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Database: PDB
Entry: 4ZGX
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HEADER    OXIDOREDUCTASE                          24-APR-15   4ZGX              
TITLE     STRUCTURE OF ALDOSTERONE SYNTHASE (CYP11B2) IN COMPLEX WITH (+)-(R)-N-
TITLE    2 (4-(4-CHLORO-3-FLUOROPHENYL)-5,6,7,8-TETRAHYDROISOQUINOLIN-8-YL)     
TITLE    3 PROPIONAMIDE                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYTOCHROME P450 11B2, MITOCHONDRIAL;                       
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 FRAGMENT: UNP RESIDUES 24-503;                                       
COMPND   5 SYNONYM: ALDOSTERONE SYNTHASE,ALDOS,ALDOSTERONE-SYNTHESIZING ENZYME, 
COMPND   6 CYPXIB2,CYTOCHROME P-450ALDO,CYTOCHROME P-450C18,STEROID 18-         
COMPND   7 HYDROXYLASE;                                                         
COMPND   8 EC: 1.14.15.4,1.14.15.5;                                             
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CYP11B2;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYTOCHROME P450, CYP11B2, ALDOSTERONE SYNTHASE, OXIDOREDUCTASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.KUGLSTATTER,C.JOSEPH                                                
REVDAT   2   04-NOV-15 4ZGX    1       JRNL                                     
REVDAT   1   07-OCT-15 4ZGX    0                                                
JRNL        AUTH   R.E.MARTIN,J.D.AEBI,B.HORNSPERGER,H.J.KREBS,B.KUHN,          
JRNL        AUTH 2 A.KUGLSTATTER,A.M.ALKER,H.P.MARKI,S.MULLER,D.BURGER,         
JRNL        AUTH 3 G.OTTAVIANI,W.RIBOULET,P.VERRY,X.TAN,K.AMREIN,A.V.MAYWEG     
JRNL        TITL   DISCOVERY OF 4-ARYL-5,6,7,8-TETRAHYDROISOQUINOLINES AS       
JRNL        TITL 2 POTENT, SELECTIVE, AND ORALLY ACTIVE ALDOSTERONE SYNTHASE    
JRNL        TITL 3 (CYP11B2) INHIBITORS: IN VIVO EVALUATION IN RODENTS AND      
JRNL        TITL 4 CYNOMOLGUS MONKEYS.                                          
JRNL        REF    J.MED.CHEM.                   V.  58  8054 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26403853                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B00851                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.4                                        
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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 88.20                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 114945                         
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)  : 0.214                          
REMARK   3   R VALUE            (WORKING SET)  : 0.212                          
REMARK   3   FREE R VALUE                      : 0.255                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.010                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 5764                           
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) : 3.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.28                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.18                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 8553                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2236                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 8124                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2212                   
REMARK   3   BIN FREE R VALUE                        : 0.2678                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.02                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 429                      
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            : 45112                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 746                                     
REMARK   3   SOLVENT ATOMS            : 817                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 83.39                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.47420                                              
REMARK   3    B22 (A**2) : -3.66840                                             
REMARK   3    B33 (A**2) : 3.19420                                              
REMARK   3    B12 (A**2) : -1.81690                                             
REMARK   3    B13 (A**2) : 0.74960                                              
REMARK   3    B23 (A**2) : 3.11360                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.644               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.501               
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      : 0.873                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.826                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 47151  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 64156  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 16095  ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 1025   ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 6896   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 47151  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 0      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 5742   ; 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   : 51815  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.03                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.27                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.07                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|34 - A|503 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   58.0123  -58.4839  112.3090           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0561 T22:    0.1506                                    
REMARK   3     T33:    0.1223 T12:   -0.1954                                    
REMARK   3     T13:   -0.0317 T23:   -0.1470                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6774 L22:    1.1930                                    
REMARK   3     L33:    2.0961 L12:   -0.3587                                    
REMARK   3     L13:   -0.1827 L23:    0.4130                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0394 S12:    0.0439 S13:   -0.0137                     
REMARK   3     S21:   -0.0091 S22:    0.1195 S23:    0.0024                     
REMARK   3     S31:   -0.0753 S32:    0.2044 S33:   -0.1590                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|34 - B|503 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):    9.6821  -82.3047  174.4053           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1016 T22:    0.2261                                    
REMARK   3     T33:    0.0382 T12:   -0.1311                                    
REMARK   3     T13:   -0.0087 T23:    0.0038                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.9460 L22:    1.4680                                    
REMARK   3     L33:    3.2192 L12:   -0.1595                                    
REMARK   3     L13:   -0.8668 L23:    0.2413                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1871 S12:    0.2182 S13:    0.1971                     
REMARK   3     S21:   -0.0923 S22:    0.1160 S23:   -0.0801                     
REMARK   3     S31:   -0.1746 S32:   -0.2889 S33:   -0.3031                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|34 - C|503 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   26.4458  -21.3695  182.8422           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1518 T22:    0.1678                                    
REMARK   3     T33:    0.0820 T12:   -0.1732                                    
REMARK   3     T13:    0.0230 T23:   -0.0361                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4713 L22:    1.8270                                    
REMARK   3     L33:    2.6480 L12:   -0.8663                                    
REMARK   3     L13:    0.5196 L23:   -0.0570                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0296 S12:   -0.0677 S13:   -0.1817                     
REMARK   3     S21:    0.2704 S22:    0.1658 S23:    0.2082                     
REMARK   3     S31:   -0.0319 S32:   -0.2719 S33:   -0.1362                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|34 - D|503 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   41.2999 -118.4554  100.7419           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1723 T22:    0.2000                                    
REMARK   3     T33:    0.1903 T12:   -0.1640                                    
REMARK   3     T13:   -0.0391 T23:   -0.1851                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9452 L22:    0.9474                                    
REMARK   3     L33:    2.3270 L12:    0.2225                                    
REMARK   3     L13:    0.1638 L23:    0.8000                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0318 S12:    0.0974 S13:   -0.0527                     
REMARK   3     S21:    0.0615 S22:    0.1841 S23:   -0.0620                     
REMARK   3     S31:    0.1771 S32:    0.3330 S33:   -0.1524                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { E|34 - E|502 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   12.9822  -40.1055  133.9094           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0925 T22:    0.2813                                    
REMARK   3     T33:    0.0619 T12:   -0.2226                                    
REMARK   3     T13:    0.0260 T23:   -0.0930                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.8532 L22:    1.5375                                    
REMARK   3     L33:    1.3611 L12:   -0.6615                                    
REMARK   3     L13:    0.1473 L23:    0.5757                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1482 S12:   -0.1221 S13:    0.0280                     
REMARK   3     S21:    0.1178 S22:    0.0446 S23:   -0.0119                     
REMARK   3     S31:   -0.1347 S32:   -0.1235 S33:    0.1036                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { F|34 - F|503 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   14.6950  -49.4570   81.3633           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0526 T22:    0.4275                                    
REMARK   3     T33:    0.0932 T12:   -0.0951                                    
REMARK   3     T13:   -0.0257 T23:   -0.2162                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4433 L22:    0.7079                                    
REMARK   3     L33:    1.8430 L12:   -0.2413                                    
REMARK   3     L13:    0.1537 L23:    0.2847                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1540 S12:    0.4223 S13:   -0.0639                     
REMARK   3     S21:   -0.1534 S22:   -0.1416 S23:    0.0278                     
REMARK   3     S31:   -0.0895 S32:   -0.1508 S33:   -0.0124                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { G|34 - G|503 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   54.4207  -91.3667  201.9790           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1357 T22:    0.6764                                    
REMARK   3     T33:    0.1933 T12:   -0.2070                                    
REMARK   3     T13:   -0.0678 T23:   -0.2889                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.5390 L22:    1.1649                                    
REMARK   3     L33:    2.7024 L12:   -0.6896                                    
REMARK   3     L13:    0.6242 L23:   -0.1892                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0501 S12:    0.2046 S13:   -0.1825                     
REMARK   3     S21:    0.1599 S22:   -0.0017 S23:    0.0173                     
REMARK   3     S31:    0.0761 S32:    0.4686 S33:   -0.0484                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: { H|34 - H|503 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   69.8886  -39.3642  158.0409           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.3444 T22:    0.5639                                    
REMARK   3     T33:    0.2510 T12:   -0.0735                                    
REMARK   3     T13:   -0.0391 T23:   -0.3802                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.7269 L22:    1.1932                                    
REMARK   3     L33:    4.1046 L12:    0.0262                                    
REMARK   3     L13:   -0.4280 L23:    0.3038                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0562 S12:   -0.2134 S13:    0.0627                     
REMARK   3     S21:   -0.0376 S22:    0.3413 S23:   -0.1414                     
REMARK   3     S31:    0.0260 S32:    0.5418 S33:   -0.2851                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: { I|34 - I|503 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   53.3526 -100.5988  149.9130           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1761 T22:    0.4391                                    
REMARK   3     T33:    0.0403 T12:   -0.2465                                    
REMARK   3     T13:    0.0065 T23:   -0.0815                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1999 L22:    1.4906                                    
REMARK   3     L33:    3.9050 L12:   -0.5908                                    
REMARK   3     L13:   -0.2283 L23:    0.7451                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0291 S12:   -0.0748 S13:   -0.2156                     
REMARK   3     S21:   -0.0268 S22:    0.1301 S23:    0.0071                     
REMARK   3     S31:    0.4517 S32:    0.4040 S33:   -0.1592                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: { J|34 - J|503 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   71.8790  -29.8472  209.7608           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.5368 T22:    0.3579                                    
REMARK   3     T33:    0.0346 T12:   -0.0346                                    
REMARK   3     T13:    0.0018 T23:   -0.0672                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.6529 L22:    1.0727                                    
REMARK   3     L33:    3.4798 L12:   -0.0670                                    
REMARK   3     L13:    0.8565 L23:    0.9831                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2117 S12:    0.2086 S13:    0.1795                     
REMARK   3     S21:    0.0729 S22:    0.0036 S23:   -0.1237                     
REMARK   3     S31:   -0.2845 S32:    0.4805 S33:   -0.2152                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: { K|34 - K|503 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):    5.7773  -58.4702  222.5638           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0842 T22:    0.0800                                    
REMARK   3     T33:    0.0234 T12:   -0.0350                                    
REMARK   3     T13:   -0.0920 T23:   -0.0521                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.5662 L22:    0.9401                                    
REMARK   3     L33:    2.5913 L12:    0.0780                                    
REMARK   3     L13:    0.6788 L23:    0.8282                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0581 S12:    0.1719 S13:    0.1508                     
REMARK   3     S21:    0.0157 S22:   -0.0607 S23:    0.0492                     
REMARK   3     S31:   -0.2110 S32:   -0.2987 S33:    0.1188                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: { L|34 - L|502 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   -1.2524 -103.3244  129.1405           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1747 T22:    0.6660                                    
REMARK   3     T33:    0.2849 T12:   -0.0555                                    
REMARK   3     T13:   -0.0361 T23:   -0.3764                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.3954 L22:    0.8055                                    
REMARK   3     L33:    2.0328 L12:   -0.5758                                    
REMARK   3     L13:    0.5376 L23:    0.2223                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0691 S12:   -0.7289 S13:    0.1234                     
REMARK   3     S21:    0.0304 S22:   -0.0054 S23:    0.1267                     
REMARK   3     S31:   -0.2548 S32:   -0.4431 S33:    0.0745                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4ZGX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209260.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 115062                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 88.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 2.400                              
REMARK 200  R MERGE                    (I) : 0.13700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.25                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
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: UNPUBLISHED STRUCTURE                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM ACETATE, BIS-TRIS, PEG3350,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12                   
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 9                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 10                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 11                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 12                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     ALA A    29                                                      
REMARK 465     ARG A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     PRO A    32                                                      
REMARK 465     ARG A    33                                                      
REMARK 465     ARG A   432                                                      
REMARK 465     GLY A   433                                                      
REMARK 465     SER A   434                                                      
REMARK 465     GLY A   435                                                      
REMARK 465     ARG A   436                                                      
REMARK 465     GLY A   504                                                      
REMARK 465     GLY A   505                                                      
REMARK 465     ARG A   506                                                      
REMARK 465     HIS A   507                                                      
REMARK 465     HIS A   508                                                      
REMARK 465     HIS A   509                                                      
REMARK 465     HIS A   510                                                      
REMARK 465     HIS A   511                                                      
REMARK 465     HIS A   512                                                      
REMARK 465     MET B    24                                                      
REMARK 465     ALA B    25                                                      
REMARK 465     THR B    26                                                      
REMARK 465     LYS B    27                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     ALA B    29                                                      
REMARK 465     ARG B    30                                                      
REMARK 465     ALA B    31                                                      
REMARK 465     PRO B    32                                                      
REMARK 465     ARG B    33                                                      
REMARK 465     ARG B   432                                                      
REMARK 465     GLY B   433                                                      
REMARK 465     SER B   434                                                      
REMARK 465     GLY B   435                                                      
REMARK 465     ARG B   436                                                      
REMARK 465     GLY B   504                                                      
REMARK 465     GLY B   505                                                      
REMARK 465     ARG B   506                                                      
REMARK 465     HIS B   507                                                      
REMARK 465     HIS B   508                                                      
REMARK 465     HIS B   509                                                      
REMARK 465     HIS B   510                                                      
REMARK 465     HIS B   511                                                      
REMARK 465     HIS B   512                                                      
REMARK 465     MET C    24                                                      
REMARK 465     ALA C    25                                                      
REMARK 465     THR C    26                                                      
REMARK 465     LYS C    27                                                      
REMARK 465     ALA C    28                                                      
REMARK 465     ALA C    29                                                      
REMARK 465     ARG C    30                                                      
REMARK 465     ALA C    31                                                      
REMARK 465     PRO C    32                                                      
REMARK 465     ARG C    33                                                      
REMARK 465     ARG C   432                                                      
REMARK 465     GLY C   433                                                      
REMARK 465     SER C   434                                                      
REMARK 465     GLY C   435                                                      
REMARK 465     ARG C   436                                                      
REMARK 465     GLY C   504                                                      
REMARK 465     GLY C   505                                                      
REMARK 465     ARG C   506                                                      
REMARK 465     HIS C   507                                                      
REMARK 465     HIS C   508                                                      
REMARK 465     HIS C   509                                                      
REMARK 465     HIS C   510                                                      
REMARK 465     HIS C   511                                                      
REMARK 465     HIS C   512                                                      
REMARK 465     MET D    24                                                      
REMARK 465     ALA D    25                                                      
REMARK 465     THR D    26                                                      
REMARK 465     LYS D    27                                                      
REMARK 465     ALA D    28                                                      
REMARK 465     ALA D    29                                                      
REMARK 465     ARG D    30                                                      
REMARK 465     ALA D    31                                                      
REMARK 465     PRO D    32                                                      
REMARK 465     ARG D    33                                                      
REMARK 465     ARG D   432                                                      
REMARK 465     GLY D   433                                                      
REMARK 465     SER D   434                                                      
REMARK 465     GLY D   435                                                      
REMARK 465     ARG D   436                                                      
REMARK 465     GLY D   504                                                      
REMARK 465     GLY D   505                                                      
REMARK 465     ARG D   506                                                      
REMARK 465     HIS D   507                                                      
REMARK 465     HIS D   508                                                      
REMARK 465     HIS D   509                                                      
REMARK 465     HIS D   510                                                      
REMARK 465     HIS D   511                                                      
REMARK 465     HIS D   512                                                      
REMARK 465     MET E    24                                                      
REMARK 465     ALA E    25                                                      
REMARK 465     THR E    26                                                      
REMARK 465     LYS E    27                                                      
REMARK 465     ALA E    28                                                      
REMARK 465     ALA E    29                                                      
REMARK 465     ARG E    30                                                      
REMARK 465     ALA E    31                                                      
REMARK 465     PRO E    32                                                      
REMARK 465     ARG E    33                                                      
REMARK 465     LEU E    83                                                      
REMARK 465     GLY E    84                                                      
REMARK 465     GLY E    85                                                      
REMARK 465     ARG E   432                                                      
REMARK 465     GLY E   433                                                      
REMARK 465     SER E   434                                                      
REMARK 465     GLY E   435                                                      
REMARK 465     ARG E   436                                                      
REMARK 465     ASN E   437                                                      
REMARK 465     PHE E   438                                                      
REMARK 465     ASN E   503                                                      
REMARK 465     GLY E   504                                                      
REMARK 465     GLY E   505                                                      
REMARK 465     ARG E   506                                                      
REMARK 465     HIS E   507                                                      
REMARK 465     HIS E   508                                                      
REMARK 465     HIS E   509                                                      
REMARK 465     HIS E   510                                                      
REMARK 465     HIS E   511                                                      
REMARK 465     HIS E   512                                                      
REMARK 465     MET F    24                                                      
REMARK 465     ALA F    25                                                      
REMARK 465     THR F    26                                                      
REMARK 465     LYS F    27                                                      
REMARK 465     ALA F    28                                                      
REMARK 465     ALA F    29                                                      
REMARK 465     ARG F    30                                                      
REMARK 465     ALA F    31                                                      
REMARK 465     PRO F    32                                                      
REMARK 465     ARG F    33                                                      
REMARK 465     GLY F    84                                                      
REMARK 465     ARG F   432                                                      
REMARK 465     GLY F   433                                                      
REMARK 465     SER F   434                                                      
REMARK 465     GLY F   435                                                      
REMARK 465     ARG F   436                                                      
REMARK 465     GLY F   504                                                      
REMARK 465     GLY F   505                                                      
REMARK 465     ARG F   506                                                      
REMARK 465     HIS F   507                                                      
REMARK 465     HIS F   508                                                      
REMARK 465     HIS F   509                                                      
REMARK 465     HIS F   510                                                      
REMARK 465     HIS F   511                                                      
REMARK 465     HIS F   512                                                      
REMARK 465     MET G    24                                                      
REMARK 465     ALA G    25                                                      
REMARK 465     THR G    26                                                      
REMARK 465     LYS G    27                                                      
REMARK 465     ALA G    28                                                      
REMARK 465     ALA G    29                                                      
REMARK 465     ARG G    30                                                      
REMARK 465     ALA G    31                                                      
REMARK 465     PRO G    32                                                      
REMARK 465     ARG G    33                                                      
REMARK 465     ARG G   432                                                      
REMARK 465     GLY G   433                                                      
REMARK 465     SER G   434                                                      
REMARK 465     GLY G   435                                                      
REMARK 465     ARG G   436                                                      
REMARK 465     GLY G   504                                                      
REMARK 465     GLY G   505                                                      
REMARK 465     ARG G   506                                                      
REMARK 465     HIS G   507                                                      
REMARK 465     HIS G   508                                                      
REMARK 465     HIS G   509                                                      
REMARK 465     HIS G   510                                                      
REMARK 465     HIS G   511                                                      
REMARK 465     HIS G   512                                                      
REMARK 465     MET H    24                                                      
REMARK 465     ALA H    25                                                      
REMARK 465     THR H    26                                                      
REMARK 465     LYS H    27                                                      
REMARK 465     ALA H    28                                                      
REMARK 465     ALA H    29                                                      
REMARK 465     ARG H    30                                                      
REMARK 465     ALA H    31                                                      
REMARK 465     PRO H    32                                                      
REMARK 465     ARG H    33                                                      
REMARK 465     ARG H   432                                                      
REMARK 465     GLY H   433                                                      
REMARK 465     SER H   434                                                      
REMARK 465     GLY H   435                                                      
REMARK 465     ARG H   436                                                      
REMARK 465     GLY H   504                                                      
REMARK 465     GLY H   505                                                      
REMARK 465     ARG H   506                                                      
REMARK 465     HIS H   507                                                      
REMARK 465     HIS H   508                                                      
REMARK 465     HIS H   509                                                      
REMARK 465     HIS H   510                                                      
REMARK 465     HIS H   511                                                      
REMARK 465     HIS H   512                                                      
REMARK 465     MET I    24                                                      
REMARK 465     ALA I    25                                                      
REMARK 465     THR I    26                                                      
REMARK 465     LYS I    27                                                      
REMARK 465     ALA I    28                                                      
REMARK 465     ALA I    29                                                      
REMARK 465     ARG I    30                                                      
REMARK 465     ALA I    31                                                      
REMARK 465     PRO I    32                                                      
REMARK 465     ARG I    33                                                      
REMARK 465     ASN I    82                                                      
REMARK 465     LEU I    83                                                      
REMARK 465     GLY I    84                                                      
REMARK 465     GLY I    85                                                      
REMARK 465     ARG I   432                                                      
REMARK 465     GLY I   433                                                      
REMARK 465     SER I   434                                                      
REMARK 465     GLY I   435                                                      
REMARK 465     ARG I   436                                                      
REMARK 465     ASN I   437                                                      
REMARK 465     PHE I   438                                                      
REMARK 465     HIS I   439                                                      
REMARK 465     GLY I   504                                                      
REMARK 465     GLY I   505                                                      
REMARK 465     ARG I   506                                                      
REMARK 465     HIS I   507                                                      
REMARK 465     HIS I   508                                                      
REMARK 465     HIS I   509                                                      
REMARK 465     HIS I   510                                                      
REMARK 465     HIS I   511                                                      
REMARK 465     HIS I   512                                                      
REMARK 465     MET J    24                                                      
REMARK 465     ALA J    25                                                      
REMARK 465     THR J    26                                                      
REMARK 465     LYS J    27                                                      
REMARK 465     ALA J    28                                                      
REMARK 465     ALA J    29                                                      
REMARK 465     ARG J    30                                                      
REMARK 465     ALA J    31                                                      
REMARK 465     PRO J    32                                                      
REMARK 465     ARG J    33                                                      
REMARK 465     LEU J    83                                                      
REMARK 465     GLY J    84                                                      
REMARK 465     ARG J   432                                                      
REMARK 465     GLY J   433                                                      
REMARK 465     SER J   434                                                      
REMARK 465     GLY J   435                                                      
REMARK 465     ARG J   436                                                      
REMARK 465     GLY J   504                                                      
REMARK 465     GLY J   505                                                      
REMARK 465     ARG J   506                                                      
REMARK 465     HIS J   507                                                      
REMARK 465     HIS J   508                                                      
REMARK 465     HIS J   509                                                      
REMARK 465     HIS J   510                                                      
REMARK 465     HIS J   511                                                      
REMARK 465     HIS J   512                                                      
REMARK 465     MET K    24                                                      
REMARK 465     ALA K    25                                                      
REMARK 465     THR K    26                                                      
REMARK 465     LYS K    27                                                      
REMARK 465     ALA K    28                                                      
REMARK 465     ALA K    29                                                      
REMARK 465     ARG K    30                                                      
REMARK 465     ALA K    31                                                      
REMARK 465     PRO K    32                                                      
REMARK 465     ARG K    33                                                      
REMARK 465     GLY K    46                                                      
REMARK 465     ASN K    47                                                      
REMARK 465     ARG K    48                                                      
REMARK 465     TRP K    49                                                      
REMARK 465     ARG K   432                                                      
REMARK 465     GLY K   433                                                      
REMARK 465     SER K   434                                                      
REMARK 465     GLY K   435                                                      
REMARK 465     ARG K   436                                                      
REMARK 465     GLY K   504                                                      
REMARK 465     GLY K   505                                                      
REMARK 465     ARG K   506                                                      
REMARK 465     HIS K   507                                                      
REMARK 465     HIS K   508                                                      
REMARK 465     HIS K   509                                                      
REMARK 465     HIS K   510                                                      
REMARK 465     HIS K   511                                                      
REMARK 465     HIS K   512                                                      
REMARK 465     MET L    24                                                      
REMARK 465     ALA L    25                                                      
REMARK 465     THR L    26                                                      
REMARK 465     LYS L    27                                                      
REMARK 465     ALA L    28                                                      
REMARK 465     ALA L    29                                                      
REMARK 465     ARG L    30                                                      
REMARK 465     ALA L    31                                                      
REMARK 465     PRO L    32                                                      
REMARK 465     ARG L    33                                                      
REMARK 465     ARG L   432                                                      
REMARK 465     GLY L   433                                                      
REMARK 465     SER L   434                                                      
REMARK 465     GLY L   435                                                      
REMARK 465     ARG L   436                                                      
REMARK 465     ASN L   437                                                      
REMARK 465     PHE L   438                                                      
REMARK 465     ASN L   503                                                      
REMARK 465     GLY L   504                                                      
REMARK 465     GLY L   505                                                      
REMARK 465     ARG L   506                                                      
REMARK 465     HIS L   507                                                      
REMARK 465     HIS L   508                                                      
REMARK 465     HIS L   509                                                      
REMARK 465     HIS L   510                                                      
REMARK 465     HIS L   511                                                      
REMARK 465     HIS L   512                                                      
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    MET A  92       10.91   -150.30                                   
REMARK 500    SER A 105     -174.15     67.98                                   
REMARK 500    ALA A 414       22.82    -74.03                                   
REMARK 500    ARG A 419       62.15     62.67                                   
REMARK 500    VAL A 441       38.24   -146.11                                   
REMARK 500    CYS A 450      129.38    -23.22                                   
REMARK 500    PHE A 487      -53.91     71.30                                   
REMARK 500    HIS B  63       40.01    -94.28                                   
REMARK 500    ASN B  82       98.34    -69.38                                   
REMARK 500    MET B  92        7.70   -151.66                                   
REMARK 500    SER B 105     -171.48     67.81                                   
REMARK 500    LEU B 380      -60.34    -96.70                                   
REMARK 500    CYS B 450      131.10    -24.29                                   
REMARK 500    PHE B 487      -54.73     67.20                                   
REMARK 500    TYR C  61       58.59   -116.85                                   
REMARK 500    MET C  92        8.53   -150.12                                   
REMARK 500    SER C 105     -172.06     67.65                                   
REMARK 500    VAL C 316      -87.49    -82.57                                   
REMARK 500    LEU C 380      -64.52    -97.85                                   
REMARK 500    ARG C 419       76.38     58.15                                   
REMARK 500    VAL C 441       40.71   -149.33                                   
REMARK 500    CYS C 450      129.85    -24.24                                   
REMARK 500    PHE C 487      -54.41     72.04                                   
REMARK 500    ASN D  47     -144.60    -84.90                                   
REMARK 500    GLN D  59       63.79      2.34                                   
REMARK 500    SER D 105     -174.05     67.09                                   
REMARK 500    PHE D 239       57.52   -114.46                                   
REMARK 500    MET D 240      144.02   -179.02                                   
REMARK 500    CYS D 450      131.30    -25.31                                   
REMARK 500    PHE D 487      -54.47     70.18                                   
REMARK 500    ASN E  47     -148.56    -92.09                                   
REMARK 500    HIS E  63       35.98    -97.01                                   
REMARK 500    MET E  92        5.91   -150.58                                   
REMARK 500    SER E 105     -172.45     67.52                                   
REMARK 500    VAL E 316      -69.47    -92.06                                   
REMARK 500    LEU E 380      -66.02    -98.87                                   
REMARK 500    CYS E 450      130.02    -23.10                                   
REMARK 500    SER E 486       59.65   -140.74                                   
REMARK 500    PHE E 487      -48.08     72.96                                   
REMARK 500    GLU F  39       36.66    -83.27                                   
REMARK 500    ASN F  47     -166.49   -106.65                                   
REMARK 500    GLN F  59       48.86     75.08                                   
REMARK 500    SER F 105     -173.74     68.58                                   
REMARK 500    ASP F 430     -169.25   -172.99                                   
REMARK 500    CYS F 450      129.84    -26.63                                   
REMARK 500    SER F 486       57.00   -140.49                                   
REMARK 500    PHE F 487      -21.17     69.20                                   
REMARK 500    LEU F 489       93.13    -54.41                                   
REMARK 500    PRO G  45       21.95    -73.47                                   
REMARK 500    ARG G  57      -85.79    -56.79                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     116 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 777        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A 778        DISTANCE =  6.12 ANGSTROMS                       
REMARK 525    HOH A 779        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH A 780        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH A 781        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH A 782        DISTANCE =  6.95 ANGSTROMS                       
REMARK 525    HOH A 783        DISTANCE =  7.07 ANGSTROMS                       
REMARK 525    HOH A 784        DISTANCE =  7.32 ANGSTROMS                       
REMARK 525    HOH A 785        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH A 786        DISTANCE =  7.44 ANGSTROMS                       
REMARK 525    HOH A 787        DISTANCE =  7.55 ANGSTROMS                       
REMARK 525    HOH A 788        DISTANCE =  7.61 ANGSTROMS                       
REMARK 525    HOH A 789        DISTANCE =  7.61 ANGSTROMS                       
REMARK 525    HOH A 790        DISTANCE =  7.65 ANGSTROMS                       
REMARK 525    HOH A 791        DISTANCE =  7.67 ANGSTROMS                       
REMARK 525    HOH A 792        DISTANCE =  7.68 ANGSTROMS                       
REMARK 525    HOH A 793        DISTANCE =  7.72 ANGSTROMS                       
REMARK 525    HOH A 794        DISTANCE =  7.79 ANGSTROMS                       
REMARK 525    HOH A 795        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH A 796        DISTANCE =  8.08 ANGSTROMS                       
REMARK 525    HOH A 797        DISTANCE =  8.12 ANGSTROMS                       
REMARK 525    HOH A 798        DISTANCE =  8.56 ANGSTROMS                       
REMARK 525    HOH A 799        DISTANCE =  8.64 ANGSTROMS                       
REMARK 525    HOH A 800        DISTANCE =  8.72 ANGSTROMS                       
REMARK 525    HOH A 801        DISTANCE =  9.30 ANGSTROMS                       
REMARK 525    HOH A 802        DISTANCE =  9.34 ANGSTROMS                       
REMARK 525    HOH A 803        DISTANCE =  9.47 ANGSTROMS                       
REMARK 525    HOH A 804        DISTANCE =  9.69 ANGSTROMS                       
REMARK 525    HOH A 805        DISTANCE = 10.25 ANGSTROMS                       
REMARK 525    HOH A 806        DISTANCE = 10.42 ANGSTROMS                       
REMARK 525    HOH A 807        DISTANCE = 11.35 ANGSTROMS                       
REMARK 525    HOH A 808        DISTANCE = 12.27 ANGSTROMS                       
REMARK 525    HOH B 763        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH B 764        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH B 765        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH B 766        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH B 767        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH B 768        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH B 769        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH B 770        DISTANCE =  7.19 ANGSTROMS                       
REMARK 525    HOH B 771        DISTANCE =  7.91 ANGSTROMS                       
REMARK 525    HOH B 772        DISTANCE =  8.32 ANGSTROMS                       
REMARK 525    HOH B 773        DISTANCE =  8.44 ANGSTROMS                       
REMARK 525    HOH B 774        DISTANCE =  8.56 ANGSTROMS                       
REMARK 525    HOH B 775        DISTANCE =  8.73 ANGSTROMS                       
REMARK 525    HOH B 776        DISTANCE =  8.89 ANGSTROMS                       
REMARK 525    HOH B 777        DISTANCE =  8.89 ANGSTROMS                       
REMARK 525    HOH B 778        DISTANCE = 10.45 ANGSTROMS                       
REMARK 525    HOH B 779        DISTANCE = 10.56 ANGSTROMS                       
REMARK 525    HOH B 780        DISTANCE = 10.94 ANGSTROMS                       
REMARK 525    HOH B 781        DISTANCE = 11.99 ANGSTROMS                       
REMARK 525    HOH C 744        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH C 745        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH C 746        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH C 747        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH C 748        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH C 749        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH C 750        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH C 751        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH C 752        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH C 753        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH C 754        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH C 755        DISTANCE =  7.22 ANGSTROMS                       
REMARK 525    HOH C 756        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH C 757        DISTANCE =  7.48 ANGSTROMS                       
REMARK 525    HOH C 758        DISTANCE =  8.45 ANGSTROMS                       
REMARK 525    HOH C 759        DISTANCE =  9.04 ANGSTROMS                       
REMARK 525    HOH C 760        DISTANCE =  9.23 ANGSTROMS                       
REMARK 525    HOH C 761        DISTANCE = 10.29 ANGSTROMS                       
REMARK 525    HOH C 762        DISTANCE = 11.61 ANGSTROMS                       
REMARK 525    HOH C 763        DISTANCE = 12.00 ANGSTROMS                       
REMARK 525    HOH C 764        DISTANCE = 14.19 ANGSTROMS                       
REMARK 525    HOH D 762        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH D 763        DISTANCE =  6.36 ANGSTROMS                       
REMARK 525    HOH D 764        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH D 765        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH D 766        DISTANCE =  6.86 ANGSTROMS                       
REMARK 525    HOH D 767        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH D 768        DISTANCE =  7.14 ANGSTROMS                       
REMARK 525    HOH D 769        DISTANCE =  7.27 ANGSTROMS                       
REMARK 525    HOH D 770        DISTANCE =  7.30 ANGSTROMS                       
REMARK 525    HOH D 771        DISTANCE =  7.33 ANGSTROMS                       
REMARK 525    HOH D 772        DISTANCE =  7.43 ANGSTROMS                       
REMARK 525    HOH D 773        DISTANCE =  7.47 ANGSTROMS                       
REMARK 525    HOH D 774        DISTANCE =  7.47 ANGSTROMS                       
REMARK 525    HOH D 775        DISTANCE =  7.49 ANGSTROMS                       
REMARK 525    HOH D 776        DISTANCE =  7.49 ANGSTROMS                       
REMARK 525    HOH D 777        DISTANCE =  7.62 ANGSTROMS                       
REMARK 525    HOH D 778        DISTANCE =  7.68 ANGSTROMS                       
REMARK 525    HOH D 779        DISTANCE =  7.70 ANGSTROMS                       
REMARK 525    HOH D 780        DISTANCE =  7.79 ANGSTROMS                       
REMARK 525    HOH D 781        DISTANCE =  7.86 ANGSTROMS                       
REMARK 525    HOH D 782        DISTANCE =  7.87 ANGSTROMS                       
REMARK 525    HOH D 783        DISTANCE =  8.05 ANGSTROMS                       
REMARK 525    HOH D 784        DISTANCE =  8.13 ANGSTROMS                       
REMARK 525    HOH D 785        DISTANCE =  8.39 ANGSTROMS                       
REMARK 525    HOH D 786        DISTANCE =  8.46 ANGSTROMS                       
REMARK 525    HOH D 787        DISTANCE =  8.65 ANGSTROMS                       
REMARK 525    HOH D 788        DISTANCE =  8.73 ANGSTROMS                       
REMARK 525    HOH D 789        DISTANCE =  8.96 ANGSTROMS                       
REMARK 525    HOH D 790        DISTANCE =  9.18 ANGSTROMS                       
REMARK 525    HOH D 791        DISTANCE =  9.32 ANGSTROMS                       
REMARK 525    HOH D 792        DISTANCE =  9.57 ANGSTROMS                       
REMARK 525    HOH D 793        DISTANCE =  9.61 ANGSTROMS                       
REMARK 525    HOH D 794        DISTANCE =  9.70 ANGSTROMS                       
REMARK 525    HOH D 795        DISTANCE =  9.86 ANGSTROMS                       
REMARK 525    HOH D 796        DISTANCE = 10.16 ANGSTROMS                       
REMARK 525    HOH D 797        DISTANCE = 10.52 ANGSTROMS                       
REMARK 525    HOH D 798        DISTANCE = 10.73 ANGSTROMS                       
REMARK 525    HOH D 799        DISTANCE = 11.03 ANGSTROMS                       
REMARK 525    HOH D 800        DISTANCE = 12.27 ANGSTROMS                       
REMARK 525    HOH E 745        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH E 746        DISTANCE =  6.19 ANGSTROMS                       
REMARK 525    HOH E 747        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH E 748        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH E 749        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH E 750        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH E 751        DISTANCE =  6.79 ANGSTROMS                       
REMARK 525    HOH E 752        DISTANCE =  7.88 ANGSTROMS                       
REMARK 525    HOH E 753        DISTANCE =  8.83 ANGSTROMS                       
REMARK 525    HOH E 754        DISTANCE = 11.90 ANGSTROMS                       
REMARK 525    HOH F 763        DISTANCE =  6.46 ANGSTROMS                       
REMARK 525    HOH F 764        DISTANCE =  6.96 ANGSTROMS                       
REMARK 525    HOH F 765        DISTANCE =  6.98 ANGSTROMS                       
REMARK 525    HOH F 766        DISTANCE =  7.88 ANGSTROMS                       
REMARK 525    HOH F 767        DISTANCE =  7.99 ANGSTROMS                       
REMARK 525    HOH F 768        DISTANCE =  8.19 ANGSTROMS                       
REMARK 525    HOH F 769        DISTANCE =  8.19 ANGSTROMS                       
REMARK 525    HOH F 770        DISTANCE =  8.20 ANGSTROMS                       
REMARK 525    HOH F 771        DISTANCE =  8.41 ANGSTROMS                       
REMARK 525    HOH F 772        DISTANCE =  9.32 ANGSTROMS                       
REMARK 525    HOH F 773        DISTANCE =  9.35 ANGSTROMS                       
REMARK 525    HOH G 734        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH G 735        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH G 736        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH G 737        DISTANCE =  6.50 ANGSTROMS                       
REMARK 525    HOH G 738        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH G 739        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH G 740        DISTANCE =  6.83 ANGSTROMS                       
REMARK 525    HOH G 741        DISTANCE =  8.30 ANGSTROMS                       
REMARK 525    HOH G 742        DISTANCE =  8.51 ANGSTROMS                       
REMARK 525    HOH G 743        DISTANCE =  8.55 ANGSTROMS                       
REMARK 525    HOH G 744        DISTANCE =  8.77 ANGSTROMS                       
REMARK 525    HOH G 745        DISTANCE =  8.83 ANGSTROMS                       
REMARK 525    HOH H 752        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH H 753        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH H 754        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH H 755        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH H 756        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH H 757        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH H 758        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH H 759        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH H 760        DISTANCE =  7.42 ANGSTROMS                       
REMARK 525    HOH H 761        DISTANCE =  8.83 ANGSTROMS                       
REMARK 525    HOH H 762        DISTANCE =  8.90 ANGSTROMS                       
REMARK 525    HOH H 763        DISTANCE =  9.04 ANGSTROMS                       
REMARK 525    HOH H 764        DISTANCE =  9.47 ANGSTROMS                       
REMARK 525    HOH H 765        DISTANCE = 10.51 ANGSTROMS                       
REMARK 525    HOH H 766        DISTANCE = 11.82 ANGSTROMS                       
REMARK 525    HOH H 767        DISTANCE = 12.79 ANGSTROMS                       
REMARK 525    HOH H 768        DISTANCE = 13.01 ANGSTROMS                       
REMARK 525    HOH I 744        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH I 745        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH I 746        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH I 747        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH I 748        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH I 749        DISTANCE =  6.95 ANGSTROMS                       
REMARK 525    HOH I 750        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH I 751        DISTANCE =  7.75 ANGSTROMS                       
REMARK 525    HOH I 752        DISTANCE =  7.85 ANGSTROMS                       
REMARK 525    HOH I 753        DISTANCE =  8.34 ANGSTROMS                       
REMARK 525    HOH I 754        DISTANCE = 10.74 ANGSTROMS                       
REMARK 525    HOH J 739        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH J 740        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH J 741        DISTANCE =  7.17 ANGSTROMS                       
REMARK 525    HOH J 742        DISTANCE =  7.21 ANGSTROMS                       
REMARK 525    HOH J 743        DISTANCE =  7.27 ANGSTROMS                       
REMARK 525    HOH J 744        DISTANCE =  7.32 ANGSTROMS                       
REMARK 525    HOH J 745        DISTANCE =  7.93 ANGSTROMS                       
REMARK 525    HOH J 746        DISTANCE =  8.27 ANGSTROMS                       
REMARK 525    HOH J 747        DISTANCE =  9.17 ANGSTROMS                       
REMARK 525    HOH J 748        DISTANCE =  9.62 ANGSTROMS                       
REMARK 525    HOH J 749        DISTANCE = 10.95 ANGSTROMS                       
REMARK 525    HOH J 750        DISTANCE = 11.59 ANGSTROMS                       
REMARK 525    HOH K 743        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH K 744        DISTANCE =  6.60 ANGSTROMS                       
REMARK 525    HOH K 745        DISTANCE =  7.03 ANGSTROMS                       
REMARK 525    HOH K 746        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH K 747        DISTANCE =  7.42 ANGSTROMS                       
REMARK 525    HOH K 748        DISTANCE =  7.46 ANGSTROMS                       
REMARK 525    HOH K 749        DISTANCE =  7.83 ANGSTROMS                       
REMARK 525    HOH K 750        DISTANCE =  7.83 ANGSTROMS                       
REMARK 525    HOH K 751        DISTANCE =  8.42 ANGSTROMS                       
REMARK 525    HOH K 752        DISTANCE = 10.96 ANGSTROMS                       
REMARK 525    HOH K 753        DISTANCE = 11.79 ANGSTROMS                       
REMARK 525    HOH L 746        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH L 747        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH L 748        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH L 749        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH L 750        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH L 751        DISTANCE =  6.62 ANGSTROMS                       
REMARK 525    HOH L 752        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH L 753        DISTANCE =  7.02 ANGSTROMS                       
REMARK 525    HOH L 754        DISTANCE =  7.12 ANGSTROMS                       
REMARK 525    HOH L 755        DISTANCE =  7.21 ANGSTROMS                       
REMARK 525    HOH L 756        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH L 757        DISTANCE =  7.55 ANGSTROMS                       
REMARK 525    HOH L 758        DISTANCE =  7.57 ANGSTROMS                       
REMARK 525    HOH L 759        DISTANCE =  8.12 ANGSTROMS                       
REMARK 525    HOH L 760        DISTANCE =  8.13 ANGSTROMS                       
REMARK 525    HOH L 761        DISTANCE =  8.18 ANGSTROMS                       
REMARK 525    HOH L 762        DISTANCE =  8.28 ANGSTROMS                       
REMARK 525    HOH L 763        DISTANCE =  8.68 ANGSTROMS                       
REMARK 525    HOH L 764        DISTANCE =  9.06 ANGSTROMS                       
REMARK 525    HOH L 765        DISTANCE =  9.20 ANGSTROMS                       
REMARK 525    HOH L 766        DISTANCE = 10.35 ANGSTROMS                       
REMARK 525    HOH L 767        DISTANCE = 11.56 ANGSTROMS                       
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                             HEM A 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 450   SG                                                     
REMARK 620 2 HEM A 601   NA   85.2                                              
REMARK 620 3 HEM A 601   NB   82.2  88.3                                        
REMARK 620 4 HEM A 601   NC   83.4 168.5  90.8                                  
REMARK 620 5 HEM A 601   ND   85.7  89.1 167.8  89.4                            
REMARK 620 6 QHC A 602   N10 175.2  93.0  93.4  98.4  98.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 450   SG                                                     
REMARK 620 2 HEM B 601   NA   89.7                                              
REMARK 620 3 HEM B 601   NB   79.6  89.1                                        
REMARK 620 4 HEM B 601   NC   81.6 171.2  89.7                                  
REMARK 620 5 HEM B 601   ND   92.7  88.0 171.7  91.9                            
REMARK 620 6 QHC B 602   N10 162.6  87.6  83.2 100.9 104.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM C 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 450   SG                                                     
REMARK 620 2 HEM C 601   NA   91.6                                              
REMARK 620 3 HEM C 601   NB   78.4  87.5                                        
REMARK 620 4 HEM C 601   NC   84.3 174.8  88.6                                  
REMARK 620 5 HEM C 601   ND   97.3  89.6 174.8  94.0                            
REMARK 620 6 QHC C 602   N10 156.0  77.7  79.7 105.0 103.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM D 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D 450   SG                                                     
REMARK 620 2 HEM D 601   NA   90.1                                              
REMARK 620 3 HEM D 601   NB   83.3  90.2                                        
REMARK 620 4 HEM D 601   NC   80.8 170.6  90.9                                  
REMARK 620 5 HEM D 601   ND   87.7  88.1 170.8  89.4                            
REMARK 620 6 QHC D 602   N10 164.9  87.1  81.9 102.3 107.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS E 450   SG                                                     
REMARK 620 2 HEM E 601   NA   90.1                                              
REMARK 620 3 HEM E 601   NB   82.2  90.3                                        
REMARK 620 4 HEM E 601   NC   82.7 172.6  90.1                                  
REMARK 620 5 HEM E 601   ND   89.1  89.7 171.2  88.8                            
REMARK 620 6 QHC E 602   N10 175.2  88.5 102.4  98.7  86.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS F 450   SG                                                     
REMARK 620 2 HEM F 601   NA   90.8                                              
REMARK 620 3 HEM F 601   NB   85.8  88.5                                        
REMARK 620 4 HEM F 601   NC   83.2 174.0  91.5                                  
REMARK 620 5 HEM F 601   ND   85.9  86.2 170.1  92.9                            
REMARK 620 6 QHC F 602   N10 168.6  90.8  82.9  95.2 105.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM I 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS I 450   SG                                                     
REMARK 620 2 HEM I 601   NA   85.5                                              
REMARK 620 3 HEM I 601   NB   83.9  87.2                                        
REMARK 620 4 HEM I 601   NC   82.5 167.5  94.8                                  
REMARK 620 5 HEM I 601   ND   86.2  87.9 169.2  88.0                            
REMARK 620 6 QHC I 602   N10 178.1  93.7  94.4  98.5  95.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM K 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 450   SG                                                     
REMARK 620 2 HEM K 601   NA   91.7                                              
REMARK 620 3 HEM K 601   NB   87.6  86.7                                        
REMARK 620 4 HEM K 601   NC   85.3 176.6  91.8                                  
REMARK 620 5 HEM K 601   ND   95.8  88.4 174.1  93.3                            
REMARK 620 6 QHC K 602   N10 167.2  90.0  79.8  92.7  96.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM L 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS L 450   SG                                                     
REMARK 620 2 HEM L 601   NA   88.4                                              
REMARK 620 3 HEM L 601   NB   83.8  89.9                                        
REMARK 620 4 HEM L 601   NC   81.0 169.3  89.7                                  
REMARK 620 5 HEM L 601   ND   88.6  89.8 172.4  89.2                            
REMARK 620 6 QHC L 602   N10 162.3  97.2  79.4  93.2 108.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM J 601  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 QHC J 602   N10                                                    
REMARK 620 2 HEM J 601   NA   92.8                                              
REMARK 620 3 HEM J 601   NB   89.0  90.7                                        
REMARK 620 4 HEM J 601   NC   99.2 168.0  89.8                                  
REMARK 620 5 HEM J 601   ND  103.3  89.0 167.8  88.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue QHC A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue QHC B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM C 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue QHC C 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM D 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue QHC D 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue QHC E 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM F 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue QHC F 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM G 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM H 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM I 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue QHC I 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM J 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue QHC J 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM K 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue QHC K 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM L 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue QHC L 602                 
DBREF  4ZGX A   28   503  UNP    P19099   C11B2_HUMAN     28    503             
DBREF  4ZGX B   28   503  UNP    P19099   C11B2_HUMAN     28    503             
DBREF  4ZGX C   28   503  UNP    P19099   C11B2_HUMAN     28    503             
DBREF  4ZGX D   28   503  UNP    P19099   C11B2_HUMAN     28    503             
DBREF  4ZGX E   28   503  UNP    P19099   C11B2_HUMAN     28    503             
DBREF  4ZGX F   28   503  UNP    P19099   C11B2_HUMAN     28    503             
DBREF  4ZGX G   28   503  UNP    P19099   C11B2_HUMAN     28    503             
DBREF  4ZGX H   28   503  UNP    P19099   C11B2_HUMAN     28    503             
DBREF  4ZGX I   28   503  UNP    P19099   C11B2_HUMAN     28    503             
DBREF  4ZGX J   28   503  UNP    P19099   C11B2_HUMAN     28    503             
DBREF  4ZGX K   28   503  UNP    P19099   C11B2_HUMAN     28    503             
DBREF  4ZGX L   28   503  UNP    P19099   C11B2_HUMAN     28    503             
SEQADV 4ZGX MET A   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA A   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR A   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS A   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY A  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY A  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG A  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS A  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS A  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS A  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS A  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS A  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS A  512  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX MET B   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA B   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR B   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS B   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY B  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY B  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG B  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS B  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS B  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS B  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS B  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS B  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS B  512  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX MET C   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA C   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR C   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS C   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY C  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY C  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG C  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS C  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS C  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS C  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS C  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS C  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS C  512  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX MET D   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA D   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR D   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS D   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY D  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY D  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG D  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS D  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS D  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS D  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS D  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS D  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS D  512  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX MET E   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA E   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR E   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS E   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY E  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY E  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG E  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS E  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS E  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS E  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS E  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS E  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS E  512  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX MET F   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA F   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR F   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS F   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY F  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY F  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG F  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS F  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS F  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS F  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS F  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS F  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS F  512  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX MET G   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA G   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR G   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS G   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY G  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY G  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG G  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS G  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS G  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS G  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS G  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS G  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS G  512  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX MET H   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA H   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR H   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS H   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY H  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY H  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG H  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS H  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS H  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS H  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS H  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS H  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS H  512  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX MET I   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA I   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR I   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS I   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY I  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY I  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG I  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS I  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS I  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS I  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS I  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS I  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS I  512  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX MET J   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA J   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR J   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS J   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY J  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY J  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG J  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS J  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS J  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS J  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS J  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS J  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS J  512  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX MET K   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA K   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR K   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS K   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY K  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY K  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG K  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS K  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS K  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS K  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS K  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS K  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS K  512  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX MET L   24  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ALA L   25  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX THR L   26  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX LYS L   27  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY L  504  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX GLY L  505  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX ARG L  506  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS L  507  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS L  508  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS L  509  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS L  510  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS L  511  UNP  P19099              EXPRESSION TAG                 
SEQADV 4ZGX HIS L  512  UNP  P19099              EXPRESSION TAG                 
SEQRES   1 A  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 A  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 A  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 A  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 A  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 A  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 A  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 A  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 A  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 A  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 A  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 A  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 A  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 A  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 A  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 A  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 A  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 A  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 A  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 A  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 A  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 A  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 A  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 A  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 A  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 A  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 A  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 A  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 A  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 A  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 A  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 A  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 A  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 A  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 A  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 A  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 A  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 A  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 B  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 B  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 B  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 B  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 B  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 B  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 B  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 B  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 B  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 B  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 B  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 B  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 B  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 B  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 B  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 B  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 B  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 B  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 B  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 B  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 B  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 B  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 B  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 B  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 B  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 B  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 B  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 B  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 B  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 B  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 B  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 B  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 B  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 B  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 B  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 B  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 B  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
SEQRES   1 C  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 C  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 C  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 C  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 C  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 C  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 C  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 C  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 C  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 C  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 C  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 C  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 C  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 C  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 C  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 C  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 C  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 C  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 C  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 C  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 C  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 C  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 C  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 C  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 C  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 C  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 C  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 C  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 C  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 C  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 C  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 C  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 C  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 C  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 C  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 C  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 C  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 C  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
SEQRES   1 D  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 D  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 D  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 D  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 D  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 D  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 D  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 D  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 D  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 D  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 D  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 D  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 D  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 D  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 D  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 D  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 D  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 D  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 D  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 D  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 D  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 D  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 D  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 D  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 D  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 D  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 D  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 D  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 D  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 D  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 D  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 D  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 D  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 D  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 D  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 D  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 D  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 D  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
SEQRES   1 E  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 E  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 E  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 E  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 E  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 E  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 E  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 E  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 E  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 E  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 E  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 E  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 E  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 E  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 E  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 E  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 E  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 E  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 E  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 E  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 E  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 E  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 E  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 E  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 E  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 E  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 E  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 E  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 E  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 E  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 E  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 E  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 E  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 E  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 E  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 E  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 E  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 E  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
SEQRES   1 F  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 F  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 F  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 F  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 F  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 F  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 F  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 F  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 F  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 F  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 F  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 F  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 F  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 F  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 F  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 F  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 F  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 F  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 F  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 F  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 F  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 F  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 F  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 F  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 F  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 F  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 F  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 F  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 F  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 F  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 F  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 F  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 F  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 F  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 F  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 F  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 F  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 F  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
SEQRES   1 G  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 G  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 G  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 G  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 G  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 G  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 G  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 G  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 G  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 G  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 G  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 G  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 G  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 G  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 G  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 G  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 G  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 G  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 G  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 G  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 G  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 G  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 G  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 G  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 G  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 G  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 G  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 G  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 G  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 G  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 G  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 G  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 G  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 G  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 G  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 G  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 G  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 G  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
SEQRES   1 H  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 H  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 H  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 H  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 H  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 H  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 H  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 H  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 H  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 H  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 H  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 H  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 H  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 H  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 H  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 H  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 H  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 H  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 H  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 H  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 H  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 H  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 H  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 H  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 H  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 H  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 H  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 H  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 H  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 H  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 H  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 H  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 H  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 H  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 H  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 H  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 H  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 H  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
SEQRES   1 I  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 I  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 I  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 I  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 I  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 I  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 I  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 I  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 I  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 I  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 I  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 I  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 I  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 I  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 I  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 I  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 I  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 I  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 I  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 I  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 I  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 I  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 I  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 I  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 I  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 I  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 I  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 I  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 I  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 I  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 I  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 I  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 I  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 I  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 I  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 I  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 I  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 I  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
SEQRES   1 J  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 J  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 J  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 J  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 J  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 J  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 J  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 J  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 J  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 J  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 J  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 J  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 J  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 J  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 J  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 J  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 J  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 J  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 J  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 J  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 J  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 J  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 J  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 J  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 J  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 J  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 J  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 J  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 J  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 J  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 J  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 J  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 J  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 J  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 J  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 J  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 J  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 J  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
SEQRES   1 K  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 K  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 K  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 K  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 K  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 K  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 K  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 K  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 K  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 K  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 K  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 K  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 K  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 K  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 K  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 K  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 K  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 K  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 K  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 K  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 K  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 K  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 K  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 K  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 K  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 K  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 K  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 K  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 K  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 K  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 K  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 K  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 K  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 K  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 K  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 K  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 K  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 K  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
SEQRES   1 L  489  MET ALA THR LYS ALA ALA ARG ALA PRO ARG THR VAL LEU          
SEQRES   2 L  489  PRO PHE GLU ALA MET PRO GLN HIS PRO GLY ASN ARG TRP          
SEQRES   3 L  489  LEU ARG LEU LEU GLN ILE TRP ARG GLU GLN GLY TYR GLU          
SEQRES   4 L  489  HIS LEU HIS LEU GLU MET HIS GLN THR PHE GLN GLU LEU          
SEQRES   5 L  489  GLY PRO ILE PHE ARG TYR ASN LEU GLY GLY PRO ARG MET          
SEQRES   6 L  489  VAL CYS VAL MET LEU PRO GLU ASP VAL GLU LYS LEU GLN          
SEQRES   7 L  489  GLN VAL ASP SER LEU HIS PRO CYS ARG MET ILE LEU GLU          
SEQRES   8 L  489  PRO TRP VAL ALA TYR ARG GLN HIS ARG GLY HIS LYS CYS          
SEQRES   9 L  489  GLY VAL PHE LEU LEU ASN GLY PRO GLU TRP ARG PHE ASN          
SEQRES  10 L  489  ARG LEU ARG LEU ASN PRO ASP VAL LEU SER PRO LYS ALA          
SEQRES  11 L  489  VAL GLN ARG PHE LEU PRO MET VAL ASP ALA VAL ALA ARG          
SEQRES  12 L  489  ASP PHE SER GLN ALA LEU LYS LYS LYS VAL LEU GLN ASN          
SEQRES  13 L  489  ALA ARG GLY SER LEU THR LEU ASP VAL GLN PRO SER ILE          
SEQRES  14 L  489  PHE HIS TYR THR ILE GLU ALA SER ASN LEU ALA LEU PHE          
SEQRES  15 L  489  GLY GLU ARG LEU GLY LEU VAL GLY HIS SER PRO SER SER          
SEQRES  16 L  489  ALA SER LEU ASN PHE LEU HIS ALA LEU GLU VAL MET PHE          
SEQRES  17 L  489  LYS SER THR VAL GLN LEU MET PHE MET PRO ARG SER LEU          
SEQRES  18 L  489  SER ARG TRP ILE SER PRO LYS VAL TRP LYS GLU HIS PHE          
SEQRES  19 L  489  GLU ALA TRP ASP CYS ILE PHE GLN TYR GLY ASP ASN CYS          
SEQRES  20 L  489  ILE GLN LYS ILE TYR GLN GLU LEU ALA PHE ASN ARG PRO          
SEQRES  21 L  489  GLN HIS TYR THR GLY ILE VAL ALA GLU LEU LEU LEU LYS          
SEQRES  22 L  489  ALA GLU LEU SER LEU GLU ALA ILE LYS ALA ASN SER MET          
SEQRES  23 L  489  GLU LEU THR ALA GLY SER VAL ASP THR THR ALA PHE PRO          
SEQRES  24 L  489  LEU LEU MET THR LEU PHE GLU LEU ALA ARG ASN PRO ASP          
SEQRES  25 L  489  VAL GLN GLN ILE LEU ARG GLN GLU SER LEU ALA ALA ALA          
SEQRES  26 L  489  ALA SER ILE SER GLU HIS PRO GLN LYS ALA THR THR GLU          
SEQRES  27 L  489  LEU PRO LEU LEU ARG ALA ALA LEU LYS GLU THR LEU ARG          
SEQRES  28 L  489  LEU TYR PRO VAL GLY LEU PHE LEU GLU ARG VAL VAL SER          
SEQRES  29 L  489  SER ASP LEU VAL LEU GLN ASN TYR HIS ILE PRO ALA GLY          
SEQRES  30 L  489  THR LEU VAL GLN VAL PHE LEU TYR SER LEU GLY ARG ASN          
SEQRES  31 L  489  ALA ALA LEU PHE PRO ARG PRO GLU ARG TYR ASN PRO GLN          
SEQRES  32 L  489  ARG TRP LEU ASP ILE ARG GLY SER GLY ARG ASN PHE HIS          
SEQRES  33 L  489  HIS VAL PRO PHE GLY PHE GLY MET ARG GLN CYS LEU GLY          
SEQRES  34 L  489  ARG ARG LEU ALA GLU ALA GLU MET LEU LEU LEU LEU HIS          
SEQRES  35 L  489  HIS VAL LEU LYS HIS PHE LEU VAL GLU THR LEU THR GLN          
SEQRES  36 L  489  GLU ASP ILE LYS MET VAL TYR SER PHE ILE LEU ARG PRO          
SEQRES  37 L  489  GLY THR SER PRO LEU LEU THR PHE ARG ALA ILE ASN GLY          
SEQRES  38 L  489  GLY ARG HIS HIS HIS HIS HIS HIS                              
HET    HEM  A 601      43                                                       
HET    QHC  A 602      23                                                       
HET    HEM  B 601      43                                                       
HET    QHC  B 602      23                                                       
HET    HEM  C 601      43                                                       
HET    QHC  C 602      23                                                       
HET    HEM  D 601      43                                                       
HET    QHC  D 602      23                                                       
HET    HEM  E 601      43                                                       
HET    QHC  E 602      23                                                       
HET    HEM  F 601      43                                                       
HET    QHC  F 602      23                                                       
HET    HEM  G 601      43                                                       
HET    HEM  H 601      43                                                       
HET    HEM  I 601      43                                                       
HET    QHC  I 602      23                                                       
HET    HEM  J 601      43                                                       
HET    QHC  J 602      23                                                       
HET    HEM  K 601      43                                                       
HET    QHC  K 602      23                                                       
HET    HEM  L 601      43                                                       
HET    QHC  L 602      23                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     QHC N-[(8R)-4-(4-CHLORO-3-FLUOROPHENYL)-5,6,7,8-                     
HETNAM   2 QHC  TETRAHYDROISOQUINOLIN-8-YL]PROPANAMIDE                          
HETSYN     HEM HEME                                                             
FORMUL  13  HEM    12(C34 H32 FE N4 O4)                                         
FORMUL  14  QHC    10(C18 H18 CL F N2 O)                                        
FORMUL  35  HOH   *817(H2 O)                                                    
HELIX    1 AA1 PRO A   37  MET A   41  5                                   5    
HELIX    2 AA2 ASN A   47  GLN A   59  1                                  13    
HELIX    3 AA3 HIS A   63  GLY A   76  1                                  14    
HELIX    4 AA4 LEU A   93  VAL A  103  1                                  11    
HELIX    5 AA5 LEU A  113  GLY A  124  1                                  12    
HELIX    6 AA6 GLY A  134  LEU A  149  1                                  16    
HELIX    7 AA7 SER A  150  LEU A  177  1                                  28    
HELIX    8 AA8 VAL A  188  GLY A  206  1                                  19    
HELIX    9 AA9 SER A  217  PHE A  239  1                                  23    
HELIX   10 AB1 PRO A  241  SER A  249  1                                   9    
HELIX   11 AB2 SER A  249  ASN A  281  1                                  33    
HELIX   12 AB3 GLY A  288  ALA A  297  1                                  10    
HELIX   13 AB4 SER A  300  ASN A  333  1                                  34    
HELIX   14 AB5 ASN A  333  ALA A  347  1                                  15    
HELIX   15 AB6 ALA A  347  HIS A  354  1                                   8    
HELIX   16 AB7 LYS A  357  LEU A  362  1                                   6    
HELIX   17 AB8 LEU A  362  TYR A  376  1                                  15    
HELIX   18 AB9 LEU A  407  GLY A  411  1                                   5    
HELIX   19 AC1 ASN A  424  ASP A  430  5                                   7    
HELIX   20 AC2 PHE A  445  GLN A  449  5                                   5    
HELIX   21 AC3 GLY A  452  HIS A  470  1                                  19    
HELIX   22 AC4 PRO B   37  MET B   41  5                                   5    
HELIX   23 AC5 ASN B   47  GLN B   59  1                                  13    
HELIX   24 AC6 HIS B   63  GLY B   76  1                                  14    
HELIX   25 AC7 LEU B   93  VAL B  103  1                                  11    
HELIX   26 AC8 LEU B  113  GLY B  124  1                                  12    
HELIX   27 AC9 GLY B  134  LEU B  149  1                                  16    
HELIX   28 AD1 SER B  150  LEU B  177  1                                  28    
HELIX   29 AD2 VAL B  188  GLY B  206  1                                  19    
HELIX   30 AD3 SER B  217  PHE B  239  1                                  23    
HELIX   31 AD4 PRO B  241  SER B  249  1                                   9    
HELIX   32 AD5 SER B  249  ASN B  281  1                                  33    
HELIX   33 AD6 GLY B  288  ALA B  297  1                                  10    
HELIX   34 AD7 SER B  300  GLY B  314  1                                  15    
HELIX   35 AD8 VAL B  316  ASN B  333  1                                  18    
HELIX   36 AD9 ASN B  333  HIS B  354  1                                  22    
HELIX   37 AE1 LYS B  357  LEU B  362  1                                   6    
HELIX   38 AE2 LEU B  362  TYR B  376  1                                  15    
HELIX   39 AE3 LEU B  407  GLY B  411  1                                   5    
HELIX   40 AE4 ASN B  424  ASP B  430  5                                   7    
HELIX   41 AE5 PHE B  445  GLN B  449  5                                   5    
HELIX   42 AE6 GLY B  452  HIS B  470  1                                  19    
HELIX   43 AE7 PRO C   37  MET C   41  5                                   5    
HELIX   44 AE8 ARG C   48  GLU C   58  1                                  11    
HELIX   45 AE9 HIS C   63  GLY C   76  1                                  14    
HELIX   46 AF1 LEU C   93  VAL C  103  1                                  11    
HELIX   47 AF2 LEU C  113  GLY C  124  1                                  12    
HELIX   48 AF3 GLY C  134  LEU C  149  1                                  16    
HELIX   49 AF4 SER C  150  LEU C  177  1                                  28    
HELIX   50 AF5 VAL C  188  GLY C  206  1                                  19    
HELIX   51 AF6 SER C  217  PHE C  239  1                                  23    
HELIX   52 AF7 PRO C  241  SER C  249  1                                   9    
HELIX   53 AF8 SER C  249  ASN C  281  1                                  33    
HELIX   54 AF9 GLY C  288  ALA C  297  1                                  10    
HELIX   55 AG1 SER C  300  GLY C  314  1                                  15    
HELIX   56 AG2 VAL C  316  ASN C  333  1                                  18    
HELIX   57 AG3 ASN C  333  HIS C  354  1                                  22    
HELIX   58 AG4 PRO C  355  THR C  359  5                                   5    
HELIX   59 AG5 LEU C  362  TYR C  376  1                                  15    
HELIX   60 AG6 LEU C  407  ASN C  413  1                                   7    
HELIX   61 AG7 ASN C  424  ASP C  430  5                                   7    
HELIX   62 AG8 PHE C  445  GLN C  449  5                                   5    
HELIX   63 AG9 GLY C  452  HIS C  470  1                                  19    
HELIX   64 AH1 PRO D   37  MET D   41  5                                   5    
HELIX   65 AH2 ARG D   48  GLU D   58  1                                  11    
HELIX   66 AH3 HIS D   63  GLY D   76  1                                  14    
HELIX   67 AH4 LEU D   93  GLN D  102  1                                  10    
HELIX   68 AH5 LEU D  113  GLY D  124  1                                  12    
HELIX   69 AH6 GLY D  134  LEU D  149  1                                  16    
HELIX   70 AH7 SER D  150  LEU D  177  1                                  28    
HELIX   71 AH8 VAL D  188  GLY D  206  1                                  19    
HELIX   72 AH9 SER D  217  PHE D  239  1                                  23    
HELIX   73 AI1 PRO D  241  SER D  249  1                                   9    
HELIX   74 AI2 SER D  249  ASN D  281  1                                  33    
HELIX   75 AI3 GLY D  288  ALA D  297  1                                  10    
HELIX   76 AI4 SER D  300  GLY D  314  1                                  15    
HELIX   77 AI5 VAL D  316  ASN D  333  1                                  18    
HELIX   78 AI6 ASN D  333  ALA D  347  1                                  15    
HELIX   79 AI7 ALA D  347  HIS D  354  1                                   8    
HELIX   80 AI8 PRO D  355  THR D  359  5                                   5    
HELIX   81 AI9 LEU D  362  TYR D  376  1                                  15    
HELIX   82 AJ1 LEU D  407  GLY D  411  1                                   5    
HELIX   83 AJ2 GLN D  426  ILE D  431  1                                   6    
HELIX   84 AJ3 PHE D  445  GLN D  449  5                                   5    
HELIX   85 AJ4 GLY D  452  HIS D  470  1                                  19    
HELIX   86 AJ5 PRO E   37  MET E   41  5                                   5    
HELIX   87 AJ6 LEU E   53  GLN E   59  1                                   7    
HELIX   88 AJ7 HIS E   63  GLY E   76  1                                  14    
HELIX   89 AJ8 LEU E   93  VAL E  103  1                                  11    
HELIX   90 AJ9 LEU E  113  ARG E  123  1                                  11    
HELIX   91 AK1 GLY E  134  LEU E  149  1                                  16    
HELIX   92 AK2 SER E  150  LEU E  177  1                                  28    
HELIX   93 AK3 VAL E  188  GLY E  206  1                                  19    
HELIX   94 AK4 SER E  217  PHE E  239  1                                  23    
HELIX   95 AK5 PRO E  241  SER E  249  1                                   9    
HELIX   96 AK6 SER E  249  ASN E  281  1                                  33    
HELIX   97 AK7 GLY E  288  ALA E  297  1                                  10    
HELIX   98 AK8 SER E  300  GLY E  314  1                                  15    
HELIX   99 AK9 VAL E  316  ASN E  333  1                                  18    
HELIX  100 AL1 ASN E  333  HIS E  354  1                                  22    
HELIX  101 AL2 LYS E  357  LEU E  362  1                                   6    
HELIX  102 AL3 LEU E  362  TYR E  376  1                                  15    
HELIX  103 AL4 LEU E  407  GLY E  411  1                                   5    
HELIX  104 AL5 ASN E  424  LEU E  429  5                                   6    
HELIX  105 AL6 PHE E  445  GLN E  449  5                                   5    
HELIX  106 AL7 GLY E  452  HIS E  470  1                                  19    
HELIX  107 AL8 PRO F   37  MET F   41  5                                   5    
HELIX  108 AL9 ARG F   48  GLN F   54  1                                   7    
HELIX  109 AM1 GLN F   54  GLN F   59  1                                   6    
HELIX  110 AM2 HIS F   63  GLY F   76  1                                  14    
HELIX  111 AM3 LEU F   93  GLN F  102  1                                  10    
HELIX  112 AM4 LEU F  113  GLY F  124  1                                  12    
HELIX  113 AM5 GLY F  134  LEU F  149  1                                  16    
HELIX  114 AM6 SER F  150  LEU F  177  1                                  28    
HELIX  115 AM7 VAL F  188  GLY F  206  1                                  19    
HELIX  116 AM8 SER F  217  PHE F  239  1                                  23    
HELIX  117 AM9 PRO F  241  SER F  249  1                                   9    
HELIX  118 AN1 SER F  249  ASN F  281  1                                  33    
HELIX  119 AN2 GLY F  288  ALA F  297  1                                  10    
HELIX  120 AN3 SER F  300  GLY F  314  1                                  15    
HELIX  121 AN4 VAL F  316  ASN F  333  1                                  18    
HELIX  122 AN5 ASN F  333  ALA F  347  1                                  15    
HELIX  123 AN6 ALA F  347  HIS F  354  1                                   8    
HELIX  124 AN7 LYS F  357  LEU F  362  1                                   6    
HELIX  125 AN8 LEU F  362  TYR F  376  1                                  15    
HELIX  126 AN9 LEU F  407  GLY F  411  1                                   5    
HELIX  127 AO1 ASN F  424  ASP F  430  5                                   7    
HELIX  128 AO2 PHE F  445  GLN F  449  5                                   5    
HELIX  129 AO3 GLY F  452  HIS F  470  1                                  19    
HELIX  130 AO4 PRO G   37  MET G   41  5                                   5    
HELIX  131 AO5 ARG G   48  GLU G   58  1                                  11    
HELIX  132 AO6 HIS G   63  GLY G   76  1                                  14    
HELIX  133 AO7 LEU G   93  GLN G  102  1                                  10    
HELIX  134 AO8 LEU G  113  GLY G  124  1                                  12    
HELIX  135 AO9 GLY G  128  LEU G  132  5                                   5    
HELIX  136 AP1 GLY G  134  LEU G  149  1                                  16    
HELIX  137 AP2 SER G  150  LEU G  177  1                                  28    
HELIX  138 AP3 VAL G  188  GLY G  206  1                                  19    
HELIX  139 AP4 SER G  217  MET G  238  1                                  22    
HELIX  140 AP5 ARG G  242  SER G  249  1                                   8    
HELIX  141 AP6 SER G  249  ASN G  281  1                                  33    
HELIX  142 AP7 GLY G  288  ALA G  297  1                                  10    
HELIX  143 AP8 SER G  300  GLY G  314  1                                  15    
HELIX  144 AP9 VAL G  316  ASN G  333  1                                  18    
HELIX  145 AQ1 ASN G  333  HIS G  354  1                                  22    
HELIX  146 AQ2 LYS G  357  LEU G  362  1                                   6    
HELIX  147 AQ3 LEU G  362  TYR G  376  1                                  15    
HELIX  148 AQ4 LEU G  407  ARG G  412  1                                   6    
HELIX  149 AQ5 PHE G  445  GLN G  449  5                                   5    
HELIX  150 AQ6 GLY G  452  HIS G  470  1                                  19    
HELIX  151 AQ7 PRO H   37  MET H   41  5                                   5    
HELIX  152 AQ8 ARG H   48  GLU H   58  1                                  11    
HELIX  153 AQ9 HIS H   63  GLY H   76  1                                  14    
HELIX  154 AR1 LEU H   93  GLN H  102  1                                  10    
HELIX  155 AR2 LEU H  113  GLY H  124  1                                  12    
HELIX  156 AR3 GLY H  134  LEU H  149  1                                  16    
HELIX  157 AR4 SER H  150  LEU H  177  1                                  28    
HELIX  158 AR5 VAL H  188  GLY H  206  1                                  19    
HELIX  159 AR6 SER H  217  PHE H  239  1                                  23    
HELIX  160 AR7 PRO H  241  SER H  249  1                                   9    
HELIX  161 AR8 SER H  249  ASN H  281  1                                  33    
HELIX  162 AR9 GLY H  288  ALA H  297  1                                  10    
HELIX  163 AS1 SER H  300  GLY H  314  1                                  15    
HELIX  164 AS2 VAL H  316  ASN H  333  1                                  18    
HELIX  165 AS3 ASN H  333  HIS H  354  1                                  22    
HELIX  166 AS4 LYS H  357  LEU H  362  1                                   6    
HELIX  167 AS5 LEU H  362  TYR H  376  1                                  15    
HELIX  168 AS6 LEU H  407  GLY H  411  1                                   5    
HELIX  169 AS7 ASN H  424  LEU H  429  5                                   6    
HELIX  170 AS8 PHE H  445  GLN H  449  5                                   5    
HELIX  171 AS9 GLY H  452  HIS H  470  1                                  19    
HELIX  172 AT1 ASN I   47  LEU I   52  1                                   6    
HELIX  173 AT2 LEU I   53  ILE I   55  5                                   3    
HELIX  174 AT3 HIS I   63  GLY I   76  1                                  14    
HELIX  175 AT4 LEU I   93  GLN I  102  1                                  10    
HELIX  176 AT5 LEU I  113  GLY I  124  1                                  12    
HELIX  177 AT6 GLY I  134  LEU I  149  1                                  16    
HELIX  178 AT7 SER I  150  LEU I  177  1                                  28    
HELIX  179 AT8 VAL I  188  GLY I  206  1                                  19    
HELIX  180 AT9 SER I  217  PHE I  239  1                                  23    
HELIX  181 AU1 PRO I  241  SER I  249  1                                   9    
HELIX  182 AU2 SER I  249  ASN I  281  1                                  33    
HELIX  183 AU3 GLY I  288  ALA I  297  1                                  10    
HELIX  184 AU4 SER I  300  GLY I  314  1                                  15    
HELIX  185 AU5 VAL I  316  ASN I  333  1                                  18    
HELIX  186 AU6 ASN I  333  HIS I  354  1                                  22    
HELIX  187 AU7 LYS I  357  LEU I  362  1                                   6    
HELIX  188 AU8 LEU I  362  TYR I  376  1                                  15    
HELIX  189 AU9 LEU I  407  GLY I  411  1                                   5    
HELIX  190 AV1 ASN I  424  ASP I  430  5                                   7    
HELIX  191 AV2 PHE I  445  GLN I  449  5                                   5    
HELIX  192 AV3 GLY I  452  HIS I  470  1                                  19    
HELIX  193 AV4 PRO J   37  MET J   41  5                                   5    
HELIX  194 AV5 GLN J   54  GLN J   59  1                                   6    
HELIX  195 AV6 HIS J   63  GLY J   76  1                                  14    
HELIX  196 AV7 LEU J   93  ASP J  104  1                                  12    
HELIX  197 AV8 LEU J  113  GLY J  124  1                                  12    
HELIX  198 AV9 GLY J  134  LEU J  149  1                                  16    
HELIX  199 AW1 SER J  150  LEU J  177  1                                  28    
HELIX  200 AW2 VAL J  188  GLY J  206  1                                  19    
HELIX  201 AW3 SER J  217  MET J  238  1                                  22    
HELIX  202 AW4 PRO J  241  SER J  249  1                                   9    
HELIX  203 AW5 SER J  249  ASN J  281  1                                  33    
HELIX  204 AW6 GLY J  288  ALA J  297  1                                  10    
HELIX  205 AW7 SER J  300  GLY J  314  1                                  15    
HELIX  206 AW8 VAL J  316  ASN J  333  1                                  18    
HELIX  207 AW9 ASN J  333  ALA J  347  1                                  15    
HELIX  208 AX1 ALA J  347  HIS J  354  1                                   8    
HELIX  209 AX2 LYS J  357  LEU J  362  1                                   6    
HELIX  210 AX3 LEU J  362  TYR J  376  1                                  15    
HELIX  211 AX4 LEU J  407  GLY J  411  1                                   5    
HELIX  212 AX5 PHE J  445  GLN J  449  5                                   5    
HELIX  213 AX6 GLY J  452  HIS J  470  1                                  19    
HELIX  214 AX7 PRO K   37  MET K   41  5                                   5    
HELIX  215 AX8 LEU K   52  GLN K   59  1                                   8    
HELIX  216 AX9 HIS K   63  GLY K   76  1                                  14    
HELIX  217 AY1 LEU K   93  VAL K  103  1                                  11    
HELIX  218 AY2 LEU K  113  GLY K  124  1                                  12    
HELIX  219 AY3 GLY K  134  LEU K  149  1                                  16    
HELIX  220 AY4 SER K  150  LEU K  177  1                                  28    
HELIX  221 AY5 VAL K  188  GLY K  206  1                                  19    
HELIX  222 AY6 SER K  217  PHE K  239  1                                  23    
HELIX  223 AY7 PRO K  241  SER K  249  1                                   9    
HELIX  224 AY8 SER K  249  ASN K  281  1                                  33    
HELIX  225 AY9 GLY K  288  ALA K  297  1                                  10    
HELIX  226 AZ1 SER K  300  GLY K  314  1                                  15    
HELIX  227 AZ2 VAL K  316  ASN K  333  1                                  18    
HELIX  228 AZ3 ASN K  333  HIS K  354  1                                  22    
HELIX  229 AZ4 PRO K  355  THR K  359  5                                   5    
HELIX  230 AZ5 LEU K  362  TYR K  376  1                                  15    
HELIX  231 AZ6 LEU K  407  GLY K  411  1                                   5    
HELIX  232 AZ7 ASN K  424  ASP K  430  5                                   7    
HELIX  233 AZ8 PHE K  445  GLN K  449  5                                   5    
HELIX  234 AZ9 GLY K  452  HIS K  470  1                                  19    
HELIX  235 BA1 PRO L   37  MET L   41  5                                   5    
HELIX  236 BA2 LEU L   52  GLU L   58  1                                   7    
HELIX  237 BA3 HIS L   63  GLY L   76  1                                  14    
HELIX  238 BA4 LEU L   93  VAL L  103  1                                  11    
HELIX  239 BA5 LEU L  113  GLY L  124  1                                  12    
HELIX  240 BA6 GLY L  134  LEU L  149  1                                  16    
HELIX  241 BA7 SER L  150  LEU L  177  1                                  28    
HELIX  242 BA8 VAL L  188  GLY L  206  1                                  19    
HELIX  243 BA9 SER L  217  PHE L  239  1                                  23    
HELIX  244 BB1 PRO L  241  TRP L  247  1                                   7    
HELIX  245 BB2 SER L  249  ASN L  281  1                                  33    
HELIX  246 BB3 GLY L  288  ALA L  297  1                                  10    
HELIX  247 BB4 SER L  300  GLY L  314  1                                  15    
HELIX  248 BB5 VAL L  316  ASN L  333  1                                  18    
HELIX  249 BB6 ASN L  333  HIS L  354  1                                  22    
HELIX  250 BB7 PRO L  355  THR L  359  5                                   5    
HELIX  251 BB8 LEU L  362  TYR L  376  1                                  15    
HELIX  252 BB9 LEU L  407  ARG L  412  1                                   6    
HELIX  253 BC1 ASN L  424  ASP L  430  5                                   7    
HELIX  254 BC2 PHE L  445  GLN L  449  5                                   5    
HELIX  255 BC3 GLY L  452  HIS L  470  1                                  19    
SHEET    1 AA1 4 ILE A  78  ARG A  80  0                                        
SHEET    2 AA1 4 MET A  88  VAL A  91 -1  O  CYS A  90   N  PHE A  79           
SHEET    3 AA1 4 LEU A 402  PHE A 406  1  O  LEU A 402   N  VAL A  89           
SHEET    4 AA1 4 PHE A 381  VAL A 385 -1  N  ARG A 384   O  VAL A 403           
SHEET    1 AA2 3 SER A 183  LEU A 186  0                                        
SHEET    2 AA2 3 LEU A 497  ALA A 501 -1  O  LEU A 497   N  LEU A 186           
SHEET    3 AA2 3 PHE A 471  GLU A 474 -1  N  GLU A 474   O  THR A 498           
SHEET    1 AA3 2 LEU A 390  LEU A 392  0                                        
SHEET    2 AA3 2 TYR A 395  ILE A 397 -1  O  ILE A 397   N  LEU A 390           
SHEET    1 AA4 2 MET A 483  TYR A 485  0                                        
SHEET    2 AA4 2 LEU A 489  PRO A 491 -1  O  ARG A 490   N  VAL A 484           
SHEET    1 AA5 4 ILE B  78  ASN B  82  0                                        
SHEET    2 AA5 4 ARG B  87  VAL B  91 -1  O  CYS B  90   N  PHE B  79           
SHEET    3 AA5 4 LEU B 402  PHE B 406  1  O  LEU B 402   N  VAL B  89           
SHEET    4 AA5 4 PHE B 381  VAL B 385 -1  N  ARG B 384   O  VAL B 403           
SHEET    1 AA6 3 SER B 183  LEU B 186  0                                        
SHEET    2 AA6 3 LEU B 497  ALA B 501 -1  O  PHE B 499   N  LEU B 184           
SHEET    3 AA6 3 PHE B 471  GLU B 474 -1  N  GLU B 474   O  THR B 498           
SHEET    1 AA7 2 LEU B 390  LEU B 392  0                                        
SHEET    2 AA7 2 TYR B 395  ILE B 397 -1  O  ILE B 397   N  LEU B 390           
SHEET    1 AA8 2 MET B 483  TYR B 485  0                                        
SHEET    2 AA8 2 LEU B 489  PRO B 491 -1  O  ARG B 490   N  VAL B 484           
SHEET    1 AA9 5 GLN C  43  ASN C  47  0                                        
SHEET    2 AA9 5 ILE C  78  ASN C  82  1  O  ARG C  80   N  HIS C  44           
SHEET    3 AA9 5 ARG C  87  VAL C  91 -1  O  CYS C  90   N  PHE C  79           
SHEET    4 AA9 5 LEU C 402  PHE C 406  1  O  GLN C 404   N  VAL C  89           
SHEET    5 AA9 5 PHE C 381  VAL C 385 -1  N  LEU C 382   O  VAL C 405           
SHEET    1 AB1 3 SER C 183  LEU C 186  0                                        
SHEET    2 AB1 3 LEU C 497  ALA C 501 -1  O  LEU C 497   N  LEU C 186           
SHEET    3 AB1 3 PHE C 471  GLU C 474 -1  N  GLU C 474   O  THR C 498           
SHEET    1 AB2 2 LEU C 390  LEU C 392  0                                        
SHEET    2 AB2 2 TYR C 395  ILE C 397 -1  O  ILE C 397   N  LEU C 390           
SHEET    1 AB3 2 MET C 483  TYR C 485  0                                        
SHEET    2 AB3 2 LEU C 489  PRO C 491 -1  O  ARG C 490   N  VAL C 484           
SHEET    1 AB4 4 ILE D  78  ASN D  82  0                                        
SHEET    2 AB4 4 ARG D  87  VAL D  91 -1  O  CYS D  90   N  PHE D  79           
SHEET    3 AB4 4 LEU D 402  PHE D 406  1  O  LEU D 402   N  VAL D  89           
SHEET    4 AB4 4 PHE D 381  VAL D 385 -1  N  ARG D 384   O  VAL D 403           
SHEET    1 AB5 3 SER D 183  LEU D 186  0                                        
SHEET    2 AB5 3 LEU D 497  ALA D 501 -1  O  PHE D 499   N  LEU D 184           
SHEET    3 AB5 3 PHE D 471  GLU D 474 -1  N  GLU D 474   O  THR D 498           
SHEET    1 AB6 2 LEU D 390  LEU D 392  0                                        
SHEET    2 AB6 2 TYR D 395  ILE D 397 -1  O  ILE D 397   N  LEU D 390           
SHEET    1 AB7 2 MET D 483  TYR D 485  0                                        
SHEET    2 AB7 2 LEU D 489  PRO D 491 -1  O  ARG D 490   N  VAL D 484           
SHEET    1 AB8 4 ILE E  78  TYR E  81  0                                        
SHEET    2 AB8 4 MET E  88  VAL E  91 -1  O  CYS E  90   N  PHE E  79           
SHEET    3 AB8 4 LEU E 402  PHE E 406  1  O  LEU E 402   N  VAL E  89           
SHEET    4 AB8 4 PHE E 381  VAL E 385 -1  N  ARG E 384   O  VAL E 403           
SHEET    1 AB9 3 SER E 183  LEU E 186  0                                        
SHEET    2 AB9 3 LEU E 497  ALA E 501 -1  O  PHE E 499   N  LEU E 184           
SHEET    3 AB9 3 PHE E 471  GLU E 474 -1  N  GLU E 474   O  THR E 498           
SHEET    1 AC1 2 LEU E 390  LEU E 392  0                                        
SHEET    2 AC1 2 TYR E 395  ILE E 397 -1  O  ILE E 397   N  LEU E 390           
SHEET    1 AC2 2 MET E 483  TYR E 485  0                                        
SHEET    2 AC2 2 LEU E 489  PRO E 491 -1  O  ARG E 490   N  VAL E 484           
SHEET    1 AC3 4 ILE F  78  TYR F  81  0                                        
SHEET    2 AC3 4 MET F  88  VAL F  91 -1  O  CYS F  90   N  PHE F  79           
SHEET    3 AC3 4 LEU F 402  PHE F 406  1  O  LEU F 402   N  VAL F  89           
SHEET    4 AC3 4 PHE F 381  VAL F 385 -1  N  ARG F 384   O  VAL F 403           
SHEET    1 AC4 3 SER F 183  ASP F 187  0                                        
SHEET    2 AC4 3 LEU F 496  ALA F 501 -1  O  PHE F 499   N  LEU F 184           
SHEET    3 AC4 3 PHE F 471  GLU F 474 -1  N  GLU F 474   O  THR F 498           
SHEET    1 AC5 2 LEU F 390  LEU F 392  0                                        
SHEET    2 AC5 2 TYR F 395  ILE F 397 -1  O  ILE F 397   N  LEU F 390           
SHEET    1 AC6 2 MET F 483  TYR F 485  0                                        
SHEET    2 AC6 2 LEU F 489  PRO F 491 -1  O  ARG F 490   N  VAL F 484           
SHEET    1 AC7 4 ILE G  78  ARG G  80  0                                        
SHEET    2 AC7 4 MET G  88  VAL G  91 -1  O  CYS G  90   N  PHE G  79           
SHEET    3 AC7 4 LEU G 402  PHE G 406  1  O  LEU G 402   N  VAL G  89           
SHEET    4 AC7 4 PHE G 381  VAL G 385 -1  N  ARG G 384   O  VAL G 403           
SHEET    1 AC8 3 SER G 183  LEU G 186  0                                        
SHEET    2 AC8 3 LEU G 497  ALA G 501 -1  O  PHE G 499   N  LEU G 184           
SHEET    3 AC8 3 PHE G 471  GLU G 474 -1  N  GLU G 474   O  THR G 498           
SHEET    1 AC9 2 LEU G 390  LEU G 392  0                                        
SHEET    2 AC9 2 TYR G 395  ILE G 397 -1  O  ILE G 397   N  LEU G 390           
SHEET    1 AD1 2 MET G 483  VAL G 484  0                                        
SHEET    2 AD1 2 ARG G 490  PRO G 491 -1  O  ARG G 490   N  VAL G 484           
SHEET    1 AD2 4 ILE H  78  ASN H  82  0                                        
SHEET    2 AD2 4 ARG H  87  VAL H  91 -1  O  CYS H  90   N  PHE H  79           
SHEET    3 AD2 4 LEU H 402  PHE H 406  1  O  PHE H 406   N  VAL H  91           
SHEET    4 AD2 4 PHE H 381  VAL H 385 -1  N  ARG H 384   O  VAL H 403           
SHEET    1 AD3 3 SER H 183  ASP H 187  0                                        
SHEET    2 AD3 3 LEU H 496  ALA H 501 -1  O  PHE H 499   N  LEU H 184           
SHEET    3 AD3 3 PHE H 471  GLU H 474 -1  N  GLU H 474   O  THR H 498           
SHEET    1 AD4 2 LEU H 390  LEU H 392  0                                        
SHEET    2 AD4 2 TYR H 395  ILE H 397 -1  O  ILE H 397   N  LEU H 390           
SHEET    1 AD5 2 MET H 483  TYR H 485  0                                        
SHEET    2 AD5 2 LEU H 489  PRO H 491 -1  O  ARG H 490   N  VAL H 484           
SHEET    1 AD6 4 ILE I  78  ARG I  80  0                                        
SHEET    2 AD6 4 MET I  88  VAL I  91 -1  O  CYS I  90   N  PHE I  79           
SHEET    3 AD6 4 LEU I 402  PHE I 406  1  O  LEU I 402   N  VAL I  89           
SHEET    4 AD6 4 PHE I 381  VAL I 385 -1  N  ARG I 384   O  VAL I 403           
SHEET    1 AD7 3 SER I 183  LEU I 186  0                                        
SHEET    2 AD7 3 LEU I 497  ALA I 501 -1  O  PHE I 499   N  LEU I 184           
SHEET    3 AD7 3 PHE I 471  GLU I 474 -1  N  GLU I 474   O  THR I 498           
SHEET    1 AD8 2 LEU I 390  LEU I 392  0                                        
SHEET    2 AD8 2 TYR I 395  ILE I 397 -1  O  ILE I 397   N  LEU I 390           
SHEET    1 AD9 2 MET I 483  TYR I 485  0                                        
SHEET    2 AD9 2 LEU I 489  PRO I 491 -1  O  ARG I 490   N  VAL I 484           
SHEET    1 AE1 4 ILE J  78  TYR J  81  0                                        
SHEET    2 AE1 4 MET J  88  VAL J  91 -1  O  CYS J  90   N  PHE J  79           
SHEET    3 AE1 4 LEU J 402  PHE J 406  1  O  LEU J 402   N  VAL J  89           
SHEET    4 AE1 4 PHE J 381  VAL J 385 -1  N  ARG J 384   O  VAL J 403           
SHEET    1 AE2 3 SER J 183  LEU J 186  0                                        
SHEET    2 AE2 3 LEU J 497  ALA J 501 -1  O  PHE J 499   N  LEU J 184           
SHEET    3 AE2 3 PHE J 471  GLU J 474 -1  N  GLU J 474   O  THR J 498           
SHEET    1 AE3 2 LEU J 390  VAL J 391  0                                        
SHEET    2 AE3 2 HIS J 396  ILE J 397 -1  O  ILE J 397   N  LEU J 390           
SHEET    1 AE4 2 MET J 483  TYR J 485  0                                        
SHEET    2 AE4 2 LEU J 489  PRO J 491 -1  O  ARG J 490   N  VAL J 484           
SHEET    1 AE5 4 ILE K  78  ARG K  80  0                                        
SHEET    2 AE5 4 MET K  88  VAL K  91 -1  O  CYS K  90   N  PHE K  79           
SHEET    3 AE5 4 LEU K 402  PHE K 406  1  O  LEU K 402   N  VAL K  89           
SHEET    4 AE5 4 PHE K 381  VAL K 385 -1  N  ARG K 384   O  VAL K 403           
SHEET    1 AE6 3 SER K 183  LEU K 186  0                                        
SHEET    2 AE6 3 LEU K 497  ALA K 501 -1  O  PHE K 499   N  LEU K 184           
SHEET    3 AE6 3 PHE K 471  GLU K 474 -1  N  GLU K 474   O  THR K 498           
SHEET    1 AE7 2 LEU K 390  LEU K 392  0                                        
SHEET    2 AE7 2 TYR K 395  ILE K 397 -1  O  ILE K 397   N  LEU K 390           
SHEET    1 AE8 2 MET K 483  TYR K 485  0                                        
SHEET    2 AE8 2 LEU K 489  PRO K 491 -1  O  ARG K 490   N  VAL K 484           
SHEET    1 AE9 4 ILE L  78  ARG L  80  0                                        
SHEET    2 AE9 4 MET L  88  VAL L  91 -1  O  CYS L  90   N  PHE L  79           
SHEET    3 AE9 4 LEU L 402  PHE L 406  1  O  GLN L 404   N  VAL L  89           
SHEET    4 AE9 4 PHE L 381  VAL L 385 -1  N  ARG L 384   O  VAL L 403           
SHEET    1 AF1 3 SER L 183  ASP L 187  0                                        
SHEET    2 AF1 3 LEU L 496  ALA L 501 -1  O  LEU L 497   N  LEU L 186           
SHEET    3 AF1 3 PHE L 471  GLU L 474 -1  N  GLU L 474   O  THR L 498           
SHEET    1 AF2 2 LEU L 390  LEU L 392  0                                        
SHEET    2 AF2 2 TYR L 395  ILE L 397 -1  O  ILE L 397   N  LEU L 390           
SHEET    1 AF3 2 MET L 483  TYR L 485  0                                        
SHEET    2 AF3 2 LEU L 489  PRO L 491 -1  O  ARG L 490   N  VAL L 484           
LINK         SG  CYS A 450                FE   HEM A 601     1555   1555  2.67  
LINK         SG  CYS B 450                FE   HEM B 601     1555   1555  2.54  
LINK         SG  CYS C 450                FE   HEM C 601     1555   1555  2.61  
LINK         SG  CYS D 450                FE   HEM D 601     1555   1555  2.65  
LINK         SG  CYS E 450                FE   HEM E 601     1555   1555  2.67  
LINK         SG  CYS F 450                FE   HEM F 601     1555   1555  2.61  
LINK         SG  CYS I 450                FE   HEM I 601     1555   1555  2.64  
LINK         SG  CYS K 450                FE   HEM K 601     1555   1555  2.51  
LINK         SG  CYS L 450                FE   HEM L 601     1555   1555  2.64  
LINK        FE   HEM A 601                 N10 QHC A 602     1555   1555  1.97  
LINK        FE   HEM B 601                 N10 QHC B 602     1555   1555  2.24  
LINK        FE   HEM C 601                 N10 QHC C 602     1555   1555  2.49  
LINK        FE   HEM D 601                 N10 QHC D 602     1555   1555  2.24  
LINK        FE   HEM E 601                 N10 QHC E 602     1555   1555  2.25  
LINK        FE   HEM F 601                 N10 QHC F 602     1555   1555  2.26  
LINK        FE   HEM I 601                 N10 QHC I 602     1555   1555  2.22  
LINK        FE   HEM J 601                 N10 QHC J 602     1555   1555  2.19  
LINK        FE   HEM K 601                 N10 QHC K 602     1555   1555  2.34  
LINK        FE   HEM L 601                 N10 QHC L 602     1555   1555  2.47  
SITE     1 AC1 22 ARG A 110  VAL A 129  PHE A 130  TRP A 137                    
SITE     2 AC1 22 ARG A 141  LEU A 311  SER A 315  THR A 318                    
SITE     3 AC1 22 THR A 319  VAL A 378  LEU A 382  ARG A 384                    
SITE     4 AC1 22 PRO A 442  PHE A 443  GLY A 444  PHE A 445                    
SITE     5 AC1 22 ARG A 448  GLN A 449  CYS A 450  ALA A 456                    
SITE     6 AC1 22 MET A 460  QHC A 602                                          
SITE     1 AC2 10 TRP A 116  PHE A 130  TRP A 260  GLU A 310                    
SITE     2 AC2 10 GLY A 314  VAL A 378  GLY A 379  PHE A 381                    
SITE     3 AC2 10 ILE A 488  HEM A 601                                          
SITE     1 AC3 22 ARG B 110  VAL B 129  PHE B 130  TRP B 137                    
SITE     2 AC3 22 ARG B 141  GLY B 314  SER B 315  THR B 318                    
SITE     3 AC3 22 THR B 319  VAL B 378  LEU B 382  ARG B 384                    
SITE     4 AC3 22 PRO B 442  PHE B 443  GLY B 444  PHE B 445                    
SITE     5 AC3 22 ARG B 448  CYS B 450  GLY B 452  LEU B 455                    
SITE     6 AC3 22 ALA B 456  QHC B 602                                          
SITE     1 AC4 10 TRP B 116  PHE B 130  GLU B 310  ALA B 313                    
SITE     2 AC4 10 GLY B 314  GLY B 379  LEU B 407  PRO B 442                    
SITE     3 AC4 10 ILE B 488  HEM B 601                                          
SITE     1 AC5 22 ARG C 110  VAL C 129  PHE C 130  TRP C 137                    
SITE     2 AC5 22 ARG C 141  GLY C 314  SER C 315  THR C 318                    
SITE     3 AC5 22 THR C 319  LEU C 382  ARG C 384  PRO C 442                    
SITE     4 AC5 22 PHE C 443  GLY C 444  PHE C 445  ARG C 448                    
SITE     5 AC5 22 CYS C 450  GLY C 452  LEU C 455  ALA C 456                    
SITE     6 AC5 22 MET C 460  QHC C 602                                          
SITE     1 AC6 11 TRP C 116  PHE C 130  GLU C 310  GLY C 314                    
SITE     2 AC6 11 GLY C 379  LEU C 380  PHE C 381  LEU C 407                    
SITE     3 AC6 11 PHE C 487  ILE C 488  HEM C 601                               
SITE     1 AC7 22 ARG D 110  VAL D 129  PHE D 130  TRP D 137                    
SITE     2 AC7 22 ARG D 141  LEU D 311  GLY D 314  SER D 315                    
SITE     3 AC7 22 THR D 318  THR D 319  LEU D 373  VAL D 378                    
SITE     4 AC7 22 LEU D 382  ARG D 384  PRO D 442  PHE D 443                    
SITE     5 AC7 22 PHE D 445  ARG D 448  GLN D 449  CYS D 450                    
SITE     6 AC7 22 LEU D 455  QHC D 602                                          
SITE     1 AC8  9 TRP D 116  PHE D 130  GLU D 310  GLY D 314                    
SITE     2 AC8  9 THR D 318  GLY D 379  PHE D 381  ILE D 488                    
SITE     3 AC8  9 HEM D 601                                                     
SITE     1 AC9 22 ARG E 110  VAL E 129  PHE E 130  TRP E 137                    
SITE     2 AC9 22 ARG E 141  GLY E 314  SER E 315  THR E 318                    
SITE     3 AC9 22 THR E 319  LEU E 373  VAL E 378  LEU E 382                    
SITE     4 AC9 22 ARG E 384  PRO E 442  PHE E 443  PHE E 445                    
SITE     5 AC9 22 ARG E 448  CYS E 450  GLY E 452  LEU E 455                    
SITE     6 AC9 22 ALA E 456  QHC E 602                                          
SITE     1 AD1  9 TRP E 116  PHE E 130  GLU E 310  GLY E 314                    
SITE     2 AD1  9 VAL E 378  GLY E 379  PHE E 381  PHE E 487                    
SITE     3 AD1  9 HEM E 601                                                     
SITE     1 AD2 20 ARG F 110  VAL F 129  PHE F 130  TRP F 137                    
SITE     2 AD2 20 ARG F 141  LEU F 311  GLY F 314  THR F 318                    
SITE     3 AD2 20 THR F 319  VAL F 378  LEU F 382  ARG F 384                    
SITE     4 AD2 20 PRO F 442  PHE F 443  PHE F 445  ARG F 448                    
SITE     5 AD2 20 CYS F 450  GLY F 452  ALA F 456  QHC F 602                    
SITE     1 AD3 11 TRP F 116  PHE F 130  GLU F 310  GLY F 314                    
SITE     2 AD3 11 GLY F 379  PHE F 381  LEU F 407  PHE F 487                    
SITE     3 AD3 11 ILE F 488  HEM F 601  HOH F 720                               
SITE     1 AD4 21 ARG G 110  VAL G 129  PHE G 130  TRP G 137                    
SITE     2 AD4 21 ARG G 141  LEU G 311  GLY G 314  SER G 315                    
SITE     3 AD4 21 THR G 318  THR G 319  VAL G 378  LEU G 382                    
SITE     4 AD4 21 ARG G 384  PRO G 442  PHE G 443  GLY G 444                    
SITE     5 AD4 21 PHE G 445  ARG G 448  CYS G 450  GLY G 452                    
SITE     6 AD4 21 ALA G 456                                                     
SITE     1 AD5 23 ARG H 110  VAL H 129  PHE H 130  TRP H 137                    
SITE     2 AD5 23 ARG H 141  LEU H 311  GLY H 314  THR H 318                    
SITE     3 AD5 23 THR H 319  LEU H 373  VAL H 378  LEU H 382                    
SITE     4 AD5 23 ARG H 384  PRO H 442  PHE H 443  GLY H 444                    
SITE     5 AD5 23 PHE H 445  ARG H 448  GLN H 449  CYS H 450                    
SITE     6 AD5 23 LEU H 451  GLY H 452  ALA H 456                               
SITE     1 AD6 22 ARG I 110  VAL I 129  PHE I 130  TRP I 137                    
SITE     2 AD6 22 ARG I 141  GLY I 314  THR I 318  THR I 319                    
SITE     3 AD6 22 VAL I 378  LEU I 382  ARG I 384  PRO I 442                    
SITE     4 AD6 22 PHE I 443  GLY I 444  PHE I 445  ARG I 448                    
SITE     5 AD6 22 GLN I 449  CYS I 450  GLY I 452  LEU I 455                    
SITE     6 AD6 22 ALA I 456  QHC I 602                                          
SITE     1 AD7  9 TRP I 116  PHE I 130  GLU I 310  ALA I 313                    
SITE     2 AD7  9 GLY I 314  GLY I 379  PHE I 381  LEU I 407                    
SITE     3 AD7  9 HEM I 601                                                     
SITE     1 AD8 21 ARG J 110  VAL J 129  TRP J 137  ARG J 141                    
SITE     2 AD8 21 LEU J 311  GLY J 314  THR J 318  THR J 319                    
SITE     3 AD8 21 LEU J 373  VAL J 378  ARG J 384  PRO J 442                    
SITE     4 AD8 21 PHE J 443  GLY J 444  PHE J 445  ARG J 448                    
SITE     5 AD8 21 CYS J 450  GLY J 452  LEU J 455  ALA J 456                    
SITE     6 AD8 21 QHC J 602                                                     
SITE     1 AD9  9 TRP J 116  PHE J 130  ALA J 313  GLY J 314                    
SITE     2 AD9  9 VAL J 378  GLY J 379  PHE J 381  PHE J 487                    
SITE     3 AD9  9 HEM J 601                                                     
SITE     1 AE1 22 ARG K 110  VAL K 129  PHE K 130  TRP K 137                    
SITE     2 AE1 22 ARG K 141  LEU K 311  GLY K 314  SER K 315                    
SITE     3 AE1 22 THR K 318  THR K 319  LEU K 373  VAL K 378                    
SITE     4 AE1 22 LEU K 382  ARG K 384  PRO K 442  PHE K 443                    
SITE     5 AE1 22 GLY K 444  ARG K 448  CYS K 450  GLY K 452                    
SITE     6 AE1 22 MET K 460  QHC K 602                                          
SITE     1 AE2  9 TRP K 116  PHE K 130  GLU K 310  GLY K 314                    
SITE     2 AE2  9 GLY K 379  PHE K 381  LEU K 407  PHE K 487                    
SITE     3 AE2  9 HEM K 601                                                     
SITE     1 AE3 21 ARG L 110  VAL L 129  PHE L 130  TRP L 137                    
SITE     2 AE3 21 ARG L 141  LEU L 311  GLY L 314  SER L 315                    
SITE     3 AE3 21 THR L 318  THR L 319  LEU L 382  GLU L 383                    
SITE     4 AE3 21 ARG L 384  PRO L 442  PHE L 443  GLY L 444                    
SITE     5 AE3 21 ARG L 448  CYS L 450  GLY L 452  MET L 460                    
SITE     6 AE3 21 QHC L 602                                                     
SITE     1 AE4 12 TRP L 116  PHE L 130  GLU L 310  GLY L 314                    
SITE     2 AE4 12 THR L 318  VAL L 378  GLY L 379  PHE L 381                    
SITE     3 AE4 12 LEU L 407  PHE L 487  ILE L 488  HEM L 601                    
CRYST1  104.700  125.960  155.230  70.25  85.87  73.84 P 1          12          
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      0.009551 -0.002768  0.000242        0.00000                         
SCALE2      0.000000  0.008266 -0.002907        0.00000                         
SCALE3      0.000000  0.000000  0.006847        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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