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Database: PDB
Entry: 2XSN
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Original site: 2XSN 
HEADER    OXIDOREDUCTASE                          29-OCT-10   2XSN              
TITLE     CRYSTAL STRUCTURE OF HUMAN TYROSINE HYDROXYLASE CATALYTIC DOMAIN      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYROSINE 3-MONOOXYGENASE;                                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 193-528;                        
COMPND   5 SYNONYM: TYROSINE 3-HYDROXYLASE, TH;                                 
COMPND   6 EC: 1.14.16.2;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: R3-PL                                     
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.C.MUNIZ,C.D.O.COOPER,W.W.YUE,E.KRYSZTOFINSKA,F.VON DELFT,S.KNAPP, 
AUTHOR   2 O.GILEADI,C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,C.BOUNTRA,            
AUTHOR   3 K.L.KAVANAGH,U.OPPERMANN                                             
REVDAT   3   24-JAN-18 2XSN    1       AUTHOR JRNL                              
REVDAT   2   05-DEC-12 2XSN    1       SOURCE AUTHOR JRNL   REMARK              
REVDAT   2 2                   1       VERSN                                    
REVDAT   1   17-NOV-10 2XSN    0                                                
JRNL        AUTH   J.R.C.MUNIZ,C.D.O.COOPER,W.W.YUE,E.KRYSZTOFINSKA,            
JRNL        AUTH 2 F.VON DELFT,S.KNAPP,O.GILEADI,C.H.ARROWSMITH,A.M.EDWARDS,    
JRNL        AUTH 3 J.WEIGELT,C.BOUNTRA,K.L.KAVANAGH,U.OPPERMANN                 
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN TYROSINE HYDROXYLASE CATALYTIC    
JRNL        TITL 2 DOMAIN                                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.68 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT 2.8.0                                     
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,              
REMARK   3               : MATTHEWS,TEN EYCK,TRONRUD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.68                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 62.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 51346                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.191                          
REMARK   3   R VALUE            (WORKING SET)  : 0.189                          
REMARK   3   FREE R VALUE                      : 0.222                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.100                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2608                           
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) : 2.68                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.75                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 100.0                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3729                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2352                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3544                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2319                   
REMARK   3   BIN FREE R VALUE                        : 0.3004                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.96                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 185                      
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            : 10661                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 227                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.81                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.31370                                              
REMARK   3    B22 (A**2) : 0.31370                                              
REMARK   3    B33 (A**2) : -0.62750                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.372               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.918                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 11004  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 14948  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 5011   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 266    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1634   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 11004  ; 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   : 1383   ; 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   : 12520  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.00                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.79                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.98                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 21                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (A 233 - A 350)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   66.0656    2.7386   17.3908           
REMARK   3    T TENSOR                                                          
REMARK   3    L TENSOR                                                          
REMARK   3    S TENSOR                                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (A 351 - A 401)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   58.4710    9.8083   26.4226           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0966 T22:   -0.0212                                    
REMARK   3     T33:   -0.0795 T12:    0.0190                                    
REMARK   3     T13:    0.0190 T23:   -0.0280                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.3412 L22:    2.2104                                    
REMARK   3     L33:    2.1367 L12:   -0.3932                                    
REMARK   3     L13:   -0.7639 L23:    0.7760                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0564 S12:    0.4775 S13:   -0.1716                     
REMARK   3     S21:   -0.4355 S22:    0.0013 S23:    0.1999                     
REMARK   3     S31:    0.0166 S32:   -0.4129 S33:    0.0551                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (A 402 - A 483)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   46.9666   11.3287   24.7079           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1283 T22:    0.0492                                    
REMARK   3     T33:   -0.0468 T12:    0.0778                                    
REMARK   3     T13:   -0.0190 T23:   -0.0112                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7335 L22:    1.7879                                    
REMARK   3     L33:    1.9495 L12:   -0.0080                                    
REMARK   3     L13:   -1.2093 L23:   -0.0508                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0392 S12:    0.4441 S13:   -0.2086                     
REMARK   3     S21:   -0.1889 S22:    0.0475 S23:    0.1531                     
REMARK   3     S31:   -0.1371 S32:   -0.7052 S33:   -0.0082                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (A 484 - A 527)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   70.1687   31.7017   31.0545           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1787 T22:    0.0893                                    
REMARK   3     T33:   -0.0058 T12:    0.0719                                    
REMARK   3     T13:   -0.0312 T23:    0.0029                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1046 L22:    1.7990                                    
REMARK   3     L33:    1.8406 L12:   -0.9479                                    
REMARK   3     L13:    0.1024 L23:   -0.2953                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0863 S12:    0.2352 S13:    0.0237                     
REMARK   3     S21:   -0.1963 S22:   -0.0891 S23:    0.6386                     
REMARK   3     S31:   -0.0720 S32:   -0.6641 S33:    0.0028                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (B 193 - B 303)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   28.4305   58.6535   35.4218           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0581 T22:   -0.1065                                    
REMARK   3     T33:    0.0307 T12:    0.1035                                    
REMARK   3     T13:    0.0499 T23:    0.0564                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8078 L22:    4.0674                                    
REMARK   3     L33:    3.2969 L12:   -1.8395                                    
REMARK   3     L13:    0.2676 L23:   -1.0099                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0477 S12:    0.0818 S13:    0.2041                     
REMARK   3     S21:   -0.0271 S22:    0.0070 S23:   -0.5044                     
REMARK   3     S31:   -0.0035 S32:   -0.0660 S33:    0.0407                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (B 304 - B 317)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   42.7315   56.5321   40.2199           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0712 T22:    0.0415                                    
REMARK   3     T33:   -0.1103 T12:   -0.0151                                    
REMARK   3     T13:   -0.0067 T23:    0.0440                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2418 L22:    0.8891                                    
REMARK   3     L33:    0.9798 L12:   -0.2980                                    
REMARK   3     L13:    0.0561 L23:   -0.1968                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0371 S12:   -0.3793 S13:   -0.0733                     
REMARK   3     S21:    0.2802 S22:    0.0447 S23:    0.0534                     
REMARK   3     S31:    0.2087 S32:   -0.3396 S33:   -0.0818                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (B 318 - B 391)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   33.5068   52.1897   30.9588           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0293 T22:    0.0172                                    
REMARK   3     T33:   -0.0076 T12:    0.0847                                    
REMARK   3     T13:   -0.0451 T23:    0.0706                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.5150 L22:   -2.5150                                    
REMARK   3     L33:    0.0000 L12:   -1.4520                                    
REMARK   3     L13:    0.8107 L23:   -0.1644                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0278 S12:   -0.1160 S13:   -0.0392                     
REMARK   3     S21:   -0.0298 S22:    0.0474 S23:   -0.1946                     
REMARK   3     S31:   -0.0157 S32:    0.0185 S33:   -0.0753                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (B 392 - B 484)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   30.9555   37.0858   29.4445           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0275 T22:   -0.0746                                    
REMARK   3     T33:   -0.0198 T12:   -0.0180                                    
REMARK   3     T13:   -0.0673 T23:    0.0366                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0011 L22:    1.0209                                    
REMARK   3     L33:    2.1715 L12:   -0.4852                                    
REMARK   3     L13:   -0.3608 L23:    0.1136                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0215 S12:   -0.1299 S13:   -0.3300                     
REMARK   3     S21:    0.1182 S22:    0.0234 S23:   -0.0405                     
REMARK   3     S31:    0.5934 S32:   -0.2793 S33:   -0.0449                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (B 485 - B 528)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   60.5504   47.9848   26.0161           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0540 T22:   -0.1821                                    
REMARK   3     T33:    0.0041 T12:   -0.0995                                    
REMARK   3     T13:   -0.1167 T23:    0.0562                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7572 L22:    3.7477                                    
REMARK   3     L33:    1.9425 L12:    0.2298                                    
REMARK   3     L13:    0.0160 L23:    0.3678                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0166 S12:    0.1320 S13:   -0.5922                     
REMARK   3     S21:    0.0039 S22:    0.0971 S23:   -0.0627                     
REMARK   3     S31:    0.7403 S32:   -0.2011 S33:   -0.1137                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (C 193 - C 349)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   60.8019   74.4716   37.8214           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0580 T22:   -0.1942                                    
REMARK   3     T33:    0.0132 T12:    0.0818                                    
REMARK   3     T13:   -0.0133 T23:    0.0138                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1873 L22:    2.0823                                    
REMARK   3     L33:    2.2363 L12:   -1.4967                                    
REMARK   3     L13:   -0.9277 L23:   -0.3631                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1616 S12:    0.0723 S13:    0.2817                     
REMARK   3     S21:   -0.3770 S22:   -0.2519 S23:   -0.4015                     
REMARK   3     S31:   -0.0957 S32:   -0.2046 S33:    0.0903                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (C 350 - C 373)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   67.9395   74.9267   34.4872           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1430 T22:   -0.1162                                    
REMARK   3     T33:   -0.0067 T12:    0.1041                                    
REMARK   3     T13:    0.0079 T23:   -0.0211                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0367 L22:    4.0467                                    
REMARK   3     L33:    1.1842 L12:    0.4962                                    
REMARK   3     L13:    0.0944 L23:   -0.8459                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0739 S12:    0.2202 S13:    0.1670                     
REMARK   3     S21:    0.0170 S22:    0.0297 S23:   -0.1561                     
REMARK   3     S31:   -0.1615 S32:    0.1368 S33:   -0.1036                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (C 374 - C 434)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   75.6736   65.8858   36.2323           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1619 T22:    0.0178                                    
REMARK   3     T33:    0.1403 T12:    0.0982                                    
REMARK   3     T13:    0.0769 T23:    0.0473                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.7991 L22:    0.4055                                    
REMARK   3     L33:    4.3136 L12:   -1.9268                                    
REMARK   3     L13:   -1.6310 L23:    0.5365                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0500 S12:   -0.0125 S13:    0.2032                     
REMARK   3     S21:    0.0890 S22:   -0.0511 S23:   -0.1813                     
REMARK   3     S31:    0.0229 S32:    0.1394 S33:    0.1012                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (C 435 - C 482)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   82.1625   63.0183   36.8832           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2295 T22:   -0.0233                                    
REMARK   3     T33:    0.1532 T12:    0.0926                                    
REMARK   3     T13:    0.0343 T23:   -0.0749                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5850 L22:    2.3459                                    
REMARK   3     L33:    0.2806 L12:    0.7788                                    
REMARK   3     L13:   -0.6751 L23:   -0.6197                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2055 S12:    0.1373 S13:   -0.1957                     
REMARK   3     S21:   -0.1276 S22:   -0.0254 S23:   -0.7360                     
REMARK   3     S31:    0.1071 S32:    0.6002 S33:   -0.1801                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (C 483 - C 535)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   57.1266   45.1700   30.6202           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3466 T22:   -0.1417                                    
REMARK   3     T33:    0.3037 T12:    0.1265                                    
REMARK   3     T13:    0.0039 T23:   -0.0050                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.4222 L22:   -0.3158                                    
REMARK   3     L33:    4.4085 L12:    0.0381                                    
REMARK   3     L13:    1.2435 L23:    0.7594                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1522 S12:    0.0967 S13:   -0.1588                     
REMARK   3     S21:   -0.0366 S22:   -0.4217 S23:   -0.5503                     
REMARK   3     S31:    0.1113 S32:    0.5638 S33:    0.2695                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (D 194 - D 264)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   97.7789   18.4676   10.8632           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0932 T22:   -0.0769                                    
REMARK   3     T33:    0.0148 T12:    0.0886                                    
REMARK   3     T13:   -0.0171 T23:   -0.0038                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7529 L22:    3.2198                                    
REMARK   3     L33:    0.6352 L12:   -1.5506                                    
REMARK   3     L13:    0.2407 L23:   -2.4111                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0420 S12:    0.0612 S13:    0.1413                     
REMARK   3     S21:   -0.0510 S22:   -0.1584 S23:   -0.1546                     
REMARK   3     S31:    0.2176 S32:   -0.0386 S33:    0.1164                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (D 265 - D 298)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  100.4714   23.8992   33.4913           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0025 T22:   -0.2490                                    
REMARK   3     T33:    0.0043 T12:    0.0012                                    
REMARK   3     T13:    0.0704 T23:   -0.0341                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.9812 L22:    0.8170                                    
REMARK   3     L33:    1.7657 L12:    0.2347                                    
REMARK   3     L13:   -1.2989 L23:   -0.8589                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1248 S12:    0.2217 S13:   -0.4939                     
REMARK   3     S21:    0.0866 S22:   -0.1891 S23:   -0.2054                     
REMARK   3     S31:   -0.2575 S32:    0.1592 S33:    0.0643                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (D 299 - D 389)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   92.5248   24.8300   19.8551           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0781 T22:    0.0699                                    
REMARK   3     T33:   -0.2543 T12:   -0.2679                                    
REMARK   3     T13:    0.0650 T23:    0.0337                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -0.5291 L22:    1.9856                                    
REMARK   3     L33:    7.0427 L12:    0.1787                                    
REMARK   3     L13:    1.5488 L23:    1.6749                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0056 S12:   -0.4896 S13:   -0.0112                     
REMARK   3     S21:    0.3638 S22:    0.0394 S23:   -0.1652                     
REMARK   3     S31:   -0.1980 S32:    0.0191 S33:   -0.0450                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (D 390 - D 428)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   96.1724   38.0946   21.2496           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0450 T22:   -0.1936                                    
REMARK   3     T33:   -0.0249 T12:   -0.0234                                    
REMARK   3     T13:    0.1212 T23:   -0.0025                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.6036 L22:    2.0002                                    
REMARK   3     L33:    1.8647 L12:   -0.4393                                    
REMARK   3     L13:   -0.1400 L23:   -0.8651                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2655 S12:   -0.4097 S13:    0.4720                     
REMARK   3     S21:    0.1834 S22:   -0.1758 S23:   -0.1695                     
REMARK   3     S31:   -0.3852 S32:    0.2221 S33:   -0.0897                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (D 429 - D 465)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):  101.4793   44.0766   21.4180           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0475 T22:   -0.2818                                    
REMARK   3     T33:    0.2666 T12:   -0.1010                                    
REMARK   3     T13:    0.2076 T23:   -0.0556                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.2219 L22:    4.2685                                    
REMARK   3     L33:    0.0321 L12:   -0.3189                                    
REMARK   3     L13:    0.5513 L23:   -0.4005                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2034 S12:   -0.3418 S13:    0.6045                     
REMARK   3     S21:    0.2285 S22:   -0.0527 S23:   -0.1169                     
REMARK   3     S31:   -0.2471 S32:    0.0071 S33:   -0.1507                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (D 466 - D 486)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   82.1895   43.3968   19.6123           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0905 T22:   -0.1928                                    
REMARK   3     T33:    0.2617 T12:   -0.2153                                    
REMARK   3     T13:    0.1657 T23:   -0.0799                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5319 L22:    4.1343                                    
REMARK   3     L33:    0.0000 L12:    3.5671                                    
REMARK   3     L13:    3.4943 L23:   -0.2316                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0487 S12:   -0.1756 S13:    0.2483                     
REMARK   3     S21:    0.1230 S22:   -0.0904 S23:    0.0141                     
REMARK   3     S31:   -0.1831 S32:    0.3612 S33:    0.0417                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: (D 487 - D 535)                                        
REMARK   3    ORIGIN FOR THE GROUP (A):   66.0628   29.6780   27.3000           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.2004 T22:   -0.2956                                    
REMARK   3     T33:    0.3040 T12:    0.1505                                    
REMARK   3     T13:    0.2068 T23:   -0.0561                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2922 L22:    5.9143                                    
REMARK   3     L33:    0.4542 L12:    0.7645                                    
REMARK   3     L13:   -0.8794 L23:   -2.8939                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0040 S12:    0.1231 S13:    0.3773                     
REMARK   3     S21:   -0.0752 S22:    0.1375 S23:   -0.0325                     
REMARK   3     S31:   -0.0970 S32:   -0.0932 S33:   -0.1335                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2XSN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-OCT-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290046005.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51392                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.680                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.60                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.68                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 11.20                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.24000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 0.1 M TRI        
REMARK 280  -SODIUM CITRATE, 30% PEG 4K.                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      112.10667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       56.05333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       84.08000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       28.02667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      140.13333            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      112.10667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       56.05333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       28.02667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       84.08000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      140.13333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12050 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 55070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -203.8 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LYS 193 TO MET                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, LYS 193 TO MET                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, LYS 193 TO MET                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, LYS 193 TO MET                        
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   528                                                      
REMARK 465     ALA A   529                                                      
REMARK 465     GLU A   530                                                      
REMARK 465     ASN A   531                                                      
REMARK 465     LEU A   532                                                      
REMARK 465     TYR A   533                                                      
REMARK 465     PHE A   534                                                      
REMARK 465     GLN A   535                                                      
REMARK 465     ALA B   529                                                      
REMARK 465     GLU B   530                                                      
REMARK 465     ASN B   531                                                      
REMARK 465     LEU B   532                                                      
REMARK 465     TYR B   533                                                      
REMARK 465     PHE B   534                                                      
REMARK 465     GLN B   535                                                      
REMARK 465     LYS C   213                                                      
REMARK 465     PHE C   214                                                      
REMARK 465     ASP C   215                                                      
REMARK 465     PRO C   216                                                      
REMARK 465     ASP C   217                                                      
REMARK 465     LEU C   218                                                      
REMARK 465     ASP C   219                                                      
REMARK 465     LEU C   220                                                      
REMARK 465     ASP C   221                                                      
REMARK 465     HIS C   222                                                      
REMARK 465     PRO C   223                                                      
REMARK 465     GLY C   224                                                      
REMARK 465     PHE C   225                                                      
REMARK 465     SER C   226                                                      
REMARK 465     ASP C   227                                                      
REMARK 465     MET D   193                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 411    CD   CE   NZ                                        
REMARK 470     GLU A 436    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 437    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 206    CE   NZ                                             
REMARK 470     LYS B 264    NZ                                                  
REMARK 470     LYS B 411    CD   CE   NZ                                        
REMARK 470     GLN B 483    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 508    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 525    OG                                                  
REMARK 470     LYS C 200    NZ                                                  
REMARK 470     VAL C 211    CG1  CG2                                            
REMARK 470     THR C 212    OG1  CG2                                            
REMARK 470     GLN C 228    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 235    CG   CD   CE   NZ                                   
REMARK 470     LYS C 411    CG   CD   CE   NZ                                   
REMARK 470     GLN C 483    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 213    CE   NZ                                             
REMARK 470     GLN D 228    CG   CD   OE1  NE2                                  
REMARK 470     GLN D 232    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 235    CD   CE   NZ                                        
REMARK 470     ARG D 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 396    CG   CD   CE   NZ                                   
REMARK 470     LYS D 411    CG   CD   CE   NZ                                   
REMARK 470     ASN D 413    CG   OD1  ND2                                       
REMARK 470     GLU D 415    CG   CD   OE1  OE2                                  
REMARK 470     LEU D 430    CG   CD1  CD2                                       
REMARK 470     LEU D 431    CG   CD1  CD2                                       
REMARK 470     GLU D 436    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 456    CG   CD   OE1  NE2                                  
REMARK 470     THR D 457    OG1  CG2                                            
REMARK 470     ARG D 476    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER D 480    OG                                                  
REMARK 470     GLN D 483    CG   CD   OE1  NE2                                  
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    CYS A 207       68.16   -104.73                                   
REMARK 500    THR A 404      -80.73   -115.84                                   
REMARK 500    GLN A 456      -62.44    -95.76                                   
REMARK 500    GLN A 483       88.44    -67.58                                   
REMARK 500    CYS B 207       67.15   -104.87                                   
REMARK 500    LEU B 387      109.52    -52.16                                   
REMARK 500    THR B 404      -73.72   -118.96                                   
REMARK 500    GLN B 456      -61.09    -95.96                                   
REMARK 500    ARG B 481       33.08    -99.14                                   
REMARK 500    GLN B 483       98.36    -67.90                                   
REMARK 500    CYS C 207       69.05   -106.20                                   
REMARK 500    THR C 404      -74.88   -129.05                                   
REMARK 500    GLN C 456      -61.07    -96.55                                   
REMARK 500    ARG C 481       32.54    -99.79                                   
REMARK 500    GLN C 483       98.05    -66.87                                   
REMARK 500    CYS D 207       68.34   -105.34                                   
REMARK 500    THR D 404      -85.16   -133.41                                   
REMARK 500    GLN D 456      -61.83    -96.00                                   
REMARK 500    ARG D 481       32.46    -98.95                                   
REMARK 500    GLN D 483       98.00    -66.99                                   
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 C2016        DISTANCE =  6.50 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                              ZN A1528  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 361   NE2                                                    
REMARK 620 2 GLU A 406   OE2  88.0                                              
REMARK 620 3 HIS A 366   NE2  96.2 102.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1529  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 406   OE2                                                    
REMARK 620 2 HOH B2068   O   141.7                                              
REMARK 620 3 HIS B 361   NE2  88.5 111.7                                        
REMARK 620 4 HIS B 366   NE2 103.7 107.1  93.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C1536  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 361   NE2                                                    
REMARK 620 2 GLU C 406   OE2  90.6                                              
REMARK 620 3 HIS C 366   NE2  91.4 103.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D1536  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 366   NE2                                                    
REMARK 620 2 HIS D 361   NE2  76.5                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1528                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1529                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1536                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 1536                 
DBREF  2XSN A  193   528  UNP    P07101   TY3H_HUMAN     193    528             
DBREF  2XSN B  193   528  UNP    P07101   TY3H_HUMAN     193    528             
DBREF  2XSN C  193   528  UNP    P07101   TY3H_HUMAN     193    528             
DBREF  2XSN D  193   528  UNP    P07101   TY3H_HUMAN     193    528             
SEQADV 2XSN MET A  193  UNP  P07101    LYS   193 ENGINEERED MUTATION            
SEQADV 2XSN ALA A  529  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN GLU A  530  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN ASN A  531  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN LEU A  532  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN TYR A  533  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN PHE A  534  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN GLN A  535  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN MET B  193  UNP  P07101    LYS   193 ENGINEERED MUTATION            
SEQADV 2XSN ALA B  529  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN GLU B  530  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN ASN B  531  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN LEU B  532  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN TYR B  533  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN PHE B  534  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN GLN B  535  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN MET C  193  UNP  P07101    LYS   193 ENGINEERED MUTATION            
SEQADV 2XSN ALA C  529  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN GLU C  530  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN ASN C  531  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN LEU C  532  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN TYR C  533  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN PHE C  534  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN GLN C  535  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN MET D  193  UNP  P07101    LYS   193 ENGINEERED MUTATION            
SEQADV 2XSN ALA D  529  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN GLU D  530  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN ASN D  531  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN LEU D  532  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN TYR D  533  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN PHE D  534  UNP  P07101              EXPRESSION TAG                 
SEQADV 2XSN GLN D  535  UNP  P07101              EXPRESSION TAG                 
SEQRES   1 A  343  MET VAL PRO TRP PHE PRO ARG LYS VAL SER GLU LEU ASP          
SEQRES   2 A  343  LYS CYS HIS HIS LEU VAL THR LYS PHE ASP PRO ASP LEU          
SEQRES   3 A  343  ASP LEU ASP HIS PRO GLY PHE SER ASP GLN VAL TYR ARG          
SEQRES   4 A  343  GLN ARG ARG LYS LEU ILE ALA GLU ILE ALA PHE GLN TYR          
SEQRES   5 A  343  ARG HIS GLY ASP PRO ILE PRO ARG VAL GLU TYR THR ALA          
SEQRES   6 A  343  GLU GLU ILE ALA THR TRP LYS GLU VAL TYR THR THR LEU          
SEQRES   7 A  343  LYS GLY LEU TYR ALA THR HIS ALA CYS GLY GLU HIS LEU          
SEQRES   8 A  343  GLU ALA PHE ALA LEU LEU GLU ARG PHE SER GLY TYR ARG          
SEQRES   9 A  343  GLU ASP ASN ILE PRO GLN LEU GLU ASP VAL SER ARG PHE          
SEQRES  10 A  343  LEU LYS GLU ARG THR GLY PHE GLN LEU ARG PRO VAL ALA          
SEQRES  11 A  343  GLY LEU LEU SER ALA ARG ASP PHE LEU ALA SER LEU ALA          
SEQRES  12 A  343  PHE ARG VAL PHE GLN CYS THR GLN TYR ILE ARG HIS ALA          
SEQRES  13 A  343  SER SER PRO MET HIS SER PRO GLU PRO ASP CYS CYS HIS          
SEQRES  14 A  343  GLU LEU LEU GLY HIS VAL PRO MET LEU ALA ASP ARG THR          
SEQRES  15 A  343  PHE ALA GLN PHE SER GLN ASP ILE GLY LEU ALA SER LEU          
SEQRES  16 A  343  GLY ALA SER ASP GLU GLU ILE GLU LYS LEU SER THR LEU          
SEQRES  17 A  343  TYR TRP PHE THR VAL GLU PHE GLY LEU CYS LYS GLN ASN          
SEQRES  18 A  343  GLY GLU VAL LYS ALA TYR GLY ALA GLY LEU LEU SER SER          
SEQRES  19 A  343  TYR GLY GLU LEU LEU HIS CYS LEU SER GLU GLU PRO GLU          
SEQRES  20 A  343  ILE ARG ALA PHE ASP PRO GLU ALA ALA ALA VAL GLN PRO          
SEQRES  21 A  343  TYR GLN ASP GLN THR TYR GLN SER VAL TYR PHE VAL SER          
SEQRES  22 A  343  GLU SER PHE SER ASP ALA LYS ASP LYS LEU ARG SER TYR          
SEQRES  23 A  343  ALA SER ARG ILE GLN ARG PRO PHE SER VAL LYS PHE ASP          
SEQRES  24 A  343  PRO TYR THR LEU ALA ILE ASP VAL LEU ASP SER PRO GLN          
SEQRES  25 A  343  ALA VAL ARG ARG SER LEU GLU GLY VAL GLN ASP GLU LEU          
SEQRES  26 A  343  ASP THR LEU ALA HIS ALA LEU SER ALA ILE GLY ALA GLU          
SEQRES  27 A  343  ASN LEU TYR PHE GLN                                          
SEQRES   1 B  343  MET VAL PRO TRP PHE PRO ARG LYS VAL SER GLU LEU ASP          
SEQRES   2 B  343  LYS CYS HIS HIS LEU VAL THR LYS PHE ASP PRO ASP LEU          
SEQRES   3 B  343  ASP LEU ASP HIS PRO GLY PHE SER ASP GLN VAL TYR ARG          
SEQRES   4 B  343  GLN ARG ARG LYS LEU ILE ALA GLU ILE ALA PHE GLN TYR          
SEQRES   5 B  343  ARG HIS GLY ASP PRO ILE PRO ARG VAL GLU TYR THR ALA          
SEQRES   6 B  343  GLU GLU ILE ALA THR TRP LYS GLU VAL TYR THR THR LEU          
SEQRES   7 B  343  LYS GLY LEU TYR ALA THR HIS ALA CYS GLY GLU HIS LEU          
SEQRES   8 B  343  GLU ALA PHE ALA LEU LEU GLU ARG PHE SER GLY TYR ARG          
SEQRES   9 B  343  GLU ASP ASN ILE PRO GLN LEU GLU ASP VAL SER ARG PHE          
SEQRES  10 B  343  LEU LYS GLU ARG THR GLY PHE GLN LEU ARG PRO VAL ALA          
SEQRES  11 B  343  GLY LEU LEU SER ALA ARG ASP PHE LEU ALA SER LEU ALA          
SEQRES  12 B  343  PHE ARG VAL PHE GLN CYS THR GLN TYR ILE ARG HIS ALA          
SEQRES  13 B  343  SER SER PRO MET HIS SER PRO GLU PRO ASP CYS CYS HIS          
SEQRES  14 B  343  GLU LEU LEU GLY HIS VAL PRO MET LEU ALA ASP ARG THR          
SEQRES  15 B  343  PHE ALA GLN PHE SER GLN ASP ILE GLY LEU ALA SER LEU          
SEQRES  16 B  343  GLY ALA SER ASP GLU GLU ILE GLU LYS LEU SER THR LEU          
SEQRES  17 B  343  TYR TRP PHE THR VAL GLU PHE GLY LEU CYS LYS GLN ASN          
SEQRES  18 B  343  GLY GLU VAL LYS ALA TYR GLY ALA GLY LEU LEU SER SER          
SEQRES  19 B  343  TYR GLY GLU LEU LEU HIS CYS LEU SER GLU GLU PRO GLU          
SEQRES  20 B  343  ILE ARG ALA PHE ASP PRO GLU ALA ALA ALA VAL GLN PRO          
SEQRES  21 B  343  TYR GLN ASP GLN THR TYR GLN SER VAL TYR PHE VAL SER          
SEQRES  22 B  343  GLU SER PHE SER ASP ALA LYS ASP LYS LEU ARG SER TYR          
SEQRES  23 B  343  ALA SER ARG ILE GLN ARG PRO PHE SER VAL LYS PHE ASP          
SEQRES  24 B  343  PRO TYR THR LEU ALA ILE ASP VAL LEU ASP SER PRO GLN          
SEQRES  25 B  343  ALA VAL ARG ARG SER LEU GLU GLY VAL GLN ASP GLU LEU          
SEQRES  26 B  343  ASP THR LEU ALA HIS ALA LEU SER ALA ILE GLY ALA GLU          
SEQRES  27 B  343  ASN LEU TYR PHE GLN                                          
SEQRES   1 C  343  MET VAL PRO TRP PHE PRO ARG LYS VAL SER GLU LEU ASP          
SEQRES   2 C  343  LYS CYS HIS HIS LEU VAL THR LYS PHE ASP PRO ASP LEU          
SEQRES   3 C  343  ASP LEU ASP HIS PRO GLY PHE SER ASP GLN VAL TYR ARG          
SEQRES   4 C  343  GLN ARG ARG LYS LEU ILE ALA GLU ILE ALA PHE GLN TYR          
SEQRES   5 C  343  ARG HIS GLY ASP PRO ILE PRO ARG VAL GLU TYR THR ALA          
SEQRES   6 C  343  GLU GLU ILE ALA THR TRP LYS GLU VAL TYR THR THR LEU          
SEQRES   7 C  343  LYS GLY LEU TYR ALA THR HIS ALA CYS GLY GLU HIS LEU          
SEQRES   8 C  343  GLU ALA PHE ALA LEU LEU GLU ARG PHE SER GLY TYR ARG          
SEQRES   9 C  343  GLU ASP ASN ILE PRO GLN LEU GLU ASP VAL SER ARG PHE          
SEQRES  10 C  343  LEU LYS GLU ARG THR GLY PHE GLN LEU ARG PRO VAL ALA          
SEQRES  11 C  343  GLY LEU LEU SER ALA ARG ASP PHE LEU ALA SER LEU ALA          
SEQRES  12 C  343  PHE ARG VAL PHE GLN CYS THR GLN TYR ILE ARG HIS ALA          
SEQRES  13 C  343  SER SER PRO MET HIS SER PRO GLU PRO ASP CYS CYS HIS          
SEQRES  14 C  343  GLU LEU LEU GLY HIS VAL PRO MET LEU ALA ASP ARG THR          
SEQRES  15 C  343  PHE ALA GLN PHE SER GLN ASP ILE GLY LEU ALA SER LEU          
SEQRES  16 C  343  GLY ALA SER ASP GLU GLU ILE GLU LYS LEU SER THR LEU          
SEQRES  17 C  343  TYR TRP PHE THR VAL GLU PHE GLY LEU CYS LYS GLN ASN          
SEQRES  18 C  343  GLY GLU VAL LYS ALA TYR GLY ALA GLY LEU LEU SER SER          
SEQRES  19 C  343  TYR GLY GLU LEU LEU HIS CYS LEU SER GLU GLU PRO GLU          
SEQRES  20 C  343  ILE ARG ALA PHE ASP PRO GLU ALA ALA ALA VAL GLN PRO          
SEQRES  21 C  343  TYR GLN ASP GLN THR TYR GLN SER VAL TYR PHE VAL SER          
SEQRES  22 C  343  GLU SER PHE SER ASP ALA LYS ASP LYS LEU ARG SER TYR          
SEQRES  23 C  343  ALA SER ARG ILE GLN ARG PRO PHE SER VAL LYS PHE ASP          
SEQRES  24 C  343  PRO TYR THR LEU ALA ILE ASP VAL LEU ASP SER PRO GLN          
SEQRES  25 C  343  ALA VAL ARG ARG SER LEU GLU GLY VAL GLN ASP GLU LEU          
SEQRES  26 C  343  ASP THR LEU ALA HIS ALA LEU SER ALA ILE GLY ALA GLU          
SEQRES  27 C  343  ASN LEU TYR PHE GLN                                          
SEQRES   1 D  343  MET VAL PRO TRP PHE PRO ARG LYS VAL SER GLU LEU ASP          
SEQRES   2 D  343  LYS CYS HIS HIS LEU VAL THR LYS PHE ASP PRO ASP LEU          
SEQRES   3 D  343  ASP LEU ASP HIS PRO GLY PHE SER ASP GLN VAL TYR ARG          
SEQRES   4 D  343  GLN ARG ARG LYS LEU ILE ALA GLU ILE ALA PHE GLN TYR          
SEQRES   5 D  343  ARG HIS GLY ASP PRO ILE PRO ARG VAL GLU TYR THR ALA          
SEQRES   6 D  343  GLU GLU ILE ALA THR TRP LYS GLU VAL TYR THR THR LEU          
SEQRES   7 D  343  LYS GLY LEU TYR ALA THR HIS ALA CYS GLY GLU HIS LEU          
SEQRES   8 D  343  GLU ALA PHE ALA LEU LEU GLU ARG PHE SER GLY TYR ARG          
SEQRES   9 D  343  GLU ASP ASN ILE PRO GLN LEU GLU ASP VAL SER ARG PHE          
SEQRES  10 D  343  LEU LYS GLU ARG THR GLY PHE GLN LEU ARG PRO VAL ALA          
SEQRES  11 D  343  GLY LEU LEU SER ALA ARG ASP PHE LEU ALA SER LEU ALA          
SEQRES  12 D  343  PHE ARG VAL PHE GLN CYS THR GLN TYR ILE ARG HIS ALA          
SEQRES  13 D  343  SER SER PRO MET HIS SER PRO GLU PRO ASP CYS CYS HIS          
SEQRES  14 D  343  GLU LEU LEU GLY HIS VAL PRO MET LEU ALA ASP ARG THR          
SEQRES  15 D  343  PHE ALA GLN PHE SER GLN ASP ILE GLY LEU ALA SER LEU          
SEQRES  16 D  343  GLY ALA SER ASP GLU GLU ILE GLU LYS LEU SER THR LEU          
SEQRES  17 D  343  TYR TRP PHE THR VAL GLU PHE GLY LEU CYS LYS GLN ASN          
SEQRES  18 D  343  GLY GLU VAL LYS ALA TYR GLY ALA GLY LEU LEU SER SER          
SEQRES  19 D  343  TYR GLY GLU LEU LEU HIS CYS LEU SER GLU GLU PRO GLU          
SEQRES  20 D  343  ILE ARG ALA PHE ASP PRO GLU ALA ALA ALA VAL GLN PRO          
SEQRES  21 D  343  TYR GLN ASP GLN THR TYR GLN SER VAL TYR PHE VAL SER          
SEQRES  22 D  343  GLU SER PHE SER ASP ALA LYS ASP LYS LEU ARG SER TYR          
SEQRES  23 D  343  ALA SER ARG ILE GLN ARG PRO PHE SER VAL LYS PHE ASP          
SEQRES  24 D  343  PRO TYR THR LEU ALA ILE ASP VAL LEU ASP SER PRO GLN          
SEQRES  25 D  343  ALA VAL ARG ARG SER LEU GLU GLY VAL GLN ASP GLU LEU          
SEQRES  26 D  343  ASP THR LEU ALA HIS ALA LEU SER ALA ILE GLY ALA GLU          
SEQRES  27 D  343  ASN LEU TYR PHE GLN                                          
HET     ZN  A1528       1                                                       
HET     ZN  B1529       1                                                       
HET     ZN  C1536       1                                                       
HET     ZN  D1536       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   9  HOH   *227(H2 O)                                                    
HELIX    1   1 VAL A  201  CYS A  207  5                                   7    
HELIX    2   2 ASP A  227  TYR A  244  1                                  18    
HELIX    3   3 THR A  256  ALA A  278  1                                  23    
HELIX    4   4 CYS A  279  SER A  293  1                                  15    
HELIX    5   5 GLN A  302  GLY A  315  1                                  14    
HELIX    6   6 SER A  326  ALA A  335  1                                  10    
HELIX    7   7 ASP A  358  HIS A  366  1                                   9    
HELIX    8   8 HIS A  366  ALA A  371  1                                   6    
HELIX    9   9 ASP A  372  LEU A  387  1                                  16    
HELIX   10  10 SER A  390  THR A  404  1                                  15    
HELIX   11  11 GLY A  420  SER A  425  1                                   6    
HELIX   12  12 SER A  426  LEU A  434  1                                   9    
HELIX   13  13 ASP A  444  VAL A  450  1                                   7    
HELIX   14  14 SER A  467  ARG A  481  1                                  15    
HELIX   15  15 SER A  502  ILE A  527  1                                  26    
HELIX   16  16 VAL B  201  CYS B  207  5                                   7    
HELIX   17  17 ASP B  227  TYR B  244  1                                  18    
HELIX   18  18 THR B  256  ALA B  278  1                                  23    
HELIX   19  19 CYS B  279  SER B  293  1                                  15    
HELIX   20  20 GLN B  302  GLY B  315  1                                  14    
HELIX   21  21 SER B  326  ALA B  335  1                                  10    
HELIX   22  22 ASP B  358  HIS B  366  1                                   9    
HELIX   23  23 HIS B  366  ALA B  371  1                                   6    
HELIX   24  24 ASP B  372  LEU B  387  1                                  16    
HELIX   25  25 SER B  390  PHE B  403  1                                  14    
HELIX   26  26 GLY B  420  SER B  425  1                                   6    
HELIX   27  27 SER B  426  LEU B  434  1                                   9    
HELIX   28  28 ASP B  444  VAL B  450  1                                   7    
HELIX   29  29 SER B  467  ARG B  481  1                                  15    
HELIX   30  30 SER B  502  GLY B  528  1                                  27    
HELIX   31  31 VAL C  201  CYS C  207  5                                   7    
HELIX   32  32 GLN C  228  TYR C  244  1                                  17    
HELIX   33  33 THR C  256  ALA C  278  1                                  23    
HELIX   34  34 CYS C  279  SER C  293  1                                  15    
HELIX   35  35 GLN C  302  THR C  314  1                                  13    
HELIX   36  36 SER C  326  ALA C  335  1                                  10    
HELIX   37  37 ASP C  358  HIS C  366  1                                   9    
HELIX   38  38 HIS C  366  ALA C  371  1                                   6    
HELIX   39  39 ASP C  372  LEU C  387  1                                  16    
HELIX   40  40 SER C  390  PHE C  403  1                                  14    
HELIX   41  41 GLY C  420  SER C  425  1                                   6    
HELIX   42  42 SER C  426  LEU C  434  1                                   9    
HELIX   43  43 ASP C  444  VAL C  450  1                                   7    
HELIX   44  44 SER C  467  ARG C  481  1                                  15    
HELIX   45  45 SER C  502  ILE C  527  1                                  26    
HELIX   46  46 VAL D  201  CYS D  207  5                                   7    
HELIX   47  47 ASP D  227  TYR D  244  1                                  18    
HELIX   48  48 THR D  256  ALA D  278  1                                  23    
HELIX   49  49 CYS D  279  SER D  293  1                                  15    
HELIX   50  50 GLN D  302  GLY D  315  1                                  14    
HELIX   51  51 SER D  326  ALA D  335  1                                  10    
HELIX   52  52 ASP D  358  HIS D  366  1                                   9    
HELIX   53  53 VAL D  367  ALA D  371  5                                   5    
HELIX   54  54 ASP D  372  LEU D  387  1                                  16    
HELIX   55  55 SER D  390  PHE D  403  1                                  14    
HELIX   56  56 GLY D  420  SER D  425  1                                   6    
HELIX   57  57 SER D  426  LEU D  434  1                                   9    
HELIX   58  58 ASP D  444  VAL D  450  1                                   7    
HELIX   59  59 SER D  467  ARG D  481  1                                  15    
HELIX   60  60 SER D  502  ILE D  527  1                                  26    
SHEET    1  AA 2 GLN A 317  PRO A 320  0                                        
SHEET    2  AA 2 VAL A 338  CYS A 341  1  O  PHE A 339   N  ARG A 319           
SHEET    1  AB 4 GLU A 415  ALA A 418  0                                        
SHEET    2  AB 4 LEU A 409  GLN A 412 -1  O  CYS A 410   N  LYS A 417           
SHEET    3  AB 4 VAL A 461  SER A 465  1  O  PHE A 463   N  LEU A 409           
SHEET    4  AB 4 GLU A 439  ALA A 442  1  O  GLU A 439   N  TYR A 462           
SHEET    1  AC 2 SER A 487  ASP A 491  0                                        
SHEET    2  AC 2 ALA A 496  LEU A 500 -1  O  ALA A 496   N  ASP A 491           
SHEET    1  BA 2 GLN B 317  PRO B 320  0                                        
SHEET    2  BA 2 VAL B 338  CYS B 341  1  O  PHE B 339   N  ARG B 319           
SHEET    1  BB 4 GLU B 415  ALA B 418  0                                        
SHEET    2  BB 4 LEU B 409  GLN B 412 -1  O  CYS B 410   N  LYS B 417           
SHEET    3  BB 4 VAL B 461  SER B 465  1  O  PHE B 463   N  LEU B 409           
SHEET    4  BB 4 GLU B 439  ALA B 442  1  O  GLU B 439   N  TYR B 462           
SHEET    1  BC 2 SER B 487  ASP B 491  0                                        
SHEET    2  BC 2 ALA B 496  LEU B 500 -1  O  ALA B 496   N  ASP B 491           
SHEET    1  CA 2 GLN C 317  PRO C 320  0                                        
SHEET    2  CA 2 VAL C 338  CYS C 341  1  O  PHE C 339   N  ARG C 319           
SHEET    1  CB 4 GLU C 415  ALA C 418  0                                        
SHEET    2  CB 4 LEU C 409  GLN C 412 -1  O  CYS C 410   N  LYS C 417           
SHEET    3  CB 4 VAL C 461  SER C 465  1  O  PHE C 463   N  LEU C 409           
SHEET    4  CB 4 GLU C 439  ALA C 442  1  O  GLU C 439   N  TYR C 462           
SHEET    1  CC 2 SER C 487  ASP C 491  0                                        
SHEET    2  CC 2 ALA C 496  LEU C 500 -1  O  ALA C 496   N  ASP C 491           
SHEET    1  DA 2 LEU D 210  VAL D 211  0                                        
SHEET    2  DA 2 LEU D 324  LEU D 325 -1  O  LEU D 324   N  VAL D 211           
SHEET    1  DB 2 GLN D 317  PRO D 320  0                                        
SHEET    2  DB 2 VAL D 338  CYS D 341  1  O  PHE D 339   N  ARG D 319           
SHEET    1  DC 4 GLU D 415  ALA D 418  0                                        
SHEET    2  DC 4 LEU D 409  GLN D 412 -1  O  CYS D 410   N  LYS D 417           
SHEET    3  DC 4 VAL D 461  SER D 465  1  O  PHE D 463   N  LEU D 409           
SHEET    4  DC 4 GLU D 439  ALA D 442  1  O  GLU D 439   N  TYR D 462           
SHEET    1  DD 2 SER D 487  ASP D 491  0                                        
SHEET    2  DD 2 ALA D 496  LEU D 500 -1  O  ALA D 496   N  ASP D 491           
LINK        ZN    ZN A1528                 NE2 HIS A 361     1555   1555  2.25  
LINK        ZN    ZN A1528                 OE2 GLU A 406     1555   1555  2.20  
LINK        ZN    ZN A1528                 NE2 HIS A 366     1555   1555  2.12  
LINK        ZN    ZN B1529                 OE2 GLU B 406     1555   1555  2.24  
LINK        ZN    ZN B1529                 O   HOH B2068     1555   1555  2.54  
LINK        ZN    ZN B1529                 NE2 HIS B 361     1555   1555  2.23  
LINK        ZN    ZN B1529                 NE2 HIS B 366     1555   1555  2.30  
LINK        ZN    ZN C1536                 NE2 HIS C 361     1555   1555  2.21  
LINK        ZN    ZN C1536                 OE2 GLU C 406     1555   1555  2.21  
LINK        ZN    ZN C1536                 NE2 HIS C 366     1555   1555  2.28  
LINK        ZN    ZN D1536                 NE2 HIS D 366     1555   1555  2.25  
LINK        ZN    ZN D1536                 NE2 HIS D 361     1555   1555  2.50  
SITE     1 AC1  4 HIS A 361  HIS A 366  GLU A 406  HOH A2067                    
SITE     1 AC2  4 HIS B 361  HIS B 366  GLU B 406  HOH B2068                    
SITE     1 AC3  3 HIS C 361  HIS C 366  GLU C 406                               
SITE     1 AC4  3 HIS D 361  HIS D 366  GLU D 406                               
CRYST1  191.420  191.420  168.160  90.00  90.00 120.00 P 65 2 2     48          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005224  0.003016  0.000000        0.00000                         
SCALE2      0.000000  0.006032  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005947        0.00000                         
MTRIX1   1  0.459700  0.887300  0.036400       34.90420    1                    
MTRIX2   1  0.000000  0.013000  0.028300       49.68180    1                    
MTRIX3   1  0.026300 -0.999300  0.000000       31.92410    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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