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Database: PDB
Entry: 6QAK
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Original site: 6QAK 
HEADER    OXIDOREDUCTASE                          19-DEC-18   6QAK              
TITLE     STRUCTURE OF HUMAN ALDH9 IN P21212 SPACE GROUP                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE;               
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: TMABADH,ALDEHYDE DEHYDROGENASE E3 ISOZYME,ALDEHYDE          
COMPND   5 DEHYDROGENASE FAMILY 9 MEMBER A1,GAMMA-AMINOBUTYRALDEHYDE            
COMPND   6 DEHYDROGENASE,R-AMINOBUTYRALDEHYDE DEHYDROGENASE;                    
COMPND   7 EC: 1.2.1.47,1.2.1.3,1.2.1.19;                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ALDH9A1, ALDH4, ALDH7, ALDH9;                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALDEHYDE DEHYDROGENASE, OXIDOREDUCTASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MORERA,A.VIGOUROUX,D.KOPECNY                                        
REVDAT   2   08-MAY-19 6QAK    1       JRNL                                     
REVDAT   1   10-APR-19 6QAK    0                                                
JRNL        AUTH   R.KONCITIKOVA,A.VIGOUROUX,M.KOPECNA,M.SEBELA,S.MORERA,       
JRNL        AUTH 2 D.KOPECNY                                                    
JRNL        TITL   KINETIC AND STRUCTURAL ANALYSIS OF HUMAN ALDH9A1.            
JRNL        REF    BIOSCI.REP.                   V.  39       2019              
JRNL        REFN                   ISSN 0144-8463                               
JRNL        PMID   30914451                                                     
JRNL        DOI    10.1042/BSR20190558                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 142732                         
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)  : 0.192                          
REMARK   3   R VALUE            (WORKING SET)  : 0.191                          
REMARK   3   FREE R VALUE                      : 0.220                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.000                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 7136                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 50                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.50                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.52                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 86.84                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2855                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2820                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2712                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2815                   
REMARK   3   BIN FREE R VALUE                        : 0.2920                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.01                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 143                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 28832                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 85                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 71.51                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -16.47000                                            
REMARK   3    B22 (A**2) : 6.97040                                              
REMARK   3    B33 (A**2) : 9.49960                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.370               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.457               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.240               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.493               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.247               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.934                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 29433  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 39821  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 10172  ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 5056   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 29433  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 3827   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 33972  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.17                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.02                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 20.64                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   21.0358   22.7390   68.3617           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1051 T22:   -0.2445                                    
REMARK   3     T33:   -0.2009 T12:   -0.0150                                    
REMARK   3     T13:    0.1170 T23:   -0.0170                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4309 L22:    1.6537                                    
REMARK   3     L33:    0.7822 L12:   -0.8785                                    
REMARK   3     L13:   -0.2454 L23:   -0.2719                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2429 S12:    0.1218 S13:    0.1855                     
REMARK   3     S21:   -0.0525 S22:   -0.1354 S23:   -0.0550                     
REMARK   3     S31:   -0.1555 S32:   -0.0331 S33:   -0.1075                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   60.6695   20.1430   63.8760           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2243 T22:   -0.2033                                    
REMARK   3     T33:   -0.0313 T12:    0.0403                                    
REMARK   3     T13:    0.0559 T23:    0.0114                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2098 L22:    1.7755                                    
REMARK   3     L33:    0.9425 L12:    0.3580                                    
REMARK   3     L13:    0.3688 L23:    0.1021                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0344 S12:   -0.0433 S13:   -0.0745                     
REMARK   3     S21:    0.0566 S22:   -0.0735 S23:   -0.4377                     
REMARK   3     S31:   -0.0105 S32:    0.0248 S33:    0.1078                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   42.5252  -17.6807   46.8324           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1190 T22:   -0.3060                                    
REMARK   3     T33:   -0.2877 T12:   -0.0473                                    
REMARK   3     T13:   -0.0122 T23:    0.0036                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9419 L22:    2.1806                                    
REMARK   3     L33:    3.9478 L12:    0.0118                                    
REMARK   3     L13:   -0.0316 L23:    1.7471                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2715 S12:   -0.0032 S13:   -0.1265                     
REMARK   3     S21:   -0.0246 S22:   -0.1903 S23:   -0.1284                     
REMARK   3     S31:    0.3759 S32:   -0.4586 S33:   -0.0812                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   34.3805  -17.0702   85.9927           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0402 T22:   -0.1831                                    
REMARK   3     T33:   -0.2693 T12:   -0.0206                                    
REMARK   3     T13:   -0.0586 T23:    0.0194                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0189 L22:    1.6834                                    
REMARK   3     L33:    1.9313 L12:    0.4245                                    
REMARK   3     L13:   -0.0858 L23:   -0.6184                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.3177 S12:   -0.1827 S13:   -0.1597                     
REMARK   3     S21:    0.2974 S22:   -0.3609 S23:   -0.2693                     
REMARK   3     S31:   -0.0116 S32:    0.3931 S33:    0.0432                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { E|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   38.2029   98.7599   34.4018           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0432 T22:   -0.2645                                    
REMARK   3     T33:   -0.3618 T12:   -0.0445                                    
REMARK   3     T13:   -0.0053 T23:    0.0345                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8196 L22:    2.7562                                    
REMARK   3     L33:    2.5632 L12:    0.0903                                    
REMARK   3     L13:   -0.0819 L23:    1.4772                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2096 S12:   -0.1571 S13:   -0.0098                     
REMARK   3     S21:    0.7405 S22:   -0.2085 S23:   -0.0371                     
REMARK   3     S31:    0.2572 S32:   -0.3902 S33:   -0.0011                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { F|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   33.3965   98.6054   -5.3993           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0569 T22:   -0.2732                                    
REMARK   3     T33:   -0.3283 T12:   -0.0484                                    
REMARK   3     T13:    0.0294 T23:    0.0367                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8020 L22:    1.7853                                    
REMARK   3     L33:    1.4129 L12:   -0.5081                                    
REMARK   3     L13:    0.1377 L23:    0.6103                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2733 S12:    0.1085 S13:    0.1348                     
REMARK   3     S21:   -0.2814 S22:   -0.1487 S23:   -0.1905                     
REMARK   3     S31:   -0.1546 S32:    0.1986 S33:   -0.1247                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { G|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   21.9548   57.5679   11.4918           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2273 T22:   -0.1585                                    
REMARK   3     T33:   -0.1843 T12:    0.0416                                    
REMARK   3     T13:   -0.0462 T23:   -0.0025                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.8052 L22:    1.9457                                    
REMARK   3     L33:    1.5259 L12:    0.7940                                    
REMARK   3     L13:    0.0909 L23:   -0.2075                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0170 S12:   -0.2682 S13:    0.0448                     
REMARK   3     S21:    0.0026 S22:   -0.0600 S23:    0.0188                     
REMARK   3     S31:    0.1445 S32:   -0.0011 S33:    0.0430                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { H|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   60.9529   63.1231   17.2536           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3016 T22:   -0.1428                                    
REMARK   3     T33:    0.0173 T12:    0.0154                                    
REMARK   3     T13:    0.0236 T23:    0.0602                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8891 L22:    2.0379                                    
REMARK   3     L33:    1.5275 L12:    0.1770                                    
REMARK   3     L13:   -0.0345 L23:   -0.4910                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1196 S12:    0.0424 S13:   -0.0142                     
REMARK   3     S21:   -0.1823 S22:   -0.2071 S23:   -0.6732                     
REMARK   3     S31:    0.0520 S32:    0.4510 S33:    0.3267                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6QAK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200013557.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUL-18                          
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               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 142787                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 13.40                              
REMARK 200  R MERGE                    (I) : 0.20800                            
REMARK 200  R SYM                      (I) : 0.20000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.65                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1A4S                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4K, SODIUM CITRATE PH 5.6,       
REMARK 280  2.5% ISOPROPANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       80.19000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       79.79500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       80.19000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       79.79500            
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                                                    
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17390 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 62440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17750 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 61760 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -13                                                      
REMARK 465     GLY A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     GLY A   232                                                      
REMARK 465     SER A   233                                                      
REMARK 465     VAL A   234                                                      
REMARK 465     PRO A   235                                                      
REMARK 465     THR A   236                                                      
REMARK 465     GLY A   237                                                      
REMARK 465     MET A   238                                                      
REMARK 465     LYS A   239                                                      
REMARK 465     ILE A   240                                                      
REMARK 465     MET A   241                                                      
REMARK 465     GLU A   242                                                      
REMARK 465     MET A   243                                                      
REMARK 465     SER A   244                                                      
REMARK 465     ALA A   245                                                      
REMARK 465     LYS A   246                                                      
REMARK 465     GLY A   247                                                      
REMARK 465     ILE A   248                                                      
REMARK 465     LYS A   249                                                      
REMARK 465     PRO A   250                                                      
REMARK 465     VAL A   251                                                      
REMARK 465     THR A   252                                                      
REMARK 465     LEU A   253                                                      
REMARK 465     GLU A   254                                                      
REMARK 465     LEU A   255                                                      
REMARK 465     MET B   -13                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     SER B    -3                                                      
REMARK 465     GLN B    -2                                                      
REMARK 465     ASP B    -1                                                      
REMARK 465     GLY B   232                                                      
REMARK 465     SER B   233                                                      
REMARK 465     VAL B   234                                                      
REMARK 465     PRO B   235                                                      
REMARK 465     THR B   236                                                      
REMARK 465     GLY B   237                                                      
REMARK 465     MET B   238                                                      
REMARK 465     LYS B   239                                                      
REMARK 465     ILE B   240                                                      
REMARK 465     MET B   241                                                      
REMARK 465     GLU B   242                                                      
REMARK 465     MET B   243                                                      
REMARK 465     SER B   244                                                      
REMARK 465     ALA B   245                                                      
REMARK 465     LYS B   246                                                      
REMARK 465     GLY B   247                                                      
REMARK 465     ILE B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     PRO B   250                                                      
REMARK 465     VAL B   251                                                      
REMARK 465     THR B   252                                                      
REMARK 465     LEU B   253                                                      
REMARK 465     GLU B   254                                                      
REMARK 465     LEU B   255                                                      
REMARK 465     MET C   -13                                                      
REMARK 465     GLY C   -12                                                      
REMARK 465     SER C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     HIS C    -8                                                      
REMARK 465     HIS C    -7                                                      
REMARK 465     HIS C    -6                                                      
REMARK 465     HIS C    -5                                                      
REMARK 465     HIS C    -4                                                      
REMARK 465     SER C    -3                                                      
REMARK 465     GLN C    -2                                                      
REMARK 465     ASP C    -1                                                      
REMARK 465     GLY C   232                                                      
REMARK 465     SER C   233                                                      
REMARK 465     VAL C   234                                                      
REMARK 465     PRO C   235                                                      
REMARK 465     THR C   236                                                      
REMARK 465     GLY C   237                                                      
REMARK 465     MET C   238                                                      
REMARK 465     LYS C   239                                                      
REMARK 465     ILE C   240                                                      
REMARK 465     MET C   241                                                      
REMARK 465     GLU C   242                                                      
REMARK 465     MET C   243                                                      
REMARK 465     SER C   244                                                      
REMARK 465     ALA C   245                                                      
REMARK 465     LYS C   246                                                      
REMARK 465     GLY C   247                                                      
REMARK 465     ILE C   248                                                      
REMARK 465     LYS C   249                                                      
REMARK 465     PRO C   250                                                      
REMARK 465     VAL C   251                                                      
REMARK 465     THR C   252                                                      
REMARK 465     LEU C   253                                                      
REMARK 465     GLU C   254                                                      
REMARK 465     LEU C   255                                                      
REMARK 465     MET D   -13                                                      
REMARK 465     GLY D   -12                                                      
REMARK 465     SER D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     HIS D    -9                                                      
REMARK 465     HIS D    -8                                                      
REMARK 465     HIS D    -7                                                      
REMARK 465     HIS D    -6                                                      
REMARK 465     HIS D    -5                                                      
REMARK 465     HIS D    -4                                                      
REMARK 465     SER D    -3                                                      
REMARK 465     GLN D    -2                                                      
REMARK 465     ASP D    -1                                                      
REMARK 465     GLY D   232                                                      
REMARK 465     SER D   233                                                      
REMARK 465     VAL D   234                                                      
REMARK 465     PRO D   235                                                      
REMARK 465     THR D   236                                                      
REMARK 465     GLY D   237                                                      
REMARK 465     MET D   238                                                      
REMARK 465     LYS D   239                                                      
REMARK 465     ILE D   240                                                      
REMARK 465     MET D   241                                                      
REMARK 465     GLU D   242                                                      
REMARK 465     MET D   243                                                      
REMARK 465     SER D   244                                                      
REMARK 465     ALA D   245                                                      
REMARK 465     LYS D   246                                                      
REMARK 465     GLY D   247                                                      
REMARK 465     ILE D   248                                                      
REMARK 465     LYS D   249                                                      
REMARK 465     PRO D   250                                                      
REMARK 465     VAL D   251                                                      
REMARK 465     THR D   252                                                      
REMARK 465     LEU D   253                                                      
REMARK 465     GLU D   254                                                      
REMARK 465     LEU D   255                                                      
REMARK 465     MET E   -13                                                      
REMARK 465     GLY E   -12                                                      
REMARK 465     SER E   -11                                                      
REMARK 465     SER E   -10                                                      
REMARK 465     HIS E    -9                                                      
REMARK 465     HIS E    -8                                                      
REMARK 465     HIS E    -7                                                      
REMARK 465     HIS E    -6                                                      
REMARK 465     HIS E    -5                                                      
REMARK 465     HIS E    -4                                                      
REMARK 465     SER E    -3                                                      
REMARK 465     GLN E    -2                                                      
REMARK 465     ASP E    -1                                                      
REMARK 465     GLY E   232                                                      
REMARK 465     SER E   233                                                      
REMARK 465     VAL E   234                                                      
REMARK 465     PRO E   235                                                      
REMARK 465     THR E   236                                                      
REMARK 465     GLY E   237                                                      
REMARK 465     MET E   238                                                      
REMARK 465     LYS E   239                                                      
REMARK 465     ILE E   240                                                      
REMARK 465     MET E   241                                                      
REMARK 465     GLU E   242                                                      
REMARK 465     MET E   243                                                      
REMARK 465     SER E   244                                                      
REMARK 465     ALA E   245                                                      
REMARK 465     LYS E   246                                                      
REMARK 465     GLY E   247                                                      
REMARK 465     ILE E   248                                                      
REMARK 465     LYS E   249                                                      
REMARK 465     PRO E   250                                                      
REMARK 465     VAL E   251                                                      
REMARK 465     THR E   252                                                      
REMARK 465     LEU E   253                                                      
REMARK 465     GLU E   254                                                      
REMARK 465     LEU E   255                                                      
REMARK 465     MET F   -13                                                      
REMARK 465     GLY F   -12                                                      
REMARK 465     SER F   -11                                                      
REMARK 465     SER F   -10                                                      
REMARK 465     HIS F    -9                                                      
REMARK 465     HIS F    -8                                                      
REMARK 465     HIS F    -7                                                      
REMARK 465     HIS F    -6                                                      
REMARK 465     HIS F    -5                                                      
REMARK 465     HIS F    -4                                                      
REMARK 465     SER F    -3                                                      
REMARK 465     GLN F    -2                                                      
REMARK 465     ASP F    -1                                                      
REMARK 465     GLY F   232                                                      
REMARK 465     SER F   233                                                      
REMARK 465     VAL F   234                                                      
REMARK 465     PRO F   235                                                      
REMARK 465     THR F   236                                                      
REMARK 465     GLY F   237                                                      
REMARK 465     MET F   238                                                      
REMARK 465     LYS F   239                                                      
REMARK 465     ILE F   240                                                      
REMARK 465     MET F   241                                                      
REMARK 465     GLU F   242                                                      
REMARK 465     MET F   243                                                      
REMARK 465     SER F   244                                                      
REMARK 465     ALA F   245                                                      
REMARK 465     LYS F   246                                                      
REMARK 465     GLY F   247                                                      
REMARK 465     ILE F   248                                                      
REMARK 465     LYS F   249                                                      
REMARK 465     PRO F   250                                                      
REMARK 465     VAL F   251                                                      
REMARK 465     THR F   252                                                      
REMARK 465     LEU F   253                                                      
REMARK 465     GLU F   254                                                      
REMARK 465     LEU F   255                                                      
REMARK 465     MET G   -13                                                      
REMARK 465     GLY G   -12                                                      
REMARK 465     SER G   -11                                                      
REMARK 465     SER G   -10                                                      
REMARK 465     HIS G    -9                                                      
REMARK 465     HIS G    -8                                                      
REMARK 465     HIS G    -7                                                      
REMARK 465     HIS G    -6                                                      
REMARK 465     HIS G    -5                                                      
REMARK 465     HIS G    -4                                                      
REMARK 465     SER G    -3                                                      
REMARK 465     GLN G    -2                                                      
REMARK 465     ASP G    -1                                                      
REMARK 465     GLY G   232                                                      
REMARK 465     SER G   233                                                      
REMARK 465     VAL G   234                                                      
REMARK 465     PRO G   235                                                      
REMARK 465     THR G   236                                                      
REMARK 465     GLY G   237                                                      
REMARK 465     MET G   238                                                      
REMARK 465     LYS G   239                                                      
REMARK 465     ILE G   240                                                      
REMARK 465     MET G   241                                                      
REMARK 465     GLU G   242                                                      
REMARK 465     MET G   243                                                      
REMARK 465     SER G   244                                                      
REMARK 465     ALA G   245                                                      
REMARK 465     LYS G   246                                                      
REMARK 465     GLY G   247                                                      
REMARK 465     ILE G   248                                                      
REMARK 465     LYS G   249                                                      
REMARK 465     PRO G   250                                                      
REMARK 465     VAL G   251                                                      
REMARK 465     THR G   252                                                      
REMARK 465     LEU G   253                                                      
REMARK 465     GLU G   254                                                      
REMARK 465     LEU G   255                                                      
REMARK 465     MET H   -13                                                      
REMARK 465     GLY H   -12                                                      
REMARK 465     SER H   -11                                                      
REMARK 465     SER H   -10                                                      
REMARK 465     HIS H    -9                                                      
REMARK 465     HIS H    -8                                                      
REMARK 465     HIS H    -7                                                      
REMARK 465     HIS H    -6                                                      
REMARK 465     HIS H    -5                                                      
REMARK 465     HIS H    -4                                                      
REMARK 465     SER H    -3                                                      
REMARK 465     GLN H    -2                                                      
REMARK 465     ASP H    -1                                                      
REMARK 465     GLY H   232                                                      
REMARK 465     SER H   233                                                      
REMARK 465     VAL H   234                                                      
REMARK 465     PRO H   235                                                      
REMARK 465     THR H   236                                                      
REMARK 465     GLY H   237                                                      
REMARK 465     MET H   238                                                      
REMARK 465     LYS H   239                                                      
REMARK 465     ILE H   240                                                      
REMARK 465     MET H   241                                                      
REMARK 465     GLU H   242                                                      
REMARK 465     MET H   243                                                      
REMARK 465     SER H   244                                                      
REMARK 465     ALA H   245                                                      
REMARK 465     LYS H   246                                                      
REMARK 465     GLY H   247                                                      
REMARK 465     ILE H   248                                                      
REMARK 465     LYS H   249                                                      
REMARK 465     PRO H   250                                                      
REMARK 465     VAL H   251                                                      
REMARK 465     THR H   252                                                      
REMARK 465     LEU H   253                                                      
REMARK 465     GLU H   254                                                      
REMARK 465     LEU H   255                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 259      114.90    -39.74                                   
REMARK 500    TYR A 448      118.58   -165.50                                   
REMARK 500    LYS B 462       30.19    -93.60                                   
REMARK 500    THR C 185       65.78   -119.62                                   
REMARK 500    LYS C 462       20.40     86.66                                   
REMARK 500    THR D 185       69.97   -117.07                                   
REMARK 500    TYR E 448      115.54   -167.58                                   
REMARK 500    LYS E 462       31.74    -80.84                                   
REMARK 500    SER E 463     -101.87    -21.04                                   
REMARK 500    ASN F 447     -177.79   -175.62                                   
REMARK 500    LYS F 462       57.51   -111.93                                   
REMARK 500    SER F 463     -110.71    -79.74                                   
REMARK 500    LYS G 298      -44.48    -27.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 514        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH A 515        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH A 516        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH A 517        DISTANCE =  7.60 ANGSTROMS                       
REMARK 525    HOH A 518        DISTANCE =  8.72 ANGSTROMS                       
REMARK 525    HOH A 519        DISTANCE = 10.02 ANGSTROMS                       
REMARK 525    HOH F 512        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH H 509        DISTANCE =  6.04 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 501                 
DBREF  6QAK A    1   494  UNP    P49189   AL9A1_HUMAN      1    494             
DBREF  6QAK B    1   494  UNP    P49189   AL9A1_HUMAN      1    494             
DBREF  6QAK C    1   494  UNP    P49189   AL9A1_HUMAN      1    494             
DBREF  6QAK D    1   494  UNP    P49189   AL9A1_HUMAN      1    494             
DBREF  6QAK E    1   494  UNP    P49189   AL9A1_HUMAN      1    494             
DBREF  6QAK F    1   494  UNP    P49189   AL9A1_HUMAN      1    494             
DBREF  6QAK G    1   494  UNP    P49189   AL9A1_HUMAN      1    494             
DBREF  6QAK H    1   494  UNP    P49189   AL9A1_HUMAN      1    494             
SEQADV 6QAK MET A  -13  UNP  P49189              INITIATING METHIONINE          
SEQADV 6QAK GLY A  -12  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER A  -11  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER A  -10  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS A   -9  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS A   -8  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS A   -7  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS A   -6  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS A   -5  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS A   -4  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER A   -3  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK GLN A   -2  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK ASP A   -1  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK PRO A    0  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK MET B  -13  UNP  P49189              INITIATING METHIONINE          
SEQADV 6QAK GLY B  -12  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER B  -11  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER B  -10  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS B   -9  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS B   -8  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS B   -7  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS B   -6  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS B   -5  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS B   -4  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER B   -3  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK GLN B   -2  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK ASP B   -1  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK PRO B    0  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK MET C  -13  UNP  P49189              INITIATING METHIONINE          
SEQADV 6QAK GLY C  -12  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER C  -11  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER C  -10  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS C   -9  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS C   -8  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS C   -7  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS C   -6  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS C   -5  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS C   -4  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER C   -3  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK GLN C   -2  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK ASP C   -1  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK PRO C    0  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK MET D  -13  UNP  P49189              INITIATING METHIONINE          
SEQADV 6QAK GLY D  -12  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER D  -11  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER D  -10  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS D   -9  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS D   -8  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS D   -7  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS D   -6  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS D   -5  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS D   -4  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER D   -3  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK GLN D   -2  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK ASP D   -1  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK PRO D    0  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK MET E  -13  UNP  P49189              INITIATING METHIONINE          
SEQADV 6QAK GLY E  -12  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER E  -11  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER E  -10  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS E   -9  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS E   -8  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS E   -7  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS E   -6  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS E   -5  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS E   -4  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER E   -3  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK GLN E   -2  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK ASP E   -1  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK PRO E    0  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK MET F  -13  UNP  P49189              INITIATING METHIONINE          
SEQADV 6QAK GLY F  -12  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER F  -11  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER F  -10  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS F   -9  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS F   -8  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS F   -7  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS F   -6  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS F   -5  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS F   -4  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER F   -3  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK GLN F   -2  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK ASP F   -1  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK PRO F    0  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK MET G  -13  UNP  P49189              INITIATING METHIONINE          
SEQADV 6QAK GLY G  -12  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER G  -11  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER G  -10  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS G   -9  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS G   -8  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS G   -7  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS G   -6  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS G   -5  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS G   -4  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER G   -3  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK GLN G   -2  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK ASP G   -1  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK PRO G    0  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK MET H  -13  UNP  P49189              INITIATING METHIONINE          
SEQADV 6QAK GLY H  -12  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER H  -11  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER H  -10  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS H   -9  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS H   -8  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS H   -7  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS H   -6  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS H   -5  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK HIS H   -4  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK SER H   -3  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK GLN H   -2  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK ASP H   -1  UNP  P49189              EXPRESSION TAG                 
SEQADV 6QAK PRO H    0  UNP  P49189              EXPRESSION TAG                 
SEQRES   1 A  508  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 A  508  PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU          
SEQRES   3 A  508  ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA          
SEQRES   4 A  508  SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG          
SEQRES   5 A  508  VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL          
SEQRES   6 A  508  ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE          
SEQRES   7 A  508  TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU          
SEQRES   8 A  508  LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU          
SEQRES   9 A  508  ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE          
SEQRES  10 A  508  PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS          
SEQRES  11 A  508  LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY          
SEQRES  12 A  508  GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR          
SEQRES  13 A  508  ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA          
SEQRES  14 A  508  TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA          
SEQRES  15 A  508  PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO          
SEQRES  16 A  508  SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU          
SEQRES  17 A  508  ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN          
SEQRES  18 A  508  VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS          
SEQRES  19 A  508  GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER          
SEQRES  20 A  508  VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS          
SEQRES  21 A  508  GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 A  508  PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA          
SEQRES  23 A  508  VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY          
SEQRES  24 A  508  GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS          
SEQRES  25 A  508  GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN          
SEQRES  26 A  508  THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP          
SEQRES  27 A  508  THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU          
SEQRES  28 A  508  ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY          
SEQRES  29 A  508  ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU          
SEQRES  30 A  508  ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS          
SEQRES  31 A  508  VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS          
SEQRES  32 A  508  GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE          
SEQRES  33 A  508  ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR          
SEQRES  34 A  508  THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE          
SEQRES  35 A  508  GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY          
SEQRES  36 A  508  THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU          
SEQRES  37 A  508  LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG          
SEQRES  38 A  508  GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU          
SEQRES  39 A  508  LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA          
SEQRES  40 A  508  PHE                                                          
SEQRES   1 B  508  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 B  508  PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU          
SEQRES   3 B  508  ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA          
SEQRES   4 B  508  SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG          
SEQRES   5 B  508  VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL          
SEQRES   6 B  508  ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE          
SEQRES   7 B  508  TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU          
SEQRES   8 B  508  LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU          
SEQRES   9 B  508  ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE          
SEQRES  10 B  508  PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS          
SEQRES  11 B  508  LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY          
SEQRES  12 B  508  GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR          
SEQRES  13 B  508  ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA          
SEQRES  14 B  508  TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA          
SEQRES  15 B  508  PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO          
SEQRES  16 B  508  SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU          
SEQRES  17 B  508  ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN          
SEQRES  18 B  508  VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS          
SEQRES  19 B  508  GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER          
SEQRES  20 B  508  VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS          
SEQRES  21 B  508  GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 B  508  PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA          
SEQRES  23 B  508  VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY          
SEQRES  24 B  508  GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS          
SEQRES  25 B  508  GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN          
SEQRES  26 B  508  THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP          
SEQRES  27 B  508  THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU          
SEQRES  28 B  508  ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY          
SEQRES  29 B  508  ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU          
SEQRES  30 B  508  ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS          
SEQRES  31 B  508  VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS          
SEQRES  32 B  508  GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE          
SEQRES  33 B  508  ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR          
SEQRES  34 B  508  THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE          
SEQRES  35 B  508  GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY          
SEQRES  36 B  508  THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU          
SEQRES  37 B  508  LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG          
SEQRES  38 B  508  GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU          
SEQRES  39 B  508  LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA          
SEQRES  40 B  508  PHE                                                          
SEQRES   1 C  508  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 C  508  PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU          
SEQRES   3 C  508  ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA          
SEQRES   4 C  508  SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG          
SEQRES   5 C  508  VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL          
SEQRES   6 C  508  ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE          
SEQRES   7 C  508  TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU          
SEQRES   8 C  508  LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU          
SEQRES   9 C  508  ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE          
SEQRES  10 C  508  PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS          
SEQRES  11 C  508  LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY          
SEQRES  12 C  508  GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR          
SEQRES  13 C  508  ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA          
SEQRES  14 C  508  TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA          
SEQRES  15 C  508  PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO          
SEQRES  16 C  508  SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU          
SEQRES  17 C  508  ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN          
SEQRES  18 C  508  VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS          
SEQRES  19 C  508  GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER          
SEQRES  20 C  508  VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS          
SEQRES  21 C  508  GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 C  508  PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA          
SEQRES  23 C  508  VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY          
SEQRES  24 C  508  GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS          
SEQRES  25 C  508  GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN          
SEQRES  26 C  508  THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP          
SEQRES  27 C  508  THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU          
SEQRES  28 C  508  ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY          
SEQRES  29 C  508  ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU          
SEQRES  30 C  508  ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS          
SEQRES  31 C  508  VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS          
SEQRES  32 C  508  GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE          
SEQRES  33 C  508  ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR          
SEQRES  34 C  508  THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE          
SEQRES  35 C  508  GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY          
SEQRES  36 C  508  THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU          
SEQRES  37 C  508  LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG          
SEQRES  38 C  508  GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU          
SEQRES  39 C  508  LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA          
SEQRES  40 C  508  PHE                                                          
SEQRES   1 D  508  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 D  508  PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU          
SEQRES   3 D  508  ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA          
SEQRES   4 D  508  SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG          
SEQRES   5 D  508  VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL          
SEQRES   6 D  508  ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE          
SEQRES   7 D  508  TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU          
SEQRES   8 D  508  LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU          
SEQRES   9 D  508  ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE          
SEQRES  10 D  508  PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS          
SEQRES  11 D  508  LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY          
SEQRES  12 D  508  GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR          
SEQRES  13 D  508  ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA          
SEQRES  14 D  508  TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA          
SEQRES  15 D  508  PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO          
SEQRES  16 D  508  SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU          
SEQRES  17 D  508  ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN          
SEQRES  18 D  508  VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS          
SEQRES  19 D  508  GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER          
SEQRES  20 D  508  VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS          
SEQRES  21 D  508  GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 D  508  PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA          
SEQRES  23 D  508  VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY          
SEQRES  24 D  508  GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS          
SEQRES  25 D  508  GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN          
SEQRES  26 D  508  THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP          
SEQRES  27 D  508  THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU          
SEQRES  28 D  508  ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY          
SEQRES  29 D  508  ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU          
SEQRES  30 D  508  ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS          
SEQRES  31 D  508  VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS          
SEQRES  32 D  508  GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE          
SEQRES  33 D  508  ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR          
SEQRES  34 D  508  THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE          
SEQRES  35 D  508  GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY          
SEQRES  36 D  508  THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU          
SEQRES  37 D  508  LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG          
SEQRES  38 D  508  GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU          
SEQRES  39 D  508  LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA          
SEQRES  40 D  508  PHE                                                          
SEQRES   1 E  508  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 E  508  PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU          
SEQRES   3 E  508  ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA          
SEQRES   4 E  508  SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG          
SEQRES   5 E  508  VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL          
SEQRES   6 E  508  ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE          
SEQRES   7 E  508  TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU          
SEQRES   8 E  508  LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU          
SEQRES   9 E  508  ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE          
SEQRES  10 E  508  PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS          
SEQRES  11 E  508  LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY          
SEQRES  12 E  508  GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR          
SEQRES  13 E  508  ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA          
SEQRES  14 E  508  TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA          
SEQRES  15 E  508  PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO          
SEQRES  16 E  508  SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU          
SEQRES  17 E  508  ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN          
SEQRES  18 E  508  VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS          
SEQRES  19 E  508  GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER          
SEQRES  20 E  508  VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS          
SEQRES  21 E  508  GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 E  508  PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA          
SEQRES  23 E  508  VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY          
SEQRES  24 E  508  GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS          
SEQRES  25 E  508  GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN          
SEQRES  26 E  508  THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP          
SEQRES  27 E  508  THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU          
SEQRES  28 E  508  ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY          
SEQRES  29 E  508  ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU          
SEQRES  30 E  508  ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS          
SEQRES  31 E  508  VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS          
SEQRES  32 E  508  GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE          
SEQRES  33 E  508  ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR          
SEQRES  34 E  508  THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE          
SEQRES  35 E  508  GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY          
SEQRES  36 E  508  THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU          
SEQRES  37 E  508  LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG          
SEQRES  38 E  508  GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU          
SEQRES  39 E  508  LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA          
SEQRES  40 E  508  PHE                                                          
SEQRES   1 F  508  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 F  508  PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU          
SEQRES   3 F  508  ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA          
SEQRES   4 F  508  SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG          
SEQRES   5 F  508  VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL          
SEQRES   6 F  508  ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE          
SEQRES   7 F  508  TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU          
SEQRES   8 F  508  LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU          
SEQRES   9 F  508  ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE          
SEQRES  10 F  508  PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS          
SEQRES  11 F  508  LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY          
SEQRES  12 F  508  GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR          
SEQRES  13 F  508  ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA          
SEQRES  14 F  508  TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA          
SEQRES  15 F  508  PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO          
SEQRES  16 F  508  SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU          
SEQRES  17 F  508  ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN          
SEQRES  18 F  508  VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS          
SEQRES  19 F  508  GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER          
SEQRES  20 F  508  VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS          
SEQRES  21 F  508  GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 F  508  PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA          
SEQRES  23 F  508  VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY          
SEQRES  24 F  508  GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS          
SEQRES  25 F  508  GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN          
SEQRES  26 F  508  THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP          
SEQRES  27 F  508  THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU          
SEQRES  28 F  508  ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY          
SEQRES  29 F  508  ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU          
SEQRES  30 F  508  ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS          
SEQRES  31 F  508  VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS          
SEQRES  32 F  508  GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE          
SEQRES  33 F  508  ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR          
SEQRES  34 F  508  THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE          
SEQRES  35 F  508  GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY          
SEQRES  36 F  508  THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU          
SEQRES  37 F  508  LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG          
SEQRES  38 F  508  GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU          
SEQRES  39 F  508  LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA          
SEQRES  40 F  508  PHE                                                          
SEQRES   1 G  508  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 G  508  PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU          
SEQRES   3 G  508  ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA          
SEQRES   4 G  508  SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG          
SEQRES   5 G  508  VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL          
SEQRES   6 G  508  ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE          
SEQRES   7 G  508  TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU          
SEQRES   8 G  508  LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU          
SEQRES   9 G  508  ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE          
SEQRES  10 G  508  PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS          
SEQRES  11 G  508  LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY          
SEQRES  12 G  508  GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR          
SEQRES  13 G  508  ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA          
SEQRES  14 G  508  TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA          
SEQRES  15 G  508  PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO          
SEQRES  16 G  508  SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU          
SEQRES  17 G  508  ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN          
SEQRES  18 G  508  VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS          
SEQRES  19 G  508  GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER          
SEQRES  20 G  508  VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS          
SEQRES  21 G  508  GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 G  508  PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA          
SEQRES  23 G  508  VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY          
SEQRES  24 G  508  GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS          
SEQRES  25 G  508  GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN          
SEQRES  26 G  508  THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP          
SEQRES  27 G  508  THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU          
SEQRES  28 G  508  ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY          
SEQRES  29 G  508  ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU          
SEQRES  30 G  508  ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS          
SEQRES  31 G  508  VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS          
SEQRES  32 G  508  GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE          
SEQRES  33 G  508  ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR          
SEQRES  34 G  508  THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE          
SEQRES  35 G  508  GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY          
SEQRES  36 G  508  THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU          
SEQRES  37 G  508  LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG          
SEQRES  38 G  508  GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU          
SEQRES  39 G  508  LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA          
SEQRES  40 G  508  PHE                                                          
SEQRES   1 H  508  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 H  508  PRO MET SER THR GLY THR PHE VAL VAL SER GLN PRO LEU          
SEQRES   3 H  508  ASN TYR ARG GLY GLY ALA ARG VAL GLU PRO ALA ASP ALA          
SEQRES   4 H  508  SER GLY THR GLU LYS ALA PHE GLU PRO ALA THR GLY ARG          
SEQRES   5 H  508  VAL ILE ALA THR PHE THR CYS SER GLY GLU LYS GLU VAL          
SEQRES   6 H  508  ASN LEU ALA VAL GLN ASN ALA LYS ALA ALA PHE LYS ILE          
SEQRES   7 H  508  TRP SER GLN LYS SER GLY MET GLU ARG CYS ARG ILE LEU          
SEQRES   8 H  508  LEU GLU ALA ALA ARG ILE ILE ARG GLU ARG GLU ASP GLU          
SEQRES   9 H  508  ILE ALA THR MET GLU CYS ILE ASN ASN GLY LYS SER ILE          
SEQRES  10 H  508  PHE GLU ALA ARG LEU ASP ILE ASP ILE SER TRP GLN CYS          
SEQRES  11 H  508  LEU GLU TYR TYR ALA GLY LEU ALA ALA SER MET ALA GLY          
SEQRES  12 H  508  GLU HIS ILE GLN LEU PRO GLY GLY SER PHE GLY TYR THR          
SEQRES  13 H  508  ARG ARG GLU PRO LEU GLY VAL CYS VAL GLY ILE GLY ALA          
SEQRES  14 H  508  TRP ASN TYR PRO PHE GLN ILE ALA SER TRP LYS SER ALA          
SEQRES  15 H  508  PRO ALA LEU ALA CYS GLY ASN ALA MET VAL PHE LYS PRO          
SEQRES  16 H  508  SER PRO PHE THR PRO VAL SER ALA LEU LEU LEU ALA GLU          
SEQRES  17 H  508  ILE TYR SER GLU ALA GLY VAL PRO PRO GLY LEU PHE ASN          
SEQRES  18 H  508  VAL VAL GLN GLY GLY ALA ALA THR GLY GLN PHE LEU CYS          
SEQRES  19 H  508  GLN HIS PRO ASP VAL ALA LYS VAL SER PHE THR GLY SER          
SEQRES  20 H  508  VAL PRO THR GLY MET LYS ILE MET GLU MET SER ALA LYS          
SEQRES  21 H  508  GLY ILE LYS PRO VAL THR LEU GLU LEU GLY GLY LYS SER          
SEQRES  22 H  508  PRO LEU ILE ILE PHE SER ASP CYS ASP MET ASN ASN ALA          
SEQRES  23 H  508  VAL LYS GLY ALA LEU MET ALA ASN PHE LEU THR GLN GLY          
SEQRES  24 H  508  GLN VAL CYS CYS ASN GLY THR ARG VAL PHE VAL GLN LYS          
SEQRES  25 H  508  GLU ILE LEU ASP LYS PHE THR GLU GLU VAL VAL LYS GLN          
SEQRES  26 H  508  THR GLN ARG ILE LYS ILE GLY ASP PRO LEU LEU GLU ASP          
SEQRES  27 H  508  THR ARG MET GLY PRO LEU ILE ASN ARG PRO HIS LEU GLU          
SEQRES  28 H  508  ARG VAL LEU GLY PHE VAL LYS VAL ALA LYS GLU GLN GLY          
SEQRES  29 H  508  ALA LYS VAL LEU CYS GLY GLY ASP ILE TYR VAL PRO GLU          
SEQRES  30 H  508  ASP PRO LYS LEU LYS ASP GLY TYR TYR MET ARG PRO CYS          
SEQRES  31 H  508  VAL LEU THR ASN CYS ARG ASP ASP MET THR CYS VAL LYS          
SEQRES  32 H  508  GLU GLU ILE PHE GLY PRO VAL MET SER ILE LEU SER PHE          
SEQRES  33 H  508  ASP THR GLU ALA GLU VAL LEU GLU ARG ALA ASN ASP THR          
SEQRES  34 H  508  THR PHE GLY LEU ALA ALA GLY VAL PHE THR ARG ASP ILE          
SEQRES  35 H  508  GLN ARG ALA HIS ARG VAL VAL ALA GLU LEU GLN ALA GLY          
SEQRES  36 H  508  THR CYS PHE ILE ASN ASN TYR ASN VAL SER PRO VAL GLU          
SEQRES  37 H  508  LEU PRO PHE GLY GLY TYR LYS LYS SER GLY PHE GLY ARG          
SEQRES  38 H  508  GLU ASN GLY ARG VAL THR ILE GLU TYR TYR SER GLN LEU          
SEQRES  39 H  508  LYS THR VAL CYS VAL GLU MET GLY ASP VAL GLU SER ALA          
SEQRES  40 H  508  PHE                                                          
HET    EDO  B 501       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   9  EDO    C2 H6 O2                                                     
FORMUL  10  HOH   *85(H2 O)                                                     
HELIX    1 AA1 GLY A   47  SER A   66  1                                  20    
HELIX    2 AA2 SER A   69  ARG A   87  1                                  19    
HELIX    3 AA3 ARG A   87  GLY A  100  1                                  14    
HELIX    4 AA4 SER A  102  SER A  126  1                                  25    
HELIX    5 AA5 PRO A  135  GLY A  137  5                                   3    
HELIX    6 AA6 TYR A  158  CYS A  173  1                                  16    
HELIX    7 AA7 VAL A  187  GLY A  200  1                                  14    
HELIX    8 AA8 GLY A  212  HIS A  222  1                                  11    
HELIX    9 AA9 ASP A  268  LEU A  282  1                                  15    
HELIX   10 AB1 THR A  283  GLN A  286  5                                   4    
HELIX   11 AB2 LYS A  298  GLN A  313  1                                  16    
HELIX   12 AB3 ASN A  332  GLN A  349  1                                  18    
HELIX   13 AB4 ASP A  364  LYS A  368  5                                   5    
HELIX   14 AB5 MET A  385  GLU A  390  1                                   6    
HELIX   15 AB6 THR A  404  ALA A  412  1                                   9    
HELIX   16 AB7 ASP A  427  LEU A  438  1                                  12    
HELIX   17 AB8 PRO A  456  TYR A  460  5                                   5    
HELIX   18 AB9 ARG A  467  TYR A  477  1                                  11    
HELIX   19 AC1 GLY B   47  SER B   66  1                                  20    
HELIX   20 AC2 SER B   69  ARG B   87  1                                  19    
HELIX   21 AC3 ARG B   87  GLY B  100  1                                  14    
HELIX   22 AC4 SER B  102  SER B  126  1                                  25    
HELIX   23 AC5 PRO B  135  GLY B  137  5                                   3    
HELIX   24 AC6 TYR B  158  CYS B  173  1                                  16    
HELIX   25 AC7 VAL B  187  GLY B  200  1                                  14    
HELIX   26 AC8 GLY B  212  HIS B  222  1                                  11    
HELIX   27 AC9 ASP B  268  LEU B  282  1                                  15    
HELIX   28 AD1 THR B  283  GLN B  286  5                                   4    
HELIX   29 AD2 LYS B  298  GLN B  313  1                                  16    
HELIX   30 AD3 ASN B  332  GLN B  349  1                                  18    
HELIX   31 AD4 ASP B  364  LYS B  368  5                                   5    
HELIX   32 AD5 MET B  385  GLU B  390  1                                   6    
HELIX   33 AD6 THR B  404  ALA B  412  1                                   9    
HELIX   34 AD7 ASP B  427  LEU B  438  1                                  12    
HELIX   35 AD8 PRO B  456  TYR B  460  5                                   5    
HELIX   36 AD9 ARG B  467  TYR B  477  1                                  11    
HELIX   37 AE1 GLY C   47  SER C   66  1                                  20    
HELIX   38 AE2 SER C   69  ARG C   87  1                                  19    
HELIX   39 AE3 ARG C   87  GLY C  100  1                                  14    
HELIX   40 AE4 SER C  102  MET C  127  1                                  26    
HELIX   41 AE5 PRO C  135  GLY C  137  5                                   3    
HELIX   42 AE6 TYR C  158  CYS C  173  1                                  16    
HELIX   43 AE7 VAL C  187  GLY C  200  1                                  14    
HELIX   44 AE8 GLY C  212  HIS C  222  1                                  11    
HELIX   45 AE9 ASP C  268  LEU C  282  1                                  15    
HELIX   46 AF1 THR C  283  GLN C  286  5                                   4    
HELIX   47 AF2 LYS C  298  GLN C  313  1                                  16    
HELIX   48 AF3 ASN C  332  GLN C  349  1                                  18    
HELIX   49 AF4 ASP C  364  LYS C  368  5                                   5    
HELIX   50 AF5 MET C  385  GLU C  390  1                                   6    
HELIX   51 AF6 THR C  404  ALA C  412  1                                   9    
HELIX   52 AF7 ASP C  427  LEU C  438  1                                  12    
HELIX   53 AF8 PRO C  456  TYR C  460  5                                   5    
HELIX   54 AF9 ARG C  467  TYR C  477  1                                  11    
HELIX   55 AG1 GLY D   47  SER D   66  1                                  20    
HELIX   56 AG2 SER D   69  ARG D   87  1                                  19    
HELIX   57 AG3 ARG D   87  GLY D  100  1                                  14    
HELIX   58 AG4 SER D  102  SER D  126  1                                  25    
HELIX   59 AG5 PRO D  135  GLY D  137  5                                   3    
HELIX   60 AG6 TYR D  158  CYS D  173  1                                  16    
HELIX   61 AG7 VAL D  187  GLY D  200  1                                  14    
HELIX   62 AG8 GLY D  212  HIS D  222  1                                  11    
HELIX   63 AG9 ASP D  268  LEU D  282  1                                  15    
HELIX   64 AH1 THR D  283  GLN D  286  5                                   4    
HELIX   65 AH2 LYS D  298  GLN D  313  1                                  16    
HELIX   66 AH3 ASN D  332  GLN D  349  1                                  18    
HELIX   67 AH4 ASP D  364  LYS D  368  5                                   5    
HELIX   68 AH5 MET D  385  GLU D  390  1                                   6    
HELIX   69 AH6 THR D  404  ALA D  412  1                                   9    
HELIX   70 AH7 ASP D  427  LEU D  438  1                                  12    
HELIX   71 AH8 PRO D  456  TYR D  460  5                                   5    
HELIX   72 AH9 ARG D  467  TYR D  477  1                                  11    
HELIX   73 AI1 GLY E   47  GLN E   67  1                                  21    
HELIX   74 AI2 SER E   69  ARG E   87  1                                  19    
HELIX   75 AI3 ARG E   87  GLY E  100  1                                  14    
HELIX   76 AI4 SER E  102  MET E  127  1                                  26    
HELIX   77 AI5 PRO E  135  GLY E  137  5                                   3    
HELIX   78 AI6 TYR E  158  GLY E  174  1                                  17    
HELIX   79 AI7 VAL E  187  GLY E  200  1                                  14    
HELIX   80 AI8 GLY E  212  HIS E  222  1                                  11    
HELIX   81 AI9 ASP E  268  LEU E  282  1                                  15    
HELIX   82 AJ1 THR E  283  GLN E  286  5                                   4    
HELIX   83 AJ2 LYS E  298  GLN E  313  1                                  16    
HELIX   84 AJ3 ASN E  332  GLN E  349  1                                  18    
HELIX   85 AJ4 ASP E  364  LYS E  368  5                                   5    
HELIX   86 AJ5 MET E  385  GLU E  390  1                                   6    
HELIX   87 AJ6 THR E  404  ALA E  412  1                                   9    
HELIX   88 AJ7 ASP E  427  LEU E  438  1                                  12    
HELIX   89 AJ8 PRO E  456  TYR E  460  5                                   5    
HELIX   90 AJ9 ARG E  467  TYR E  477  1                                  11    
HELIX   91 AK1 GLY F   47  SER F   66  1                                  20    
HELIX   92 AK2 SER F   69  ARG F   87  1                                  19    
HELIX   93 AK3 ARG F   87  GLY F  100  1                                  14    
HELIX   94 AK4 SER F  102  SER F  126  1                                  25    
HELIX   95 AK5 TYR F  158  CYS F  173  1                                  16    
HELIX   96 AK6 VAL F  187  GLY F  200  1                                  14    
HELIX   97 AK7 GLY F  212  HIS F  222  1                                  11    
HELIX   98 AK8 ASP F  268  LEU F  282  1                                  15    
HELIX   99 AK9 THR F  283  GLN F  286  5                                   4    
HELIX  100 AL1 LYS F  298  GLN F  313  1                                  16    
HELIX  101 AL2 ASN F  332  GLN F  349  1                                  18    
HELIX  102 AL3 ASP F  364  LYS F  368  5                                   5    
HELIX  103 AL4 MET F  385  GLU F  390  1                                   6    
HELIX  104 AL5 THR F  404  ALA F  412  1                                   9    
HELIX  105 AL6 ASP F  427  LEU F  438  1                                  12    
HELIX  106 AL7 PRO F  456  TYR F  460  5                                   5    
HELIX  107 AL8 ARG F  467  TYR F  477  1                                  11    
HELIX  108 AL9 GLY G   47  SER G   66  1                                  20    
HELIX  109 AM1 SER G   69  ARG G   87  1                                  19    
HELIX  110 AM2 ARG G   87  GLY G  100  1                                  14    
HELIX  111 AM3 SER G  102  SER G  126  1                                  25    
HELIX  112 AM4 PRO G  135  GLY G  137  5                                   3    
HELIX  113 AM5 TYR G  158  CYS G  173  1                                  16    
HELIX  114 AM6 VAL G  187  GLY G  200  1                                  14    
HELIX  115 AM7 GLY G  212  HIS G  222  1                                  11    
HELIX  116 AM8 ASP G  268  LEU G  282  1                                  15    
HELIX  117 AM9 THR G  283  GLN G  286  5                                   4    
HELIX  118 AN1 LYS G  298  GLN G  313  1                                  16    
HELIX  119 AN2 ASN G  332  GLN G  349  1                                  18    
HELIX  120 AN3 ASP G  364  LYS G  368  5                                   5    
HELIX  121 AN4 MET G  385  GLU G  390  1                                   6    
HELIX  122 AN5 THR G  404  ALA G  412  1                                   9    
HELIX  123 AN6 ASP G  427  LEU G  438  1                                  12    
HELIX  124 AN7 PRO G  456  TYR G  460  5                                   5    
HELIX  125 AN8 ARG G  467  TYR G  477  1                                  11    
HELIX  126 AN9 GLY H   47  GLN H   67  1                                  21    
HELIX  127 AO1 SER H   69  ARG H   87  1                                  19    
HELIX  128 AO2 ARG H   87  GLY H  100  1                                  14    
HELIX  129 AO3 SER H  102  MET H  127  1                                  26    
HELIX  130 AO4 TYR H  158  CYS H  173  1                                  16    
HELIX  131 AO5 VAL H  187  GLY H  200  1                                  14    
HELIX  132 AO6 GLY H  212  HIS H  222  1                                  11    
HELIX  133 AO7 ASP H  268  LEU H  282  1                                  15    
HELIX  134 AO8 THR H  283  GLN H  286  5                                   4    
HELIX  135 AO9 LYS H  298  GLN H  313  1                                  16    
HELIX  136 AP1 ASN H  332  GLN H  349  1                                  18    
HELIX  137 AP2 ASP H  364  LYS H  368  5                                   5    
HELIX  138 AP3 MET H  385  GLU H  390  1                                   6    
HELIX  139 AP4 THR H  404  ALA H  412  1                                   9    
HELIX  140 AP5 ASP H  427  LEU H  438  1                                  12    
HELIX  141 AP6 PRO H  456  TYR H  460  5                                   5    
HELIX  142 AP7 ARG H  467  TYR H  477  1                                  11    
SHEET    1 AA1 2 ASN A  13  ARG A  15  0                                        
SHEET    2 AA1 2 ALA A  18  VAL A  20 -1  O  ALA A  18   N  ARG A  15           
SHEET    1 AA2 2 ALA A  25  PHE A  32  0                                        
SHEET    2 AA2 2 VAL A  39  SER A  46 -1  O  CYS A  45   N  GLY A  27           
SHEET    1 AA320 LYS B 352  CYS B 355  0                                        
SHEET    2 AA320 CYS B 376  THR B 379 -1  O  VAL B 377   N  LEU B 354           
SHEET    3 AA320 VAL B 396  PHE B 402  1  O  MET B 397   N  LEU B 378           
SHEET    4 AA320 ARG B 293  GLN B 297  1  N  VAL B 294   O  SER B 398           
SHEET    5 AA320 PRO B 260  ILE B 263  1  N  ILE B 263   O  PHE B 295           
SHEET    6 AA320 ALA B 420  PHE B 424  1  O  GLY B 422   N  ILE B 262           
SHEET    7 AA320 THR B 442  ILE B 445  1  O  PHE B 444   N  VAL B 423           
SHEET    8 AA320 SER A 478  VAL A 485  1  N  THR A 482   O  CYS B 443           
SHEET    9 AA320 PHE A 139  PRO A 146 -1  N  PHE A 139   O  VAL A 485           
SHEET   10 AA320 GLY A 129  GLN A 133 -1  N  ILE A 132   O  GLY A 140           
SHEET   11 AA320 GLY C 129  GLN C 133 -1  O  HIS C 131   N  GLY A 129           
SHEET   12 AA320 PHE C 139  PRO C 146 -1  O  GLY C 140   N  ILE C 132           
SHEET   13 AA320 SER C 478  VAL C 485 -1  O  VAL C 485   N  PHE C 139           
SHEET   14 AA320 THR D 442  ILE D 445  1  O  CYS D 443   N  THR C 482           
SHEET   15 AA320 ALA D 420  PHE D 424  1  N  ALA D 421   O  PHE D 444           
SHEET   16 AA320 PRO D 260  ILE D 263  1  N  ILE D 262   O  GLY D 422           
SHEET   17 AA320 ARG D 293  GLN D 297  1  O  PHE D 295   N  ILE D 263           
SHEET   18 AA320 VAL D 396  PHE D 402  1  O  SER D 398   N  VAL D 294           
SHEET   19 AA320 CYS D 376  THR D 379  1  N  LEU D 378   O  MET D 397           
SHEET   20 AA320 LYS D 352  CYS D 355 -1  N  LEU D 354   O  VAL D 377           
SHEET    1 AA4 4 PHE A 206  VAL A 208  0                                        
SHEET    2 AA4 4 ALA A 176  LYS A 180  1  N  PHE A 179   O  ASN A 207           
SHEET    3 AA4 4 VAL A 149  ILE A 153  1  N  GLY A 152   O  LYS A 180           
SHEET    4 AA4 4 VAL A 225  SER A 229  1  O  SER A 229   N  VAL A 151           
SHEET    1 AA520 LYS A 352  CYS A 355  0                                        
SHEET    2 AA520 CYS A 376  THR A 379 -1  O  VAL A 377   N  LEU A 354           
SHEET    3 AA520 VAL A 396  PHE A 402  1  O  MET A 397   N  LEU A 378           
SHEET    4 AA520 ARG A 293  GLN A 297  1  N  VAL A 294   O  SER A 398           
SHEET    5 AA520 PRO A 260  ILE A 263  1  N  ILE A 263   O  PHE A 295           
SHEET    6 AA520 ALA A 420  PHE A 424  1  O  GLY A 422   N  ILE A 262           
SHEET    7 AA520 THR A 442  ILE A 445  1  O  PHE A 444   N  VAL A 423           
SHEET    8 AA520 SER B 478  VAL B 485  1  O  THR B 482   N  CYS A 443           
SHEET    9 AA520 PHE B 139  PRO B 146 -1  N  PHE B 139   O  VAL B 485           
SHEET   10 AA520 GLY B 129  GLN B 133 -1  N  ILE B 132   O  GLY B 140           
SHEET   11 AA520 GLY D 129  GLN D 133 -1  O  HIS D 131   N  GLY B 129           
SHEET   12 AA520 PHE D 139  PRO D 146 -1  O  GLY D 140   N  ILE D 132           
SHEET   13 AA520 SER D 478  VAL D 485 -1  O  VAL D 485   N  PHE D 139           
SHEET   14 AA520 THR C 442  ILE C 445  1  N  CYS C 443   O  THR D 482           
SHEET   15 AA520 ALA C 420  PHE C 424  1  N  VAL C 423   O  PHE C 444           
SHEET   16 AA520 PRO C 260  ILE C 263  1  N  ILE C 262   O  GLY C 422           
SHEET   17 AA520 ARG C 293  GLN C 297  1  O  PHE C 295   N  ILE C 263           
SHEET   18 AA520 VAL C 396  PHE C 402  1  O  SER C 398   N  VAL C 294           
SHEET   19 AA520 CYS C 376  THR C 379  1  N  LEU C 378   O  MET C 397           
SHEET   20 AA520 LYS C 352  CYS C 355 -1  N  LEU C 354   O  VAL C 377           
SHEET    1 AA6 2 ASN B  13  ARG B  15  0                                        
SHEET    2 AA6 2 ALA B  18  VAL B  20 -1  O  ALA B  18   N  ARG B  15           
SHEET    1 AA7 2 GLY B  27  PHE B  32  0                                        
SHEET    2 AA7 2 VAL B  39  CYS B  45 -1  O  CYS B  45   N  GLY B  27           
SHEET    1 AA8 4 PHE B 206  VAL B 208  0                                        
SHEET    2 AA8 4 ALA B 176  LYS B 180  1  N  PHE B 179   O  ASN B 207           
SHEET    3 AA8 4 VAL B 149  ILE B 153  1  N  GLY B 152   O  LYS B 180           
SHEET    4 AA8 4 VAL B 225  SER B 229  1  O  SER B 229   N  VAL B 151           
SHEET    1 AA9 2 ASN C  13  ARG C  15  0                                        
SHEET    2 AA9 2 ALA C  18  VAL C  20 -1  O  ALA C  18   N  ARG C  15           
SHEET    1 AB1 2 ALA C  25  PHE C  32  0                                        
SHEET    2 AB1 2 VAL C  39  SER C  46 -1  O  ALA C  41   N  ALA C  31           
SHEET    1 AB2 4 PHE C 206  VAL C 208  0                                        
SHEET    2 AB2 4 ALA C 176  LYS C 180  1  N  PHE C 179   O  ASN C 207           
SHEET    3 AB2 4 VAL C 149  ILE C 153  1  N  GLY C 152   O  LYS C 180           
SHEET    4 AB2 4 VAL C 225  SER C 229  1  O  SER C 229   N  VAL C 151           
SHEET    1 AB3 2 ASN D  13  ARG D  15  0                                        
SHEET    2 AB3 2 ALA D  18  VAL D  20 -1  O  ALA D  18   N  ARG D  15           
SHEET    1 AB4 2 ALA D  25  PHE D  32  0                                        
SHEET    2 AB4 2 VAL D  39  SER D  46 -1  O  CYS D  45   N  GLY D  27           
SHEET    1 AB5 4 PHE D 206  VAL D 208  0                                        
SHEET    2 AB5 4 ALA D 176  LYS D 180  1  N  PHE D 179   O  ASN D 207           
SHEET    3 AB5 4 VAL D 149  ILE D 153  1  N  GLY D 152   O  LYS D 180           
SHEET    4 AB5 4 VAL D 225  SER D 229  1  O  SER D 229   N  VAL D 151           
SHEET    1 AB6 2 ASN E  13  ARG E  15  0                                        
SHEET    2 AB6 2 ALA E  18  VAL E  20 -1  O  VAL E  20   N  ASN E  13           
SHEET    1 AB7 2 ALA E  25  PHE E  32  0                                        
SHEET    2 AB7 2 VAL E  39  SER E  46 -1  O  ALA E  41   N  ALA E  31           
SHEET    1 AB820 LYS F 352  CYS F 355  0                                        
SHEET    2 AB820 CYS F 376  CYS F 381 -1  O  VAL F 377   N  LEU F 354           
SHEET    3 AB820 VAL F 396  PHE F 402  1  O  MET F 397   N  LEU F 378           
SHEET    4 AB820 ARG F 293  GLN F 297  1  N  VAL F 294   O  SER F 398           
SHEET    5 AB820 PRO F 260  ILE F 263  1  N  ILE F 263   O  PHE F 295           
SHEET    6 AB820 ALA F 420  PHE F 424  1  O  GLY F 422   N  ILE F 262           
SHEET    7 AB820 THR F 442  ILE F 445  1  O  PHE F 444   N  VAL F 423           
SHEET    8 AB820 SER E 478  VAL E 485  1  N  CYS E 484   O  ILE F 445           
SHEET    9 AB820 PHE E 139  PRO E 146 -1  N  PHE E 139   O  VAL E 485           
SHEET   10 AB820 GLY E 129  GLN E 133 -1  N  ILE E 132   O  GLY E 140           
SHEET   11 AB820 GLY G 129  GLN G 133 -1  O  HIS G 131   N  GLY E 129           
SHEET   12 AB820 PHE G 139  PRO G 146 -1  O  GLY G 140   N  ILE G 132           
SHEET   13 AB820 SER G 478  VAL G 485 -1  O  VAL G 485   N  PHE G 139           
SHEET   14 AB820 THR H 442  ILE H 445  1  O  ILE H 445   N  CYS G 484           
SHEET   15 AB820 ALA H 420  PHE H 424  1  N  VAL H 423   O  PHE H 444           
SHEET   16 AB820 PRO H 260  ILE H 263  1  N  ILE H 262   O  GLY H 422           
SHEET   17 AB820 ARG H 293  GLN H 297  1  O  PHE H 295   N  ILE H 263           
SHEET   18 AB820 VAL H 396  PHE H 402  1  O  SER H 398   N  VAL H 294           
SHEET   19 AB820 CYS H 376  THR H 379  1  N  LEU H 378   O  MET H 397           
SHEET   20 AB820 LYS H 352  CYS H 355 -1  N  LEU H 354   O  VAL H 377           
SHEET    1 AB9 4 PHE E 206  VAL E 208  0                                        
SHEET    2 AB9 4 ALA E 176  LYS E 180  1  N  PHE E 179   O  ASN E 207           
SHEET    3 AB9 4 VAL E 149  ILE E 153  1  N  GLY E 152   O  LYS E 180           
SHEET    4 AB9 4 VAL E 225  SER E 229  1  O  SER E 229   N  VAL E 151           
SHEET    1 AC120 LYS E 352  CYS E 355  0                                        
SHEET    2 AC120 CYS E 376  THR E 379 -1  O  VAL E 377   N  LEU E 354           
SHEET    3 AC120 VAL E 396  PHE E 402  1  O  MET E 397   N  LEU E 378           
SHEET    4 AC120 ARG E 293  GLN E 297  1  N  VAL E 294   O  SER E 398           
SHEET    5 AC120 PRO E 260  ILE E 263  1  N  ILE E 263   O  PHE E 295           
SHEET    6 AC120 ALA E 420  PHE E 424  1  O  GLY E 422   N  ILE E 262           
SHEET    7 AC120 THR E 442  ILE E 445  1  O  PHE E 444   N  VAL E 423           
SHEET    8 AC120 SER F 478  VAL F 485  1  O  THR F 482   N  CYS E 443           
SHEET    9 AC120 PHE F 139  PRO F 146 -1  N  GLU F 145   O  GLN F 479           
SHEET   10 AC120 GLY F 129  GLN F 133 -1  N  ILE F 132   O  GLY F 140           
SHEET   11 AC120 GLY H 129  GLN H 133 -1  O  GLY H 129   N  HIS F 131           
SHEET   12 AC120 PHE H 139  PRO H 146 -1  O  GLY H 140   N  ILE H 132           
SHEET   13 AC120 SER H 478  VAL H 485 -1  O  VAL H 485   N  PHE H 139           
SHEET   14 AC120 THR G 442  ILE G 445  1  N  CYS G 443   O  THR H 482           
SHEET   15 AC120 ALA G 420  PHE G 424  1  N  VAL G 423   O  PHE G 444           
SHEET   16 AC120 PRO G 260  ILE G 263  1  N  ILE G 262   O  GLY G 422           
SHEET   17 AC120 ARG G 293  GLN G 297  1  O  PHE G 295   N  ILE G 263           
SHEET   18 AC120 VAL G 396  PHE G 402  1  O  SER G 398   N  VAL G 294           
SHEET   19 AC120 CYS G 376  THR G 379  1  N  LEU G 378   O  MET G 397           
SHEET   20 AC120 LYS G 352  CYS G 355 -1  N  LEU G 354   O  VAL G 377           
SHEET    1 AC2 2 ASN F  13  ARG F  15  0                                        
SHEET    2 AC2 2 ALA F  18  VAL F  20 -1  O  ALA F  18   N  ARG F  15           
SHEET    1 AC3 2 ALA F  25  PHE F  32  0                                        
SHEET    2 AC3 2 VAL F  39  SER F  46 -1  O  CYS F  45   N  GLY F  27           
SHEET    1 AC4 4 PHE F 206  VAL F 208  0                                        
SHEET    2 AC4 4 ALA F 176  LYS F 180  1  N  PHE F 179   O  ASN F 207           
SHEET    3 AC4 4 VAL F 149  ILE F 153  1  N  CYS F 150   O  VAL F 178           
SHEET    4 AC4 4 LYS F 227  SER F 229  1  O  SER F 229   N  ILE F 153           
SHEET    1 AC5 2 ASN G  13  ARG G  15  0                                        
SHEET    2 AC5 2 ALA G  18  VAL G  20 -1  O  ALA G  18   N  ARG G  15           
SHEET    1 AC6 2 ALA G  25  PHE G  32  0                                        
SHEET    2 AC6 2 VAL G  39  SER G  46 -1  O  CYS G  45   N  GLY G  27           
SHEET    1 AC7 4 PHE G 206  VAL G 208  0                                        
SHEET    2 AC7 4 ALA G 176  LYS G 180  1  N  PHE G 179   O  ASN G 207           
SHEET    3 AC7 4 VAL G 149  ILE G 153  1  N  GLY G 152   O  LYS G 180           
SHEET    4 AC7 4 VAL G 225  SER G 229  1  O  SER G 229   N  VAL G 151           
SHEET    1 AC8 2 ASN H  13  ARG H  15  0                                        
SHEET    2 AC8 2 ALA H  18  VAL H  20 -1  O  ALA H  18   N  ARG H  15           
SHEET    1 AC9 2 ALA H  25  PHE H  32  0                                        
SHEET    2 AC9 2 VAL H  39  SER H  46 -1  O  CYS H  45   N  GLY H  27           
SHEET    1 AD1 4 PHE H 206  VAL H 208  0                                        
SHEET    2 AD1 4 ALA H 176  LYS H 180  1  N  PHE H 179   O  ASN H 207           
SHEET    3 AD1 4 VAL H 149  ILE H 153  1  N  CYS H 150   O  ALA H 176           
SHEET    4 AD1 4 VAL H 225  SER H 229  1  O  SER H 229   N  VAL H 151           
SITE     1 AC1  1 GLN B 217                                                     
CRYST1  160.380  159.590  160.610  90.00  90.00  90.00 P 21 21 2    32          
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      0.006235  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006266  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006226        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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