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Database: PDB
Entry: 3QGA
LinkDB: 3QGA
Original site: 3QGA 
HEADER    HYDROLASE                               24-JAN-11   3QGA              
TITLE     3.0 A MODEL OF IRON CONTAINING UREASE UREA2B2 FROM HELICOBACTER       
TITLE    2 MUSTELAE                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FUSION OF UREASE BETA AND GAMMA SUBUNITS;                  
COMPND   3 CHAIN: A, D, G, J, M, P;                                             
COMPND   4 SYNONYM: UREA2;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: UREASE SUBUNIT BETA 2;                                     
COMPND   8 CHAIN: C, F, I, L, O, R;                                             
COMPND   9 SYNONYM: UREB2, UREA AMIDOHYDROLASE SUBUNIT BETA 2;                  
COMPND  10 EC: 3.5.1.5;                                                         
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HELICOBACTER MUSTELAE;                          
SOURCE   3 ORGANISM_COMMON: CAMPYLOBACTER MUSTELAE;                             
SOURCE   4 ORGANISM_TAXID: 679897;                                              
SOURCE   5 STRAIN: ATCC 43772 / LMG 18044 / NCTC 12198 / 12198;                 
SOURCE   6 GENE: HMU13020, UREA2;                                               
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD;                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PEC015;                                   
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HELICOBACTER MUSTELAE;                          
SOURCE  14 ORGANISM_COMMON: CAMPYLOBACTER MUSTELAE;                             
SOURCE  15 ORGANISM_TAXID: 679897;                                              
SOURCE  16 STRAIN: ATCC 43772 / LMG 18044 / NCTC 12198 / 12198;                 
SOURCE  17 GENE: HMU13010, UREB2;                                               
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD;                                 
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PEC015                                    
KEYWDS    IRON METALLOENZYME, ALPHA-BETA BARREL, UREASE, HYDROLASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.E.TRONRUD,A.ROBBINS,P.A.KARPLUS                                     
REVDAT   2   24-AUG-11 3QGA    1       JRNL                                     
REVDAT   1   10-AUG-11 3QGA    0                                                
JRNL        AUTH   E.L.CARTER,D.E.TRONRUD,S.R.TABER,P.A.KARPLUS,R.P.HAUSINGER   
JRNL        TITL   IRON-CONTAINING UREASE IN A PATHOGENIC BACTERIUM.            
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108 13095 2011              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   21788478                                                     
JRNL        DOI    10.1073/PNAS.1106915108                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.8.0                                         
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 145355                         
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)  : 0.171                          
REMARK   3   R VALUE            (WORKING SET)  : 0.170                          
REMARK   3   FREE R VALUE                      : 0.189                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.010                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 7283                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.00                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.08                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 9985                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2379                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 9508                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2371                   
REMARK   3   BIN FREE R VALUE                        : 0.2554                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.78                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 477                      
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            : 36408                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 606                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 59.84                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.60730                                              
REMARK   3    B22 (A**2) : -1.93460                                             
REMARK   3    B33 (A**2) : 1.32730                                              
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) : 0.32                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.931                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.913                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 37158  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 50160  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 12954  ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 930    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 5406   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 37140  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : 6      ; 0.000  ; HARMONIC            
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 4932   ; 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   : 42620  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.17                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.75                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 20.38                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION:   C    1    C  568                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   15.2475  -94.3102   82.3624           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0425 T22:   -0.1046                                    
REMARK   3     T33:   -0.0342 T12:   -0.0133                                    
REMARK   3     T13:    0.0249 T23:    0.0226                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6302 L22:    0.3533                                    
REMARK   3     L33:    0.4139 L12:   -0.0851                                    
REMARK   3     L13:    0.0244 L23:    0.0535                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0021 S12:    0.1033 S13:   -0.0057                     
REMARK   3     S21:   -0.0856 S22:    0.0057 S23:   -0.0516                     
REMARK   3     S31:   -0.0026 S32:    0.0414 S33:   -0.0078                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION:   F    1    F  568                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   25.9124  -69.9023  119.6110           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0664 T22:   -0.0704                                    
REMARK   3     T33:    0.0018 T12:   -0.0388                                    
REMARK   3     T13:   -0.0066 T23:    0.0247                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5094 L22:    0.5064                                    
REMARK   3     L33:    0.3226 L12:   -0.0690                                    
REMARK   3     L13:   -0.0541 L23:    0.0570                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0057 S12:   -0.0351 S13:    0.0622                     
REMARK   3     S21:    0.0628 S22:    0.0042 S23:   -0.0421                     
REMARK   3     S31:   -0.0455 S32:    0.0298 S33:    0.0016                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION:   I    1    I  568                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -17.0946  -70.6866  104.3940           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0883 T22:   -0.0987                                    
REMARK   3     T33:    0.0272 T12:    0.0057                                    
REMARK   3     T13:    0.0057 T23:    0.0574                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3910 L22:    0.4418                                    
REMARK   3     L33:    0.4418 L12:   -0.0470                                    
REMARK   3     L13:    0.1043 L23:    0.0214                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0105 S12:    0.0017 S13:    0.0685                     
REMARK   3     S21:   -0.0366 S22:   -0.0017 S23:    0.0632                     
REMARK   3     S31:   -0.0155 S32:   -0.0405 S33:    0.0122                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION:   L    1    L  568                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   49.3619 -107.6360  133.6550           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0884 T22:   -0.0194                                    
REMARK   3     T33:   -0.0118 T12:   -0.0160                                    
REMARK   3     T13:   -0.0077 T23:   -0.0002                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4403 L22:    0.5922                                    
REMARK   3     L33:    0.4957 L12:   -0.0681                                    
REMARK   3     L13:   -0.0975 L23:    0.1722                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0068 S12:   -0.0401 S13:   -0.0114                     
REMARK   3     S21:   -0.0062 S22:    0.0276 S23:   -0.1023                     
REMARK   3     S31:   -0.0104 S32:    0.0951 S33:   -0.0208                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION:   O    1    O  568                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   29.3260 -145.8850  148.7340           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0386 T22:   -0.0218                                    
REMARK   3     T33:   -0.0041 T12:    0.0291                                    
REMARK   3     T13:   -0.0322 T23:   -0.0052                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.4343 L22:    0.3629                                    
REMARK   3     L33:    0.5077 L12:    0.0048                                    
REMARK   3     L13:   -0.0893 L23:   -0.0466                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0038 S12:   -0.1298 S13:   -0.0941                     
REMARK   3     S21:    0.0590 S22:    0.0134 S23:   -0.0501                     
REMARK   3     S31:    0.0555 S32:   -0.0073 S33:   -0.0096                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION:   R    1    R  568                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   22.6750 -106.3280  170.6700           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0089 T22:    0.1061                                    
REMARK   3     T33:   -0.1064 T12:    0.0420                                    
REMARK   3     T13:   -0.0216 T23:   -0.0351                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3511 L22:    0.5377                                    
REMARK   3     L33:    0.4773 L12:    0.1012                                    
REMARK   3     L13:   -0.0877 L23:   -0.0413                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0038 S12:   -0.1223 S13:    0.0758                     
REMARK   3     S21:    0.0897 S22:    0.0160 S23:   -0.0121                     
REMARK   3     S31:   -0.0375 S32:    0.0460 S33:   -0.0197                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION:   A    1    A  108                                     
REMARK   3    ORIGIN FOR THE GROUP (A):    0.9554  -62.9257   77.0586           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0020 T22:   -0.1053                                    
REMARK   3     T33:   -0.0224 T12:   -0.0138                                    
REMARK   3     T13:    0.0085 T23:    0.1232                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6889 L22:    0.8771                                    
REMARK   3     L33:    1.3667 L12:   -0.0770                                    
REMARK   3     L13:   -0.2000 L23:    0.4563                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0068 S12:    0.0766 S13:    0.1113                     
REMARK   3     S21:   -0.1392 S22:   -0.0233 S23:   -0.0575                     
REMARK   3     S31:   -0.0271 S32:   -0.0823 S33:    0.0165                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION:   A  118    A  225                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -34.0930  -94.0826   72.5090           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0850 T22:   -0.0320                                    
REMARK   3     T33:   -0.0477 T12:    0.0311                                    
REMARK   3     T13:   -0.0647 T23:    0.0773                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1856 L22:    0.9498                                    
REMARK   3     L33:    0.7448 L12:   -0.6710                                    
REMARK   3     L13:    0.3194 L23:    0.6056                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0093 S12:    0.1295 S13:    0.0537                     
REMARK   3     S21:   -0.1861 S22:    0.0316 S23:    0.1480                     
REMARK   3     S31:   -0.0633 S32:   -0.1499 S33:   -0.0223                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION:   D    1    D  108                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   28.1988  -63.5045   85.3361           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0832 T22:   -0.0968                                    
REMARK   3     T33:    0.0380 T12:   -0.0802                                    
REMARK   3     T13:    0.0409 T23:    0.0724                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1605 L22:    0.9536                                    
REMARK   3     L33:    1.2119 L12:   -0.1459                                    
REMARK   3     L13:    0.9674 L23:   -0.2448                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0096 S12:    0.0481 S13:   -0.0029                     
REMARK   3     S21:   -0.0318 S22:    0.0095 S23:   -0.1240                     
REMARK   3     S31:   -0.0245 S32:    0.0306 S33:   -0.0191                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION:   D  118    D  225                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   56.3820 -100.3780   93.4520           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1251 T22:   -0.0653                                    
REMARK   3     T33:    0.0247 T12:   -0.0256                                    
REMARK   3     T13:    0.0869 T23:   -0.0128                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6199 L22:    1.3196                                    
REMARK   3     L33:    1.5786 L12:   -0.0564                                    
REMARK   3     L13:    0.1988 L23:    0.8071                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0167 S12:    0.1769 S13:   -0.0180                     
REMARK   3     S21:   -0.0134 S22:    0.0104 S23:   -0.0567                     
REMARK   3     S31:    0.0462 S32:    0.2018 S33:    0.0063                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION:   G    1    G  108                                     
REMARK   3    ORIGIN FOR THE GROUP (A):    9.1914  -48.1743  100.1810           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0671 T22:   -0.1828                                    
REMARK   3     T33:    0.0857 T12:   -0.0380                                    
REMARK   3     T13:   -0.0025 T23:    0.0766                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9812 L22:    0.4645                                    
REMARK   3     L33:    0.6436 L12:   -0.9840                                    
REMARK   3     L13:   -0.2662 L23:    0.1229                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0149 S12:   -0.0182 S13:    0.0986                     
REMARK   3     S21:   -0.0395 S22:    0.0135 S23:    0.0042                     
REMARK   3     S31:   -0.0156 S32:   -0.0199 S33:    0.0014                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION:   G  118    G  225                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.2387  -48.5767  146.3410           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0058 T22:   -0.1224                                    
REMARK   3     T33:    0.0233 T12:    0.0109                                    
REMARK   3     T13:   -0.0176 T23:   -0.0759                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.7814 L22:    0.0005                                    
REMARK   3     L33:    2.7000 L12:    0.2628                                    
REMARK   3     L13:    0.6508 L23:    0.2334                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0277 S12:   -0.2058 S13:    0.2095                     
REMARK   3     S21:    0.0803 S22:    0.0028 S23:   -0.0535                     
REMARK   3     S31:   -0.0848 S32:    0.0375 S33:   -0.0305                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION:   J    1    J  108                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   56.1241 -108.5040  167.8900           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1042 T22:    0.1825                                    
REMARK   3     T33:    0.0268 T12:   -0.0177                                    
REMARK   3     T13:   -0.0730 T23:   -0.0548                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0740 L22:    1.0227                                    
REMARK   3     L33:    1.0541 L12:    0.0333                                    
REMARK   3     L13:   -0.3262 L23:   -0.5461                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0174 S12:   -0.0822 S13:   -0.0038                     
REMARK   3     S21:    0.0862 S22:    0.0338 S23:   -0.0434                     
REMARK   3     S31:   -0.0252 S32:    0.1104 S33:   -0.0164                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION:   J  118    J  225                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   35.7100  -66.8276  159.7540           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0342 T22:    0.0258                                    
REMARK   3     T33:   -0.0325 T12:   -0.0567                                    
REMARK   3     T13:   -0.0246 T23:   -0.1014                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0661 L22:    2.0135                                    
REMARK   3     L33:    1.1344 L12:   -0.0084                                    
REMARK   3     L13:   -0.1284 L23:    0.1174                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0131 S12:   -0.2356 S13:    0.0940                     
REMARK   3     S21:    0.0922 S22:    0.0023 S23:    0.0160                     
REMARK   3     S31:   -0.1131 S32:    0.0534 S33:    0.0108                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION:   M    1    M  108                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   61.2687 -132.4380  153.0170           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0816 T22:    0.0726                                    
REMARK   3     T33:    0.0779 T12:    0.0785                                    
REMARK   3     T13:   -0.0764 T23:   -0.0071                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.1361 L22:    2.1600                                    
REMARK   3     L33:    0.7222 L12:    0.4296                                    
REMARK   3     L13:    0.1082 L23:    0.2399                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0148 S12:   -0.0443 S13:   -0.0440                     
REMARK   3     S21:   -0.0504 S22:    0.0250 S23:   -0.1361                     
REMARK   3     S31:   -0.0135 S32:   -0.0424 S33:   -0.0398                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION:   M  118    M  225                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   56.5859 -140.3360  106.8050           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1491 T22:   -0.1121                                    
REMARK   3     T33:    0.0127 T12:    0.0514                                    
REMARK   3     T13:    0.0692 T23:   -0.0600                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4990 L22:    1.9632                                    
REMARK   3     L33:    1.9154 L12:    0.9847                                    
REMARK   3     L13:   -0.7884 L23:   -0.2805                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0054 S12:    0.1922 S13:   -0.0641                     
REMARK   3     S21:   -0.0662 S22:    0.0299 S23:   -0.1681                     
REMARK   3     S31:    0.0172 S32:    0.0930 S33:   -0.0354                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION:   P    1    P  108                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   44.2853 -133.2480  176.0550           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0476 T22:    0.1810                                    
REMARK   3     T33:   -0.1115 T12:    0.0548                                    
REMARK   3     T13:   -0.0909 T23:    0.0127                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9350 L22:    1.4508                                    
REMARK   3     L33:    1.3562 L12:   -0.4930                                    
REMARK   3     L13:   -0.9257 L23:    0.5611                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0032 S12:   -0.1978 S13:    0.0360                     
REMARK   3     S21:    0.0817 S22:    0.0214 S23:   -0.1238                     
REMARK   3     S31:    0.0421 S32:   -0.0024 S33:   -0.0247                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION:   P  118    P  225                                     
REMARK   3    ORIGIN FOR THE GROUP (A):    0.6857 -150.5460  180.4940           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0930 T22:    0.0614                                    
REMARK   3     T33:   -0.1413 T12:    0.0039                                    
REMARK   3     T13:    0.0042 T23:    0.0664                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2347 L22:    2.7093                                    
REMARK   3     L33:    0.0958 L12:    0.4412                                    
REMARK   3     L13:   -0.6227 L23:   -0.1440                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0190 S12:   -0.0835 S13:   -0.2186                     
REMARK   3     S21:    0.1772 S22:    0.0303 S23:    0.0576                     
REMARK   3     S31:    0.0777 S32:    0.0088 S33:   -0.0493                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3QGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063607.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-SEP-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9765                             
REMARK 200  MONOCHROMATOR                  : ASYMMETRIC CUT SINGLE CRYSTAL      
REMARK 200                                   SI(220)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 145678                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.998                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 67.292                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : 0.20100                            
REMARK 200  R SYM                      (I) : 0.20100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.80900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1EJX                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 6.7 MG/ML PROTEIN, 6.7 MM TRIS, 20%      
REMARK 280  MPD, 0.07 M SODIUM ACETATE, 0.013 M CALCIUM CHLORIDE, PH 7.4,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       83.49000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      111.97000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      197.93500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       83.49000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      111.97000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      197.93500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       83.49000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      111.97000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      197.93500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       83.49000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      111.97000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      197.93500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 24-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, F, G, I, J, L, M,            
REMARK 350                    AND CHAINS: O, P, R                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -223.94000            
REMARK 350   BIOMT3   2  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     GLU C   329                                                      
REMARK 465     ASP C   330                                                      
REMARK 465     LEU C   331                                                      
REMARK 465     GLN C   332                                                      
REMARK 465     GLU F   329                                                      
REMARK 465     ASP F   330                                                      
REMARK 465     LEU F   331                                                      
REMARK 465     GLN F   332                                                      
REMARK 465     GLU I   329                                                      
REMARK 465     ASP I   330                                                      
REMARK 465     LEU I   331                                                      
REMARK 465     GLN I   332                                                      
REMARK 465     GLU L   329                                                      
REMARK 465     ASP L   330                                                      
REMARK 465     LEU L   331                                                      
REMARK 465     GLN L   332                                                      
REMARK 465     GLU O   329                                                      
REMARK 465     ASP O   330                                                      
REMARK 465     LEU O   331                                                      
REMARK 465     GLN O   332                                                      
REMARK 465     GLU R   329                                                      
REMARK 465     ASP R   330                                                      
REMARK 465     LEU R   331                                                      
REMARK 465     GLN R   332                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS C 325    CD   CE   NZ                                        
REMARK 470     ARG C 326    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 337    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F 325    CD   CE   NZ                                        
REMARK 470     ARG F 326    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG F 337    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS I 325    CD   CE   NZ                                        
REMARK 470     ARG I 326    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG I 337    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS L 325    CD   CE   NZ                                        
REMARK 470     ARG L 326    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG L 337    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS O 325    CD   CE   NZ                                        
REMARK 470     ARG O 326    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG O 337    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS R 325    CD   CE   NZ                                        
REMARK 470     ARG R 326    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG R 337    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 151      129.45    -32.83                                   
REMARK 500    MET A 198      -97.13     55.52                                   
REMARK 500    LYS C  48     -158.90    -86.68                                   
REMARK 500    ILE C  50       78.08    -69.50                                   
REMARK 500    MET C  54     -101.63   -113.57                                   
REMARK 500    ASP C 249       88.35    -68.11                                   
REMARK 500    HIS C 273       63.09     28.18                                   
REMARK 500    HIS C 281      117.35    -25.87                                   
REMARK 500    LEU C 314       12.57    -67.33                                   
REMARK 500    ASP C 315      -37.05   -144.17                                   
REMARK 500    SER C 362      111.73    -27.88                                   
REMARK 500    ALA C 364       46.19   -144.61                                   
REMARK 500    MET C 365       51.76     88.79                                   
REMARK 500    THR C 409      -86.67   -115.27                                   
REMARK 500    ASP C 461      121.96    -37.27                                   
REMARK 500    ALA C 464      145.13    -28.10                                   
REMARK 500    ALA C 562      -97.51   -145.64                                   
REMARK 500    ASN D 151      129.19    -31.40                                   
REMARK 500    MET D 198      -98.23     54.27                                   
REMARK 500    LYS F  48     -158.05    -86.66                                   
REMARK 500    ILE F  50       78.21    -69.59                                   
REMARK 500    MET F  54     -103.39   -112.29                                   
REMARK 500    PRO F 162       49.47    -80.37                                   
REMARK 500    ASN F 199       75.32    -65.45                                   
REMARK 500    ASN F 252       47.59     39.81                                   
REMARK 500    HIS F 273       56.10     32.34                                   
REMARK 500    HIS F 281      113.33    -18.26                                   
REMARK 500    LEU F 314       12.83    -66.99                                   
REMARK 500    ASP F 315      -37.89   -144.56                                   
REMARK 500    ASP F 361       32.61     76.18                                   
REMARK 500    SER F 362      109.48    -35.16                                   
REMARK 500    ALA F 364       47.38   -141.19                                   
REMARK 500    MET F 365       52.56     84.38                                   
REMARK 500    THR F 409      -86.73   -113.98                                   
REMARK 500    ASP F 461      121.33    -37.83                                   
REMARK 500    ALA F 464      146.70    -28.19                                   
REMARK 500    ALA F 562      -97.14   -146.05                                   
REMARK 500    ASN G 151      129.07    -31.48                                   
REMARK 500    MET G 198      -97.89     55.84                                   
REMARK 500    LYS I  48     -156.65    -86.82                                   
REMARK 500    ILE I  50       77.56    -68.02                                   
REMARK 500    MET I  54     -102.28   -113.35                                   
REMARK 500    ASN I 199       79.38    -68.65                                   
REMARK 500    HIS I 273       63.67     30.38                                   
REMARK 500    HIS I 281      112.41    -26.10                                   
REMARK 500    LEU I 314       11.52    -66.34                                   
REMARK 500    ASP I 315      -37.00   -144.06                                   
REMARK 500    SER I 362      120.84    -33.29                                   
REMARK 500    GLN I 363       15.51     52.93                                   
REMARK 500    MET I 365       54.63     79.15                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     112 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG C 339        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE C 410        24.4      L          L   OUTSIDE RANGE           
REMARK 500    HIS C 416        24.9      L          L   OUTSIDE RANGE           
REMARK 500    ARG F 339        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE F 410        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ASP I 284        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ARG I 339        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE I 410        24.5      L          L   OUTSIDE RANGE           
REMARK 500    HIS I 416        24.9      L          L   OUTSIDE RANGE           
REMARK 500    THR L 300        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ARG L 339        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE L 410        24.4      L          L   OUTSIDE RANGE           
REMARK 500    HIS L 416        24.8      L          L   OUTSIDE RANGE           
REMARK 500    THR O 300        25.0      L          L   OUTSIDE RANGE           
REMARK 500    ARG O 339        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE O 410        24.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS O 416        24.7      L          L   OUTSIDE RANGE           
REMARK 500    VAL R 251        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ARG R 339        23.6      L          L   OUTSIDE RANGE           
REMARK 500    ILE R 410        24.8      L          L   OUTSIDE RANGE           
REMARK 500    HIS R 416        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE L 775  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L 361   OD1                                                    
REMARK 620 2 HIS L 137   NE2  99.3                                              
REMARK 620 3 KCX L 218   OQ2 161.2  84.7                                        
REMARK 620 4 HIS L 135   NE2  79.4  98.3  81.8                                  
REMARK 620 5 HOH L 780   O    79.5 174.9  98.0  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C 775  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 361   OD1                                                    
REMARK 620 2 HIS C 137   NE2  87.6                                              
REMARK 620 3 KCX C 218   OQ2 154.3  92.6                                        
REMARK 620 4 HIS C 135   NE2  74.5 100.1  80.2                                  
REMARK 620 5 HOH C 780   O    83.0 168.9  98.4  82.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE F 775  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F 361   OD1                                                    
REMARK 620 2 KCX F 218   OQ2 170.4                                              
REMARK 620 3 HIS F 137   NE2  93.7  92.9                                        
REMARK 620 4 HIS F 135   NE2  84.8  86.6 108.2                                  
REMARK 620 5 HOH F 780   O    86.1  87.4 179.6  72.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE R 775  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP R 361   OD1                                                    
REMARK 620 2 HIS R 137   NE2  85.6                                              
REMARK 620 3 KCX R 218   OQ2 158.2  89.7                                        
REMARK 620 4 HIS R 135   NE2  74.4  95.3  84.9                                  
REMARK 620 5 HOH R 780   O    82.0 166.8 100.2  76.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE O 775  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP O 361   OD1                                                    
REMARK 620 2 HIS O 137   NE2  93.6                                              
REMARK 620 3 HIS O 135   NE2  78.6 106.3                                        
REMARK 620 4 KCX O 218   OQ2 166.8  82.0  90.8                                  
REMARK 620 5 HOH O 780   O    77.6 160.4  89.3 110.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE R 774  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS R 247   ND1                                                    
REMARK 620 2 KCX R 218   OQ1  96.2                                              
REMARK 620 3 HIS R 273   NE2  88.3  96.8                                        
REMARK 620 4 HOH R 780   O   164.1  88.2  76.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE I 775  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I 137   NE2                                                    
REMARK 620 2 KCX I 218   OQ2 100.8                                              
REMARK 620 3 HIS I 135   NE2 102.2  95.9                                        
REMARK 620 4 ASP I 361   OD1  82.1 172.4  76.6                                  
REMARK 620 5 HOH I 780   O   148.6 104.2  93.8  75.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE I 774  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I 247   ND1                                                    
REMARK 620 2 HIS I 273   NE2  84.3                                              
REMARK 620 3 KCX I 218   OQ1  94.2  92.3                                        
REMARK 620 4 HOH I 780   O   163.2  83.4  97.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE L 774  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX L 218   OQ1                                                    
REMARK 620 2 HIS L 247   ND1  97.4                                              
REMARK 620 3 HIS L 273   NE2 102.3  89.3                                        
REMARK 620 4 HOH L 780   O    95.3 164.4  79.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE O 774  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS O 247   ND1                                                    
REMARK 620 2 KCX O 218   OQ1  99.7                                              
REMARK 620 3 HIS O 273   NE2  90.6 106.9                                        
REMARK 620 4 HOH O 780   O   159.4 100.7  80.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE F 774  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F 273   NE2                                                    
REMARK 620 2 KCX F 218   OQ1  96.6                                              
REMARK 620 3 HIS F 247   ND1  86.3  95.2                                        
REMARK 620 4 HOH F 780   O    78.6  81.2 163.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C 774  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX C 218   OQ1                                                    
REMARK 620 2 HIS C 273   NE2 103.7                                              
REMARK 620 3 HIS C 247   ND1 102.3  93.7                                        
REMARK 620 4 HOH C 780   O    97.4  79.4 160.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 774                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 775                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE F 774                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE F 775                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE I 774                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE I 775                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE L 774                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE L 775                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE O 774                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE O 775                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE R 774                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE R 775                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QGK   RELATED DB: PDB                                   
REMARK 900 MODEL REFINED USING THE SAME DATA BUT WITHOUT ORDERED                
REMARK 900 SOLVENT                                                              
DBREF  3QGA A    1   225  UNP    D3UJ81   D3UJ81_HELM1     1    225             
DBREF  3QGA C    1   568  UNP    D3UJ80   D3UJ80_HELM1     1    568             
DBREF  3QGA D    1   225  UNP    D3UJ81   D3UJ81_HELM1     1    225             
DBREF  3QGA F    1   568  UNP    D3UJ80   D3UJ80_HELM1     1    568             
DBREF  3QGA G    1   225  UNP    D3UJ81   D3UJ81_HELM1     1    225             
DBREF  3QGA I    1   568  UNP    D3UJ80   D3UJ80_HELM1     1    568             
DBREF  3QGA J    1   225  UNP    D3UJ81   D3UJ81_HELM1     1    225             
DBREF  3QGA L    1   568  UNP    D3UJ80   D3UJ80_HELM1     1    568             
DBREF  3QGA M    1   225  UNP    D3UJ81   D3UJ81_HELM1     1    225             
DBREF  3QGA O    1   568  UNP    D3UJ80   D3UJ80_HELM1     1    568             
DBREF  3QGA P    1   225  UNP    D3UJ81   D3UJ81_HELM1     1    225             
DBREF  3QGA R    1   568  UNP    D3UJ80   D3UJ80_HELM1     1    568             
SEQRES   1 A  225  FME LYS LEU THR PRO LYS GLU GLN GLU LYS PHE LEU LEU          
SEQRES   2 A  225  TYR TYR ALA GLY GLU VAL ALA ARG LYS ARG LYS GLU GLU          
SEQRES   3 A  225  GLY LEU LYS LEU ASN GLN PRO GLU ALA ILE ALA TYR ILE          
SEQRES   4 A  225  SER ALA HIS ILE MET ASP GLU ALA ARG ARG GLY LYS LYS          
SEQRES   5 A  225  THR VAL ALA GLN LEU MET GLU GLU CYS VAL HIS PHE LEU          
SEQRES   6 A  225  LYS LYS ASP GLU VAL MET PRO GLY VAL GLY ASN MET VAL          
SEQRES   7 A  225  PRO ASP LEU GLY VAL GLU ALA ASN PHE PRO ASP GLY THR          
SEQRES   8 A  225  LYS LEU VAL THR VAL ASN TRP PRO ILE GLU PRO ASP ASP          
SEQRES   9 A  225  PHE LYS ALA GLY GLU ILE LYS PHE ALA SER ASP LYS ASP          
SEQRES  10 A  225  ILE GLU LEU ASN ALA GLY LYS GLU ILE THR GLU LEU LYS          
SEQRES  11 A  225  VAL THR ASN LYS GLY PRO LYS SER LEU HIS VAL GLY SER          
SEQRES  12 A  225  HIS PHE HIS PHE PHE GLU ALA ASN ARG ALA LEU GLU PHE          
SEQRES  13 A  225  ASP ARG GLU LYS ALA TYR GLY LYS ARG LEU ASP ILE PRO          
SEQRES  14 A  225  SER GLY ASN THR LEU ARG ILE GLY ALA GLY GLU THR LYS          
SEQRES  15 A  225  THR VAL HIS LEU ILE PRO ILE GLY GLY SER LYS LYS ILE          
SEQRES  16 A  225  ILE GLY MET ASN GLY LEU LEU ASN GLY ILE ALA ASP ASP          
SEQRES  17 A  225  LEU HIS LYS GLN LYS ALA LEU GLU LYS ALA LYS HIS HIS          
SEQRES  18 A  225  GLY PHE ILE LYS                                              
SEQRES   1 C  568  MET LYS MET LYS ARG GLN GLU TYR VAL ASN THR TYR GLY          
SEQRES   2 C  568  PRO THR THR GLY ASP LYS VAL ARG LEU GLY ASP THR ASP          
SEQRES   3 C  568  LEU TRP ALA GLU VAL GLU HIS ASP TYR THR VAL TYR GLY          
SEQRES   4 C  568  GLU GLU LEU LYS PHE GLY ALA GLY LYS THR ILE ARG GLU          
SEQRES   5 C  568  GLY MET GLY GLN SER ASN SER PRO ASP GLU ASN THR LEU          
SEQRES   6 C  568  ASP LEU VAL ILE THR ASN ALA LEU ILE ILE ASP TYR THR          
SEQRES   7 C  568  GLY ILE TYR LYS ALA ASP ILE GLY ILE LYS ASN GLY LYS          
SEQRES   8 C  568  ILE HIS GLY ILE GLY LYS ALA GLY ASN LYS ASP MET GLN          
SEQRES   9 C  568  ASP GLY VAL THR PRO HIS MET VAL VAL GLY VAL GLY THR          
SEQRES  10 C  568  GLU ALA LEU ALA GLY GLU GLY MET ILE ILE THR ALA GLY          
SEQRES  11 C  568  GLY ILE ASP SER HIS THR HIS PHE LEU SER PRO GLN GLN          
SEQRES  12 C  568  PHE PRO THR ALA LEU ALA ASN GLY VAL THR THR MET PHE          
SEQRES  13 C  568  GLY GLY GLY THR GLY PRO VAL ASP GLY THR ASN ALA THR          
SEQRES  14 C  568  THR ILE THR PRO GLY VAL TRP ASN LEU HIS ARG MET LEU          
SEQRES  15 C  568  ARG ALA ALA GLU GLU TYR GLY MET ASN VAL GLY LEU LEU          
SEQRES  16 C  568  GLY LYS GLY ASN SER SER SER ARG ALA GLN LEU VAL GLU          
SEQRES  17 C  568  GLN VAL LYS ALA GLY ALA ILE GLY PHE KCX LEU HIS GLU          
SEQRES  18 C  568  ASP TRP GLY THR THR PRO SER ALA ILE ASP HIS CYS LEU          
SEQRES  19 C  568  SER VAL ALA ASP GLU TYR ASP VAL GLN VAL CYS ILE HIS          
SEQRES  20 C  568  THR ASP THR VAL ASN GLU ALA GLY TYR VAL ASP ASP THR          
SEQRES  21 C  568  LEU ARG ALA MET ASN GLY ARG ALA ILE HIS ALA TYR HIS          
SEQRES  22 C  568  ILE GLU GLY ALA GLY GLY GLY HIS SER PRO ASP VAL ILE          
SEQRES  23 C  568  THR MET ALA GLY GLU VAL ASN ILE LEU PRO SER SER THR          
SEQRES  24 C  568  THR PRO THR ILE PRO TYR THR ILE ASN THR VAL ALA GLU          
SEQRES  25 C  568  HIS LEU ASP MET LEU MET THR CYS HIS HIS LEU ASP LYS          
SEQRES  26 C  568  ARG ILE ARG GLU ASP LEU GLN PHE SER GLN SER ARG ILE          
SEQRES  27 C  568  ARG PRO GLY SER ILE ALA ALA GLU ASP THR LEU HIS ASP          
SEQRES  28 C  568  MET GLY VAL ILE ALA MET THR SER SER ASP SER GLN ALA          
SEQRES  29 C  568  MET GLY ARG ALA GLY GLU VAL ILE PRO ARG THR TRP GLN          
SEQRES  30 C  568  THR ALA ASP LYS ASN LYS LYS GLU PHE GLY ARG LEU THR          
SEQRES  31 C  568  GLU GLU LYS GLY ASP ASN ASP ASN PHE ARG ILE LYS ARG          
SEQRES  32 C  568  TYR ILE SER LYS TYR THR ILE ASN PRO ALA ILE THR HIS          
SEQRES  33 C  568  GLY VAL SER GLU TYR ILE GLY SER VAL GLU GLU GLY LYS          
SEQRES  34 C  568  ILE ALA ASP LEU VAL VAL TRP ASN PRO ALA PHE PHE GLY          
SEQRES  35 C  568  VAL LYS PRO LYS ILE ILE ILE LYS GLY GLY MET VAL VAL          
SEQRES  36 C  568  PHE SER GLU MET GLY ASP SER ASN ALA SER VAL PRO THR          
SEQRES  37 C  568  PRO GLN PRO VAL TYR TYR ARG GLU MET PHE GLY HIS HIS          
SEQRES  38 C  568  GLY LYS ALA LYS PHE ASP THR SER ILE THR PHE VAL SER          
SEQRES  39 C  568  LYS VAL ALA TYR GLU ASN GLY ILE LYS GLU LYS LEU GLY          
SEQRES  40 C  568  LEU GLU ARG LYS VAL LEU PRO VAL LYS ASN CYS ARG ASN          
SEQRES  41 C  568  VAL THR LYS LYS ASP PHE LYS PHE ASN ASN THR THR ALA          
SEQRES  42 C  568  LYS ILE THR VAL ASN PRO GLU THR PHE GLU VAL PHE VAL          
SEQRES  43 C  568  ASN GLY LYS LEU CYS THR SER LYS PRO ALA THR GLU VAL          
SEQRES  44 C  568  ALA LEU ALA SER ARG TYR THR PHE PHE                          
SEQRES   1 D  225  FME LYS LEU THR PRO LYS GLU GLN GLU LYS PHE LEU LEU          
SEQRES   2 D  225  TYR TYR ALA GLY GLU VAL ALA ARG LYS ARG LYS GLU GLU          
SEQRES   3 D  225  GLY LEU LYS LEU ASN GLN PRO GLU ALA ILE ALA TYR ILE          
SEQRES   4 D  225  SER ALA HIS ILE MET ASP GLU ALA ARG ARG GLY LYS LYS          
SEQRES   5 D  225  THR VAL ALA GLN LEU MET GLU GLU CYS VAL HIS PHE LEU          
SEQRES   6 D  225  LYS LYS ASP GLU VAL MET PRO GLY VAL GLY ASN MET VAL          
SEQRES   7 D  225  PRO ASP LEU GLY VAL GLU ALA ASN PHE PRO ASP GLY THR          
SEQRES   8 D  225  LYS LEU VAL THR VAL ASN TRP PRO ILE GLU PRO ASP ASP          
SEQRES   9 D  225  PHE LYS ALA GLY GLU ILE LYS PHE ALA SER ASP LYS ASP          
SEQRES  10 D  225  ILE GLU LEU ASN ALA GLY LYS GLU ILE THR GLU LEU LYS          
SEQRES  11 D  225  VAL THR ASN LYS GLY PRO LYS SER LEU HIS VAL GLY SER          
SEQRES  12 D  225  HIS PHE HIS PHE PHE GLU ALA ASN ARG ALA LEU GLU PHE          
SEQRES  13 D  225  ASP ARG GLU LYS ALA TYR GLY LYS ARG LEU ASP ILE PRO          
SEQRES  14 D  225  SER GLY ASN THR LEU ARG ILE GLY ALA GLY GLU THR LYS          
SEQRES  15 D  225  THR VAL HIS LEU ILE PRO ILE GLY GLY SER LYS LYS ILE          
SEQRES  16 D  225  ILE GLY MET ASN GLY LEU LEU ASN GLY ILE ALA ASP ASP          
SEQRES  17 D  225  LEU HIS LYS GLN LYS ALA LEU GLU LYS ALA LYS HIS HIS          
SEQRES  18 D  225  GLY PHE ILE LYS                                              
SEQRES   1 F  568  MET LYS MET LYS ARG GLN GLU TYR VAL ASN THR TYR GLY          
SEQRES   2 F  568  PRO THR THR GLY ASP LYS VAL ARG LEU GLY ASP THR ASP          
SEQRES   3 F  568  LEU TRP ALA GLU VAL GLU HIS ASP TYR THR VAL TYR GLY          
SEQRES   4 F  568  GLU GLU LEU LYS PHE GLY ALA GLY LYS THR ILE ARG GLU          
SEQRES   5 F  568  GLY MET GLY GLN SER ASN SER PRO ASP GLU ASN THR LEU          
SEQRES   6 F  568  ASP LEU VAL ILE THR ASN ALA LEU ILE ILE ASP TYR THR          
SEQRES   7 F  568  GLY ILE TYR LYS ALA ASP ILE GLY ILE LYS ASN GLY LYS          
SEQRES   8 F  568  ILE HIS GLY ILE GLY LYS ALA GLY ASN LYS ASP MET GLN          
SEQRES   9 F  568  ASP GLY VAL THR PRO HIS MET VAL VAL GLY VAL GLY THR          
SEQRES  10 F  568  GLU ALA LEU ALA GLY GLU GLY MET ILE ILE THR ALA GLY          
SEQRES  11 F  568  GLY ILE ASP SER HIS THR HIS PHE LEU SER PRO GLN GLN          
SEQRES  12 F  568  PHE PRO THR ALA LEU ALA ASN GLY VAL THR THR MET PHE          
SEQRES  13 F  568  GLY GLY GLY THR GLY PRO VAL ASP GLY THR ASN ALA THR          
SEQRES  14 F  568  THR ILE THR PRO GLY VAL TRP ASN LEU HIS ARG MET LEU          
SEQRES  15 F  568  ARG ALA ALA GLU GLU TYR GLY MET ASN VAL GLY LEU LEU          
SEQRES  16 F  568  GLY LYS GLY ASN SER SER SER ARG ALA GLN LEU VAL GLU          
SEQRES  17 F  568  GLN VAL LYS ALA GLY ALA ILE GLY PHE KCX LEU HIS GLU          
SEQRES  18 F  568  ASP TRP GLY THR THR PRO SER ALA ILE ASP HIS CYS LEU          
SEQRES  19 F  568  SER VAL ALA ASP GLU TYR ASP VAL GLN VAL CYS ILE HIS          
SEQRES  20 F  568  THR ASP THR VAL ASN GLU ALA GLY TYR VAL ASP ASP THR          
SEQRES  21 F  568  LEU ARG ALA MET ASN GLY ARG ALA ILE HIS ALA TYR HIS          
SEQRES  22 F  568  ILE GLU GLY ALA GLY GLY GLY HIS SER PRO ASP VAL ILE          
SEQRES  23 F  568  THR MET ALA GLY GLU VAL ASN ILE LEU PRO SER SER THR          
SEQRES  24 F  568  THR PRO THR ILE PRO TYR THR ILE ASN THR VAL ALA GLU          
SEQRES  25 F  568  HIS LEU ASP MET LEU MET THR CYS HIS HIS LEU ASP LYS          
SEQRES  26 F  568  ARG ILE ARG GLU ASP LEU GLN PHE SER GLN SER ARG ILE          
SEQRES  27 F  568  ARG PRO GLY SER ILE ALA ALA GLU ASP THR LEU HIS ASP          
SEQRES  28 F  568  MET GLY VAL ILE ALA MET THR SER SER ASP SER GLN ALA          
SEQRES  29 F  568  MET GLY ARG ALA GLY GLU VAL ILE PRO ARG THR TRP GLN          
SEQRES  30 F  568  THR ALA ASP LYS ASN LYS LYS GLU PHE GLY ARG LEU THR          
SEQRES  31 F  568  GLU GLU LYS GLY ASP ASN ASP ASN PHE ARG ILE LYS ARG          
SEQRES  32 F  568  TYR ILE SER LYS TYR THR ILE ASN PRO ALA ILE THR HIS          
SEQRES  33 F  568  GLY VAL SER GLU TYR ILE GLY SER VAL GLU GLU GLY LYS          
SEQRES  34 F  568  ILE ALA ASP LEU VAL VAL TRP ASN PRO ALA PHE PHE GLY          
SEQRES  35 F  568  VAL LYS PRO LYS ILE ILE ILE LYS GLY GLY MET VAL VAL          
SEQRES  36 F  568  PHE SER GLU MET GLY ASP SER ASN ALA SER VAL PRO THR          
SEQRES  37 F  568  PRO GLN PRO VAL TYR TYR ARG GLU MET PHE GLY HIS HIS          
SEQRES  38 F  568  GLY LYS ALA LYS PHE ASP THR SER ILE THR PHE VAL SER          
SEQRES  39 F  568  LYS VAL ALA TYR GLU ASN GLY ILE LYS GLU LYS LEU GLY          
SEQRES  40 F  568  LEU GLU ARG LYS VAL LEU PRO VAL LYS ASN CYS ARG ASN          
SEQRES  41 F  568  VAL THR LYS LYS ASP PHE LYS PHE ASN ASN THR THR ALA          
SEQRES  42 F  568  LYS ILE THR VAL ASN PRO GLU THR PHE GLU VAL PHE VAL          
SEQRES  43 F  568  ASN GLY LYS LEU CYS THR SER LYS PRO ALA THR GLU VAL          
SEQRES  44 F  568  ALA LEU ALA SER ARG TYR THR PHE PHE                          
SEQRES   1 G  225  FME LYS LEU THR PRO LYS GLU GLN GLU LYS PHE LEU LEU          
SEQRES   2 G  225  TYR TYR ALA GLY GLU VAL ALA ARG LYS ARG LYS GLU GLU          
SEQRES   3 G  225  GLY LEU LYS LEU ASN GLN PRO GLU ALA ILE ALA TYR ILE          
SEQRES   4 G  225  SER ALA HIS ILE MET ASP GLU ALA ARG ARG GLY LYS LYS          
SEQRES   5 G  225  THR VAL ALA GLN LEU MET GLU GLU CYS VAL HIS PHE LEU          
SEQRES   6 G  225  LYS LYS ASP GLU VAL MET PRO GLY VAL GLY ASN MET VAL          
SEQRES   7 G  225  PRO ASP LEU GLY VAL GLU ALA ASN PHE PRO ASP GLY THR          
SEQRES   8 G  225  LYS LEU VAL THR VAL ASN TRP PRO ILE GLU PRO ASP ASP          
SEQRES   9 G  225  PHE LYS ALA GLY GLU ILE LYS PHE ALA SER ASP LYS ASP          
SEQRES  10 G  225  ILE GLU LEU ASN ALA GLY LYS GLU ILE THR GLU LEU LYS          
SEQRES  11 G  225  VAL THR ASN LYS GLY PRO LYS SER LEU HIS VAL GLY SER          
SEQRES  12 G  225  HIS PHE HIS PHE PHE GLU ALA ASN ARG ALA LEU GLU PHE          
SEQRES  13 G  225  ASP ARG GLU LYS ALA TYR GLY LYS ARG LEU ASP ILE PRO          
SEQRES  14 G  225  SER GLY ASN THR LEU ARG ILE GLY ALA GLY GLU THR LYS          
SEQRES  15 G  225  THR VAL HIS LEU ILE PRO ILE GLY GLY SER LYS LYS ILE          
SEQRES  16 G  225  ILE GLY MET ASN GLY LEU LEU ASN GLY ILE ALA ASP ASP          
SEQRES  17 G  225  LEU HIS LYS GLN LYS ALA LEU GLU LYS ALA LYS HIS HIS          
SEQRES  18 G  225  GLY PHE ILE LYS                                              
SEQRES   1 I  568  MET LYS MET LYS ARG GLN GLU TYR VAL ASN THR TYR GLY          
SEQRES   2 I  568  PRO THR THR GLY ASP LYS VAL ARG LEU GLY ASP THR ASP          
SEQRES   3 I  568  LEU TRP ALA GLU VAL GLU HIS ASP TYR THR VAL TYR GLY          
SEQRES   4 I  568  GLU GLU LEU LYS PHE GLY ALA GLY LYS THR ILE ARG GLU          
SEQRES   5 I  568  GLY MET GLY GLN SER ASN SER PRO ASP GLU ASN THR LEU          
SEQRES   6 I  568  ASP LEU VAL ILE THR ASN ALA LEU ILE ILE ASP TYR THR          
SEQRES   7 I  568  GLY ILE TYR LYS ALA ASP ILE GLY ILE LYS ASN GLY LYS          
SEQRES   8 I  568  ILE HIS GLY ILE GLY LYS ALA GLY ASN LYS ASP MET GLN          
SEQRES   9 I  568  ASP GLY VAL THR PRO HIS MET VAL VAL GLY VAL GLY THR          
SEQRES  10 I  568  GLU ALA LEU ALA GLY GLU GLY MET ILE ILE THR ALA GLY          
SEQRES  11 I  568  GLY ILE ASP SER HIS THR HIS PHE LEU SER PRO GLN GLN          
SEQRES  12 I  568  PHE PRO THR ALA LEU ALA ASN GLY VAL THR THR MET PHE          
SEQRES  13 I  568  GLY GLY GLY THR GLY PRO VAL ASP GLY THR ASN ALA THR          
SEQRES  14 I  568  THR ILE THR PRO GLY VAL TRP ASN LEU HIS ARG MET LEU          
SEQRES  15 I  568  ARG ALA ALA GLU GLU TYR GLY MET ASN VAL GLY LEU LEU          
SEQRES  16 I  568  GLY LYS GLY ASN SER SER SER ARG ALA GLN LEU VAL GLU          
SEQRES  17 I  568  GLN VAL LYS ALA GLY ALA ILE GLY PHE KCX LEU HIS GLU          
SEQRES  18 I  568  ASP TRP GLY THR THR PRO SER ALA ILE ASP HIS CYS LEU          
SEQRES  19 I  568  SER VAL ALA ASP GLU TYR ASP VAL GLN VAL CYS ILE HIS          
SEQRES  20 I  568  THR ASP THR VAL ASN GLU ALA GLY TYR VAL ASP ASP THR          
SEQRES  21 I  568  LEU ARG ALA MET ASN GLY ARG ALA ILE HIS ALA TYR HIS          
SEQRES  22 I  568  ILE GLU GLY ALA GLY GLY GLY HIS SER PRO ASP VAL ILE          
SEQRES  23 I  568  THR MET ALA GLY GLU VAL ASN ILE LEU PRO SER SER THR          
SEQRES  24 I  568  THR PRO THR ILE PRO TYR THR ILE ASN THR VAL ALA GLU          
SEQRES  25 I  568  HIS LEU ASP MET LEU MET THR CYS HIS HIS LEU ASP LYS          
SEQRES  26 I  568  ARG ILE ARG GLU ASP LEU GLN PHE SER GLN SER ARG ILE          
SEQRES  27 I  568  ARG PRO GLY SER ILE ALA ALA GLU ASP THR LEU HIS ASP          
SEQRES  28 I  568  MET GLY VAL ILE ALA MET THR SER SER ASP SER GLN ALA          
SEQRES  29 I  568  MET GLY ARG ALA GLY GLU VAL ILE PRO ARG THR TRP GLN          
SEQRES  30 I  568  THR ALA ASP LYS ASN LYS LYS GLU PHE GLY ARG LEU THR          
SEQRES  31 I  568  GLU GLU LYS GLY ASP ASN ASP ASN PHE ARG ILE LYS ARG          
SEQRES  32 I  568  TYR ILE SER LYS TYR THR ILE ASN PRO ALA ILE THR HIS          
SEQRES  33 I  568  GLY VAL SER GLU TYR ILE GLY SER VAL GLU GLU GLY LYS          
SEQRES  34 I  568  ILE ALA ASP LEU VAL VAL TRP ASN PRO ALA PHE PHE GLY          
SEQRES  35 I  568  VAL LYS PRO LYS ILE ILE ILE LYS GLY GLY MET VAL VAL          
SEQRES  36 I  568  PHE SER GLU MET GLY ASP SER ASN ALA SER VAL PRO THR          
SEQRES  37 I  568  PRO GLN PRO VAL TYR TYR ARG GLU MET PHE GLY HIS HIS          
SEQRES  38 I  568  GLY LYS ALA LYS PHE ASP THR SER ILE THR PHE VAL SER          
SEQRES  39 I  568  LYS VAL ALA TYR GLU ASN GLY ILE LYS GLU LYS LEU GLY          
SEQRES  40 I  568  LEU GLU ARG LYS VAL LEU PRO VAL LYS ASN CYS ARG ASN          
SEQRES  41 I  568  VAL THR LYS LYS ASP PHE LYS PHE ASN ASN THR THR ALA          
SEQRES  42 I  568  LYS ILE THR VAL ASN PRO GLU THR PHE GLU VAL PHE VAL          
SEQRES  43 I  568  ASN GLY LYS LEU CYS THR SER LYS PRO ALA THR GLU VAL          
SEQRES  44 I  568  ALA LEU ALA SER ARG TYR THR PHE PHE                          
SEQRES   1 J  225  FME LYS LEU THR PRO LYS GLU GLN GLU LYS PHE LEU LEU          
SEQRES   2 J  225  TYR TYR ALA GLY GLU VAL ALA ARG LYS ARG LYS GLU GLU          
SEQRES   3 J  225  GLY LEU LYS LEU ASN GLN PRO GLU ALA ILE ALA TYR ILE          
SEQRES   4 J  225  SER ALA HIS ILE MET ASP GLU ALA ARG ARG GLY LYS LYS          
SEQRES   5 J  225  THR VAL ALA GLN LEU MET GLU GLU CYS VAL HIS PHE LEU          
SEQRES   6 J  225  LYS LYS ASP GLU VAL MET PRO GLY VAL GLY ASN MET VAL          
SEQRES   7 J  225  PRO ASP LEU GLY VAL GLU ALA ASN PHE PRO ASP GLY THR          
SEQRES   8 J  225  LYS LEU VAL THR VAL ASN TRP PRO ILE GLU PRO ASP ASP          
SEQRES   9 J  225  PHE LYS ALA GLY GLU ILE LYS PHE ALA SER ASP LYS ASP          
SEQRES  10 J  225  ILE GLU LEU ASN ALA GLY LYS GLU ILE THR GLU LEU LYS          
SEQRES  11 J  225  VAL THR ASN LYS GLY PRO LYS SER LEU HIS VAL GLY SER          
SEQRES  12 J  225  HIS PHE HIS PHE PHE GLU ALA ASN ARG ALA LEU GLU PHE          
SEQRES  13 J  225  ASP ARG GLU LYS ALA TYR GLY LYS ARG LEU ASP ILE PRO          
SEQRES  14 J  225  SER GLY ASN THR LEU ARG ILE GLY ALA GLY GLU THR LYS          
SEQRES  15 J  225  THR VAL HIS LEU ILE PRO ILE GLY GLY SER LYS LYS ILE          
SEQRES  16 J  225  ILE GLY MET ASN GLY LEU LEU ASN GLY ILE ALA ASP ASP          
SEQRES  17 J  225  LEU HIS LYS GLN LYS ALA LEU GLU LYS ALA LYS HIS HIS          
SEQRES  18 J  225  GLY PHE ILE LYS                                              
SEQRES   1 L  568  MET LYS MET LYS ARG GLN GLU TYR VAL ASN THR TYR GLY          
SEQRES   2 L  568  PRO THR THR GLY ASP LYS VAL ARG LEU GLY ASP THR ASP          
SEQRES   3 L  568  LEU TRP ALA GLU VAL GLU HIS ASP TYR THR VAL TYR GLY          
SEQRES   4 L  568  GLU GLU LEU LYS PHE GLY ALA GLY LYS THR ILE ARG GLU          
SEQRES   5 L  568  GLY MET GLY GLN SER ASN SER PRO ASP GLU ASN THR LEU          
SEQRES   6 L  568  ASP LEU VAL ILE THR ASN ALA LEU ILE ILE ASP TYR THR          
SEQRES   7 L  568  GLY ILE TYR LYS ALA ASP ILE GLY ILE LYS ASN GLY LYS          
SEQRES   8 L  568  ILE HIS GLY ILE GLY LYS ALA GLY ASN LYS ASP MET GLN          
SEQRES   9 L  568  ASP GLY VAL THR PRO HIS MET VAL VAL GLY VAL GLY THR          
SEQRES  10 L  568  GLU ALA LEU ALA GLY GLU GLY MET ILE ILE THR ALA GLY          
SEQRES  11 L  568  GLY ILE ASP SER HIS THR HIS PHE LEU SER PRO GLN GLN          
SEQRES  12 L  568  PHE PRO THR ALA LEU ALA ASN GLY VAL THR THR MET PHE          
SEQRES  13 L  568  GLY GLY GLY THR GLY PRO VAL ASP GLY THR ASN ALA THR          
SEQRES  14 L  568  THR ILE THR PRO GLY VAL TRP ASN LEU HIS ARG MET LEU          
SEQRES  15 L  568  ARG ALA ALA GLU GLU TYR GLY MET ASN VAL GLY LEU LEU          
SEQRES  16 L  568  GLY LYS GLY ASN SER SER SER ARG ALA GLN LEU VAL GLU          
SEQRES  17 L  568  GLN VAL LYS ALA GLY ALA ILE GLY PHE KCX LEU HIS GLU          
SEQRES  18 L  568  ASP TRP GLY THR THR PRO SER ALA ILE ASP HIS CYS LEU          
SEQRES  19 L  568  SER VAL ALA ASP GLU TYR ASP VAL GLN VAL CYS ILE HIS          
SEQRES  20 L  568  THR ASP THR VAL ASN GLU ALA GLY TYR VAL ASP ASP THR          
SEQRES  21 L  568  LEU ARG ALA MET ASN GLY ARG ALA ILE HIS ALA TYR HIS          
SEQRES  22 L  568  ILE GLU GLY ALA GLY GLY GLY HIS SER PRO ASP VAL ILE          
SEQRES  23 L  568  THR MET ALA GLY GLU VAL ASN ILE LEU PRO SER SER THR          
SEQRES  24 L  568  THR PRO THR ILE PRO TYR THR ILE ASN THR VAL ALA GLU          
SEQRES  25 L  568  HIS LEU ASP MET LEU MET THR CYS HIS HIS LEU ASP LYS          
SEQRES  26 L  568  ARG ILE ARG GLU ASP LEU GLN PHE SER GLN SER ARG ILE          
SEQRES  27 L  568  ARG PRO GLY SER ILE ALA ALA GLU ASP THR LEU HIS ASP          
SEQRES  28 L  568  MET GLY VAL ILE ALA MET THR SER SER ASP SER GLN ALA          
SEQRES  29 L  568  MET GLY ARG ALA GLY GLU VAL ILE PRO ARG THR TRP GLN          
SEQRES  30 L  568  THR ALA ASP LYS ASN LYS LYS GLU PHE GLY ARG LEU THR          
SEQRES  31 L  568  GLU GLU LYS GLY ASP ASN ASP ASN PHE ARG ILE LYS ARG          
SEQRES  32 L  568  TYR ILE SER LYS TYR THR ILE ASN PRO ALA ILE THR HIS          
SEQRES  33 L  568  GLY VAL SER GLU TYR ILE GLY SER VAL GLU GLU GLY LYS          
SEQRES  34 L  568  ILE ALA ASP LEU VAL VAL TRP ASN PRO ALA PHE PHE GLY          
SEQRES  35 L  568  VAL LYS PRO LYS ILE ILE ILE LYS GLY GLY MET VAL VAL          
SEQRES  36 L  568  PHE SER GLU MET GLY ASP SER ASN ALA SER VAL PRO THR          
SEQRES  37 L  568  PRO GLN PRO VAL TYR TYR ARG GLU MET PHE GLY HIS HIS          
SEQRES  38 L  568  GLY LYS ALA LYS PHE ASP THR SER ILE THR PHE VAL SER          
SEQRES  39 L  568  LYS VAL ALA TYR GLU ASN GLY ILE LYS GLU LYS LEU GLY          
SEQRES  40 L  568  LEU GLU ARG LYS VAL LEU PRO VAL LYS ASN CYS ARG ASN          
SEQRES  41 L  568  VAL THR LYS LYS ASP PHE LYS PHE ASN ASN THR THR ALA          
SEQRES  42 L  568  LYS ILE THR VAL ASN PRO GLU THR PHE GLU VAL PHE VAL          
SEQRES  43 L  568  ASN GLY LYS LEU CYS THR SER LYS PRO ALA THR GLU VAL          
SEQRES  44 L  568  ALA LEU ALA SER ARG TYR THR PHE PHE                          
SEQRES   1 M  225  FME LYS LEU THR PRO LYS GLU GLN GLU LYS PHE LEU LEU          
SEQRES   2 M  225  TYR TYR ALA GLY GLU VAL ALA ARG LYS ARG LYS GLU GLU          
SEQRES   3 M  225  GLY LEU LYS LEU ASN GLN PRO GLU ALA ILE ALA TYR ILE          
SEQRES   4 M  225  SER ALA HIS ILE MET ASP GLU ALA ARG ARG GLY LYS LYS          
SEQRES   5 M  225  THR VAL ALA GLN LEU MET GLU GLU CYS VAL HIS PHE LEU          
SEQRES   6 M  225  LYS LYS ASP GLU VAL MET PRO GLY VAL GLY ASN MET VAL          
SEQRES   7 M  225  PRO ASP LEU GLY VAL GLU ALA ASN PHE PRO ASP GLY THR          
SEQRES   8 M  225  LYS LEU VAL THR VAL ASN TRP PRO ILE GLU PRO ASP ASP          
SEQRES   9 M  225  PHE LYS ALA GLY GLU ILE LYS PHE ALA SER ASP LYS ASP          
SEQRES  10 M  225  ILE GLU LEU ASN ALA GLY LYS GLU ILE THR GLU LEU LYS          
SEQRES  11 M  225  VAL THR ASN LYS GLY PRO LYS SER LEU HIS VAL GLY SER          
SEQRES  12 M  225  HIS PHE HIS PHE PHE GLU ALA ASN ARG ALA LEU GLU PHE          
SEQRES  13 M  225  ASP ARG GLU LYS ALA TYR GLY LYS ARG LEU ASP ILE PRO          
SEQRES  14 M  225  SER GLY ASN THR LEU ARG ILE GLY ALA GLY GLU THR LYS          
SEQRES  15 M  225  THR VAL HIS LEU ILE PRO ILE GLY GLY SER LYS LYS ILE          
SEQRES  16 M  225  ILE GLY MET ASN GLY LEU LEU ASN GLY ILE ALA ASP ASP          
SEQRES  17 M  225  LEU HIS LYS GLN LYS ALA LEU GLU LYS ALA LYS HIS HIS          
SEQRES  18 M  225  GLY PHE ILE LYS                                              
SEQRES   1 O  568  MET LYS MET LYS ARG GLN GLU TYR VAL ASN THR TYR GLY          
SEQRES   2 O  568  PRO THR THR GLY ASP LYS VAL ARG LEU GLY ASP THR ASP          
SEQRES   3 O  568  LEU TRP ALA GLU VAL GLU HIS ASP TYR THR VAL TYR GLY          
SEQRES   4 O  568  GLU GLU LEU LYS PHE GLY ALA GLY LYS THR ILE ARG GLU          
SEQRES   5 O  568  GLY MET GLY GLN SER ASN SER PRO ASP GLU ASN THR LEU          
SEQRES   6 O  568  ASP LEU VAL ILE THR ASN ALA LEU ILE ILE ASP TYR THR          
SEQRES   7 O  568  GLY ILE TYR LYS ALA ASP ILE GLY ILE LYS ASN GLY LYS          
SEQRES   8 O  568  ILE HIS GLY ILE GLY LYS ALA GLY ASN LYS ASP MET GLN          
SEQRES   9 O  568  ASP GLY VAL THR PRO HIS MET VAL VAL GLY VAL GLY THR          
SEQRES  10 O  568  GLU ALA LEU ALA GLY GLU GLY MET ILE ILE THR ALA GLY          
SEQRES  11 O  568  GLY ILE ASP SER HIS THR HIS PHE LEU SER PRO GLN GLN          
SEQRES  12 O  568  PHE PRO THR ALA LEU ALA ASN GLY VAL THR THR MET PHE          
SEQRES  13 O  568  GLY GLY GLY THR GLY PRO VAL ASP GLY THR ASN ALA THR          
SEQRES  14 O  568  THR ILE THR PRO GLY VAL TRP ASN LEU HIS ARG MET LEU          
SEQRES  15 O  568  ARG ALA ALA GLU GLU TYR GLY MET ASN VAL GLY LEU LEU          
SEQRES  16 O  568  GLY LYS GLY ASN SER SER SER ARG ALA GLN LEU VAL GLU          
SEQRES  17 O  568  GLN VAL LYS ALA GLY ALA ILE GLY PHE KCX LEU HIS GLU          
SEQRES  18 O  568  ASP TRP GLY THR THR PRO SER ALA ILE ASP HIS CYS LEU          
SEQRES  19 O  568  SER VAL ALA ASP GLU TYR ASP VAL GLN VAL CYS ILE HIS          
SEQRES  20 O  568  THR ASP THR VAL ASN GLU ALA GLY TYR VAL ASP ASP THR          
SEQRES  21 O  568  LEU ARG ALA MET ASN GLY ARG ALA ILE HIS ALA TYR HIS          
SEQRES  22 O  568  ILE GLU GLY ALA GLY GLY GLY HIS SER PRO ASP VAL ILE          
SEQRES  23 O  568  THR MET ALA GLY GLU VAL ASN ILE LEU PRO SER SER THR          
SEQRES  24 O  568  THR PRO THR ILE PRO TYR THR ILE ASN THR VAL ALA GLU          
SEQRES  25 O  568  HIS LEU ASP MET LEU MET THR CYS HIS HIS LEU ASP LYS          
SEQRES  26 O  568  ARG ILE ARG GLU ASP LEU GLN PHE SER GLN SER ARG ILE          
SEQRES  27 O  568  ARG PRO GLY SER ILE ALA ALA GLU ASP THR LEU HIS ASP          
SEQRES  28 O  568  MET GLY VAL ILE ALA MET THR SER SER ASP SER GLN ALA          
SEQRES  29 O  568  MET GLY ARG ALA GLY GLU VAL ILE PRO ARG THR TRP GLN          
SEQRES  30 O  568  THR ALA ASP LYS ASN LYS LYS GLU PHE GLY ARG LEU THR          
SEQRES  31 O  568  GLU GLU LYS GLY ASP ASN ASP ASN PHE ARG ILE LYS ARG          
SEQRES  32 O  568  TYR ILE SER LYS TYR THR ILE ASN PRO ALA ILE THR HIS          
SEQRES  33 O  568  GLY VAL SER GLU TYR ILE GLY SER VAL GLU GLU GLY LYS          
SEQRES  34 O  568  ILE ALA ASP LEU VAL VAL TRP ASN PRO ALA PHE PHE GLY          
SEQRES  35 O  568  VAL LYS PRO LYS ILE ILE ILE LYS GLY GLY MET VAL VAL          
SEQRES  36 O  568  PHE SER GLU MET GLY ASP SER ASN ALA SER VAL PRO THR          
SEQRES  37 O  568  PRO GLN PRO VAL TYR TYR ARG GLU MET PHE GLY HIS HIS          
SEQRES  38 O  568  GLY LYS ALA LYS PHE ASP THR SER ILE THR PHE VAL SER          
SEQRES  39 O  568  LYS VAL ALA TYR GLU ASN GLY ILE LYS GLU LYS LEU GLY          
SEQRES  40 O  568  LEU GLU ARG LYS VAL LEU PRO VAL LYS ASN CYS ARG ASN          
SEQRES  41 O  568  VAL THR LYS LYS ASP PHE LYS PHE ASN ASN THR THR ALA          
SEQRES  42 O  568  LYS ILE THR VAL ASN PRO GLU THR PHE GLU VAL PHE VAL          
SEQRES  43 O  568  ASN GLY LYS LEU CYS THR SER LYS PRO ALA THR GLU VAL          
SEQRES  44 O  568  ALA LEU ALA SER ARG TYR THR PHE PHE                          
SEQRES   1 P  225  FME LYS LEU THR PRO LYS GLU GLN GLU LYS PHE LEU LEU          
SEQRES   2 P  225  TYR TYR ALA GLY GLU VAL ALA ARG LYS ARG LYS GLU GLU          
SEQRES   3 P  225  GLY LEU LYS LEU ASN GLN PRO GLU ALA ILE ALA TYR ILE          
SEQRES   4 P  225  SER ALA HIS ILE MET ASP GLU ALA ARG ARG GLY LYS LYS          
SEQRES   5 P  225  THR VAL ALA GLN LEU MET GLU GLU CYS VAL HIS PHE LEU          
SEQRES   6 P  225  LYS LYS ASP GLU VAL MET PRO GLY VAL GLY ASN MET VAL          
SEQRES   7 P  225  PRO ASP LEU GLY VAL GLU ALA ASN PHE PRO ASP GLY THR          
SEQRES   8 P  225  LYS LEU VAL THR VAL ASN TRP PRO ILE GLU PRO ASP ASP          
SEQRES   9 P  225  PHE LYS ALA GLY GLU ILE LYS PHE ALA SER ASP LYS ASP          
SEQRES  10 P  225  ILE GLU LEU ASN ALA GLY LYS GLU ILE THR GLU LEU LYS          
SEQRES  11 P  225  VAL THR ASN LYS GLY PRO LYS SER LEU HIS VAL GLY SER          
SEQRES  12 P  225  HIS PHE HIS PHE PHE GLU ALA ASN ARG ALA LEU GLU PHE          
SEQRES  13 P  225  ASP ARG GLU LYS ALA TYR GLY LYS ARG LEU ASP ILE PRO          
SEQRES  14 P  225  SER GLY ASN THR LEU ARG ILE GLY ALA GLY GLU THR LYS          
SEQRES  15 P  225  THR VAL HIS LEU ILE PRO ILE GLY GLY SER LYS LYS ILE          
SEQRES  16 P  225  ILE GLY MET ASN GLY LEU LEU ASN GLY ILE ALA ASP ASP          
SEQRES  17 P  225  LEU HIS LYS GLN LYS ALA LEU GLU LYS ALA LYS HIS HIS          
SEQRES  18 P  225  GLY PHE ILE LYS                                              
SEQRES   1 R  568  MET LYS MET LYS ARG GLN GLU TYR VAL ASN THR TYR GLY          
SEQRES   2 R  568  PRO THR THR GLY ASP LYS VAL ARG LEU GLY ASP THR ASP          
SEQRES   3 R  568  LEU TRP ALA GLU VAL GLU HIS ASP TYR THR VAL TYR GLY          
SEQRES   4 R  568  GLU GLU LEU LYS PHE GLY ALA GLY LYS THR ILE ARG GLU          
SEQRES   5 R  568  GLY MET GLY GLN SER ASN SER PRO ASP GLU ASN THR LEU          
SEQRES   6 R  568  ASP LEU VAL ILE THR ASN ALA LEU ILE ILE ASP TYR THR          
SEQRES   7 R  568  GLY ILE TYR LYS ALA ASP ILE GLY ILE LYS ASN GLY LYS          
SEQRES   8 R  568  ILE HIS GLY ILE GLY LYS ALA GLY ASN LYS ASP MET GLN          
SEQRES   9 R  568  ASP GLY VAL THR PRO HIS MET VAL VAL GLY VAL GLY THR          
SEQRES  10 R  568  GLU ALA LEU ALA GLY GLU GLY MET ILE ILE THR ALA GLY          
SEQRES  11 R  568  GLY ILE ASP SER HIS THR HIS PHE LEU SER PRO GLN GLN          
SEQRES  12 R  568  PHE PRO THR ALA LEU ALA ASN GLY VAL THR THR MET PHE          
SEQRES  13 R  568  GLY GLY GLY THR GLY PRO VAL ASP GLY THR ASN ALA THR          
SEQRES  14 R  568  THR ILE THR PRO GLY VAL TRP ASN LEU HIS ARG MET LEU          
SEQRES  15 R  568  ARG ALA ALA GLU GLU TYR GLY MET ASN VAL GLY LEU LEU          
SEQRES  16 R  568  GLY LYS GLY ASN SER SER SER ARG ALA GLN LEU VAL GLU          
SEQRES  17 R  568  GLN VAL LYS ALA GLY ALA ILE GLY PHE KCX LEU HIS GLU          
SEQRES  18 R  568  ASP TRP GLY THR THR PRO SER ALA ILE ASP HIS CYS LEU          
SEQRES  19 R  568  SER VAL ALA ASP GLU TYR ASP VAL GLN VAL CYS ILE HIS          
SEQRES  20 R  568  THR ASP THR VAL ASN GLU ALA GLY TYR VAL ASP ASP THR          
SEQRES  21 R  568  LEU ARG ALA MET ASN GLY ARG ALA ILE HIS ALA TYR HIS          
SEQRES  22 R  568  ILE GLU GLY ALA GLY GLY GLY HIS SER PRO ASP VAL ILE          
SEQRES  23 R  568  THR MET ALA GLY GLU VAL ASN ILE LEU PRO SER SER THR          
SEQRES  24 R  568  THR PRO THR ILE PRO TYR THR ILE ASN THR VAL ALA GLU          
SEQRES  25 R  568  HIS LEU ASP MET LEU MET THR CYS HIS HIS LEU ASP LYS          
SEQRES  26 R  568  ARG ILE ARG GLU ASP LEU GLN PHE SER GLN SER ARG ILE          
SEQRES  27 R  568  ARG PRO GLY SER ILE ALA ALA GLU ASP THR LEU HIS ASP          
SEQRES  28 R  568  MET GLY VAL ILE ALA MET THR SER SER ASP SER GLN ALA          
SEQRES  29 R  568  MET GLY ARG ALA GLY GLU VAL ILE PRO ARG THR TRP GLN          
SEQRES  30 R  568  THR ALA ASP LYS ASN LYS LYS GLU PHE GLY ARG LEU THR          
SEQRES  31 R  568  GLU GLU LYS GLY ASP ASN ASP ASN PHE ARG ILE LYS ARG          
SEQRES  32 R  568  TYR ILE SER LYS TYR THR ILE ASN PRO ALA ILE THR HIS          
SEQRES  33 R  568  GLY VAL SER GLU TYR ILE GLY SER VAL GLU GLU GLY LYS          
SEQRES  34 R  568  ILE ALA ASP LEU VAL VAL TRP ASN PRO ALA PHE PHE GLY          
SEQRES  35 R  568  VAL LYS PRO LYS ILE ILE ILE LYS GLY GLY MET VAL VAL          
SEQRES  36 R  568  PHE SER GLU MET GLY ASP SER ASN ALA SER VAL PRO THR          
SEQRES  37 R  568  PRO GLN PRO VAL TYR TYR ARG GLU MET PHE GLY HIS HIS          
SEQRES  38 R  568  GLY LYS ALA LYS PHE ASP THR SER ILE THR PHE VAL SER          
SEQRES  39 R  568  LYS VAL ALA TYR GLU ASN GLY ILE LYS GLU LYS LEU GLY          
SEQRES  40 R  568  LEU GLU ARG LYS VAL LEU PRO VAL LYS ASN CYS ARG ASN          
SEQRES  41 R  568  VAL THR LYS LYS ASP PHE LYS PHE ASN ASN THR THR ALA          
SEQRES  42 R  568  LYS ILE THR VAL ASN PRO GLU THR PHE GLU VAL PHE VAL          
SEQRES  43 R  568  ASN GLY LYS LEU CYS THR SER LYS PRO ALA THR GLU VAL          
SEQRES  44 R  568  ALA LEU ALA SER ARG TYR THR PHE PHE                          
MODRES 3QGA FME A    1  MET  N-FORMYLMETHIONINE                                 
MODRES 3QGA KCX C  218  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3QGA FME D    1  MET  N-FORMYLMETHIONINE                                 
MODRES 3QGA KCX F  218  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3QGA FME G    1  MET  N-FORMYLMETHIONINE                                 
MODRES 3QGA KCX I  218  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3QGA FME J    1  MET  N-FORMYLMETHIONINE                                 
MODRES 3QGA KCX L  218  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3QGA FME M    1  MET  N-FORMYLMETHIONINE                                 
MODRES 3QGA KCX O  218  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 3QGA FME P    1  MET  N-FORMYLMETHIONINE                                 
MODRES 3QGA KCX R  218  LYS  LYSINE NZ-CARBOXYLIC ACID                          
HET    FME  A   1      10                                                       
HET    KCX  C 218      12                                                       
HET    FME  D   1      10                                                       
HET    KCX  F 218      12                                                       
HET    FME  G   1      10                                                       
HET    KCX  I 218      12                                                       
HET    FME  J   1      10                                                       
HET    KCX  L 218      12                                                       
HET    FME  M   1      10                                                       
HET    KCX  O 218      12                                                       
HET    FME  P   1      10                                                       
HET    KCX  R 218      12                                                       
HET     FE  C 774       1                                                       
HET     FE  C 775       1                                                       
HET     FE  F 774       1                                                       
HET     FE  F 775       1                                                       
HET     FE  I 774       1                                                       
HET     FE  I 775       1                                                       
HET     FE  L 774       1                                                       
HET     FE  L 775       1                                                       
HET     FE  O 774       1                                                       
HET     FE  O 775       1                                                       
HET     FE  R 774       1                                                       
HET     FE  R 775       1                                                       
HETNAM     FME N-FORMYLMETHIONINE                                               
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM      FE FE (III) ION                                                     
FORMUL   1  FME    6(C6 H11 N O3 S)                                             
FORMUL   2  KCX    6(C7 H14 N2 O4)                                              
FORMUL  13   FE    12(FE 3+)                                                    
FORMUL  25  HOH   *606(H2 O)                                                    
HELIX    1   1 THR A    4  GLU A   26  1                                  23    
HELIX    2   2 ASN A   31  GLY A   50  1                                  20    
HELIX    3   3 THR A   53  CYS A   61  1                                   9    
HELIX    4   4 LYS A   67  VAL A   70  5                                   4    
HELIX    5   5 GLY A   73  VAL A   78  1                                   6    
HELIX    6   6 HIS A  146  ALA A  150  5                                   5    
HELIX    7   7 ASP A  157  TYR A  162  5                                   6    
HELIX    8   8 ASP A  208  HIS A  221  1                                  14    
HELIX    9   9 LYS C    4  GLY C   13  1                                  10    
HELIX   10  10 GLN C  142  ALA C  149  1                                   8    
HELIX   11  11 VAL C  163  THR C  169  1                                   7    
HELIX   12  12 PRO C  173  ALA C  185  1                                  13    
HELIX   13  13 GLU C  186  TYR C  188  5                                   3    
HELIX   14  14 SER C  202  ALA C  212  1                                  11    
HELIX   15  15 ASP C  222  GLY C  224  5                                   3    
HELIX   16  16 THR C  226  ASP C  241  1                                  16    
HELIX   17  17 TYR C  256  ASN C  265  1                                  10    
HELIX   18  18 ASP C  284  GLU C  291  5                                   8    
HELIX   19  19 PRO C  301  ILE C  303  5                                   3    
HELIX   20  20 ASN C  308  HIS C  321  1                                  14    
HELIX   21  21 SER C  334  MET C  352  1                                  19    
HELIX   22  22 GLU C  370  GLY C  387  1                                  18    
HELIX   23  23 ASP C  397  LYS C  407  1                                  11    
HELIX   24  24 THR C  409  HIS C  416  1                                   8    
HELIX   25  25 ASN C  437  PHE C  441  5                                   5    
HELIX   26  26 PHE C  478  HIS C  481  5                                   4    
HELIX   27  27 LYS C  483  SER C  489  1                                   7    
HELIX   28  28 SER C  494  ASN C  500  1                                   7    
HELIX   29  29 GLY C  501  LEU C  506  1                                   6    
HELIX   30  30 THR C  522  PHE C  526  5                                   5    
HELIX   31  31 THR D    4  GLU D   26  1                                  23    
HELIX   32  32 ASN D   31  GLY D   50  1                                  20    
HELIX   33  33 THR D   53  CYS D   61  1                                   9    
HELIX   34  34 LYS D   67  VAL D   70  5                                   4    
HELIX   35  35 GLY D   73  VAL D   78  1                                   6    
HELIX   36  36 HIS D  146  ALA D  150  5                                   5    
HELIX   37  37 ASP D  157  TYR D  162  5                                   6    
HELIX   38  38 ASP D  208  HIS D  221  1                                  14    
HELIX   39  39 LYS F    4  GLY F   13  1                                  10    
HELIX   40  40 GLN F  142  ALA F  149  1                                   8    
HELIX   41  41 VAL F  163  THR F  169  1                                   7    
HELIX   42  42 PRO F  173  ALA F  185  1                                  13    
HELIX   43  43 GLU F  186  TYR F  188  5                                   3    
HELIX   44  44 SER F  202  ALA F  212  1                                  11    
HELIX   45  45 ASP F  222  GLY F  224  5                                   3    
HELIX   46  46 THR F  226  ASP F  241  1                                  16    
HELIX   47  47 TYR F  256  ASN F  265  1                                  10    
HELIX   48  48 ASP F  284  GLU F  291  5                                   8    
HELIX   49  49 PRO F  301  ILE F  303  5                                   3    
HELIX   50  50 ASN F  308  HIS F  321  1                                  14    
HELIX   51  51 SER F  334  MET F  352  1                                  19    
HELIX   52  52 GLU F  370  GLY F  387  1                                  18    
HELIX   53  53 ASP F  397  LYS F  407  1                                  11    
HELIX   54  54 THR F  409  HIS F  416  1                                   8    
HELIX   55  55 ASN F  437  PHE F  441  5                                   5    
HELIX   56  56 PHE F  478  HIS F  481  5                                   4    
HELIX   57  57 LYS F  483  SER F  489  1                                   7    
HELIX   58  58 SER F  494  ASN F  500  1                                   7    
HELIX   59  59 GLY F  501  LEU F  506  1                                   6    
HELIX   60  60 THR F  522  PHE F  526  5                                   5    
HELIX   61  61 THR G    4  GLU G   26  1                                  23    
HELIX   62  62 ASN G   31  GLY G   50  1                                  20    
HELIX   63  63 THR G   53  CYS G   61  1                                   9    
HELIX   64  64 LYS G   67  VAL G   70  5                                   4    
HELIX   65  65 GLY G   73  VAL G   78  1                                   6    
HELIX   66  66 HIS G  146  ALA G  150  5                                   5    
HELIX   67  67 ASP G  157  TYR G  162  5                                   6    
HELIX   68  68 ASP G  208  HIS G  221  1                                  14    
HELIX   69  69 LYS I    4  GLY I   13  1                                  10    
HELIX   70  70 GLN I  142  ALA I  149  1                                   8    
HELIX   71  71 VAL I  163  THR I  169  1                                   7    
HELIX   72  72 PRO I  173  ALA I  185  1                                  13    
HELIX   73  73 GLU I  186  TYR I  188  5                                   3    
HELIX   74  74 SER I  202  ALA I  212  1                                  11    
HELIX   75  75 ASP I  222  GLY I  224  5                                   3    
HELIX   76  76 THR I  226  ASP I  241  1                                  16    
HELIX   77  77 TYR I  256  ASN I  265  1                                  10    
HELIX   78  78 ASP I  284  GLU I  291  5                                   8    
HELIX   79  79 PRO I  301  ILE I  303  5                                   3    
HELIX   80  80 ASN I  308  HIS I  321  1                                  14    
HELIX   81  81 SER I  334  MET I  352  1                                  19    
HELIX   82  82 GLU I  370  GLY I  387  1                                  18    
HELIX   83  83 ASP I  397  LYS I  407  1                                  11    
HELIX   84  84 THR I  409  HIS I  416  1                                   8    
HELIX   85  85 ASN I  437  PHE I  441  5                                   5    
HELIX   86  86 PHE I  478  HIS I  481  5                                   4    
HELIX   87  87 LYS I  483  SER I  489  1                                   7    
HELIX   88  88 SER I  494  ASN I  500  1                                   7    
HELIX   89  89 GLY I  501  LEU I  506  1                                   6    
HELIX   90  90 THR I  522  PHE I  526  5                                   5    
HELIX   91  91 THR J    4  GLU J   26  1                                  23    
HELIX   92  92 ASN J   31  GLY J   50  1                                  20    
HELIX   93  93 THR J   53  CYS J   61  1                                   9    
HELIX   94  94 LYS J   67  VAL J   70  5                                   4    
HELIX   95  95 GLY J   73  VAL J   78  1                                   6    
HELIX   96  96 HIS J  146  ALA J  150  5                                   5    
HELIX   97  97 ASP J  157  TYR J  162  5                                   6    
HELIX   98  98 ASP J  208  HIS J  221  1                                  14    
HELIX   99  99 LYS L    4  GLY L   13  1                                  10    
HELIX  100 100 GLN L  142  ALA L  149  1                                   8    
HELIX  101 101 VAL L  163  THR L  169  1                                   7    
HELIX  102 102 PRO L  173  ALA L  185  1                                  13    
HELIX  103 103 GLU L  186  TYR L  188  5                                   3    
HELIX  104 104 SER L  202  ALA L  212  1                                  11    
HELIX  105 105 ASP L  222  GLY L  224  5                                   3    
HELIX  106 106 THR L  226  ASP L  241  1                                  16    
HELIX  107 107 TYR L  256  ASN L  265  1                                  10    
HELIX  108 108 ASP L  284  GLU L  291  5                                   8    
HELIX  109 109 PRO L  301  ILE L  303  5                                   3    
HELIX  110 110 ASN L  308  HIS L  321  1                                  14    
HELIX  111 111 SER L  334  MET L  352  1                                  19    
HELIX  112 112 GLU L  370  GLY L  387  1                                  18    
HELIX  113 113 ASP L  397  LYS L  407  1                                  11    
HELIX  114 114 THR L  409  HIS L  416  1                                   8    
HELIX  115 115 ASN L  437  PHE L  441  5                                   5    
HELIX  116 116 PHE L  478  HIS L  481  5                                   4    
HELIX  117 117 LYS L  483  SER L  489  1                                   7    
HELIX  118 118 SER L  494  ASN L  500  1                                   7    
HELIX  119 119 GLY L  501  LEU L  506  1                                   6    
HELIX  120 120 THR L  522  PHE L  526  5                                   5    
HELIX  121 121 THR M    4  GLU M   26  1                                  23    
HELIX  122 122 ASN M   31  GLY M   50  1                                  20    
HELIX  123 123 THR M   53  CYS M   61  1                                   9    
HELIX  124 124 LYS M   67  VAL M   70  5                                   4    
HELIX  125 125 GLY M   73  VAL M   78  1                                   6    
HELIX  126 126 HIS M  146  ALA M  150  5                                   5    
HELIX  127 127 ASP M  157  TYR M  162  5                                   6    
HELIX  128 128 ASP M  208  HIS M  221  1                                  14    
HELIX  129 129 LYS O    4  GLY O   13  1                                  10    
HELIX  130 130 GLN O  142  ALA O  149  1                                   8    
HELIX  131 131 VAL O  163  THR O  169  1                                   7    
HELIX  132 132 PRO O  173  ALA O  185  1                                  13    
HELIX  133 133 GLU O  186  TYR O  188  5                                   3    
HELIX  134 134 SER O  202  ALA O  212  1                                  11    
HELIX  135 135 ASP O  222  GLY O  224  5                                   3    
HELIX  136 136 THR O  226  ASP O  241  1                                  16    
HELIX  137 137 TYR O  256  ASN O  265  1                                  10    
HELIX  138 138 ASP O  284  GLU O  291  5                                   8    
HELIX  139 139 PRO O  301  ILE O  303  5                                   3    
HELIX  140 140 ASN O  308  HIS O  321  1                                  14    
HELIX  141 141 SER O  334  MET O  352  1                                  19    
HELIX  142 142 GLU O  370  GLY O  387  1                                  18    
HELIX  143 143 ASP O  397  LYS O  407  1                                  11    
HELIX  144 144 THR O  409  HIS O  416  1                                   8    
HELIX  145 145 ASN O  437  PHE O  441  5                                   5    
HELIX  146 146 PHE O  478  HIS O  481  5                                   4    
HELIX  147 147 LYS O  483  SER O  489  1                                   7    
HELIX  148 148 SER O  494  ASN O  500  1                                   7    
HELIX  149 149 GLY O  501  LEU O  506  1                                   6    
HELIX  150 150 THR O  522  PHE O  526  5                                   5    
HELIX  151 151 THR P    4  GLU P   26  1                                  23    
HELIX  152 152 ASN P   31  GLY P   50  1                                  20    
HELIX  153 153 THR P   53  CYS P   61  1                                   9    
HELIX  154 154 LYS P   67  VAL P   70  5                                   4    
HELIX  155 155 GLY P   73  VAL P   78  1                                   6    
HELIX  156 156 HIS P  146  ALA P  150  5                                   5    
HELIX  157 157 ASP P  157  TYR P  162  5                                   6    
HELIX  158 158 ASP P  208  HIS P  221  1                                  14    
HELIX  159 159 LYS R    4  GLY R   13  1                                  10    
HELIX  160 160 GLN R  142  ALA R  149  1                                   8    
HELIX  161 161 VAL R  163  THR R  169  1                                   7    
HELIX  162 162 PRO R  173  ALA R  185  1                                  13    
HELIX  163 163 GLU R  186  TYR R  188  5                                   3    
HELIX  164 164 SER R  202  ALA R  212  1                                  11    
HELIX  165 165 ASP R  222  GLY R  224  5                                   3    
HELIX  166 166 THR R  226  ASP R  241  1                                  16    
HELIX  167 167 TYR R  256  ASN R  265  1                                  10    
HELIX  168 168 ASP R  284  GLU R  291  5                                   8    
HELIX  169 169 PRO R  301  ILE R  303  5                                   3    
HELIX  170 170 ASN R  308  HIS R  321  1                                  14    
HELIX  171 171 SER R  334  MET R  352  1                                  19    
HELIX  172 172 GLU R  370  GLY R  387  1                                  18    
HELIX  173 173 ASP R  397  LYS R  407  1                                  11    
HELIX  174 174 THR R  409  HIS R  416  1                                   8    
HELIX  175 175 ASN R  437  PHE R  441  5                                   5    
HELIX  176 176 PHE R  478  HIS R  481  5                                   4    
HELIX  177 177 LYS R  483  SER R  489  1                                   7    
HELIX  178 178 SER R  494  ASN R  500  1                                   7    
HELIX  179 179 GLY R  501  LEU R  506  1                                   6    
HELIX  180 180 THR R  522  PHE R  526  5                                   5    
SHEET    1   A 2 ASP A  80  PHE A  87  0                                        
SHEET    2   A 2 GLY A  90  ASN A  97 -1  O  VAL A  96   N  LEU A  81           
SHEET    1   B 3 ILE A 110  LYS A 111  0                                        
SHEET    2   B 3 LYS C  19  ARG C  21 -1  O  LYS C  19   N  LYS A 111           
SHEET    3   B 3 TRP C  28  GLU C  30 -1  O  ALA C  29   N  VAL C  20           
SHEET    1   C 2 ILE A 118  GLU A 119  0                                        
SHEET    2   C 2 LYS C   2  MET C   3 -1  O  MET C   3   N  ILE A 118           
SHEET    1   D 4 LEU A 154  GLU A 155  0                                        
SHEET    2   D 4 THR A 127  ASN A 133 -1  N  THR A 132   O  GLU A 155           
SHEET    3   D 4 THR A 181  PRO A 188 -1  O  VAL A 184   N  LEU A 129           
SHEET    4   D 4 LYS A 164  LEU A 166 -1  N  ARG A 165   O  ILE A 187           
SHEET    1   E 2 LEU A 139  GLY A 142  0                                        
SHEET    2   E 2 THR A 173  ILE A 176 -1  O  ILE A 176   N  LEU A 139           
SHEET    1   F 2 LYS A 194  ILE A 196  0                                        
SHEET    2   F 2 GLY A 204  ILE A 205 -1  O  GLY A 204   N  ILE A 196           
SHEET    1   G 4 LYS C  91  GLY C  96  0                                        
SHEET    2   G 4 GLY C  79  LYS C  88 -1  N  GLY C  86   O  GLY C  94           
SHEET    3   G 4 LEU C  67  ASP C  76 -1  N  ILE C  69   O  ILE C  85           
SHEET    4   G 4 GLU C 118  ALA C 121  1  O  LEU C 120   N  VAL C  68           
SHEET    1   H 8 LYS C  91  GLY C  96  0                                        
SHEET    2   H 8 GLY C  79  LYS C  88 -1  N  GLY C  86   O  GLY C  94           
SHEET    3   H 8 LEU C  67  ASP C  76 -1  N  ILE C  69   O  ILE C  85           
SHEET    4   H 8 ILE C 126  ALA C 129  1  O  ILE C 127   N  LEU C  73           
SHEET    5   H 8 LEU C 433  TRP C 436 -1  O  TRP C 436   N  ILE C 126           
SHEET    6   H 8 ILE C 447  LYS C 450 -1  O  ILE C 449   N  LEU C 433           
SHEET    7   H 8 MET C 453  MET C 459 -1  O  MET C 453   N  LYS C 450           
SHEET    8   H 8 TYR C 473  GLU C 476 -1  O  TYR C 473   N  MET C 459           
SHEET    1   I 8 GLY C 131  HIS C 137  0                                        
SHEET    2   I 8 VAL C 152  GLY C 158  1  O  THR C 154   N  ASP C 133           
SHEET    3   I 8 ASN C 191  LYS C 197  1  O  ASN C 191   N  MET C 155           
SHEET    4   I 8 GLY C 216  HIS C 220  1  O  KCX C 218   N  GLY C 196           
SHEET    5   I 8 GLN C 243  HIS C 247  1  O  CYS C 245   N  LEU C 219           
SHEET    6   I 8 ILE C 269  ALA C 271  1  O  HIS C 270   N  VAL C 244           
SHEET    7   I 8 ILE C 294  THR C 299  1  O  LEU C 295   N  ILE C 269           
SHEET    8   I 8 MET C 357  SER C 359  1  O  SER C 359   N  SER C 298           
SHEET    1   J 5 GLY C 131  HIS C 137  0                                        
SHEET    2   J 5 VAL C 152  GLY C 158  1  O  THR C 154   N  ASP C 133           
SHEET    3   J 5 ASN C 191  LYS C 197  1  O  ASN C 191   N  MET C 155           
SHEET    4   J 5 ILE C 490  VAL C 493  1  O  PHE C 492   N  VAL C 192           
SHEET    5   J 5 LYS C 511  PRO C 514  1  O  LYS C 511   N  THR C 491           
SHEET    1   K 3 ILE C 535  VAL C 537  0                                        
SHEET    2   K 3 VAL C 544  VAL C 546 -1  O  PHE C 545   N  THR C 536           
SHEET    3   K 3 LYS C 549  CYS C 551 -1  O  CYS C 551   N  VAL C 544           
SHEET    1   L 2 ASP D  80  PHE D  87  0                                        
SHEET    2   L 2 GLY D  90  ASN D  97 -1  O  VAL D  96   N  LEU D  81           
SHEET    1   M 3 ILE D 110  LYS D 111  0                                        
SHEET    2   M 3 LYS F  19  ARG F  21 -1  O  LYS F  19   N  LYS D 111           
SHEET    3   M 3 TRP F  28  GLU F  30 -1  O  ALA F  29   N  VAL F  20           
SHEET    1   N 2 ILE D 118  GLU D 119  0                                        
SHEET    2   N 2 LYS F   2  MET F   3 -1  O  MET F   3   N  ILE D 118           
SHEET    1   O 4 LEU D 154  GLU D 155  0                                        
SHEET    2   O 4 THR D 127  ASN D 133 -1  N  THR D 132   O  GLU D 155           
SHEET    3   O 4 THR D 181  PRO D 188 -1  O  VAL D 184   N  LEU D 129           
SHEET    4   O 4 LYS D 164  LEU D 166 -1  N  ARG D 165   O  ILE D 187           
SHEET    1   P 2 LEU D 139  GLY D 142  0                                        
SHEET    2   P 2 THR D 173  ILE D 176 -1  O  ILE D 176   N  LEU D 139           
SHEET    1   Q 2 LYS D 194  ILE D 196  0                                        
SHEET    2   Q 2 GLY D 204  ILE D 205 -1  O  GLY D 204   N  ILE D 196           
SHEET    1   R 4 LYS F  91  GLY F  96  0                                        
SHEET    2   R 4 GLY F  79  LYS F  88 -1  N  GLY F  86   O  GLY F  94           
SHEET    3   R 4 LEU F  67  ASP F  76 -1  N  ILE F  69   O  ILE F  85           
SHEET    4   R 4 GLU F 118  ALA F 121  1  O  LEU F 120   N  VAL F  68           
SHEET    1   S 8 LYS F  91  GLY F  96  0                                        
SHEET    2   S 8 GLY F  79  LYS F  88 -1  N  GLY F  86   O  GLY F  94           
SHEET    3   S 8 LEU F  67  ASP F  76 -1  N  ILE F  69   O  ILE F  85           
SHEET    4   S 8 ILE F 126  ALA F 129  1  O  ILE F 127   N  LEU F  73           
SHEET    5   S 8 LEU F 433  TRP F 436 -1  O  TRP F 436   N  ILE F 126           
SHEET    6   S 8 ILE F 447  LYS F 450 -1  O  ILE F 449   N  LEU F 433           
SHEET    7   S 8 MET F 453  MET F 459 -1  O  MET F 453   N  LYS F 450           
SHEET    8   S 8 TYR F 473  GLU F 476 -1  O  TYR F 473   N  MET F 459           
SHEET    1   T 8 GLY F 131  HIS F 137  0                                        
SHEET    2   T 8 VAL F 152  GLY F 158  1  O  PHE F 156   N  ASP F 133           
SHEET    3   T 8 ASN F 191  LYS F 197  1  O  ASN F 191   N  MET F 155           
SHEET    4   T 8 GLY F 216  HIS F 220  1  O  KCX F 218   N  GLY F 196           
SHEET    5   T 8 GLN F 243  HIS F 247  1  O  CYS F 245   N  LEU F 219           
SHEET    6   T 8 ILE F 269  ALA F 271  1  O  HIS F 270   N  VAL F 244           
SHEET    7   T 8 ILE F 294  THR F 299  1  O  LEU F 295   N  ILE F 269           
SHEET    8   T 8 MET F 357  SER F 359  1  O  SER F 359   N  SER F 298           
SHEET    1   U 5 GLY F 131  HIS F 137  0                                        
SHEET    2   U 5 VAL F 152  GLY F 158  1  O  PHE F 156   N  ASP F 133           
SHEET    3   U 5 ASN F 191  LYS F 197  1  O  ASN F 191   N  MET F 155           
SHEET    4   U 5 ILE F 490  VAL F 493  1  O  PHE F 492   N  VAL F 192           
SHEET    5   U 5 LYS F 511  PRO F 514  1  O  LYS F 511   N  THR F 491           
SHEET    1   V 3 ILE F 535  VAL F 537  0                                        
SHEET    2   V 3 VAL F 544  VAL F 546 -1  O  PHE F 545   N  THR F 536           
SHEET    3   V 3 LYS F 549  CYS F 551 -1  O  CYS F 551   N  VAL F 544           
SHEET    1   W 2 ASP G  80  PHE G  87  0                                        
SHEET    2   W 2 GLY G  90  ASN G  97 -1  O  VAL G  96   N  LEU G  81           
SHEET    1   X 3 ILE G 110  LYS G 111  0                                        
SHEET    2   X 3 LYS I  19  ARG I  21 -1  O  LYS I  19   N  LYS G 111           
SHEET    3   X 3 TRP I  28  GLU I  30 -1  O  ALA I  29   N  VAL I  20           
SHEET    1   Y 2 ILE G 118  GLU G 119  0                                        
SHEET    2   Y 2 LYS I   2  MET I   3 -1  O  MET I   3   N  ILE G 118           
SHEET    1   Z 4 LEU G 154  GLU G 155  0                                        
SHEET    2   Z 4 THR G 127  ASN G 133 -1  N  THR G 132   O  GLU G 155           
SHEET    3   Z 4 THR G 181  PRO G 188 -1  O  VAL G 184   N  LEU G 129           
SHEET    4   Z 4 LYS G 164  LEU G 166 -1  N  ARG G 165   O  ILE G 187           
SHEET    1  AA 2 LEU G 139  GLY G 142  0                                        
SHEET    2  AA 2 THR G 173  ILE G 176 -1  O  ILE G 176   N  LEU G 139           
SHEET    1  AB 2 LYS G 194  ILE G 196  0                                        
SHEET    2  AB 2 GLY G 204  ILE G 205 -1  O  GLY G 204   N  ILE G 196           
SHEET    1  AC 4 LYS I  91  GLY I  96  0                                        
SHEET    2  AC 4 GLY I  79  LYS I  88 -1  N  GLY I  86   O  GLY I  94           
SHEET    3  AC 4 LEU I  67  ASP I  76 -1  N  ILE I  69   O  ILE I  85           
SHEET    4  AC 4 GLU I 118  ALA I 121  1  O  LEU I 120   N  VAL I  68           
SHEET    1  AD 8 LYS I  91  GLY I  96  0                                        
SHEET    2  AD 8 GLY I  79  LYS I  88 -1  N  GLY I  86   O  GLY I  94           
SHEET    3  AD 8 LEU I  67  ASP I  76 -1  N  ILE I  69   O  ILE I  85           
SHEET    4  AD 8 ILE I 126  ALA I 129  1  O  ILE I 127   N  LEU I  73           
SHEET    5  AD 8 LEU I 433  TRP I 436 -1  O  TRP I 436   N  ILE I 126           
SHEET    6  AD 8 ILE I 447  LYS I 450 -1  O  ILE I 449   N  LEU I 433           
SHEET    7  AD 8 MET I 453  MET I 459 -1  O  MET I 453   N  LYS I 450           
SHEET    8  AD 8 TYR I 473  GLU I 476 -1  O  TYR I 473   N  MET I 459           
SHEET    1  AE 8 GLY I 131  HIS I 137  0                                        
SHEET    2  AE 8 VAL I 152  GLY I 158  1  O  THR I 154   N  ASP I 133           
SHEET    3  AE 8 ASN I 191  LYS I 197  1  O  ASN I 191   N  MET I 155           
SHEET    4  AE 8 GLY I 216  HIS I 220  1  O  KCX I 218   N  GLY I 196           
SHEET    5  AE 8 GLN I 243  HIS I 247  1  O  CYS I 245   N  LEU I 219           
SHEET    6  AE 8 ILE I 269  ALA I 271  1  O  HIS I 270   N  VAL I 244           
SHEET    7  AE 8 ILE I 294  THR I 299  1  O  LEU I 295   N  ILE I 269           
SHEET    8  AE 8 MET I 357  SER I 359  1  O  SER I 359   N  SER I 298           
SHEET    1  AF 5 GLY I 131  HIS I 137  0                                        
SHEET    2  AF 5 VAL I 152  GLY I 158  1  O  THR I 154   N  ASP I 133           
SHEET    3  AF 5 ASN I 191  LYS I 197  1  O  ASN I 191   N  MET I 155           
SHEET    4  AF 5 ILE I 490  VAL I 493  1  O  PHE I 492   N  VAL I 192           
SHEET    5  AF 5 LYS I 511  PRO I 514  1  O  LYS I 511   N  THR I 491           
SHEET    1  AG 3 ILE I 535  VAL I 537  0                                        
SHEET    2  AG 3 VAL I 544  VAL I 546 -1  O  PHE I 545   N  THR I 536           
SHEET    3  AG 3 LYS I 549  CYS I 551 -1  O  CYS I 551   N  VAL I 544           
SHEET    1  AH 2 ASP J  80  PHE J  87  0                                        
SHEET    2  AH 2 GLY J  90  ASN J  97 -1  O  VAL J  96   N  LEU J  81           
SHEET    1  AI 3 ILE J 110  LYS J 111  0                                        
SHEET    2  AI 3 LYS L  19  ARG L  21 -1  O  LYS L  19   N  LYS J 111           
SHEET    3  AI 3 TRP L  28  GLU L  30 -1  O  ALA L  29   N  VAL L  20           
SHEET    1  AJ 2 ILE J 118  GLU J 119  0                                        
SHEET    2  AJ 2 LYS L   2  MET L   3 -1  O  MET L   3   N  ILE J 118           
SHEET    1  AK 4 LEU J 154  GLU J 155  0                                        
SHEET    2  AK 4 THR J 127  ASN J 133 -1  N  THR J 132   O  GLU J 155           
SHEET    3  AK 4 THR J 181  PRO J 188 -1  O  VAL J 184   N  LEU J 129           
SHEET    4  AK 4 LYS J 164  LEU J 166 -1  N  ARG J 165   O  ILE J 187           
SHEET    1  AL 2 LEU J 139  GLY J 142  0                                        
SHEET    2  AL 2 THR J 173  ILE J 176 -1  O  ILE J 176   N  LEU J 139           
SHEET    1  AM 2 LYS J 194  ILE J 196  0                                        
SHEET    2  AM 2 GLY J 204  ILE J 205 -1  O  GLY J 204   N  ILE J 196           
SHEET    1  AN 4 LYS L  91  GLY L  96  0                                        
SHEET    2  AN 4 GLY L  79  LYS L  88 -1  N  GLY L  86   O  GLY L  94           
SHEET    3  AN 4 LEU L  67  ASP L  76 -1  N  ILE L  69   O  ILE L  85           
SHEET    4  AN 4 GLU L 118  ALA L 121  1  O  LEU L 120   N  VAL L  68           
SHEET    1  AO 8 LYS L  91  GLY L  96  0                                        
SHEET    2  AO 8 GLY L  79  LYS L  88 -1  N  GLY L  86   O  GLY L  94           
SHEET    3  AO 8 LEU L  67  ASP L  76 -1  N  ILE L  69   O  ILE L  85           
SHEET    4  AO 8 ILE L 126  ALA L 129  1  O  ILE L 127   N  LEU L  73           
SHEET    5  AO 8 LEU L 433  TRP L 436 -1  O  TRP L 436   N  ILE L 126           
SHEET    6  AO 8 ILE L 447  LYS L 450 -1  O  ILE L 449   N  LEU L 433           
SHEET    7  AO 8 MET L 453  MET L 459 -1  O  MET L 453   N  LYS L 450           
SHEET    8  AO 8 TYR L 473  GLU L 476 -1  O  TYR L 473   N  MET L 459           
SHEET    1  AP 8 GLY L 131  HIS L 137  0                                        
SHEET    2  AP 8 VAL L 152  GLY L 158  1  O  THR L 154   N  ASP L 133           
SHEET    3  AP 8 ASN L 191  LYS L 197  1  O  ASN L 191   N  MET L 155           
SHEET    4  AP 8 GLY L 216  HIS L 220  1  O  KCX L 218   N  GLY L 196           
SHEET    5  AP 8 GLN L 243  HIS L 247  1  O  HIS L 247   N  LEU L 219           
SHEET    6  AP 8 ILE L 269  ALA L 271  1  O  HIS L 270   N  VAL L 244           
SHEET    7  AP 8 ILE L 294  THR L 299  1  O  LEU L 295   N  ILE L 269           
SHEET    8  AP 8 MET L 357  SER L 359  1  O  SER L 359   N  SER L 298           
SHEET    1  AQ 5 GLY L 131  HIS L 137  0                                        
SHEET    2  AQ 5 VAL L 152  GLY L 158  1  O  THR L 154   N  ASP L 133           
SHEET    3  AQ 5 ASN L 191  LYS L 197  1  O  ASN L 191   N  MET L 155           
SHEET    4  AQ 5 ILE L 490  VAL L 493  1  O  PHE L 492   N  VAL L 192           
SHEET    5  AQ 5 LYS L 511  PRO L 514  1  O  LYS L 511   N  THR L 491           
SHEET    1  AR 3 ILE L 535  VAL L 537  0                                        
SHEET    2  AR 3 VAL L 544  VAL L 546 -1  O  PHE L 545   N  THR L 536           
SHEET    3  AR 3 LYS L 549  CYS L 551 -1  O  LYS L 549   N  VAL L 546           
SHEET    1  AS 2 ASP M  80  PHE M  87  0                                        
SHEET    2  AS 2 GLY M  90  ASN M  97 -1  O  VAL M  96   N  LEU M  81           
SHEET    1  AT 3 ILE M 110  LYS M 111  0                                        
SHEET    2  AT 3 LYS O  19  ARG O  21 -1  O  LYS O  19   N  LYS M 111           
SHEET    3  AT 3 TRP O  28  GLU O  30 -1  O  ALA O  29   N  VAL O  20           
SHEET    1  AU 2 ILE M 118  GLU M 119  0                                        
SHEET    2  AU 2 LYS O   2  MET O   3 -1  O  MET O   3   N  ILE M 118           
SHEET    1  AV 4 LEU M 154  GLU M 155  0                                        
SHEET    2  AV 4 THR M 127  ASN M 133 -1  N  THR M 132   O  GLU M 155           
SHEET    3  AV 4 THR M 181  PRO M 188 -1  O  VAL M 184   N  LEU M 129           
SHEET    4  AV 4 LYS M 164  LEU M 166 -1  N  ARG M 165   O  ILE M 187           
SHEET    1  AW 2 LEU M 139  GLY M 142  0                                        
SHEET    2  AW 2 THR M 173  ILE M 176 -1  O  ILE M 176   N  LEU M 139           
SHEET    1  AX 2 LYS M 194  ILE M 196  0                                        
SHEET    2  AX 2 GLY M 204  ILE M 205 -1  O  GLY M 204   N  ILE M 196           
SHEET    1  AY 4 LYS O  91  GLY O  96  0                                        
SHEET    2  AY 4 GLY O  79  LYS O  88 -1  N  GLY O  86   O  GLY O  94           
SHEET    3  AY 4 LEU O  67  ASP O  76 -1  N  ILE O  69   O  ILE O  85           
SHEET    4  AY 4 GLU O 118  ALA O 121  1  O  LEU O 120   N  VAL O  68           
SHEET    1  AZ 8 LYS O  91  GLY O  96  0                                        
SHEET    2  AZ 8 GLY O  79  LYS O  88 -1  N  GLY O  86   O  GLY O  94           
SHEET    3  AZ 8 LEU O  67  ASP O  76 -1  N  ILE O  69   O  ILE O  85           
SHEET    4  AZ 8 ILE O 126  ALA O 129  1  O  ILE O 127   N  LEU O  73           
SHEET    5  AZ 8 LEU O 433  TRP O 436 -1  O  TRP O 436   N  ILE O 126           
SHEET    6  AZ 8 ILE O 447  LYS O 450 -1  O  ILE O 449   N  LEU O 433           
SHEET    7  AZ 8 MET O 453  MET O 459 -1  O  MET O 453   N  LYS O 450           
SHEET    8  AZ 8 TYR O 473  GLU O 476 -1  O  TYR O 473   N  MET O 459           
SHEET    1  BA 8 GLY O 131  HIS O 137  0                                        
SHEET    2  BA 8 VAL O 152  GLY O 158  1  O  PHE O 156   N  THR O 136           
SHEET    3  BA 8 ASN O 191  LYS O 197  1  O  ASN O 191   N  MET O 155           
SHEET    4  BA 8 GLY O 216  HIS O 220  1  O  KCX O 218   N  GLY O 196           
SHEET    5  BA 8 GLN O 243  HIS O 247  1  O  CYS O 245   N  LEU O 219           
SHEET    6  BA 8 ILE O 269  ALA O 271  1  O  HIS O 270   N  VAL O 244           
SHEET    7  BA 8 ILE O 294  THR O 299  1  O  LEU O 295   N  ILE O 269           
SHEET    8  BA 8 MET O 357  SER O 359  1  O  SER O 359   N  SER O 298           
SHEET    1  BB 5 GLY O 131  HIS O 137  0                                        
SHEET    2  BB 5 VAL O 152  GLY O 158  1  O  PHE O 156   N  THR O 136           
SHEET    3  BB 5 ASN O 191  LYS O 197  1  O  ASN O 191   N  MET O 155           
SHEET    4  BB 5 ILE O 490  VAL O 493  1  O  PHE O 492   N  VAL O 192           
SHEET    5  BB 5 LYS O 511  PRO O 514  1  O  LYS O 511   N  THR O 491           
SHEET    1  BC 3 ILE O 535  VAL O 537  0                                        
SHEET    2  BC 3 VAL O 544  VAL O 546 -1  O  PHE O 545   N  THR O 536           
SHEET    3  BC 3 LYS O 549  CYS O 551 -1  O  CYS O 551   N  VAL O 544           
SHEET    1  BD 2 ASP P  80  PHE P  87  0                                        
SHEET    2  BD 2 GLY P  90  ASN P  97 -1  O  VAL P  96   N  LEU P  81           
SHEET    1  BE 3 ILE P 110  LYS P 111  0                                        
SHEET    2  BE 3 LYS R  19  ARG R  21 -1  O  LYS R  19   N  LYS P 111           
SHEET    3  BE 3 TRP R  28  GLU R  30 -1  O  ALA R  29   N  VAL R  20           
SHEET    1  BF 2 ILE P 118  GLU P 119  0                                        
SHEET    2  BF 2 LYS R   2  MET R   3 -1  O  MET R   3   N  ILE P 118           
SHEET    1  BG 4 LEU P 154  GLU P 155  0                                        
SHEET    2  BG 4 THR P 127  ASN P 133 -1  N  THR P 132   O  GLU P 155           
SHEET    3  BG 4 THR P 181  PRO P 188 -1  O  VAL P 184   N  LEU P 129           
SHEET    4  BG 4 LYS P 164  LEU P 166 -1  N  ARG P 165   O  ILE P 187           
SHEET    1  BH 2 LEU P 139  GLY P 142  0                                        
SHEET    2  BH 2 THR P 173  ILE P 176 -1  O  ILE P 176   N  LEU P 139           
SHEET    1  BI 2 LYS P 194  ILE P 196  0                                        
SHEET    2  BI 2 GLY P 204  ILE P 205 -1  O  GLY P 204   N  ILE P 196           
SHEET    1  BJ 4 LYS R  91  GLY R  96  0                                        
SHEET    2  BJ 4 GLY R  79  LYS R  88 -1  N  GLY R  86   O  GLY R  94           
SHEET    3  BJ 4 LEU R  67  ASP R  76 -1  N  ILE R  69   O  ILE R  85           
SHEET    4  BJ 4 GLU R 118  ALA R 121  1  O  LEU R 120   N  VAL R  68           
SHEET    1  BK 8 LYS R  91  GLY R  96  0                                        
SHEET    2  BK 8 GLY R  79  LYS R  88 -1  N  GLY R  86   O  GLY R  94           
SHEET    3  BK 8 LEU R  67  ASP R  76 -1  N  ILE R  69   O  ILE R  85           
SHEET    4  BK 8 ILE R 126  ALA R 129  1  O  ILE R 127   N  LEU R  73           
SHEET    5  BK 8 LEU R 433  TRP R 436 -1  O  TRP R 436   N  ILE R 126           
SHEET    6  BK 8 ILE R 447  LYS R 450 -1  O  ILE R 449   N  LEU R 433           
SHEET    7  BK 8 MET R 453  MET R 459 -1  O  MET R 453   N  LYS R 450           
SHEET    8  BK 8 TYR R 473  GLU R 476 -1  O  TYR R 473   N  MET R 459           
SHEET    1  BL 8 GLY R 131  HIS R 137  0                                        
SHEET    2  BL 8 VAL R 152  GLY R 158  1  O  PHE R 156   N  ASP R 133           
SHEET    3  BL 8 ASN R 191  LYS R 197  1  O  ASN R 191   N  MET R 155           
SHEET    4  BL 8 GLY R 216  HIS R 220  1  O  KCX R 218   N  GLY R 196           
SHEET    5  BL 8 GLN R 243  HIS R 247  1  O  HIS R 247   N  LEU R 219           
SHEET    6  BL 8 ILE R 269  ALA R 271  1  O  HIS R 270   N  VAL R 244           
SHEET    7  BL 8 ILE R 294  THR R 299  1  O  LEU R 295   N  ILE R 269           
SHEET    8  BL 8 MET R 357  SER R 359  1  O  SER R 359   N  SER R 298           
SHEET    1  BM 5 GLY R 131  HIS R 137  0                                        
SHEET    2  BM 5 VAL R 152  GLY R 158  1  O  PHE R 156   N  ASP R 133           
SHEET    3  BM 5 ASN R 191  LYS R 197  1  O  ASN R 191   N  MET R 155           
SHEET    4  BM 5 ILE R 490  VAL R 493  1  O  PHE R 492   N  VAL R 192           
SHEET    5  BM 5 LYS R 511  PRO R 514  1  O  LYS R 511   N  THR R 491           
SHEET    1  BN 3 ILE R 535  VAL R 537  0                                        
SHEET    2  BN 3 VAL R 544  VAL R 546 -1  O  PHE R 545   N  THR R 536           
SHEET    3  BN 3 LYS R 549  CYS R 551 -1  O  CYS R 551   N  VAL R 544           
LINK         C   PHE C 217                 N   KCX C 218     1555   1555  1.33  
LINK         C   KCX C 218                 N   LEU C 219     1555   1555  1.34  
LINK         C   PHE F 217                 N   KCX F 218     1555   1555  1.32  
LINK         C   KCX F 218                 N   LEU F 219     1555   1555  1.34  
LINK         C   PHE I 217                 N   KCX I 218     1555   1555  1.32  
LINK         C   KCX I 218                 N   LEU I 219     1555   1555  1.36  
LINK         C   PHE L 217                 N   KCX L 218     1555   1555  1.33  
LINK         C   KCX L 218                 N   LEU L 219     1555   1555  1.36  
LINK         C   PHE O 217                 N   KCX O 218     1555   1555  1.33  
LINK         C   KCX O 218                 N   LEU O 219     1555   1555  1.34  
LINK         C   PHE R 217                 N   KCX R 218     1555   1555  1.32  
LINK         C   KCX R 218                 N   LEU R 219     1555   1555  1.35  
LINK         OD1 ASP L 361                FE    FE L 775     1555   1555  1.90  
LINK         OD1 ASP C 361                FE    FE C 775     1555   1555  1.94  
LINK         OD1 ASP F 361                FE    FE F 775     1555   1555  1.95  
LINK         OD1 ASP R 361                FE    FE R 775     1555   1555  2.00  
LINK         OD1 ASP O 361                FE    FE O 775     1555   1555  2.03  
LINK         OQ2 KCX F 218                FE    FE F 775     1555   1555  2.03  
LINK         NE2 HIS L 137                FE    FE L 775     1555   1555  2.05  
LINK         NE2 HIS C 137                FE    FE C 775     1555   1555  2.07  
LINK         ND1 HIS R 247                FE    FE R 774     1555   1555  2.11  
LINK         NE2 HIS I 137                FE    FE I 775     1555   1555  2.13  
LINK         ND1 HIS I 247                FE    FE I 774     1555   1555  2.13  
LINK         OQ1 KCX L 218                FE    FE L 774     1555   1555  2.13  
LINK         OQ2 KCX I 218                FE    FE I 775     1555   1555  2.14  
LINK         NE2 HIS R 137                FE    FE R 775     1555   1555  2.16  
LINK         NE2 HIS F 137                FE    FE F 775     1555   1555  2.16  
LINK         ND1 HIS O 247                FE    FE O 774     1555   1555  2.17  
LINK         NE2 HIS I 135                FE    FE I 775     1555   1555  2.18  
LINK         NE2 HIS F 273                FE    FE F 774     1555   1555  2.18  
LINK         ND1 HIS L 247                FE    FE L 774     1555   1555  2.19  
LINK         NE2 HIS O 137                FE    FE O 775     1555   1555  2.19  
LINK         OQ2 KCX L 218                FE    FE L 775     1555   1555  2.19  
LINK         OQ1 KCX O 218                FE    FE O 774     1555   1555  2.20  
LINK         OQ1 KCX F 218                FE    FE F 774     1555   1555  2.21  
LINK         OD1 ASP I 361                FE    FE I 775     1555   1555  2.21  
LINK         NE2 HIS O 135                FE    FE O 775     1555   1555  2.22  
LINK         OQ1 KCX C 218                FE    FE C 774     1555   1555  2.23  
LINK         NE2 HIS C 273                FE    FE C 774     1555   1555  2.24  
LINK         NE2 HIS L 135                FE    FE L 775     1555   1555  2.24  
LINK         OQ1 KCX R 218                FE    FE R 774     1555   1555  2.25  
LINK         ND1 HIS F 247                FE    FE F 774     1555   1555  2.26  
LINK         NE2 HIS O 273                FE    FE O 774     1555   1555  2.27  
LINK         OQ2 KCX O 218                FE    FE O 775     1555   1555  2.28  
LINK         NE2 HIS I 273                FE    FE I 774     1555   1555  2.30  
LINK         OQ2 KCX R 218                FE    FE R 775     1555   1555  2.30  
LINK         NE2 HIS L 273                FE    FE L 774     1555   1555  2.30  
LINK         ND1 HIS C 247                FE    FE C 774     1555   1555  2.30  
LINK         OQ2 KCX C 218                FE    FE C 775     1555   1555  2.31  
LINK         OQ1 KCX I 218                FE    FE I 774     1555   1555  2.34  
LINK         NE2 HIS R 273                FE    FE R 774     1555   1555  2.36  
LINK         NE2 HIS F 135                FE    FE F 775     1555   1555  2.37  
LINK         NE2 HIS C 135                FE    FE C 775     1555   1555  2.45  
LINK         NE2 HIS R 135                FE    FE R 775     1555   1555  2.45  
LINK        FE    FE R 774                 O   HOH R 780     1555   1555  2.08  
LINK        FE    FE R 775                 O   HOH R 780     1555   1555  2.08  
LINK        FE    FE F 775                 O   HOH F 780     1555   1555  2.08  
LINK        FE    FE F 774                 O   HOH F 780     1555   1555  2.08  
LINK        FE    FE L 774                 O   HOH L 780     1555   1555  2.09  
LINK        FE    FE I 774                 O   HOH I 780     1555   1555  2.09  
LINK        FE    FE C 775                 O   HOH C 780     1555   1555  2.09  
LINK        FE    FE L 775                 O   HOH L 780     1555   1555  2.09  
LINK        FE    FE I 775                 O   HOH I 780     1555   1555  2.09  
LINK        FE    FE C 774                 O   HOH C 780     1555   1555  2.09  
LINK        FE    FE O 775                 O   HOH O 780     1555   1555  2.09  
LINK        FE    FE O 774                 O   HOH O 780     1555   1555  2.10  
LINK         C   FME A   1                 N   LYS A   2     1555   1555  1.37  
LINK         C   FME D   1                 N   LYS D   2     1555   1555  1.37  
LINK         C   FME G   1                 N   LYS G   2     1555   1555  1.37  
LINK         C   FME J   1                 N   LYS J   2     1555   1555  1.36  
LINK         C   FME M   1                 N   LYS M   2     1555   1555  1.37  
LINK         C   FME P   1                 N   LYS P   2     1555   1555  1.36  
CISPEP   1 SER C  282    PRO C  283          0         3.11                     
CISPEP   2 ILE C  303    PRO C  304          0        -3.68                     
CISPEP   3 GLN C  470    PRO C  471          0         1.31                     
CISPEP   4 SER F  282    PRO F  283          0         5.13                     
CISPEP   5 ILE F  303    PRO F  304          0        -3.42                     
CISPEP   6 GLN F  470    PRO F  471          0         0.90                     
CISPEP   7 SER I  282    PRO I  283          0         4.23                     
CISPEP   8 ILE I  303    PRO I  304          0        -3.88                     
CISPEP   9 GLN I  470    PRO I  471          0         0.83                     
CISPEP  10 SER L  282    PRO L  283          0         4.00                     
CISPEP  11 ILE L  303    PRO L  304          0        -3.54                     
CISPEP  12 GLN L  470    PRO L  471          0         0.51                     
CISPEP  13 SER O  282    PRO O  283          0         4.29                     
CISPEP  14 ILE O  303    PRO O  304          0        -3.28                     
CISPEP  15 GLN O  470    PRO O  471          0         1.77                     
CISPEP  16 SER R  282    PRO R  283          0         3.86                     
CISPEP  17 ILE R  303    PRO R  304          0        -3.07                     
CISPEP  18 GLN R  470    PRO R  471          0         0.75                     
SITE     1 AC1  7 KCX C 218  HIS C 220  HIS C 247  HIS C 273                    
SITE     2 AC1  7 GLY C 278   FE C 775  HOH C 780                               
SITE     1 AC2  6 HIS C 135  HIS C 137  KCX C 218  ASP C 361                    
SITE     2 AC2  6  FE C 774  HOH C 780                                          
SITE     1 AC3  6 KCX F 218  HIS F 220  HIS F 247  HIS F 273                    
SITE     2 AC3  6  FE F 775  HOH F 780                                          
SITE     1 AC4  6 HIS F 135  HIS F 137  KCX F 218  ASP F 361                    
SITE     2 AC4  6  FE F 774  HOH F 780                                          
SITE     1 AC5  7 KCX I 218  HIS I 220  HIS I 247  HIS I 273                    
SITE     2 AC5  7 GLY I 278   FE I 775  HOH I 780                               
SITE     1 AC6  6 HIS I 135  HIS I 137  KCX I 218  ASP I 361                    
SITE     2 AC6  6  FE I 774  HOH I 780                                          
SITE     1 AC7  6 KCX L 218  HIS L 220  HIS L 247  HIS L 273                    
SITE     2 AC7  6  FE L 775  HOH L 780                                          
SITE     1 AC8  6 HIS L 135  HIS L 137  KCX L 218  ASP L 361                    
SITE     2 AC8  6  FE L 774  HOH L 780                                          
SITE     1 AC9  7 KCX O 218  HIS O 220  HIS O 247  HIS O 273                    
SITE     2 AC9  7 GLY O 278   FE O 775  HOH O 780                               
SITE     1 BC1  6 HIS O 135  HIS O 137  KCX O 218  ASP O 361                    
SITE     2 BC1  6  FE O 774  HOH O 780                                          
SITE     1 BC2  7 KCX R 218  HIS R 220  HIS R 247  HIS R 273                    
SITE     2 BC2  7 GLY R 278   FE R 775  HOH R 780                               
SITE     1 BC3  6 HIS R 135  HIS R 137  KCX R 218  ASP R 361                    
SITE     2 BC3  6  FE R 774  HOH R 780                                          
CRYST1  166.980  223.940  395.870  90.00  90.00  90.00 I 2 2 2      48          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005989  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004465  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002526        0.00000                         
HETATM    1  N   FME A   1       2.580 -55.515 102.764  1.00 43.68           N  
ANISOU    1  N   FME A   1     5774   5130   5692   -128   -252    421       N  
HETATM    2  CN  FME A   1       1.779 -55.090 103.737  1.00 43.74           C  
ANISOU    2  CN  FME A   1     5801   5160   5657   -127   -237    375       C  
HETATM    3  O1  FME A   1       2.186 -54.821 104.873  1.00 44.04           O  
ANISOU    3  O1  FME A   1     5851   5231   5653   -124   -268    318       O  
HETATM    4  CA  FME A   1       2.095 -55.869 101.422  1.00 42.58           C  
ANISOU    4  CA  FME A   1     5628   4957   5594   -131   -217    486       C  
HETATM    5  CB  FME A   1       3.260 -56.330 100.533  1.00 44.01           C  
ANISOU    5  CB  FME A   1     5787   5120   5814   -131   -240    524       C  
HETATM    6  CG  FME A   1       4.146 -55.212 100.037  1.00 47.17           C  
ANISOU    6  CG  FME A   1     6140   5478   6302   -148   -248    492       C  
HETATM    7  SD  FME A   1       5.411 -55.795  98.861  1.00 50.40           S  
ANISOU    7  SD  FME A   1     6517   5872   6759   -153   -257    539       S  
HETATM    8  CE  FME A   1       4.490 -55.747  97.373  1.00 46.12           C  
ANISOU    8  CE  FME A   1     5988   5281   6254   -157   -203    603       C  
HETATM    9  C   FME A   1       1.045 -56.995 101.458  1.00 48.54           C  
ANISOU    9  C   FME A   1     6423   5741   6281   -130   -186    532       C  
HETATM   10  O   FME A   1       0.078 -56.944 100.688  1.00 48.86           O  
ANISOU   10  O   FME A   1     6453   5766   6344   -135   -147    556       O  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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