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Database: PDB
Entry: 1H3I
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HEADER    TRANSFERASE                             04-SEP-02   1H3I              
TITLE     CRYSTAL STRUCTURE OF THE HISTONE METHYLTRANSFERASE SET7/9             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HISTONE H3 LYSINE 4 SPECIFIC METHYLTRANSFERASE;            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: N-DOMAIN, SET-DOMAIN, RESIDUES 52-344;                     
COMPND   5 SYNONYM: HISTONE H3-K4, METHYLTRANSFERASE;                           
COMPND   6 EC: 2.1.1.43;                                                        
COMPND   7 ENGINEERED: 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: 562                                         
KEYWDS    TRANSFERASE, METHYLTRANSFERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.WILSON,C.JING,P.A.WALKER,S.R.MARTIN,S.A.HOWELL,                   
AUTHOR   2 G.M.BLACKBURN,S.J.GAMBLIN,B.XIAO                                     
REVDAT   2   24-FEB-09 1H3I    1       VERSN                                    
REVDAT   1   11-NOV-02 1H3I    0                                                
JRNL        AUTH   J.R.WILSON,C.JING,P.A.WALKER,S.R.MARTIN,S.A.HOWELL,          
JRNL        AUTH 2 G.M.BLACKBURN,S.J.GAMBLIN,B.XIAO                             
JRNL        TITL   CRYSTAL STRUCTURE AND FUNCTIONAL ANALYSIS OF THE             
JRNL        TITL 2 HISTONE METHYLTRANSFERASE SET7/9                             
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 111   105 2002              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   12372304                                                     
JRNL        DOI    10.1016/S0092-8674(02)00964-9                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.1  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 34521                          
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) : 0.212                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1820                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2404                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 122                          
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4588                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 3                                       
REMARK   3   SOLVENT ATOMS            : 344                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.09000                                             
REMARK   3    B22 (A**2) : -2.43000                                             
REMARK   3    B33 (A**2) : 3.51000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.263         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.209         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.141         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.105         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.940                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.917                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4708 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6396 ; 1.445 ; 1.950       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   584 ; 3.768 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   781 ;18.794 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   668 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3728 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2228 ; 0.268 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   681 ; 0.170 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     7 ; 0.092 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   103 ; 0.286 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.114 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2898 ; 1.720 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4662 ; 3.046 ; 5.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1810 ; 3.952 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1734 ; 5.749 ; 8.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    52        A    95                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.1270  13.5140  -4.0850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2352 T22:   0.5732                                     
REMARK   3      T33:   0.0881 T12:   0.0032                                     
REMARK   3      T13:   0.0411 T23:  -0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4606 L22:   1.0678                                     
REMARK   3      L33:   3.9867 L12:   0.6805                                     
REMARK   3      L13:   0.3930 L23:  -0.0569                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0366 S12:   0.1803 S13:   0.1098                       
REMARK   3      S21:   0.0288 S22:   0.0498 S23:   0.0943                       
REMARK   3      S31:   0.0080 S32:   0.0616 S33:  -0.0132                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    96        A   192                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.9980   4.0380 -19.4140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2080 T22:   0.5659                                     
REMARK   3      T33:   0.1117 T12:  -0.0058                                     
REMARK   3      T13:   0.0260 T23:  -0.0451                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9984 L22:   1.6506                                     
REMARK   3      L33:   3.9589 L12:   0.6868                                     
REMARK   3      L13:   0.9595 L23:   1.4734                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0367 S12:  -0.1079 S13:  -0.0476                       
REMARK   3      S21:   0.1568 S22:  -0.1261 S23:   0.1635                       
REMARK   3      S31:   0.1854 S32:  -0.1718 S33:   0.0894                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   193        A   264                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.3650   0.3140 -43.8730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2357 T22:   0.5136                                     
REMARK   3      T33:   0.1068 T12:  -0.0217                                     
REMARK   3      T13:  -0.0558 T23:  -0.0284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6676 L22:   0.7894                                     
REMARK   3      L33:   2.8105 L12:  -0.3177                                     
REMARK   3      L13:  -0.9310 L23:   0.3949                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0490 S12:   0.0412 S13:   0.0569                       
REMARK   3      S21:   0.0041 S22:   0.0116 S23:  -0.0032                       
REMARK   3      S31:  -0.0742 S32:  -0.0593 S33:   0.0374                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   265        A   344                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2760   3.7430 -44.3680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2546 T22:   0.5297                                     
REMARK   3      T33:   0.1034 T12:  -0.0113                                     
REMARK   3      T13:  -0.0483 T23:  -0.0358                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1051 L22:   1.2182                                     
REMARK   3      L33:   2.8947 L12:  -0.1205                                     
REMARK   3      L13:  -0.5652 L23:  -0.0508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0135 S12:  -0.0280 S13:   0.0634                       
REMARK   3      S21:   0.0056 S22:  -0.0595 S23:  -0.0339                       
REMARK   3      S31:  -0.2531 S32:   0.2380 S33:   0.0460                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    52        B    95                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.5180  23.6950  49.8460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3410 T22:   0.5515                                     
REMARK   3      T33:   0.0244 T12:   0.0767                                     
REMARK   3      T13:   0.0911 T23:   0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.7671 L22:  11.2864                                     
REMARK   3      L33:   7.8401 L12:  -4.8112                                     
REMARK   3      L13:  -1.2122 L23:  -2.3058                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3878 S12:  -0.7989 S13:  -0.7159                       
REMARK   3      S21:   0.5774 S22:   0.2769 S23:   0.9507                       
REMARK   3      S31:   0.2258 S32:  -0.0797 S33:   0.1109                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    96        B   192                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8710  18.5620  34.4340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2823 T22:   0.5512                                     
REMARK   3      T33:   0.0127 T12:   0.0519                                     
REMARK   3      T13:  -0.0233 T23:   0.0385                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4820 L22:   1.7501                                     
REMARK   3      L33:   4.9226 L12:  -0.2542                                     
REMARK   3      L13:  -2.2317 L23:   0.3816                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2220 S12:  -0.4239 S13:  -0.1873                       
REMARK   3      S21:   0.3580 S22:   0.0167 S23:  -0.0867                       
REMARK   3      S31:  -0.0427 S32:   0.3579 S33:   0.2053                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   193        B   264                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.8450  27.2170  10.2430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2765 T22:   0.5601                                     
REMARK   3      T33:   0.1197 T12:   0.0046                                     
REMARK   3      T13:  -0.0065 T23:  -0.0183                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5299 L22:   1.0621                                     
REMARK   3      L33:   1.4887 L12:  -0.0841                                     
REMARK   3      L13:  -0.2043 L23:  -0.4517                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0337 S12:  -0.0073 S13:   0.0478                       
REMARK   3      S21:   0.0442 S22:  -0.0479 S23:  -0.0776                       
REMARK   3      S31:  -0.1424 S32:   0.0126 S33:   0.0816                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   265        B   344                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7530  28.0980   9.7510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2864 T22:   0.5287                                     
REMARK   3      T33:   0.1135 T12:   0.0062                                     
REMARK   3      T13:  -0.0013 T23:  -0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0341 L22:   1.4084                                     
REMARK   3      L33:   1.9054 L12:  -0.0064                                     
REMARK   3      L13:  -0.1096 L23:  -0.3782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0189 S12:  -0.0466 S13:   0.0674                       
REMARK   3      S21:  -0.0416 S22:  -0.0073 S23:   0.0570                       
REMARK   3      S31:  -0.2415 S32:  -0.1123 S33:   0.0262                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   W     1        W   403                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3880  13.5970  -6.5730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2260 T22:   0.5133                                     
REMARK   3      T33:   0.0436 T12:  -0.0195                                     
REMARK   3      T13:  -0.0023 T23:   0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0801 L22:   0.2213                                     
REMARK   3      L33:   0.5581 L12:  -0.1089                                     
REMARK   3      L13:  -0.0654 L23:   0.1934                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0172 S12:  -0.0029 S13:  -0.0272                       
REMARK   3      S21:   0.0663 S22:  -0.0043 S23:   0.0231                       
REMARK   3      S31:   0.0886 S32:  -0.0421 S33:   0.0215                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1H3I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  05-SEP-02.                 
REMARK 100 THE PDBE ID CODE IS EBI-11339.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794, 0.9394, 0.9800             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37053                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       33.04500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.07500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.41500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.07500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.04500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.41500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    GLY A   117  -  O    HOH A  2055              2.03            
REMARK 500   O    GLU B   279  -  ND2  ASN B   282              2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  55   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 136   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    GLU A 279   N   -  CA  -  C   ANGL. DEV. =  19.6 DEGREES          
REMARK 500    PRO A 280   C   -  N   -  CA  ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    VAL B 130   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES          
REMARK 500    ASP B 306   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 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    THR A 100       -4.33    -46.88                                   
REMARK 500    ARG A 152      -58.49   -132.79                                   
REMARK 500    GLU A 176       12.97     54.74                                   
REMARK 500    THR A 197     -164.51   -113.98                                   
REMARK 500    SER A 202      148.01    179.34                                   
REMARK 500    SER A 224      169.14    167.11                                   
REMARK 500    GLU A 279       -8.29    -37.34                                   
REMARK 500    CYS A 288       18.81   -148.16                                   
REMARK 500    HIS A 339       87.51   -167.20                                   
REMARK 500    ASP B  66       -1.49     74.93                                   
REMARK 500    ARG B 152      -48.33   -134.86                                   
REMARK 500    ASP B 194       69.22   -155.69                                   
REMARK 500    THR B 197     -164.64   -120.88                                   
REMARK 500    ILE B 223       43.03   -105.76                                   
REMARK 500    SER B 224      167.69    165.97                                   
REMARK 500    VAL B 277       78.33   -115.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A 279        22.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU B 279        17.3      L          L   OUTSIDE RANGE           
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 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                              MG A1345  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2149   O                                                      
REMARK 620 2 HOH A2133   O   156.8                                              
REMARK 620 3 HOH A2134   O    75.1  82.7                                        
REMARK 620 4 HOH A2147   O    90.4  78.5  78.4                                  
REMARK 620 5 HOH B2119   O    88.8  93.5  79.1 156.9                            
REMARK 620 6 HOH A2150   O    86.9 115.5 161.8 104.7  98.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1346  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 279   OE1                                                    
REMARK 620 2 GLU B 279   OE1 103.0                                              
REMARK 620 3 GLU A 279   OE2  44.8 143.0                                        
REMARK 620 4 GLU B 279   OE2 146.6  47.8 168.3                                  
REMARK 620 5 HIS A 283   NE2 107.0 126.3  86.5  85.9                            
REMARK 620 6 HIS B 283   NE2 113.8  94.0  86.9  87.7 112.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1346  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2128   O                                                      
REMARK 620 2 HOH B2123   O    87.2                                              
REMARK 620 3 HOH B2140   O   177.1  90.4                                        
REMARK 620 4 HOH B2143   O    80.9  92.7  97.6                                  
REMARK 620 5 HOH B2125   O    88.7  84.0  92.7 169.2                            
REMARK 620 6 HOH B2141   O    91.4 178.2  91.0  85.9  97.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1345                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG A1346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1346                 
DBREF  1H3I A   52   344  UNP    Q8WTS6   Q8WTS6         106    398             
DBREF  1H3I B   52   344  UNP    Q8WTS6   Q8WTS6         106    398             
SEQRES   1 A  293  PHE PHE PHE ASP GLY SER THR LEU GLU GLY TYR TYR VAL          
SEQRES   2 A  293  ASP ASP ALA LEU GLN GLY GLN GLY VAL TYR THR TYR GLU          
SEQRES   3 A  293  ASP GLY GLY VAL LEU GLN GLY THR TYR VAL ASP GLY GLU          
SEQRES   4 A  293  LEU ASN GLY PRO ALA GLN GLU TYR ASP THR ASP GLY ARG          
SEQRES   5 A  293  LEU ILE PHE LYS GLY GLN TYR LYS ASP ASN ILE ARG HIS          
SEQRES   6 A  293  GLY VAL CYS TRP ILE TYR TYR PRO ASP GLY GLY SER LEU          
SEQRES   7 A  293  VAL GLY GLU VAL ASN GLU ASP GLY GLU MET THR GLY GLU          
SEQRES   8 A  293  LYS ILE ALA TYR VAL TYR PRO ASP GLU ARG THR ALA LEU          
SEQRES   9 A  293  TYR GLY LYS PHE ILE ASP GLY GLU MET ILE GLU GLY LYS          
SEQRES  10 A  293  LEU ALA THR LEU MET SER THR GLU GLU GLY ARG PRO HIS          
SEQRES  11 A  293  PHE GLU LEU MET PRO GLY ASN SER VAL TYR HIS PHE ASP          
SEQRES  12 A  293  LYS SER THR SER SER CYS ILE SER THR ASN ALA LEU LEU          
SEQRES  13 A  293  PRO ASP PRO TYR GLU SER GLU ARG VAL TYR VAL ALA GLU          
SEQRES  14 A  293  SER LEU ILE SER SER ALA GLY GLU GLY LEU PHE SER LYS          
SEQRES  15 A  293  VAL ALA VAL GLY PRO ASN THR VAL MET SER PHE TYR ASN          
SEQRES  16 A  293  GLY VAL ARG ILE THR HIS GLN GLU VAL ASP SER ARG ASP          
SEQRES  17 A  293  TRP ALA LEU ASN GLY ASN THR LEU SER LEU ASP GLU GLU          
SEQRES  18 A  293  THR VAL ILE ASP VAL PRO GLU PRO TYR ASN HIS VAL SER          
SEQRES  19 A  293  LYS TYR CYS ALA SER LEU GLY HIS LYS ALA ASN HIS SER          
SEQRES  20 A  293  PHE THR PRO ASN CYS ILE TYR ASP MET PHE VAL HIS PRO          
SEQRES  21 A  293  ARG PHE GLY PRO ILE LYS CYS ILE ARG THR LEU ARG ALA          
SEQRES  22 A  293  VAL GLU ALA ASP GLU GLU LEU THR VAL ALA TYR GLY TYR          
SEQRES  23 A  293  ASP HIS SER PRO PRO GLY LYS                                  
SEQRES   1 B  293  PHE PHE PHE ASP GLY SER THR LEU GLU GLY TYR TYR VAL          
SEQRES   2 B  293  ASP ASP ALA LEU GLN GLY GLN GLY VAL TYR THR TYR GLU          
SEQRES   3 B  293  ASP GLY GLY VAL LEU GLN GLY THR TYR VAL ASP GLY GLU          
SEQRES   4 B  293  LEU ASN GLY PRO ALA GLN GLU TYR ASP THR ASP GLY ARG          
SEQRES   5 B  293  LEU ILE PHE LYS GLY GLN TYR LYS ASP ASN ILE ARG HIS          
SEQRES   6 B  293  GLY VAL CYS TRP ILE TYR TYR PRO ASP GLY GLY SER LEU          
SEQRES   7 B  293  VAL GLY GLU VAL ASN GLU ASP GLY GLU MET THR GLY GLU          
SEQRES   8 B  293  LYS ILE ALA TYR VAL TYR PRO ASP GLU ARG THR ALA LEU          
SEQRES   9 B  293  TYR GLY LYS PHE ILE ASP GLY GLU MET ILE GLU GLY LYS          
SEQRES  10 B  293  LEU ALA THR LEU MET SER THR GLU GLU GLY ARG PRO HIS          
SEQRES  11 B  293  PHE GLU LEU MET PRO GLY ASN SER VAL TYR HIS PHE ASP          
SEQRES  12 B  293  LYS SER THR SER SER CYS ILE SER THR ASN ALA LEU LEU          
SEQRES  13 B  293  PRO ASP PRO TYR GLU SER GLU ARG VAL TYR VAL ALA GLU          
SEQRES  14 B  293  SER LEU ILE SER SER ALA GLY GLU GLY LEU PHE SER LYS          
SEQRES  15 B  293  VAL ALA VAL GLY PRO ASN THR VAL MET SER PHE TYR ASN          
SEQRES  16 B  293  GLY VAL ARG ILE THR HIS GLN GLU VAL ASP SER ARG ASP          
SEQRES  17 B  293  TRP ALA LEU ASN GLY ASN THR LEU SER LEU ASP GLU GLU          
SEQRES  18 B  293  THR VAL ILE ASP VAL PRO GLU PRO TYR ASN HIS VAL SER          
SEQRES  19 B  293  LYS TYR CYS ALA SER LEU GLY HIS LYS ALA ASN HIS SER          
SEQRES  20 B  293  PHE THR PRO ASN CYS ILE TYR ASP MET PHE VAL HIS PRO          
SEQRES  21 B  293  ARG PHE GLY PRO ILE LYS CYS ILE ARG THR LEU ARG ALA          
SEQRES  22 B  293  VAL GLU ALA ASP GLU GLU LEU THR VAL ALA TYR GLY TYR          
SEQRES  23 B  293  ASP HIS SER PRO PRO GLY LYS                                  
HET     MG  A1345       1                                                       
HET     MG  A1346       1                                                       
HET     MG  B1346       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3   MG    3(MG 2+)                                                     
FORMUL   6  HOH   *344(H2 O1)                                                   
HELIX    1   1 ASP A  209  GLU A  214  1                                   6    
HELIX    2   2 THR A  251  ARG A  258  1                                   8    
HELIX    3   3 ASP A  259  ASN A  263  5                                   5    
HELIX    4   4 LEU A  291  ALA A  295  5                                   5    
HELIX    5   5 ASP B  209  GLU B  214  1                                   6    
HELIX    6   6 THR B  251  ARG B  258  1                                   8    
HELIX    7   7 ASP B  259  ASN B  263  5                                   5    
HELIX    8   8 LEU B  291  ALA B  295  5                                   5    
SHEET    1  AA10 GLY A  61  VAL A  64  0                                        
SHEET    2  AA10 ALA A  67  THR A  75 -1  O  ALA A  67   N  VAL A  64           
SHEET    3  AA10 VAL A  81  VAL A  87 -1  O  LEU A  82   N  TYR A  74           
SHEET    4  AA10 GLU A  90  TYR A  98 -1  O  GLU A  90   N  VAL A  87           
SHEET    5  AA10 LEU A 104  LYS A 111 -1  N  ILE A 105   O  GLU A  97           
SHEET    6  AA10 VAL A 118  TYR A 122 -1  O  TRP A 120   N  LYS A 107           
SHEET    7  AA10 SER A 128  GLU A 132 -1  O  LEU A 129   N  ILE A 121           
SHEET    8  AA10 GLY A 141  VAL A 147 -1  O  ALA A 145   N  VAL A 130           
SHEET    9  AA10 THR A 153  ILE A 160 -1  O  LEU A 155   N  TYR A 146           
SHEET   10  AA10 GLU A 163  SER A 174 -1  O  GLU A 163   N  ILE A 160           
SHEET    1  AB 6 GLY A  61  VAL A  64  0                                        
SHEET    2  AB 6 ALA A  67  THR A  75 -1  O  ALA A  67   N  VAL A  64           
SHEET    3  AB 6 VAL A  81  VAL A  87 -1  O  LEU A  82   N  TYR A  74           
SHEET    4  AB 6 GLU A  90  TYR A  98 -1  O  GLU A  90   N  VAL A  87           
SHEET    5  AB 6 LEU A 104  LYS A 111 -1  N  ILE A 105   O  GLU A  97           
SHEET    6  AB 6 ILE A 114  ARG A 115 -1  O  ILE A 114   N  LYS A 111           
SHEET    1  AC 4 VAL A 216  GLU A 220  0                                        
SHEET    2  AC 4 GLU A 228  SER A 232 -1  O  GLY A 229   N  ALA A 219           
SHEET    3  AC 4 GLU A 330  ALA A 334 -1  N  LEU A 331   O  LEU A 230           
SHEET    4  AC 4 ASN A 296  SER A 298  1  O  ASN A 296   N  VAL A 333           
SHEET    1  AD 3 VAL A 241  TYR A 245  0                                        
SHEET    2  AD 3 GLY A 314  THR A 321 -1  O  LYS A 317   N  TYR A 245           
SHEET    3  AD 3 CYS A 303  HIS A 310 -1  O  ILE A 304   N  ARG A 320           
SHEET    1  AE 3 VAL A 248  ILE A 250  0                                        
SHEET    2  AE 3 VAL A 274  ASP A 276 -1  O  VAL A 274   N  ILE A 250           
SHEET    3  AE 3 THR A 266  SER A 268 -1  O  LEU A 267   N  ILE A 275           
SHEET    1  BA10 TYR B  62  VAL B  64  0                                        
SHEET    2  BA10 ALA B  67  THR B  75 -1  O  ALA B  67   N  VAL B  64           
SHEET    3  BA10 VAL B  81  VAL B  87 -1  O  LEU B  82   N  TYR B  74           
SHEET    4  BA10 GLU B  90  TYR B  98 -1  O  GLU B  90   N  VAL B  87           
SHEET    5  BA10 LEU B 104  LYS B 111 -1  N  ILE B 105   O  GLU B  97           
SHEET    6  BA10 VAL B 118  TYR B 122 -1  O  TRP B 120   N  LYS B 107           
SHEET    7  BA10 SER B 128  GLU B 132 -1  O  LEU B 129   N  ILE B 121           
SHEET    8  BA10 GLY B 141  VAL B 147 -1  O  ALA B 145   N  VAL B 130           
SHEET    9  BA10 THR B 153  ILE B 160 -1  O  LEU B 155   N  TYR B 146           
SHEET   10  BA10 GLU B 163  THR B 175 -1  O  GLU B 163   N  ILE B 160           
SHEET    1  BB 6 TYR B  62  VAL B  64  0                                        
SHEET    2  BB 6 ALA B  67  THR B  75 -1  O  ALA B  67   N  VAL B  64           
SHEET    3  BB 6 VAL B  81  VAL B  87 -1  O  LEU B  82   N  TYR B  74           
SHEET    4  BB 6 GLU B  90  TYR B  98 -1  O  GLU B  90   N  VAL B  87           
SHEET    5  BB 6 LEU B 104  LYS B 111 -1  N  ILE B 105   O  GLU B  97           
SHEET    6  BB 6 ILE B 114  ARG B 115 -1  O  ILE B 114   N  LYS B 111           
SHEET    1  BC 4 VAL B 216  GLU B 220  0                                        
SHEET    2  BC 4 GLU B 228  SER B 232 -1  O  GLY B 229   N  ALA B 219           
SHEET    3  BC 4 GLU B 330  ALA B 334 -1  N  LEU B 331   O  LEU B 230           
SHEET    4  BC 4 ASN B 296  SER B 298  1  O  ASN B 296   N  VAL B 333           
SHEET    1  BD 3 VAL B 241  TYR B 245  0                                        
SHEET    2  BD 3 GLY B 314  THR B 321 -1  O  LYS B 317   N  TYR B 245           
SHEET    3  BD 3 CYS B 303  HIS B 310 -1  O  ILE B 304   N  ARG B 320           
SHEET    1  BE 3 VAL B 248  ILE B 250  0                                        
SHEET    2  BE 3 VAL B 274  ASP B 276 -1  O  VAL B 274   N  ILE B 250           
SHEET    3  BE 3 THR B 266  SER B 268 -1  O  LEU B 267   N  ILE B 275           
LINK        MG    MG A1345                 O   HOH A2149     1555   1555  2.11  
LINK        MG    MG A1345                 O   HOH A2133     1555   1555  2.01  
LINK        MG    MG A1345                 O   HOH A2134     1555   1555  2.19  
LINK        MG    MG A1345                 O   HOH A2147     1555   1555  2.02  
LINK        MG    MG A1345                 O   HOH B2119     1555   2554  1.91  
LINK        MG    MG A1345                 O   HOH A2150     1555   1555  2.61  
LINK        MG    MG A1346                 OE1 GLU A 279     1555   2555  1.70  
LINK        MG    MG A1346                 OE1 GLU B 279     1555   1555  1.96  
LINK        MG    MG A1346                 OE2 GLU A 279     1555   2555  3.04  
LINK        MG    MG A1346                 OE2 GLU B 279     1555   1555  2.94  
LINK        MG    MG A1346                 NE2 HIS A 283     1555   2555  1.98  
LINK        MG    MG A1346                 NE2 HIS B 283     1555   1555  2.01  
LINK        MG    MG B1346                 O   HOH B2123     1555   1555  1.89  
LINK        MG    MG B1346                 O   HOH B2140     1555   1555  2.03  
LINK        MG    MG B1346                 O   HOH B2143     1555   1555  2.10  
LINK        MG    MG B1346                 O   HOH B2125     1555   1555  1.81  
LINK        MG    MG B1346                 O   HOH B2141     1555   1555  1.91  
LINK        MG    MG B1346                 O   HOH A2128     1555   2555  1.93  
SITE     1 AC1  6 HOH A2133  HOH A2134  HOH A2147  HOH A2149                    
SITE     2 AC1  6 HOH A2150  HOH B2119                                          
SITE     1 AC2  4 GLU A 279  HIS A 283  GLU B 279  HIS B 283                    
SITE     1 AC3  6 HOH A2128  HOH B2123  HOH B2125  HOH B2140                    
SITE     2 AC3  6 HOH B2141  HOH B2143                                          
CRYST1   66.090   82.830  116.150  90.00  90.00  90.00 P 21 21 21    8          
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      0.015131  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012073  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008609        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system