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Database: PDB
Entry: 3ISM
LinkDB: 3ISM
Original site: 3ISM 
HEADER    HYDROLASE INHIBITOR/HYDROLASE           26-AUG-09   3ISM              
TITLE     CRYSTAL STRUCTURE OF THE ENDOG/ENDOGI COMPLEX: MECHANISM OF ENDOG     
TITLE    2 INHIBITION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CG8862;                                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 56-310;                                       
COMPND   5 SYNONYM: ENDONUCLEASE G, ENDOG, LD35517P;                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CG4930;                                                    
COMPND   9 CHAIN: C;                                                            
COMPND  10 SYNONYM: ENDOGI, SD16985P;                                           
COMPND  11 EC: 3.6.1.3;                                                         
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
SOURCE   5 GENE: CG8862, DMEL_CG8862, ENDOG;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C43(DE3);                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21D;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE  13 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE  14 ORGANISM_TAXID: 7227;                                                
SOURCE  15 GENE: ENDOGI, BG:DS07473.2, CG4930, DMEL_CG4930;                     
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: C43(DE3);                                  
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET21D                                    
KEYWDS    ENDONUCLEASE, ENDONUCLEASE INHIBITOR COMPLEX, METAL COMPLEX,          
KEYWDS   2 HYDROLASE, HYDROLASE INHIBITOR-HYDROLASE COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.LOLL,M.GEBHARDT,E.WAHLE,A.MEINHART                                  
REVDAT   5   01-NOV-23 3ISM    1       REMARK                                   
REVDAT   4   10-NOV-21 3ISM    1       REMARK SEQADV LINK                       
REVDAT   3   13-JUL-11 3ISM    1       VERSN                                    
REVDAT   2   02-FEB-11 3ISM    1       JRNL                                     
REVDAT   1   08-SEP-09 3ISM    0                                                
JRNL        AUTH   B.LOLL,M.GEBHARDT,E.WAHLE,A.MEINHART                         
JRNL        TITL   CRYSTAL STRUCTURE OF THE ENDOG/ENDOGI COMPLEX: MECHANISM OF  
JRNL        TITL 2 ENDOG INHIBITION.                                            
JRNL        REF    NUCLEIC ACIDS RES.            V.  37  7312 2009              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   19783821                                                     
JRNL        DOI    10.1093/NAR/GKP770                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 45828                          
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) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2412                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3325                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 175                          
REMARK   3   BIN FREE R VALUE                    : 0.2310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6299                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 328                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 38.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.91000                                             
REMARK   3    B22 (A**2) : 0.37000                                              
REMARK   3    B33 (A**2) : 0.54000                                              
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): 0.248         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.192         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.128         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.380         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6611 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8994 ; 1.150 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   818 ; 5.896 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   351 ;31.428 ;23.761       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1112 ;14.109 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    51 ;18.608 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   951 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5184 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2975 ; 0.179 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4472 ; 0.304 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   757 ; 0.167 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.074 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    41 ; 0.150 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.236 ; 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):  4066 ; 0.533 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6429 ; 0.878 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2900 ; 1.378 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2542 ; 2.030 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    67        A    90                          
REMARK   3    RESIDUE RANGE :   B    65        B    90                          
REMARK   3    ORIGIN FOR THE GROUP (A): -36.6570 -37.5862   9.7591              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1299 T22:   0.0335                                     
REMARK   3      T33:  -0.0347 T12:  -0.0248                                     
REMARK   3      T13:  -0.0231 T23:  -0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8226 L22:   2.4607                                     
REMARK   3      L33:   3.9245 L12:  -0.1361                                     
REMARK   3      L13:  -0.1889 L23:  -3.0449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0391 S12:  -0.1066 S13:  -0.0711                       
REMARK   3      S21:  -0.1113 S22:  -0.0320 S23:   0.4865                       
REMARK   3      S31:   0.3028 S32:  -0.0162 S33:  -0.0071                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    91        A   311                          
REMARK   3    RESIDUE RANGE :   B    91        B   311                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.9544 -37.8831  13.8288              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2317 T22:  -0.1255                                     
REMARK   3      T33:  -0.1951 T12:  -0.0005                                     
REMARK   3      T13:  -0.0163 T23:  -0.0144                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8963 L22:   2.1689                                     
REMARK   3      L33:   1.2657 L12:   0.4545                                     
REMARK   3      L13:  -0.2030 L23:  -0.6744                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0022 S12:  -0.0461 S13:  -0.0495                       
REMARK   3      S21:   0.0373 S22:   0.0387 S23:   0.0114                       
REMARK   3      S31:   0.1234 S32:  -0.0621 S33:  -0.0365                       
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 :   C    21        C    48                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.4390  -8.6385  38.5849              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0228 T22:   0.0331                                     
REMARK   3      T33:   0.0151 T12:  -0.0316                                     
REMARK   3      T13:   0.0411 T23:   0.0270                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.1000 L22:  11.6546                                     
REMARK   3      L33:   9.1676 L12:   6.9412                                     
REMARK   3      L13:   1.3458 L23:   1.0511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4222 S12:  -0.8898 S13:  -0.4457                       
REMARK   3      S21:   0.8194 S22:  -0.4351 S23:   0.4712                       
REMARK   3      S31:   0.4476 S32:  -0.5885 S33:   0.0129                       
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 :   C    49        C   174                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3314   0.0046  23.1348              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0569 T22:  -0.0918                                     
REMARK   3      T33:  -0.0467 T12:   0.0018                                     
REMARK   3      T13:   0.0166 T23:  -0.0311                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7572 L22:   2.2423                                     
REMARK   3      L33:   1.8696 L12:   0.9993                                     
REMARK   3      L13:   0.1975 L23:   0.1852                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0809 S12:   0.0278 S13:   0.0910                       
REMARK   3      S21:  -0.1321 S22:   0.0726 S23:  -0.1112                       
REMARK   3      S31:  -0.2346 S32:   0.1284 S33:   0.0083                       
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 :   C   219        C   274                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.3325 -75.1461  -0.3549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2486 T22:   0.1945                                     
REMARK   3      T33:   0.1520 T12:   0.0021                                     
REMARK   3      T13:   0.0313 T23:  -0.0471                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.3852 L22:  26.3459                                     
REMARK   3      L33:  14.7836 L12: -10.0861                                     
REMARK   3      L13:   4.5175 L23:  -4.5964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0948 S12:   0.3209 S13:   0.0997                       
REMARK   3      S21:  -0.5330 S22:  -0.3902 S23:  -0.7682                       
REMARK   3      S31:  -0.5427 S32:   0.0560 S33:   0.4850                       
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 :   C   275        C   354                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.1249 -79.3061  14.9819              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2398 T22:   0.0747                                     
REMARK   3      T33:   0.1781 T12:  -0.0619                                     
REMARK   3      T13:  -0.0635 T23:   0.0739                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1324 L22:  12.5569                                     
REMARK   3      L33:   2.9862 L12:  -2.4272                                     
REMARK   3      L13:   1.1477 L23:   1.6759                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1757 S12:  -0.1067 S13:  -0.2258                       
REMARK   3      S21:   0.2185 S22:   0.0229 S23:  -0.2127                       
REMARK   3      S31:   0.5108 S32:  -0.2280 S33:  -0.1986                       
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   : 1.20                                          
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 3ISM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-AUG-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054814.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0075                             
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46364                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.230                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.9                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.18400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.20100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
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: 2O3B                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V)PEG 2000 MME, PH 8.5, VAPOR      
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
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       35.39500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.54000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.57500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.54000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.39500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.57500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    55                                                      
REMARK 465     LEU A    56                                                      
REMARK 465     ILE A    57                                                      
REMARK 465     PRO A    58                                                      
REMARK 465     ALA A    59                                                      
REMARK 465     GLN A    60                                                      
REMARK 465     GLU A    61                                                      
REMARK 465     ASN A    62                                                      
REMARK 465     ASN A    63                                                      
REMARK 465     VAL A    64                                                      
REMARK 465     SER A    65                                                      
REMARK 465     LEU A    66                                                      
REMARK 465     ALA A   312                                                      
REMARK 465     ALA A   313                                                      
REMARK 465     LEU A   314                                                      
REMARK 465     GLU A   315                                                      
REMARK 465     HIS A   316                                                      
REMARK 465     HIS A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     HIS A   319                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     MET B    55                                                      
REMARK 465     LEU B    56                                                      
REMARK 465     ILE B    57                                                      
REMARK 465     PRO B    58                                                      
REMARK 465     ALA B    59                                                      
REMARK 465     GLN B    60                                                      
REMARK 465     GLU B    61                                                      
REMARK 465     ASN B    62                                                      
REMARK 465     ASN B    63                                                      
REMARK 465     VAL B    64                                                      
REMARK 465     ALA B   312                                                      
REMARK 465     ALA B   313                                                      
REMARK 465     LEU B   314                                                      
REMARK 465     GLU B   315                                                      
REMARK 465     HIS B   316                                                      
REMARK 465     HIS B   317                                                      
REMARK 465     HIS B   318                                                      
REMARK 465     HIS B   319                                                      
REMARK 465     HIS B   320                                                      
REMARK 465     HIS B   321                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     LYS C     3                                                      
REMARK 465     ARG C     4                                                      
REMARK 465     LYS C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     GLU C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     THR C     9                                                      
REMARK 465     GLN C    10                                                      
REMARK 465     SER C    11                                                      
REMARK 465     ASP C    12                                                      
REMARK 465     LYS C    13                                                      
REMARK 465     MET C    14                                                      
REMARK 465     ALA C    15                                                      
REMARK 465     THR C    16                                                      
REMARK 465     ALA C    17                                                      
REMARK 465     GLU C    18                                                      
REMARK 465     LYS C    19                                                      
REMARK 465     VAL C    20                                                      
REMARK 465     ALA C   175                                                      
REMARK 465     ALA C   176                                                      
REMARK 465     LEU C   177                                                      
REMARK 465     GLU C   178                                                      
REMARK 465     GLU C   179                                                      
REMARK 465     GLN C   180                                                      
REMARK 465     ALA C   181                                                      
REMARK 465     SER C   182                                                      
REMARK 465     LEU C   183                                                      
REMARK 465     ASP C   184                                                      
REMARK 465     GLN C   185                                                      
REMARK 465     ASP C   186                                                      
REMARK 465     GLY C   187                                                      
REMARK 465     PRO C   188                                                      
REMARK 465     ALA C   189                                                      
REMARK 465     THR C   190                                                      
REMARK 465     PRO C   191                                                      
REMARK 465     THR C   192                                                      
REMARK 465     THR C   193                                                      
REMARK 465     PRO C   194                                                      
REMARK 465     GLY C   195                                                      
REMARK 465     GLU C   196                                                      
REMARK 465     LEU C   197                                                      
REMARK 465     SER C   198                                                      
REMARK 465     ALA C   199                                                      
REMARK 465     ASP C   200                                                      
REMARK 465     ASP C   201                                                      
REMARK 465     ALA C   202                                                      
REMARK 465     ALA C   203                                                      
REMARK 465     ALA C   204                                                      
REMARK 465     LEU C   205                                                      
REMARK 465     SER C   206                                                      
REMARK 465     GLY C   207                                                      
REMARK 465     GLU C   208                                                      
REMARK 465     PHE C   209                                                      
REMARK 465     GLU C   210                                                      
REMARK 465     ALA C   211                                                      
REMARK 465     THR C   212                                                      
REMARK 465     LEU C   213                                                      
REMARK 465     THR C   214                                                      
REMARK 465     LYS C   215                                                      
REMARK 465     GLU C   216                                                      
REMARK 465     ASN C   217                                                      
REMARK 465     PRO C   218                                                      
REMARK 465     LEU C   231                                                      
REMARK 465     THR C   232                                                      
REMARK 465     LYS C   233                                                      
REMARK 465     GLY C   354                                                      
REMARK 465     PRO C   355                                                      
REMARK 465     VAL C   356                                                      
REMARK 465     ASN C   357                                                      
REMARK 465     ASP C   358                                                      
REMARK 465     ASP C   359                                                      
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    PHE A 186      -94.31   -147.15                                   
REMARK 500    ASP A 189     -100.57   -131.45                                   
REMARK 500    ASP A 222      -31.73    -37.29                                   
REMARK 500    MET B  77       30.71    -94.08                                   
REMARK 500    ASP B  92       11.76   -145.22                                   
REMARK 500    PHE B 186      -91.11   -153.52                                   
REMARK 500    ASP B 189     -102.65   -129.58                                   
REMARK 500    ASP C 103       74.00   -166.24                                   
REMARK 500    VAL C 130      -69.57   -103.90                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A   1  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A   2   O                                                      
REMARK 620 2 HOH A   3   O    97.4                                              
REMARK 620 3 HOH A   4   O   164.6  97.6                                        
REMARK 620 4 HOH A   5   O    91.0  86.9  86.4                                  
REMARK 620 5 HOH A   6   O    84.5 178.1  80.5  92.7                            
REMARK 620 6 ASN A 187   OD1  99.3  86.4  85.1 168.4  93.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B   1  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B   2   O                                                      
REMARK 620 2 HOH B   3   O   101.3                                              
REMARK 620 3 HOH B   4   O   166.4  88.7                                        
REMARK 620 4 HOH B   5   O    99.7  89.3  89.6                                  
REMARK 620 5 ASN B 187   OD1  87.9  77.3  85.2 165.7                            
REMARK 620 6 HOH C 360   O    85.1 172.7  84.5  93.1  99.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 6989                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2O3B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE COMPLEX OF NUCLEASE A (NUCA) WITH INTRA-CELLULAR   
REMARK 900 INHIBITOR NUIA                                                       
REMARK 900 RELATED ID: 1ZM8   RELATED DB: PDB                                   
REMARK 900 APO CRYSTAL STRUCTURE OF NUCLEASE A FROM ANABAENA SP.                
REMARK 900 RELATED ID: 1QAE   RELATED DB: PDB                                   
REMARK 900 THE ACTIVE SITE OF SERRATIA ENDONUCLEASE CONTAINS A CONSERVED        
REMARK 900 MAGNESIUM-WATER CLUSTER                                              
DBREF  3ISM A   56   310  UNP    Q7JXB9   Q7JXB9_DROME    56    310             
DBREF  3ISM B   56   310  UNP    Q7JXB9   Q7JXB9_DROME    56    310             
DBREF  3ISM C    1   359  UNP    Q9V3V9   Q9V3V9_DROME     1    359             
SEQADV 3ISM MET A   55  UNP  Q7JXB9              INITIATING METHIONINE          
SEQADV 3ISM ALA A  311  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM ALA A  312  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM ALA A  313  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM LEU A  314  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM GLU A  315  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS A  316  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS A  317  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS A  318  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS A  319  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS A  320  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS A  321  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM MET B   55  UNP  Q7JXB9              INITIATING METHIONINE          
SEQADV 3ISM ALA B  311  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM ALA B  312  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM ALA B  313  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM LEU B  314  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM GLU B  315  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS B  316  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS B  317  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS B  318  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS B  319  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS B  320  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM HIS B  321  UNP  Q7JXB9              EXPRESSION TAG                 
SEQADV 3ISM ALA C    2  UNP  Q9V3V9    SER     2 ENGINEERED MUTATION            
SEQRES   1 A  267  MET LEU ILE PRO ALA GLN GLU ASN ASN VAL SER LEU THR          
SEQRES   2 A  267  ALA THR PRO SER ARG ILE GLY GLN ILE MET LYS TYR GLY          
SEQRES   3 A  267  PHE PRO GLY LEU ASP HIS VAL ARG SER HIS SER ASP TYR          
SEQRES   4 A  267  VAL LEU SER TYR ASP ARG ARG ASN ARG VAL PRO HIS TRP          
SEQRES   5 A  267  VAL PHE GLU HIS LEU THR ALA GLU SER VAL ALA LYS ASN          
SEQRES   6 A  267  ASP ALA VAL ASP ARG SER LYS CYS ASP PHE LYS GLN ASP          
SEQRES   7 A  267  GLU SER ILE HIS PRO PHE PHE ARG SER GLN ASN THR ASP          
SEQRES   8 A  267  TYR ARG ARG SER GLY TYR ASP ARG GLY HIS MET ALA ALA          
SEQRES   9 A  267  ALA GLY ASN HIS ARG LEU HIS GLN LYS HIS CYS ASP GLU          
SEQRES  10 A  267  THR PHE TYR LEU SER ASN MET ALA PRO GLN VAL GLY GLN          
SEQRES  11 A  267  GLY PHE ASN ARG ASP ALA TRP ASN THR LEU GLU ALA HIS          
SEQRES  12 A  267  VAL ARG ARG LEU THR LYS THR TYR SER ASN VAL TYR VAL          
SEQRES  13 A  267  CYS THR GLY PRO LEU TYR LEU PRO HIS LYS GLU ASP ASP          
SEQRES  14 A  267  GLY LYS SER TYR VAL LYS TYR GLU VAL ILE GLY ALA ASN          
SEQRES  15 A  267  THR VAL ALA VAL PRO THR HIS PHE TYR LYS VAL ILE VAL          
SEQRES  16 A  267  GLY GLU SER ALA ASP HIS LYS LEU HIS MET GLU SER TYR          
SEQRES  17 A  267  VAL MET PRO ASN GLN VAL ILE SER ASN ASP THR PRO ILE          
SEQRES  18 A  267  SER VAL PHE GLN VAL PRO PRO GLU SER VAL GLU ARG SER          
SEQRES  19 A  267  ALA GLY LEU LEU PHE PHE ASP GLN ILE ASN ARG LYS GLN          
SEQRES  20 A  267  LEU THR THR ILE ASN GLY LYS LYS VAL ALA ALA ALA LEU          
SEQRES  21 A  267  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  267  MET LEU ILE PRO ALA GLN GLU ASN ASN VAL SER LEU THR          
SEQRES   2 B  267  ALA THR PRO SER ARG ILE GLY GLN ILE MET LYS TYR GLY          
SEQRES   3 B  267  PHE PRO GLY LEU ASP HIS VAL ARG SER HIS SER ASP TYR          
SEQRES   4 B  267  VAL LEU SER TYR ASP ARG ARG ASN ARG VAL PRO HIS TRP          
SEQRES   5 B  267  VAL PHE GLU HIS LEU THR ALA GLU SER VAL ALA LYS ASN          
SEQRES   6 B  267  ASP ALA VAL ASP ARG SER LYS CYS ASP PHE LYS GLN ASP          
SEQRES   7 B  267  GLU SER ILE HIS PRO PHE PHE ARG SER GLN ASN THR ASP          
SEQRES   8 B  267  TYR ARG ARG SER GLY TYR ASP ARG GLY HIS MET ALA ALA          
SEQRES   9 B  267  ALA GLY ASN HIS ARG LEU HIS GLN LYS HIS CYS ASP GLU          
SEQRES  10 B  267  THR PHE TYR LEU SER ASN MET ALA PRO GLN VAL GLY GLN          
SEQRES  11 B  267  GLY PHE ASN ARG ASP ALA TRP ASN THR LEU GLU ALA HIS          
SEQRES  12 B  267  VAL ARG ARG LEU THR LYS THR TYR SER ASN VAL TYR VAL          
SEQRES  13 B  267  CYS THR GLY PRO LEU TYR LEU PRO HIS LYS GLU ASP ASP          
SEQRES  14 B  267  GLY LYS SER TYR VAL LYS TYR GLU VAL ILE GLY ALA ASN          
SEQRES  15 B  267  THR VAL ALA VAL PRO THR HIS PHE TYR LYS VAL ILE VAL          
SEQRES  16 B  267  GLY GLU SER ALA ASP HIS LYS LEU HIS MET GLU SER TYR          
SEQRES  17 B  267  VAL MET PRO ASN GLN VAL ILE SER ASN ASP THR PRO ILE          
SEQRES  18 B  267  SER VAL PHE GLN VAL PRO PRO GLU SER VAL GLU ARG SER          
SEQRES  19 B  267  ALA GLY LEU LEU PHE PHE ASP GLN ILE ASN ARG LYS GLN          
SEQRES  20 B  267  LEU THR THR ILE ASN GLY LYS LYS VAL ALA ALA ALA LEU          
SEQRES  21 B  267  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 C  359  MET ALA LYS ARG LYS ALA GLU ASP THR GLN SER ASP LYS          
SEQRES   2 C  359  MET ALA THR ALA GLU LYS VAL ALA GLN ASN ASP TYR THR          
SEQRES   3 C  359  ILE GLY LEU VAL ASP PRO VAL LYS ASP TYR GLN LYS LEU          
SEQRES   4 C  359  ILE GLU THR ARG VAL GLN VAL ASP GLU ILE VAL ASP ASP          
SEQRES   5 C  359  ASP VAL THR LYS GLU ASN PHE ASP ARG THR ALA ALA ALA          
SEQRES   6 C  359  ALA ARG ASP VAL ILE TRP ARG LEU LEU PHE ASP GLU ALA          
SEQRES   7 C  359  GLY THR SER GLN SER ASN THR GLU LYS ALA SER GLN LEU          
SEQRES   8 C  359  LEU GLU GLU TYR ARG GLY ASP ALA CYS PHE TYR ASP PRO          
SEQRES   9 C  359  THR PRO TYR ASN GLU TRP ILE VAL LYS LEU ARG ASP GLU          
SEQRES  10 C  359  VAL LEU LYS LYS GLU LEU LEU ASP PHE TRP ARG ASP VAL          
SEQRES  11 C  359  LEU VAL LYS LYS GLN LEU GLY PRO CYS TRP SER ARG ASP          
SEQRES  12 C  359  SER ASP LEU PHE ASP SER ASP ASP THR PRO PRO LEU GLU          
SEQRES  13 C  359  PHE TYR ALA HIS ALA GLY CYS THR ALA PRO PHE ALA ALA          
SEQRES  14 C  359  SER LEU LYS VAL ARG ALA ALA LEU GLU GLU GLN ALA SER          
SEQRES  15 C  359  LEU ASP GLN ASP GLY PRO ALA THR PRO THR THR PRO GLY          
SEQRES  16 C  359  GLU LEU SER ALA ASP ASP ALA ALA ALA LEU SER GLY GLU          
SEQRES  17 C  359  PHE GLU ALA THR LEU THR LYS GLU ASN PRO LEU GLU GLU          
SEQRES  18 C  359  TYR ARG THR LEU MET LYS ARG PHE VAL LEU THR LYS ILE          
SEQRES  19 C  359  ILE VAL PRO ASP SER VAL HIS GLN ALA SER VAL LYS LYS          
SEQRES  20 C  359  ILE ALA ALA ALA ALA ARG GLU ILE ILE TRP LYS LEU LEU          
SEQRES  21 C  359  PHE ASP GLY THR PRO SER ALA GLU ASP GLN ASN LYS ALA          
SEQRES  22 C  359  ALA GLU LEU LEU GLN GLU TYR LYS GLY ASP ALA GLY PHE          
SEQRES  23 C  359  TYR GLY PRO ASP ASP TYR ASN SER TRP ILE PHE ASN LEU          
SEQRES  24 C  359  ARG ASP GLU VAL LEU THR LYS GLU LEU LEU ASP PHE TRP          
SEQRES  25 C  359  ARG ASP LYS MET VAL LYS MET GLU LEU GLY PRO SER CYS          
SEQRES  26 C  359  ALA ARG ASP SER ASP TYR TYR ASP ASN GLU ASP PRO LEU          
SEQRES  27 C  359  PRO PHE GLU PHE TYR GLU LYS ALA GLY CYS LYS ALA PRO          
SEQRES  28 C  359  PHE GLU GLY PRO VAL ASN ASP ASP                              
HET     MG  A   1       1                                                       
HET    TRS  A6989       8                                                       
HET     MG  B   1       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  TRS    C4 H12 N O3 1+                                               
FORMUL   7  HOH   *328(H2 O)                                                    
HELIX    1   1 SER A   71  MET A   77  1                                   7    
HELIX    2   2 ASP A  123  CYS A  127  5                                   5    
HELIX    3   3 HIS A  136  ARG A  140  5                                   5    
HELIX    4   4 GLN A  142  ARG A  147  1                                   6    
HELIX    5   5 ALA A  158  HIS A  162  5                                   5    
HELIX    6   6 HIS A  165  GLU A  171  1                                   7    
HELIX    7   7 THR A  172  SER A  176  5                                   5    
HELIX    8   8 ASP A  189  LEU A  201  1                                  13    
HELIX    9   9 THR A  202  THR A  204  5                                   3    
HELIX   10  10 PRO A  274  GLN A  279  5                                   6    
HELIX   11  11 PRO A  281  GLY A  290  1                                  10    
HELIX   12  12 THR B   69  MET B   77  1                                   9    
HELIX   13  13 THR B  112  ALA B  117  1                                   6    
HELIX   14  14 ASP B  123  CYS B  127  5                                   5    
HELIX   15  15 HIS B  136  ARG B  140  5                                   5    
HELIX   16  16 GLN B  142  ARG B  147  1                                   6    
HELIX   17  17 ALA B  158  HIS B  162  5                                   5    
HELIX   18  18 HIS B  165  GLU B  171  1                                   7    
HELIX   19  19 THR B  172  SER B  176  5                                   5    
HELIX   20  20 ASP B  189  LEU B  201  1                                  13    
HELIX   21  21 THR B  202  THR B  204  5                                   3    
HELIX   22  22 PRO B  274  GLN B  279  5                                   6    
HELIX   23  23 PRO B  281  GLY B  290  1                                  10    
HELIX   24  24 ASN B  298  LEU B  302  5                                   5    
HELIX   25  25 ASP C   31  VAL C   44  1                                  14    
HELIX   26  26 ASP C   51  ASP C   76  1                                  26    
HELIX   27  27 THR C   80  ASP C  103  1                                  24    
HELIX   28  28 ASP C  103  LYS C  121  1                                  19    
HELIX   29  29 LEU C  123  VAL C  130  1                                   8    
HELIX   30  30 LEU C  155  ALA C  159  5                                   5    
HELIX   31  31 PHE C  167  ARG C  174  1                                   8    
HELIX   32  32 LEU C  219  VAL C  230  1                                  12    
HELIX   33  33 PRO C  237  ASP C  262  1                                  26    
HELIX   34  34 SER C  266  GLY C  288  1                                  23    
HELIX   35  35 PRO C  289  LYS C  306  1                                  18    
HELIX   36  36 LEU C  308  LYS C  315  1                                   8    
HELIX   37  37 PRO C  339  GLU C  344  1                                   6    
SHEET    1   A 8 VAL A  87  SER A  89  0                                        
SHEET    2   A 8 VAL A  94  ASP A  98 -1  O  LEU A  95   N  ARG A  88           
SHEET    3   A 8 VAL A 103  LEU A 111 -1  O  TRP A 106   N  SER A  96           
SHEET    4   A 8 ASN A 207  LEU A 215 -1  O  VAL A 208   N  LEU A 111           
SHEET    5   A 8 HIS A 243  GLU A 251 -1  O  VAL A 249   N  TYR A 209           
SHEET    6   A 8 LEU A 257  PRO A 265 -1  O  GLU A 260   N  ILE A 248           
SHEET    7   A 8 THR A 304  ILE A 305  1  O  THR A 304   N  MET A 259           
SHEET    8   A 8 LYS A 308  LYS A 309 -1  O  LYS A 308   N  ILE A 305           
SHEET    1   B 2 ASP A 152  HIS A 155  0                                        
SHEET    2   B 2 MET A 178  GLN A 181 -1  O  GLN A 181   N  ASP A 152           
SHEET    1   C 4 PRO A 218  LYS A 220  0                                        
SHEET    2   C 4 SER A 226  ILE A 233 -1  O  TYR A 227   N  HIS A 219           
SHEET    3   C 4 SER B 226  ILE B 233 -1  O  VAL B 228   N  TYR A 230           
SHEET    4   C 4 HIS B 219  LYS B 220 -1  N  HIS B 219   O  TYR B 227           
SHEET    1   D 4 VAL A 238  ALA A 239  0                                        
SHEET    2   D 4 SER A 226  ILE A 233 -1  N  ILE A 233   O  VAL A 238           
SHEET    3   D 4 SER B 226  ILE B 233 -1  O  VAL B 228   N  TYR A 230           
SHEET    4   D 4 VAL B 238  ALA B 239 -1  O  VAL B 238   N  ILE B 233           
SHEET    1   E 8 VAL B  87  SER B  89  0                                        
SHEET    2   E 8 VAL B  94  ASP B  98 -1  O  LEU B  95   N  ARG B  88           
SHEET    3   E 8 VAL B 103  LEU B 111 -1  O  HIS B 105   N  SER B  96           
SHEET    4   E 8 ASN B 207  LEU B 215 -1  O  VAL B 208   N  LEU B 111           
SHEET    5   E 8 HIS B 243  GLU B 251 -1  O  VAL B 249   N  TYR B 209           
SHEET    6   E 8 LEU B 257  PRO B 265 -1  O  GLU B 260   N  ILE B 248           
SHEET    7   E 8 THR B 304  ILE B 305  1  O  THR B 304   N  MET B 259           
SHEET    8   E 8 LYS B 308  LYS B 309 -1  O  LYS B 308   N  ILE B 305           
SHEET    1   F 2 ASP B 152  HIS B 155  0                                        
SHEET    2   F 2 MET B 178  GLN B 181 -1  O  GLN B 181   N  ASP B 152           
LINK        MG    MG A   1                 O   HOH A   2     1555   1555  2.12  
LINK        MG    MG A   1                 O   HOH A   3     1555   1555  2.09  
LINK        MG    MG A   1                 O   HOH A   4     1555   1555  2.14  
LINK        MG    MG A   1                 O   HOH A   5     1555   1555  2.01  
LINK        MG    MG A   1                 O   HOH A   6     1555   1555  2.19  
LINK        MG    MG A   1                 OD1 ASN A 187     1555   1555  2.00  
LINK        MG    MG B   1                 O   HOH B   2     1555   1555  1.96  
LINK        MG    MG B   1                 O   HOH B   3     1555   1555  2.13  
LINK        MG    MG B   1                 O   HOH B   4     1555   1555  2.20  
LINK        MG    MG B   1                 O   HOH B   5     1555   1555  1.89  
LINK        MG    MG B   1                 OD1 ASN B 187     1555   1555  2.17  
LINK        MG    MG B   1                 O   HOH C 360     1555   1555  2.11  
SITE     1 AC1  6 HOH A   2  HOH A   3  HOH A   4  HOH A   5                    
SITE     2 AC1  6 HOH A   6  ASN A 187                                          
SITE     1 AC2  8 SER A 125  CYS A 127  ASP A 128  LYS C  56                    
SITE     2 AC2  8 ASP C 103  PRO C 104  THR C 105  LEU C 146                    
SITE     1 AC3  6 HOH B   2  HOH B   3  HOH B   4  HOH B   5                    
SITE     2 AC3  6 ASN B 187  HOH C 360                                          
CRYST1   70.790  109.150  121.080  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      0.014126  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009162  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008259        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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