ILE VAL GLY VAL PHE TYR LYS ALA ASN          
SEQRES   2 L  351  GLU TYR ALA THR LYS ASN PRO ASN PHE LEU GLY CYS VAL          
SEQRES   3 L  351  GLU ASN ALA LEU GLY ILE ARG ASP TRP LEU GLU SER GLN          
SEQRES   4 L  351  GLY HIS GLN TYR ILE VAL THR ASP ASP LYS GLU GLY PRO          
SEQRES   5 L  351  ASP CYS GLU LEU GLU LYS HIS ILE PRO ASP LEU HIS VAL          
SEQRES   6 L  351  LEU ILE SER THR PRO PHE HIS PRO ALA TYR VAL THR ALA          
SEQRES   7 L  351  GLU ARG ILE LYS LYS ALA LYS ASN LEU LYS LEU LEU LEU          
SEQRES   8 L  351  THR ALA GLY ILE GLY SER ASP HIS ILE ASP LEU GLN ALA          
SEQRES   9 L  351  ALA ALA ALA ALA GLY LEU THR VAL ALA GLU VAL THR GLY          
SEQRES  10 L  351  SER ASN VAL VAL SER VAL ALA GLU ASP GLU LEU MET ARG          
SEQRES  11 L  351  ILE LEU ILE LEU MET ARG ASN PHE VAL PRO GLY TYR ASN          
SEQRES  12 L  351  GLN VAL VAL LYS GLY GLU TRP ASN VAL ALA GLY ILE ALA          
SEQRES  13 L  351  TYR ARG ALA TYR ASP LEU GLU GLY LYS THR ILE GLY THR          
SEQRES  14 L  351  VAL GLY ALA GLY ARG ILE GLY LYS LEU LEU LEU GLN ARG          
SEQRES  15 L  351  LEU LYS PRO PHE GLY CYS ASN LEU LEU TYR HIS ASP ARG          
SEQRES  16 L  351  LEU GLN MET ALA PRO GLU LEU GLU LYS GLU THR GLY ALA          
SEQRES  17 L  351  LYS PHE VAL GLU ASP LEU ASN GLU MET LEU PRO LYS CYS          
SEQRES  18 L  351  ASP VAL ILE VAL ILE ASN MET PRO LEU THR GLU LYS THR          
SEQRES  19 L  351  ARG GLY MET PHE ASN LYS GLU LEU ILE GLY LYS LEU LYS          
SEQRES  20 L  351  LYS GLY VAL LEU ILE VAL ASN ASN ALA ARG GLY ALA ILE          
SEQRES  21 L  351  MET GLU ARG GLN ALA VAL VAL ASP ALA VAL GLU SER GLY          
SEQRES  22 L  351  HIS ILE GLY GLY TYR SER GLY ASP VAL TRP ASP PRO GLN          
SEQRES  23 L  351  PRO ALA PRO LYS ASP HIS PRO TRP ARG TYR MET PRO ASN          
SEQRES  24 L  351  GLN ALA MET THR PRO HIS THR SER GLY THR THR ILE ASP          
SEQRES  25 L  351  ALA GLN LEU ARG TYR ALA ALA GLY THR LYS ASP MET LEU          
SEQRES  26 L  351  GLU ARG TYR PHE LYS GLY GLU ASP PHE PRO THR GLU ASN          
SEQRES  27 L  351  TYR ILE VAL LYS ASP GLY GLU LEU ALA PRO GLN TYR ARG          
HET    NAD  A 401      44                                                       
HET    AZI  A 403       3                                                       
HET    SO4  A   1       5                                                       
HET    NAD  B 401      44                                                       
HET    AZI  B 403       3                                                       
HET    SO4  B   2       5                                                       
HET    GOL  B  16       6                                                       
HET    NAD  C 401      44                                                       
HET    AZI  C 403       3                                                       
HET    SO4  C   3       5                                                       
HET    GOL  C  10       6                                                       
HET    GOL  C  17       6                                                       
HET    NAD  D 401      44                                                       
HET    AZI  D 403       3                                                       
HET    SO4  D   4       5                                                       
HET    GOL  D  11       6                                                       
HET    GOL  D  18       6                                                       
HET    GOL  D  22       6                                                       
HET    GOL  D  25       6                                                       
HET    NAD  E 401      44                                                       
HET    AZI  E 403       3                                                       
HET    GOL  E 379       6                                                       
HET    NAD  F 401      44                                                       
HET    AZI  F 403       3                                                       
HET    SO4  F  20       5                                                       
HET    GOL  F  26       6                                                       
HET    NAD  G 401      44                                                       
HET    AZI  G 403       3                                                       
HET    SO4  G   5       5                                                       
HET    GOL  G   9       6                                                       
HET    NAD  H 401      44                                                       
HET    AZI  H 403       3                                                       
HET    SO4  H   6       5                                                       
HET    GOL  H  12       6                                                       
HET    GOL  H  27       6                                                       
HET    NAD  I 401      44                                                       
HET    AZI  I 403       3                                                       
HET    SO4  I   7       5                                                       
HET    GOL  I  13       6                                                       
HET    GOL  I  19       6                                                       
HET    GOL  I  23       6                                                       
HET    NAD  J 401      44                                                       
HET    AZI  J 403       3                                                       
HET    NAD  K 401      44                                                       
HET    AZI  K 403       3                                                       
HET    SO4  K   8       5                                                       
HET    GOL  K  14       6                                                       
HET    GOL  K  15       6                                                       
HET    GOL  K  24       6                                                       
HET    NAD  L 401      44                                                       
HET    AZI  L 403       3                                                       
HET    GOL  L  21       6                                                       
HETNAM     NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE                                
HETNAM     AZI AZIDE ION                                                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
FORMUL  13  NAD    12(C21 H27 N7 O14 P2)                                        
FORMUL  14  AZI    12(N3 1-)                                                    
FORMUL  15  SO4    9(O4 S 2-)                                                   
FORMUL  19  GOL    19(C3 H8 O3)                                                 
FORMUL  65  HOH   *3745(H2 O)                                                   
HELIX    1   1 ALA A   39  LYS A   45  5                                   7    
HELIX    2   2 ASN A   55  GLY A   58  5                                   4    
HELIX    3   3 ILE A   59  GLN A   66  1                                   8    
HELIX    4   4 CYS A   81  ILE A   87  1                                   7    
HELIX    5   5 THR A  104  ALA A  111  1                                   8    
HELIX    6   6 ASP A  128  GLY A  136  1                                   9    
HELIX    7   7 ASN A  146  ARG A  163  1                                  18    
HELIX    8   8 ASN A  164  LYS A  174  1                                  11    
HELIX    9   9 VAL A  179  TYR A  184  1                                   6    
HELIX   10  10 GLY A  200  LYS A  211  1                                  12    
HELIX   11  11 PRO A  212  GLY A  214  5                                   3    
HELIX   12  12 ALA A  226  GLY A  234  1                                   9    
HELIX   13  13 ASP A  240  LEU A  245  1                                   6    
HELIX   14  14 PRO A  246  CYS A  248  5                                   3    
HELIX   15  15 ASN A  266  LYS A  272  1                                   7    
HELIX   16  16 ARG A  284  MET A  288  5                                   5    
HELIX   17  17 GLU A  289  SER A  299  1                                  11    
HELIX   18  18 HIS A  319  TYR A  323  5                                   5    
HELIX   19  19 THR A  333  THR A  336  5                                   4    
HELIX   20  20 THR A  337  GLY A  358  1                                  22    
HELIX   21  21 PRO A  362  GLU A  364  5                                   3    
HELIX   22  22 PRO A  375  ARG A  378  5                                   4    
HELIX   23  23 ALA B   39  ASN B   46  5                                   8    
HELIX   24  24 ASN B   55  GLY B   58  5                                   4    
HELIX   25  25 ILE B   59  SER B   65  1                                   7    
HELIX   26  26 CYS B   81  ILE B   87  1                                   7    
HELIX   27  27 THR B  104  ALA B  111  1                                   8    
HELIX   28  28 ASP B  128  ALA B  135  1                                   8    
HELIX   29  29 ASN B  146  ARG B  163  1                                  18    
HELIX   30  30 ASN B  164  GLY B  175  1                                  12    
HELIX   31  31 VAL B  179  TYR B  184  1                                   6    
HELIX   32  32 GLY B  200  LYS B  211  1                                  12    
HELIX   33  33 PRO B  212  GLY B  214  5                                   3    
HELIX   34  34 ALA B  226  GLY B  234  1                                   9    
HELIX   35  35 ASP B  240  LEU B  245  1                                   6    
HELIX   36  36 PRO B  246  CYS B  248  5                                   3    
HELIX   37  37 ASN B  266  LYS B  272  1                                   7    
HELIX   38  38 ARG B  284  MET B  288  5                                   5    
HELIX   39  39 GLU B  289  SER B  299  1                                  11    
HELIX   40  40 HIS B  319  TYR B  323  5                                   5    
HELIX   41  41 THR B  333  THR B  336  5                                   4    
HELIX   42  42 THR B  337  LYS B  357  1                                  21    
HELIX   43  43 PRO B  362  GLU B  364  5                                   3    
HELIX   44  44 PRO B  375  ARG B  378  5                                   4    
HELIX   45  45 ALA C   39  LYS C   45  5                                   7    
HELIX   46  46 ASN C   55  GLY C   58  5                                   4    
HELIX   47  47 ILE C   59  GLN C   66  1                                   8    
HELIX   48  48 CYS C   81  ILE C   87  1                                   7    
HELIX   49  49 THR C  104  ALA C  111  1                                   8    
HELIX   50  50 ASP C  128  ALA C  135  1                                   8    
HELIX   51  51 ASN C  146  ARG C  163  1                                  18    
HELIX   52  52 ASN C  164  LYS C  174  1                                  11    
HELIX   53  53 VAL C  179  TYR C  184  1                                   6    
HELIX   54  54 GLY C  200  LYS C  211  1                                  12    
HELIX   55  55 PRO C  212  GLY C  214  5                                   3    
HELIX   56  56 ALA C  226  GLY C  234  1                                   9    
HELIX   57  57 ASP C  240  LEU C  245  1                                   6    
HELIX   58  58 PRO C  246  CYS C  248  5                                   3    
HELIX   59  59 ASN C  266  LYS C  272  1                                   7    
HELIX   60  60 ARG C  284  MET C  288  5                                   5    
HELIX   61  61 GLU C  289  GLY C  300  1                                  12    
HELIX   62  62 HIS C  319  TYR C  323  5                                   5    
HELIX   63  63 THR C  333  THR C  336  5                                   4    
HELIX   64  64 THR C  337  LYS C  357  1                                  21    
HELIX   65  65 PRO C  362  GLU C  364  5                                   3    
HELIX   66  66 PRO C  375  ARG C  378  5                                   4    
HELIX   67  67 ALA D   39  ASN D   46  5                                   8    
HELIX   68  68 ASN D   55  GLY D   58  5                                   4    
HELIX   69  69 ILE D   59  GLN D   66  1                                   8    
HELIX   70  70 CYS D   81  ILE D   87  1                                   7    
HELIX   71  71 THR D  104  ALA D  111  1                                   8    
HELIX   72  72 ASP D  128  GLY D  136  1                                   9    
HELIX   73  73 ASN D  146  ARG D  163  1                                  18    
HELIX   74  74 ASN D  164  LYS D  174  1                                  11    
HELIX   75  75 VAL D  179  TYR D  184  1                                   6    
HELIX   76  76 GLY D  200  LYS D  211  1                                  12    
HELIX   77  77 PRO D  212  GLY D  214  5                                   3    
HELIX   78  78 ALA D  226  GLY D  234  1                                   9    
HELIX   79  79 ASP D  240  LEU D  245  1                                   6    
HELIX   80  80 PRO D  246  CYS D  248  5                                   3    
HELIX   81  81 ASN D  266  LYS D  272  1                                   7    
HELIX   82  82 ARG D  284  MET D  288  5                                   5    
HELIX   83  83 GLU D  289  SER D  299  1                                  11    
HELIX   84  84 HIS D  319  TYR D  323  5                                   5    
HELIX   85  85 THR D  333  THR D  336  5                                   4    
HELIX   86  86 THR D  337  LYS D  357  1                                  21    
HELIX   87  87 PRO D  362  GLU D  364  5                                   3    
HELIX   88  88 PRO D  375  ARG D  378  5                                   4    
HELIX   89  89 ALA E   39  LYS E   45  5                                   7    
HELIX   90  90 ASN E   55  GLY E   58  5                                   4    
HELIX   91  91 ILE E   59  GLN E   66  1                                   8    
HELIX   92  92 CYS E   81  ILE E   87  1                                   7    
HELIX   93  93 THR E  104  ALA E  111  1                                   8    
HELIX   94  94 ASP E  128  ALA E  135  1                                   8    
HELIX   95  95 ASN E  146  ARG E  163  1                                  18    
HELIX   96  96 ASN E  164  LYS E  174  1                                  11    
HELIX   97  97 VAL E  179  TYR E  184  1                                   6    
HELIX   98  98 GLY E  200  LYS E  211  1                                  12    
HELIX   99  99 PRO E  212  GLY E  214  5                                   3    
HELIX  100 100 ALA E  226  GLY E  234  1                                   9    
HELIX  101 101 ASP E  240  LEU E  245  1                                   6    
HELIX  102 102 PRO E  246  CYS E  248  5                                   3    
HELIX  103 103 ASN E  266  LYS E  272  1                                   7    
HELIX  104 104 ARG E  284  MET E  288  5                                   5    
HELIX  105 105 GLU E  289  SER E  299  1                                  11    
HELIX  106 106 HIS E  319  TYR E  323  5                                   5    
HELIX  107 107 THR E  333  THR E  336  5                                   4    
HELIX  108 108 THR E  337  LYS E  357  1                                  21    
HELIX  109 109 PRO E  362  GLU E  364  5                                   3    
HELIX  110 110 PRO E  375  ARG E  378  5                                   4    
HELIX  111 111 ALA F   39  ALA F   43  5                                   5    
HELIX  112 112 ASN F   55  GLY F   58  5                                   4    
HELIX  113 113 ILE F   59  SER F   65  1                                   7    
HELIX  114 114 CYS F   81  ILE F   87  1                                   7    
HELIX  115 115 THR F  104  ALA F  111  1                                   8    
HELIX  116 116 ASP F  128  ALA F  135  1                                   8    
HELIX  117 117 ASN F  146  ASN F  164  1                                  19    
HELIX  118 118 ASN F  164  LYS F  174  1                                  11    
HELIX  119 119 ASN F  178  TYR F  184  1                                   7    
HELIX  120 120 GLY F  200  LYS F  211  1                                  12    
HELIX  121 121 PRO F  212  GLY F  214  5                                   3    
HELIX  122 122 ALA F  226  GLY F  234  1                                   9    
HELIX  123 123 ASP F  240  LEU F  245  1                                   6    
HELIX  124 124 PRO F  246  CYS F  248  5                                   3    
HELIX  125 125 ASN F  266  LYS F  272  1                                   7    
HELIX  126 126 ARG F  284  MET F  288  5                                   5    
HELIX  127 127 GLU F  289  SER F  299  1                                  11    
HELIX  128 128 HIS F  319  TYR F  323  5                                   5    
HELIX  129 129 THR F  333  THR F  336  5                                   4    
HELIX  130 130 THR F  337  LYS F  357  1                                  21    
HELIX  131 131 PRO F  362  GLU F  364  5                                   3    
HELIX  132 132 PRO F  375  ARG F  378  5                                   4    
HELIX  133 133 ALA G   39  ASN G   46  5                                   8    
HELIX  134 134 ASN G   55  GLY G   58  5                                   4    
HELIX  135 135 ILE G   59  GLN G   66  1                                   8    
HELIX  136 136 CYS G   81  ILE G   87  1                                   7    
HELIX  137 137 THR G  104  ALA G  111  1                                   8    
HELIX  138 138 ASP G  128  ALA G  135  1                                   8    
HELIX  139 139 ASN G  146  ARG G  163  1                                  18    
HELIX  140 140 ASN G  164  LYS G  174  1                                  11    
HELIX  141 141 ASN G  178  TYR G  184  1                                   7    
HELIX  142 142 GLY G  200  LYS G  211  1                                  12    
HELIX  143 143 PRO G  212  GLY G  214  5                                   3    
HELIX  144 144 ALA G  226  GLY G  234  1                                   9    
HELIX  145 145 ASP G  240  LEU G  245  1                                   6    
HELIX  146 146 PRO G  246  CYS G  248  5                                   3    
HELIX  147 147 ASN G  266  LYS G  272  1                                   7    
HELIX  148 148 ARG G  284  MET G  288  5                                   5    
HELIX  149 149 GLU G  289  SER G  299  1                                  11    
HELIX  150 150 HIS G  319  TYR G  323  5                                   5    
HELIX  151 151 THR G  333  THR G  336  5                                   4    
HELIX  152 152 THR G  337  LYS G  357  1                                  21    
HELIX  153 153 PRO G  362  GLU G  364  5                                   3    
HELIX  154 154 PRO G  375  ARG G  378  5                                   4    
HELIX  155 155 ALA H   39  ALA H   43  5                                   5    
HELIX  156 156 ASN H   55  GLY H   58  5                                   4    
HELIX  157 157 ILE H   59  SER H   65  1                                   7    
HELIX  158 158 CYS H   81  ILE H   87  1                                   7    
HELIX  159 159 THR H  104  ALA H  111  1                                   8    
HELIX  160 160 ASP H  128  ALA H  135  1                                   8    
HELIX  161 161 ASN H  146  ASN H  164  1                                  19    
HELIX  162 162 ASN H  164  LYS H  174  1                                  11    
HELIX  163 163 VAL H  179  TYR H  184  1                                   6    
HELIX  164 164 GLY H  200  LYS H  211  1                                  12    
HELIX  165 165 PRO H  212  GLY H  214  5                                   3    
HELIX  166 166 ALA H  226  GLY H  234  1                                   9    
HELIX  167 167 ASP H  240  LEU H  245  1                                   6    
HELIX  168 168 PRO H  246  CYS H  248  5                                   3    
HELIX  169 169 ASN H  266  LYS H  272  1                                   7    
HELIX  170 170 ARG H  284  MET H  288  5                                   5    
HELIX  171 171 GLU H  289  SER H  299  1                                  11    
HELIX  172 172 HIS H  319  TYR H  323  5                                   5    
HELIX  173 173 THR H  333  THR H  336  5                                   4    
HELIX  174 174 THR H  337  LYS H  357  1                                  21    
HELIX  175 175 PRO H  362  GLU H  364  5                                   3    
HELIX  176 176 PRO H  375  ARG H  378  5                                   4    
HELIX  177 177 ALA I   39  THR I   44  5                                   6    
HELIX  178 178 ASN I   55  GLY I   58  5                                   4    
HELIX  179 179 ILE I   59  GLN I   66  1                                   8    
HELIX  180 180 CYS I   81  ILE I   87  1                                   7    
HELIX  181 181 THR I  104  ALA I  111  1                                   8    
HELIX  182 182 ASP I  128  ALA I  135  1                                   8    
HELIX  183 183 ASN I  146  ARG I  163  1                                  18    
HELIX  184 184 ASN I  164  LYS I  174  1                                  11    
HELIX  185 185 ASN I  178  TYR I  184  1                                   7    
HELIX  186 186 GLY I  200  LYS I  211  1                                  12    
HELIX  187 187 PRO I  212  GLY I  214  5                                   3    
HELIX  188 188 ALA I  226  GLY I  234  1                                   9    
HELIX  189 189 ASP I  240  LEU I  245  1                                   6    
HELIX  190 190 PRO I  246  CYS I  248  5                                   3    
HELIX  191 191 ASN I  266  GLY I  271  1                                   6    
HELIX  192 192 ARG I  284  MET I  288  5                                   5    
HELIX  193 193 GLU I  289  SER I  299  1                                  11    
HELIX  194 194 HIS I  319  TYR I  323  5                                   5    
HELIX  195 195 THR I  333  THR I  336  5                                   4    
HELIX  196 196 THR I  337  LYS I  357  1                                  21    
HELIX  197 197 PRO I  362  GLU I  364  5                                   3    
HELIX  198 198 PRO I  375  ARG I  378  5                                   4    
HELIX  199 199 ALA J   39  ASN J   46  5                                   8    
HELIX  200 200 ASN J   55  GLY J   58  5                                   4    
HELIX  201 201 ILE J   59  SER J   65  1                                   7    
HELIX  202 202 CYS J   81  ILE J   87  1                                   7    
HELIX  203 203 THR J  104  ALA J  111  1                                   8    
HELIX  204 204 ASP J  128  ALA J  135  1                                   8    
HELIX  205 205 ASN J  146  ARG J  163  1                                  18    
HELIX  206 206 ASN J  164  LYS J  174  1                                  11    
HELIX  207 207 ASN J  178  TYR J  184  1                                   7    
HELIX  208 208 GLY J  200  LYS J  211  1                                  12    
HELIX  209 209 PRO J  212  GLY J  214  5                                   3    
HELIX  210 210 ALA J  226  GLY J  234  1                                   9    
HELIX  211 211 ASP J  240  LEU J  245  1                                   6    
HELIX  212 212 ASN J  266  GLY J  271  1                                   6    
HELIX  213 213 ARG J  284  MET J  288  5                                   5    
HELIX  214 214 GLU J  289  SER J  299  1                                  11    
HELIX  215 215 HIS J  319  TYR J  323  5                                   5    
HELIX  216 216 THR J  333  THR J  336  5                                   4    
HELIX  217 217 THR J  337  LYS J  357  1                                  21    
HELIX  218 218 PRO J  362  GLU J  364  5                                   3    
HELIX  219 219 PRO J  375  ARG J  378  5                                   4    
HELIX  220 220 ALA K   39  THR K   44  5                                   6    
HELIX  221 221 ASN K   55  GLY K   58  5                                   4    
HELIX  222 222 ILE K   59  GLN K   66  1                                   8    
HELIX  223 223 CYS K   81  ILE K   87  1                                   7    
HELIX  224 224 THR K  104  ALA K  111  1                                   8    
HELIX  225 225 ASP K  128  ALA K  135  1                                   8    
HELIX  226 226 ASN K  146  ARG K  163  1                                  18    
HELIX  227 227 ASN K  164  GLY K  175  1                                  12    
HELIX  228 228 ASN K  178  TYR K  184  1                                   7    
HELIX  229 229 GLY K  200  LYS K  211  1                                  12    
HELIX  230 230 PRO K  212  GLY K  214  5                                   3    
HELIX  231 231 ALA K  226  GLY K  234  1                                   9    
HELIX  232 232 ASP K  240  LEU K  245  1                                   6    
HELIX  233 233 PRO K  246  CYS K  248  5                                   3    
HELIX  234 234 ASN K  266  LYS K  272  1                                   7    
HELIX  235 235 ARG K  284  MET K  288  5                                   5    
HELIX  236 236 GLU K  289  SER K  299  1                                  11    
HELIX  237 237 HIS K  319  TYR K  323  5                                   5    
HELIX  238 238 THR K  333  THR K  336  5                                   4    
HELIX  239 239 THR K  337  LYS K  357  1                                  21    
HELIX  240 240 PRO K  362  GLU K  364  5                                   3    
HELIX  241 241 PRO K  375  ARG K  378  5                                   4    
HELIX  242 242 ALA L   39  LYS L   45  5                                   7    
HELIX  243 243 ASN L   55  GLY L   58  5                                   4    
HELIX  244 244 ILE L   59  GLN L   66  1                                   8    
HELIX  245 245 CYS L   81  ILE L   87  1                                   7    
HELIX  246 246 THR L  104  ALA L  111  1                                   8    
HELIX  247 247 ASP L  128  ALA L  135  1                                   8    
HELIX  248 248 ASN L  146  ARG L  163  1                                  18    
HELIX  249 249 ASN L  164  LYS L  174  1                                  11    
HELIX  250 250 VAL L  179  TYR L  184  1                                   6    
HELIX  251 251 GLY L  200  LYS L  211  1                                  12    
HELIX  252 252 PRO L  212  GLY L  214  5                                   3    
HELIX  253 253 ALA L  226  GLY L  234  1                                   9    
HELIX  254 254 ASP L  240  LEU L  245  1                                   6    
HELIX  255 255 PRO L  246  CYS L  248  5                                   3    
HELIX  256 256 ASN L  266  LYS L  272  1                                   7    
HELIX  257 257 ARG L  284  MET L  288  5                                   5    
HELIX  258 258 GLU L  289  SER L  299  1                                  11    
HELIX  259 259 HIS L  319  TYR L  323  5                                   5    
HELIX  260 260 THR L  333  THR L  336  5                                   4    
HELIX  261 261 THR L  337  GLY L  358  1                                  22    
HELIX  262 262 PRO L  362  GLU L  364  5                                   3    
HELIX  263 263 PRO L  375  ARG L  378  5                                   4    
SHEET    1   A 7 GLN A  69  THR A  73  0                                        
SHEET    2   A 7 LYS A  31  VAL A  35  1  N  ILE A  32   O  GLN A  69           
SHEET    3   A 7 VAL A  92  SER A  95  1  O  ILE A  94   N  VAL A  33           
SHEET    4   A 7 LEU A 116  THR A 119  1  O  LEU A 118   N  SER A  95           
SHEET    5   A 7 THR A 138  GLU A 141  1  O  THR A 138   N  LEU A 117           
SHEET    6   A 7 TYR A 366  LYS A 369 -1  O  ILE A 367   N  VAL A 139           
SHEET    7   A 7 GLU A 372  LEU A 373 -1  O  GLU A 372   N  LYS A 369           
SHEET    1   B 6 LYS A 236  PHE A 237  0                                        
SHEET    2   B 6 ASN A 216  HIS A 220  1  N  TYR A 219   O  LYS A 236           
SHEET    3   B 6 THR A 193  VAL A 197  1  N  ILE A 194   O  LEU A 218           
SHEET    4   B 6 VAL A 250  ILE A 253  1  O  VAL A 250   N  GLY A 195           
SHEET    5   B 6 VAL A 277  ASN A 281  1  O  VAL A 280   N  ILE A 253           
SHEET    6   B 6 ILE A 302  SER A 306  1  O  SER A 306   N  ASN A 281           
SHEET    1   C 7 GLN B  69  THR B  73  0                                        
SHEET    2   C 7 LYS B  31  VAL B  35  1  N  ILE B  32   O  GLN B  69           
SHEET    3   C 7 VAL B  92  SER B  95  1  O  ILE B  94   N  VAL B  33           
SHEET    4   C 7 LEU B 116  THR B 119  1  O  LEU B 118   N  SER B  95           
SHEET    5   C 7 THR B 138  GLU B 141  1  O  ALA B 140   N  THR B 119           
SHEET    6   C 7 TYR B 366  LYS B 369 -1  O  ILE B 367   N  VAL B 139           
SHEET    7   C 7 GLU B 372  LEU B 373 -1  O  GLU B 372   N  LYS B 369           
SHEET    1   D 6 LYS B 236  PHE B 237  0                                        
SHEET    2   D 6 ASN B 216  HIS B 220  1  N  TYR B 219   O  LYS B 236           
SHEET    3   D 6 THR B 193  VAL B 197  1  N  ILE B 194   O  LEU B 218           
SHEET    4   D 6 VAL B 250  ILE B 253  1  O  VAL B 252   N  VAL B 197           
SHEET    5   D 6 VAL B 277  ASN B 281  1  O  VAL B 280   N  ILE B 253           
SHEET    6   D 6 ILE B 302  SER B 306  1  O  SER B 306   N  ILE B 279           
SHEET    1   E 7 GLN C  69  THR C  73  0                                        
SHEET    2   E 7 LYS C  31  VAL C  35  1  N  GLY C  34   O  ILE C  71           
SHEET    3   E 7 VAL C  92  SER C  95  1  O  ILE C  94   N  VAL C  33           
SHEET    4   E 7 LEU C 116  THR C 119  1  O  LEU C 118   N  SER C  95           
SHEET    5   E 7 THR C 138  GLU C 141  1  O  ALA C 140   N  THR C 119           
SHEET    6   E 7 TYR C 366  LYS C 369 -1  O  ILE C 367   N  VAL C 139           
SHEET    7   E 7 GLU C 372  LEU C 373 -1  O  GLU C 372   N  LYS C 369           
SHEET    1   F 6 LYS C 236  PHE C 237  0                                        
SHEET    2   F 6 ASN C 216  HIS C 220  1  N  TYR C 219   O  LYS C 236           
SHEET    3   F 6 THR C 193  VAL C 197  1  N  THR C 196   O  HIS C 220           
SHEET    4   F 6 VAL C 250  ILE C 253  1  O  VAL C 252   N  VAL C 197           
SHEET    5   F 6 LEU C 278  ASN C 281  1  O  VAL C 280   N  ILE C 251           
SHEET    6   F 6 GLY C 304  SER C 306  1  O  GLY C 304   N  ILE C 279           
SHEET    1   G 7 GLN D  69  THR D  73  0                                        
SHEET    2   G 7 LYS D  31  VAL D  35  1  N  ILE D  32   O  GLN D  69           
SHEET    3   G 7 VAL D  92  SER D  95  1  O  ILE D  94   N  VAL D  33           
SHEET    4   G 7 LEU D 116  THR D 119  1  O  LEU D 118   N  SER D  95           
SHEET    5   G 7 THR D 138  GLU D 141  1  O  THR D 138   N  LEU D 117           
SHEET    6   G 7 TYR D 366  LYS D 369 -1  O  ILE D 367   N  VAL D 139           
SHEET    7   G 7 GLU D 372  LEU D 373 -1  O  GLU D 372   N  LYS D 369           
SHEET    1   H 6 LYS D 236  PHE D 237  0                                        
SHEET    2   H 6 ASN D 216  HIS D 220  1  N  LEU D 217   O  LYS D 236           
SHEET    3   H 6 THR D 193  VAL D 197  1  N  ILE D 194   O  LEU D 218           
SHEET    4   H 6 VAL D 250  ILE D 253  1  O  VAL D 252   N  VAL D 197           
SHEET    5   H 6 VAL D 277  ASN D 281  1  O  VAL D 280   N  ILE D 253           
SHEET    6   H 6 ILE D 302  SER D 306  1  O  GLY D 304   N  ILE D 279           
SHEET    1   I 7 GLN E  69  THR E  73  0                                        
SHEET    2   I 7 LYS E  31  VAL E  35  1  N  ILE E  32   O  GLN E  69           
SHEET    3   I 7 VAL E  92  SER E  95  1  O  ILE E  94   N  VAL E  33           
SHEET    4   I 7 LEU E 116  THR E 119  1  O  LEU E 118   N  SER E  95           
SHEET    5   I 7 THR E 138  GLU E 141  1  O  ALA E 140   N  THR E 119           
SHEET    6   I 7 TYR E 366  LYS E 369 -1  O  ILE E 367   N  VAL E 139           
SHEET    7   I 7 GLU E 372  LEU E 373 -1  O  GLU E 372   N  LYS E 369           
SHEET    1   J 6 LYS E 236  PHE E 237  0                                        
SHEET    2   J 6 ASN E 216  HIS E 220  1  N  TYR E 219   O  LYS E 236           
SHEET    3   J 6 THR E 193  VAL E 197  1  N  ILE E 194   O  LEU E 218           
SHEET    4   J 6 VAL E 250  ILE E 253  1  O  VAL E 252   N  VAL E 197           
SHEET    5   J 6 VAL E 277  ASN E 281  1  O  LEU E 278   N  ILE E 251           
SHEET    6   J 6 ILE E 302  GLY E 307  1  O  GLY E 304   N  ILE E 279           
SHEET    1   K 7 GLN F  69  THR F  73  0                                        
SHEET    2   K 7 LYS F  31  VAL F  35  1  N  ILE F  32   O  ILE F  71           
SHEET    3   K 7 VAL F  92  SER F  95  1  O  ILE F  94   N  VAL F  33           
SHEET    4   K 7 LEU F 116  THR F 119  1  O  LEU F 118   N  SER F  95           
SHEET    5   K 7 THR F 138  GLU F 141  1  O  THR F 138   N  LEU F 117           
SHEET    6   K 7 TYR F 366  LYS F 369 -1  O  ILE F 367   N  VAL F 139           
SHEET    7   K 7 GLU F 372  LEU F 373 -1  O  GLU F 372   N  LYS F 369           
SHEET    1   L 6 LYS F 236  PHE F 237  0                                        
SHEET    2   L 6 ASN F 216  HIS F 220  1  N  LEU F 217   O  LYS F 236           
SHEET    3   L 6 THR F 193  VAL F 197  1  N  ILE F 194   O  LEU F 218           
SHEET    4   L 6 VAL F 250  ILE F 253  1  O  VAL F 252   N  VAL F 197           
SHEET    5   L 6 VAL F 277  ASN F 281  1  O  VAL F 280   N  ILE F 251           
SHEET    6   L 6 ILE F 302  SER F 306  1  O  GLY F 304   N  ILE F 279           
SHEET    1   M 7 GLN G  69  THR G  73  0                                        
SHEET    2   M 7 LYS G  31  VAL G  35  1  N  ILE G  32   O  GLN G  69           
SHEET    3   M 7 VAL G  92  SER G  95  1  O  ILE G  94   N  VAL G  33           
SHEET    4   M 7 LEU G 116  THR G 119  1  O  LEU G 118   N  SER G  95           
SHEET    5   M 7 THR G 138  GLU G 141  1  O  ALA G 140   N  THR G 119           
SHEET    6   M 7 TYR G 366  LYS G 369 -1  O  ILE G 367   N  VAL G 139           
SHEET    7   M 7 GLU G 372  LEU G 373 -1  O  GLU G 372   N  LYS G 369           
SHEET    1   N 6 LYS G 236  PHE G 237  0                                        
SHEET    2   N 6 ASN G 216  HIS G 220  1  N  TYR G 219   O  LYS G 236           
SHEET    3   N 6 THR G 193  VAL G 197  1  N  ILE G 194   O  LEU G 218           
SHEET    4   N 6 VAL G 250  ILE G 253  1  O  VAL G 252   N  VAL G 197           
SHEET    5   N 6 VAL G 277  ASN G 281  1  O  LEU G 278   N  ILE G 251           
SHEET    6   N 6 ILE G 302  GLY G 307  1  O  GLY G 304   N  ILE G 279           
SHEET    1   O 7 GLN H  69  THR H  73  0                                        
SHEET    2   O 7 LYS H  31  VAL H  35  1  N  ILE H  32   O  GLN H  69           
SHEET    3   O 7 VAL H  92  SER H  95  1  O  ILE H  94   N  VAL H  33           
SHEET    4   O 7 LEU H 116  THR H 119  1  O  LEU H 118   N  SER H  95           
SHEET    5   O 7 THR H 138  GLU H 141  1  O  THR H 138   N  LEU H 117           
SHEET    6   O 7 TYR H 366  LYS H 369 -1  O  ILE H 367   N  VAL H 139           
SHEET    7   O 7 GLU H 372  LEU H 373 -1  O  GLU H 372   N  LYS H 369           
SHEET    1   P 6 LYS H 236  PHE H 237  0                                        
SHEET    2   P 6 ASN H 216  HIS H 220  1  N  LEU H 217   O  LYS H 236           
SHEET    3   P 6 THR H 193  VAL H 197  1  N  ILE H 194   O  LEU H 218           
SHEET    4   P 6 VAL H 250  ILE H 253  1  O  VAL H 252   N  VAL H 197           
SHEET    5   P 6 VAL H 277  ASN H 281  1  O  VAL H 280   N  ILE H 253           
SHEET    6   P 6 ILE H 302  SER H 306  1  O  SER H 306   N  ILE H 279           
SHEET    1   Q 7 GLN I  69  THR I  73  0                                        
SHEET    2   Q 7 LYS I  31  VAL I  35  1  N  ILE I  32   O  GLN I  69           
SHEET    3   Q 7 VAL I  92  SER I  95  1  O  ILE I  94   N  VAL I  35           
SHEET    4   Q 7 LEU I 116  THR I 119  1  O  LEU I 116   N  LEU I  93           
SHEET    5   Q 7 THR I 138  GLU I 141  1  O  ALA I 140   N  LEU I 117           
SHEET    6   Q 7 TYR I 366  LYS I 369 -1  O  ILE I 367   N  VAL I 139           
SHEET    7   Q 7 GLU I 372  LEU I 373 -1  O  GLU I 372   N  LYS I 369           
SHEET    1   R 6 LYS I 236  PHE I 237  0                                        
SHEET    2   R 6 ASN I 216  HIS I 220  1  N  TYR I 219   O  LYS I 236           
SHEET    3   R 6 THR I 193  VAL I 197  1  N  ILE I 194   O  LEU I 218           
SHEET    4   R 6 VAL I 250  ILE I 253  1  O  VAL I 252   N  VAL I 197           
SHEET    5   R 6 VAL I 277  ASN I 281  1  O  LEU I 278   N  ILE I 251           
SHEET    6   R 6 ILE I 302  SER I 306  1  O  GLY I 304   N  ILE I 279           
SHEET    1   S 7 GLN J  69  THR J  73  0                                        
SHEET    2   S 7 LYS J  31  VAL J  35  1  N  ILE J  32   O  GLN J  69           
SHEET    3   S 7 VAL J  92  SER J  95  1  O  ILE J  94   N  VAL J  33           
SHEET    4   S 7 LEU J 116  THR J 119  1  O  LEU J 118   N  SER J  95           
SHEET    5   S 7 THR J 138  GLU J 141  1  O  THR J 138   N  LEU J 117           
SHEET    6   S 7 TYR J 366  LYS J 369 -1  O  ILE J 367   N  VAL J 139           
SHEET    7   S 7 GLU J 372  LEU J 373 -1  O  GLU J 372   N  LYS J 369           
SHEET    1   T 6 LYS J 236  PHE J 237  0                                        
SHEET    2   T 6 ASN J 216  HIS J 220  1  N  TYR J 219   O  LYS J 236           
SHEET    3   T 6 THR J 193  VAL J 197  1  N  ILE J 194   O  LEU J 218           
SHEET    4   T 6 VAL J 250  ILE J 253  1  O  VAL J 252   N  VAL J 197           
SHEET    5   T 6 VAL J 277  ASN J 281  1  O  LEU J 278   N  ILE J 251           
SHEET    6   T 6 ILE J 302  SER J 306  1  O  SER J 306   N  ILE J 279           
SHEET    1   U 7 GLN K  69  THR K  73  0                                        
SHEET    2   U 7 LYS K  31  VAL K  35  1  N  ILE K  32   O  GLN K  69           
SHEET    3   U 7 VAL K  92  SER K  95  1  O  ILE K  94   N  VAL K  33           
SHEET    4   U 7 LEU K 116  THR K 119  1  O  LEU K 118   N  SER K  95           
SHEET    5   U 7 THR K 138  GLU K 141  1  O  THR K 138   N  LEU K 117           
SHEET    6   U 7 TYR K 366  LYS K 369 -1  O  ILE K 367   N  VAL K 139           
SHEET    7   U 7 GLU K 372  LEU K 373 -1  O  GLU K 372   N  LYS K 369           
SHEET    1   V 6 LYS K 236  PHE K 237  0                                        
SHEET    2   V 6 ASN K 216  HIS K 220  1  N  TYR K 219   O  LYS K 236           
SHEET    3   V 6 THR K 193  VAL K 197  1  N  ILE K 194   O  LEU K 218           
SHEET    4   V 6 VAL K 250  ILE K 253  1  O  VAL K 250   N  GLY K 195           
SHEET    5   V 6 VAL K 277  ASN K 281  1  O  VAL K 280   N  ILE K 253           
SHEET    6   V 6 ILE K 302  SER K 306  1  O  GLY K 304   N  ILE K 279           
SHEET    1   W 7 GLN L  69  THR L  73  0                                        
SHEET    2   W 7 LYS L  31  VAL L  35  1  N  ILE L  32   O  GLN L  69           
SHEET    3   W 7 VAL L  92  SER L  95  1  O  ILE L  94   N  VAL L  33           
SHEET    4   W 7 LEU L 116  THR L 119  1  O  LEU L 118   N  SER L  95           
SHEET    5   W 7 THR L 138  GLU L 141  1  O  THR L 138   N  LEU L 117           
SHEET    6   W 7 TYR L 366  LYS L 369 -1  O  ILE L 367   N  VAL L 139           
SHEET    7   W 7 GLU L 372  LEU L 373 -1  O  GLU L 372   N  LYS L 369           
SHEET    1   X 6 LYS L 236  PHE L 237  0                                        
SHEET    2   X 6 ASN L 216  HIS L 220  1  N  TYR L 219   O  LYS L 236           
SHEET    3   X 6 THR L 193  VAL L 197  1  N  THR L 196   O  HIS L 220           
SHEET    4   X 6 VAL L 250  ILE L 253  1  O  VAL L 252   N  VAL L 197           
SHEET    5   X 6 VAL L 277  ASN L 281  1  O  LEU L 278   N  ILE L 251           
SHEET    6   X 6 ILE L 302  SER L 306  1  O  SER L 306   N  ASN L 281           
CISPEP   1 ASP A  311    PRO A  312          0       -10.57                     
CISPEP   2 GLN A  313    PRO A  314          0         0.31                     
CISPEP   3 ASP B  311    PRO B  312          0        -5.75                     
CISPEP   4 GLN B  313    PRO B  314          0        -1.68                     
CISPEP   5 ASP C  311    PRO C  312          0        -9.45                     
CISPEP   6 GLN C  313    PRO C  314          0        -3.63                     
CISPEP   7 ASP D  311    PRO D  312          0        -2.49                     
CISPEP   8 GLN D  313    PRO D  314          0        -3.65                     
CISPEP   9 ASP E  311    PRO E  312          0        -4.00                     
CISPEP  10 GLN E  313    PRO E  314          0        -2.36                     
CISPEP  11 ASP F  311    PRO F  312          0        -6.31                     
CISPEP  12 GLN F  313    PRO F  314          0         1.24                     
CISPEP  13 ASP G  311    PRO G  312          0        -4.19                     
CISPEP  14 GLN G  313    PRO G  314          0        -4.58                     
CISPEP  15 ASP H  311    PRO H  312          0        -3.27                     
CISPEP  16 GLN H  313    PRO H  314          0        -8.08                     
CISPEP  17 ASP I  311    PRO I  312          0         0.28                     
CISPEP  18 GLN I  313    PRO I  314          0        -3.55                     
CISPEP  19 ASP J  311    PRO J  312          0        -4.06                     
CISPEP  20 GLN J  313    PRO J  314          0        -6.77                     
CISPEP  21 ASP K  311    PRO K  312          0        -5.81                     
CISPEP  22 GLN K  313    PRO K  314          0        -3.64                     
CISPEP  23 ASP L  311    PRO L  312          0        -9.22                     
CISPEP  24 GLN L  313    PRO L  314          0        -1.49                     
SITE     1 AC1 32 ILE A 122  ASN A 146  VAL A 147  VAL A 150                    
SITE     2 AC1 32 GLY A 200  ARG A 201  ILE A 202  ASP A 221                    
SITE     3 AC1 32 ARG A 222  MET A 255  PRO A 256  ASN A 282                    
SITE     4 AC1 32 ALA A 283  ARG A 284  ASP A 308  HIS A 332                    
SITE     5 AC1 32 SER A 334  GLY A 335  GLN A 376  TYR A 377                    
SITE     6 AC1 32 HOH A 383  AZI A 403  HOH A 585  HOH A 586                    
SITE     7 AC1 32 HOH A 588  HOH A 589  HOH A 590  HOH A 591                    
SITE     8 AC1 32 HOH A 592  HOH A 593  HOH A 595  HOH A 596                    
SITE     1 AC2  7 PRO A  97  PHE A  98  ILE A 122  ASN A 146                    
SITE     2 AC2  7 ARG A 284  HIS A 332  NAD A 401                               
SITE     1 AC3  2 ARG A 354  PRO A 362                                          
SITE     1 AC4 34 HOH B  14  ILE B 122  ASN B 146  VAL B 147                    
SITE     2 AC4 34 VAL B 150  GLY B 200  ARG B 201  ILE B 202                    
SITE     3 AC4 34 ASP B 221  ARG B 222  MET B 255  PRO B 256                    
SITE     4 AC4 34 ASN B 282  ALA B 283  ARG B 284  ASP B 308                    
SITE     5 AC4 34 VAL B 309  HIS B 332  SER B 334  GLY B 335                    
SITE     6 AC4 34 GLN B 376  TYR B 377  AZI B 403  HOH B 413                    
SITE     7 AC4 34 HOH B 588  HOH B 589  HOH B 591  HOH B 592                    
SITE     8 AC4 34 HOH B 593  HOH B 594  HOH B 595  HOH B 596                    
SITE     9 AC4 34 HOH B 597  HOH B 598                                          
SITE     1 AC5  7 PRO B  97  PHE B  98  ILE B 122  ASN B 146                    
SITE     2 AC5  7 ARG B 284  HIS B 332  NAD B 401                               
SITE     1 AC6  3 HOH B  27  ARG B 354  PRO B 362                               
SITE     1 AC7  5 TYR B 184  ARG B 185  ASN B 326  HOH B 611                    
SITE     2 AC7  5 HOH B 687                                                     
SITE     1 AC8 33 ILE C 122  ASN C 146  VAL C 147  VAL C 150                    
SITE     2 AC8 33 GLY C 200  ARG C 201  ILE C 202  ASP C 221                    
SITE     3 AC8 33 ARG C 222  MET C 255  PRO C 256  ASN C 282                    
SITE     4 AC8 33 ALA C 283  ARG C 284  ASP C 308  VAL C 309                    
SITE     5 AC8 33 HIS C 332  SER C 334  GLY C 335  GLN C 376                    
SITE     6 AC8 33 AZI C 403  HOH C 430  HOH C 548  HOH C 549                    
SITE     7 AC8 33 HOH C 551  HOH C 552  HOH C 553  HOH C 554                    
SITE     8 AC8 33 HOH C 555  HOH C 557  HOH C 558  HOH C 559                    
SITE     9 AC8 33 HOH C 667                                                     
SITE     1 AC9  7 PRO C  97  PHE C  98  ILE C 122  ASN C 146                    
SITE     2 AC9  7 ARG C 284  HIS C 332  NAD C 401                               
SITE     1 BC1  3 ARG C 354  PRO C 362  HOH C 665                               
SITE     1 BC2  4 ARG C 378  HOH C 688  ARG E  60  ASP E  61                    
SITE     1 BC3  3 TYR C 184  ARG C 185  ASN C 326                               
SITE     1 BC4 32 HOH D   3  HOH D   6  ILE D 122  ASN D 146                    
SITE     2 BC4 32 VAL D 147  VAL D 150  GLY D 200  ARG D 201                    
SITE     3 BC4 32 ILE D 202  ASP D 221  ARG D 222  MET D 255                    
SITE     4 BC4 32 PRO D 256  ASN D 282  ALA D 283  ARG D 284                    
SITE     5 BC4 32 ASP D 308  HIS D 332  SER D 334  GLY D 335                    
SITE     6 BC4 32 GLN D 376  AZI D 403  HOH D 562  HOH D 563                    
SITE     7 BC4 32 HOH D 565  HOH D 566  HOH D 567  HOH D 568                    
SITE     8 BC4 32 HOH D 569  HOH D 570  HOH D 571  HOH D 649                    
SITE     1 BC5  7 PRO D  97  PHE D  98  ILE D 122  ASN D 146                    
SITE     2 BC5  7 ARG D 284  HIS D 332  NAD D 401                               
SITE     1 BC6  3 ARG D 354  PRO D 362  HOH D 670                               
SITE     1 BC7  3 ARG D 378  HOH J  11  ASP J  61                               
SITE     1 BC8  3 TYR D 184  ARG D 185  ASN D 326                               
SITE     1 BC9  4 ASN D 170  LYS D 174  HOH D 506  HOH D 579                    
SITE     1 CC1  2 HIS D 126  HOH D 391                                          
SITE     1 CC2 32 ASN E 146  VAL E 147  VAL E 150  GLY E 200                    
SITE     2 CC2 32 ARG E 201  ILE E 202  ASP E 221  ARG E 222                    
SITE     3 CC2 32 MET E 255  PRO E 256  ASN E 282  ALA E 283                    
SITE     4 CC2 32 ARG E 284  ASP E 308  VAL E 309  HIS E 332                    
SITE     5 CC2 32 SER E 334  GLY E 335  GLN E 376  AZI E 403                    
SITE     6 CC2 32 HOH E 565  HOH E 566  HOH E 568  HOH E 569                    
SITE     7 CC2 32 HOH E 570  HOH E 571  HOH E 572  HOH E 574                    
SITE     8 CC2 32 HOH E 575  HOH E 654  HOH H 509  HOH H 510                    
SITE     1 CC3  8 PRO E  97  PHE E  98  GLY E 121  ILE E 122                    
SITE     2 CC3  8 ASN E 146  ARG E 284  HIS E 332  NAD E 401                    
SITE     1 CC4  6 HOH E  22  ASP E 125  HIS E 126  ASP E 128                    
SITE     2 CC4  6 HOH E 513  HOH E 514                                          
SITE     1 CC5 33 ASN F 146  VAL F 147  VAL F 150  GLY F 200                    
SITE     2 CC5 33 ARG F 201  ILE F 202  HIS F 220  ASP F 221                    
SITE     3 CC5 33 ARG F 222  MET F 255  PRO F 256  ASN F 282                    
SITE     4 CC5 33 ALA F 283  ARG F 284  ASP F 308  VAL F 309                    
SITE     5 CC5 33 HIS F 332  SER F 334  GLY F 335  GLN F 376                    
SITE     6 CC5 33 AZI F 403  HOH F 405  HOH F 410  HOH F 534                    
SITE     7 CC5 33 HOH F 535  HOH F 537  HOH F 538  HOH F 539                    
SITE     8 CC5 33 HOH F 540  HOH F 541  HOH F 542  HOH F 543                    
SITE     9 CC5 33 HOH F 544                                                     
SITE     1 CC6  7 PRO F  97  PHE F  98  ILE F 122  ASN F 146                    
SITE     2 CC6  7 ARG F 284  HIS F 332  NAD F 401                               
SITE     1 CC7  4 ARG F 354  PRO F 362  HOH F 402  HOH F 631                    
SITE     1 CC8  7 TYR F 102  VAL F 103  HIS F 126  ASP F 128                    
SITE     2 CC8  7 HOH F 508  HOH F 545  HOH F 614                               
SITE     1 CC9 33 HOH G  21  PHE G  98  ILE G 122  ASN G 146                    
SITE     2 CC9 33 VAL G 147  VAL G 150  GLY G 200  ARG G 201                    
SITE     3 CC9 33 ILE G 202  ASP G 221  ARG G 222  MET G 255                    
SITE     4 CC9 33 PRO G 256  ASN G 282  ALA G 283  ARG G 284                    
SITE     5 CC9 33 ASP G 308  HIS G 332  SER G 334  GLY G 335                    
SITE     6 CC9 33 GLN G 376  HOH G 402  AZI G 403  HOH G 479                    
SITE     7 CC9 33 HOH G 543  HOH G 544  HOH G 546  HOH G 547                    
SITE     8 CC9 33 HOH G 548  HOH G 549  HOH G 551  HOH I 502                    
SITE     9 CC9 33 HOH I 503                                                     
SITE     1 DC1  7 PRO G  97  PHE G  98  ILE G 122  ASN G 146                    
SITE     2 DC1  7 ARG G 284  HIS G 332  NAD G 401                               
SITE     1 DC2  5 THR G 138  LYS G 369  ASP G 370  HOH G 456                    
SITE     2 DC2  5 HOH G 627                                                     
SITE     1 DC3  5 ARG B 378  ARG G  60  ASP G  61  HOH G 498                    
SITE     2 DC3  5 HOH G 532                                                     
SITE     1 DC4 33 PHE H  98  ILE H 122  ASN H 146  VAL H 147                    
SITE     2 DC4 33 VAL H 150  GLY H 200  ARG H 201  ILE H 202                    
SITE     3 DC4 33 ASP H 221  ARG H 222  MET H 255  PRO H 256                    
SITE     4 DC4 33 ASN H 282  ALA H 283  ARG H 284  ASP H 308                    
SITE     5 DC4 33 HIS H 332  SER H 334  GLY H 335  GLN H 376                    
SITE     6 DC4 33 AZI H 403  HOH H 543  HOH H 544  HOH H 546                    
SITE     7 DC4 33 HOH H 547  HOH H 548  HOH H 549  HOH H 550                    
SITE     8 DC4 33 HOH H 551  HOH H 553  HOH H 554  HOH H 555                    
SITE     9 DC4 33 HOH H 625                                                     
SITE     1 DC5  7 PRO H  97  PHE H  98  ILE H 122  ASN H 146                    
SITE     2 DC5  7 ARG H 284  HIS H 332  NAD H 401                               
SITE     1 DC6  5 GOL H  12  LYS H 115  THR H 138  LYS H 369                    
SITE     2 DC6  5 HOH H 558                                                     
SITE     1 DC7  7 SO4 H   6  TYR H 355  GLU H 359  PHE H 361                    
SITE     2 DC7  7 TYR H 366  HOH H 391  HOH H 482                               
SITE     1 DC8  6 HOH H  17  TYR H 102  THR H 104  HIS H 126                    
SITE     2 DC8  6 ASP H 128  HOH H 556                                          
SITE     1 DC9 32 ILE I 122  ASN I 146  VAL I 147  VAL I 150                    
SITE     2 DC9 32 GLY I 200  ARG I 201  ILE I 202  ASP I 221                    
SITE     3 DC9 32 ARG I 222  MET I 255  PRO I 256  ASN I 282                    
SITE     4 DC9 32 ALA I 283  ARG I 284  ASP I 308  VAL I 309                    
SITE     5 DC9 32 HIS I 332  SER I 334  GLY I 335  GLN I 376                    
SITE     6 DC9 32 AZI I 403  HOH I 521  HOH I 522  HOH I 524                    
SITE     7 DC9 32 HOH I 525  HOH I 526  HOH I 527  HOH I 528                    
SITE     8 DC9 32 HOH I 529  HOH I 531  HOH I 532  HOH I 613                    
SITE     1 EC1  7 PRO I  97  PHE I  98  ILE I 122  ASN I 146                    
SITE     2 EC1  7 ARG I 284  HIS I 332  NAD I 401                               
SITE     1 EC2  5 GOL I  13  LYS I 115  THR I 138  LYS I 369                    
SITE     2 EC2  5 HOH I 536                                                     
SITE     1 EC3  7 SO4 I   7  ARG I 354  TYR I 355  GLU I 359                    
SITE     2 EC3  7 PHE I 361  TYR I 366  HOH I 594                               
SITE     1 EC4  4 LEU I  57  LEU I 342  ALA I 346  HOH I 513                    
SITE     1 EC5  6 TYR I 102  HIS I 126  ASP I 128  HOH I 418                    
SITE     2 EC5  6 HOH I 490  HOH I 534                                          
SITE     1 EC6 31 HOH J  18  PHE J  98  ILE J 122  ASN J 146                    
SITE     2 EC6 31 VAL J 147  VAL J 150  GLY J 200  ARG J 201                    
SITE     3 EC6 31 ILE J 202  ASP J 221  ARG J 222  MET J 255                    
SITE     4 EC6 31 PRO J 256  ASN J 282  ARG J 284  ASP J 308                    
SITE     5 EC6 31 VAL J 309  HIS J 332  SER J 334  GLY J 335                    
SITE     6 EC6 31 GLN J 376  AZI J 403  HOH J 410  HOH J 495                    
SITE     7 EC6 31 HOH J 496  HOH J 498  HOH J 499  HOH J 500                    
SITE     8 EC6 31 HOH J 501  HOH K 484  HOH K 485                               
SITE     1 EC7  7 PRO J  97  PHE J  98  ILE J 122  ASN J 146                    
SITE     2 EC7  7 ARG J 284  HIS J 332  NAD J 401                               
SITE     1 EC8 33 ILE K 122  ASN K 146  VAL K 147  VAL K 150                    
SITE     2 EC8 33 GLY K 200  ARG K 201  ILE K 202  ASP K 221                    
SITE     3 EC8 33 ARG K 222  MET K 255  PRO K 256  ASN K 282                    
SITE     4 EC8 33 ALA K 283  ARG K 284  ASP K 308  VAL K 309                    
SITE     5 EC8 33 HIS K 332  SER K 334  GLY K 335  GLN K 376                    
SITE     6 EC8 33 AZI K 403  HOH K 509  HOH K 510  HOH K 512                    
SITE     7 EC8 33 HOH K 513  HOH K 514  HOH K 515  HOH K 516                    
SITE     8 EC8 33 HOH K 517  HOH K 519  HOH K 520  HOH K 521                    
SITE     9 EC8 33 HOH K 645                                                     
SITE     1 EC9  7 PRO K  97  PHE K  98  ILE K 122  ASN K 146                    
SITE     2 EC9  7 ARG K 284  HIS K 332  NAD K 401                               
SITE     1 FC1  6 HOH I 633  GOL K  14  LYS K 115  THR K 138                    
SITE     2 FC1  6 LYS K 369  HOH K 524                                          
SITE     1 FC2  9 SO4 K   8  ARG K 354  TYR K 355  GLY K 358                    
SITE     2 FC2  9 GLU K 359  PHE K 361  TYR K 366  HOH K 629                    
SITE     3 FC2  9 HOH K 630                                                     
SITE     1 FC3  7 GLU J 364  HOH J 405  TYR K 366  LYS K 369                    
SITE     2 FC3  7 GLU K 372  ALA K 374  ARG K 378                               
SITE     1 FC4  5 TYR K 102  HIS K 126  ASP K 128  HOH K 522                    
SITE     2 FC4  5 HOH K 624                                                     
SITE     1 FC5 34 ILE L 122  ASN L 146  VAL L 147  VAL L 150                    
SITE     2 FC5 34 GLY L 200  ARG L 201  ILE L 202  ASP L 221                    
SITE     3 FC5 34 ARG L 222  MET L 255  PRO L 256  ASN L 282                    
SITE     4 FC5 34 ALA L 283  ARG L 284  ASP L 308  VAL L 309                    
SITE     5 FC5 34 HIS L 332  SER L 334  GLY L 335  GLN L 376                    
SITE     6 FC5 34 AZI L 403  HOH L 547  HOH L 548  HOH L 550                    
SITE     7 FC5 34 HOH L 551  HOH L 552  HOH L 553  HOH L 554                    
SITE     8 FC5 34 HOH L 555  HOH L 557  HOH L 558  HOH L 559                    
SITE     9 FC5 34 HOH L 610  HOH L 615                                          
SITE     1 FC6  7 PRO L  97  PHE L  98  ILE L 122  ASN L 146                    
SITE     2 FC6  7 ARG L 284  HIS L 332  NAD L 401                               
SITE     1 FC7  6 TYR L 102  HIS L 126  ASP L 128  HOH L 388                    
SITE     2 FC7  6 HOH L 560  HOH L 644                                          
CRYST1  229.620  217.680  139.110  90.00  92.62  90.00 C 1 2 1      48          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004355  0.000000  0.000200        0.00000                         
SCALE2      0.000000  0.004594  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007196        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system