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Database: PDB
Entry: 4MB1
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HEADER    HYDROLASE                               19-AUG-13   4MB1              
TITLE     THE STRUCTURE OF MALL MUTANT ENZYME G202P FROM BACILLUS SUBTILUS      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OLIGO-1,6-GLUCOSIDASE 1;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: DEXTRIN 6-ALPHA-D-GLUCANOHYDROLASE, OLIGOSACCHARIDE ALPHA-1,
COMPND   5 6-GLUCOSIDASE 1, SUCRASE-ISOMALTASE 1, ISOMALTASE 1;                 
COMPND   6 EC: 3.2.1.10;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;              
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: MALL, YVDL, BSU34560;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMID;                               
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PPROEX HTB                                
KEYWDS    TIM BARREL, ALPHA GLUCOSIDASE, HYDROLASE                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.K.HOBBS,W.JIAO,A.D.EASTER,E.J.PARKER,L.A.SCHIPPER,V.L.ARCUS         
REVDAT   3   28-FEB-24 4MB1    1       REMARK SEQADV LINK                       
REVDAT   2   27-NOV-13 4MB1    1       JRNL                                     
REVDAT   1   25-SEP-13 4MB1    0                                                
JRNL        AUTH   J.K.HOBBS,W.JIAO,A.D.EASTER,E.J.PARKER,L.A.SCHIPPER,         
JRNL        AUTH 2 V.L.ARCUS                                                    
JRNL        TITL   CHANGE IN HEAT CAPACITY FOR ENZYME CATALYSIS DETERMINES      
JRNL        TITL 2 TEMPERATURE DEPENDENCE OF ENZYME CATALYZED RATES.            
JRNL        REF    ACS CHEM.BIOL.                V.   8  2388 2013              
JRNL        REFN                   ISSN 1554-8929                               
JRNL        PMID   24015933                                                     
JRNL        DOI    10.1021/CB4005029                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 104495                         
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) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5251                            
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) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7169                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.69                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 353                          
REMARK   3   BIN FREE R VALUE                    : 0.2580                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4613                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9                                       
REMARK   3   SOLVENT ATOMS            : 498                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 10.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.37000                                             
REMARK   3    B22 (A**2) : 0.67000                                              
REMARK   3    B33 (A**2) : -0.16000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.18000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.064         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.066         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.040         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.772         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4788 ; 0.022 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4352 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6493 ; 2.142 ; 1.937       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10038 ; 0.962 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   571 ; 6.829 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   260 ;35.243 ;24.500       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   824 ;12.406 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;15.799 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   651 ; 0.142 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5481 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1166 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : 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     3        A   206                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6587 -15.9800  26.8146              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0720 T22:   0.0011                                     
REMARK   3      T33:   0.0779 T12:  -0.0027                                     
REMARK   3      T13:   0.0119 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5558 L22:   0.7990                                     
REMARK   3      L33:   0.6831 L12:  -0.1618                                     
REMARK   3      L13:   0.2192 L23:  -0.4107                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0366 S12:   0.0154 S13:  -0.0802                       
REMARK   3      S21:   0.0279 S22:  -0.0052 S23:   0.0429                       
REMARK   3      S31:   0.0513 S32:  -0.0067 S33:  -0.0314                       
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   207        A   214                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.2469 -13.6841  39.2847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1285 T22:   0.1471                                     
REMARK   3      T33:   0.2285 T12:  -0.0048                                     
REMARK   3      T13:  -0.0826 T23:  -0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7496 L22:   7.9025                                     
REMARK   3      L33:   6.6062 L12:  -0.7635                                     
REMARK   3      L13:   2.1198 L23:   4.2630                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0587 S12:   0.0619 S13:  -0.0418                       
REMARK   3      S21:   0.5645 S22:   0.2465 S23:  -0.9106                       
REMARK   3      S31:   0.1166 S32:   0.4423 S33:  -0.1878                       
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   215        A   240                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.3488 -16.7426  28.5404              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0924 T22:   0.0922                                     
REMARK   3      T33:   0.1319 T12:   0.0138                                     
REMARK   3      T13:  -0.0002 T23:   0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3944 L22:   4.2675                                     
REMARK   3      L33:   3.8413 L12:   0.4467                                     
REMARK   3      L13:   0.5359 L23:   2.6558                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0291 S12:  -0.0027 S13:  -0.0160                       
REMARK   3      S21:   0.0389 S22:   0.1227 S23:  -0.2967                       
REMARK   3      S31:  -0.0932 S32:   0.4415 S33:  -0.0936                       
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   241        A   388                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.7076  -1.5124  16.6449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0619 T22:   0.0236                                     
REMARK   3      T33:   0.0646 T12:   0.0051                                     
REMARK   3      T13:   0.0130 T23:   0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5082 L22:   0.7648                                     
REMARK   3      L33:   0.6655 L12:   0.2038                                     
REMARK   3      L13:   0.0360 L23:  -0.1318                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0238 S12:   0.0066 S13:  -0.0313                       
REMARK   3      S21:   0.0097 S22:  -0.0251 S23:  -0.0769                       
REMARK   3      S31:   0.0252 S32:   0.0792 S33:   0.0013                       
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 :   A   389        A   452                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9248   7.3571  28.3159              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0965 T22:   0.0106                                     
REMARK   3      T33:   0.0753 T12:  -0.0013                                     
REMARK   3      T13:   0.0319 T23:  -0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8149 L22:   0.2399                                     
REMARK   3      L33:   1.0355 L12:  -0.1688                                     
REMARK   3      L13:   0.9415 L23:  -0.1429                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0059 S12:  -0.1051 S13:   0.0845                       
REMARK   3      S21:   0.0847 S22:  -0.0107 S23:   0.0104                       
REMARK   3      S31:  -0.0895 S32:  -0.0309 S33:   0.0048                       
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 :   A   453        A   500                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.5638   3.6314   0.9020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1047 T22:   0.0484                                     
REMARK   3      T33:   0.0515 T12:   0.0020                                     
REMARK   3      T13:   0.0137 T23:   0.0166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4190 L22:   0.7271                                     
REMARK   3      L33:   0.9623 L12:  -0.4086                                     
REMARK   3      L13:  -0.7501 L23:   0.3932                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0416 S12:   0.2427 S13:  -0.0864                       
REMARK   3      S21:  -0.0637 S22:   0.0173 S23:  -0.0166                       
REMARK   3      S31:   0.0436 S32:  -0.0398 S33:   0.0242                       
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 :   A   501        A   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8100  10.0306  -4.2346              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1048 T22:   0.0575                                     
REMARK   3      T33:   0.0861 T12:  -0.0082                                     
REMARK   3      T13:   0.0248 T23:   0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0927 L22:   1.2363                                     
REMARK   3      L33:   2.3594 L12:  -0.3587                                     
REMARK   3      L13:  -0.6958 L23:   0.0734                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0032 S12:   0.1299 S13:   0.0552                       
REMARK   3      S21:  -0.1192 S22:   0.0751 S23:  -0.1204                       
REMARK   3      S31:  -0.0536 S32:   0.0314 S33:  -0.0719                       
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 :   A   538        A   543                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5374  15.8557  -8.6295              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7429 T22:   0.8039                                     
REMARK   3      T33:   0.6311 T12:   0.1697                                     
REMARK   3      T13:   0.1258 T23:   0.0736                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5699 L22:   0.4731                                     
REMARK   3      L33:   1.8700 L12:  -1.7346                                     
REMARK   3      L13:   3.4909 L23:  -0.9244                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5439 S12:   0.9266 S13:  -0.5635                       
REMARK   3      S21:  -0.1308 S22:  -0.2194 S23:   0.2416                       
REMARK   3      S31:   0.2167 S32:   0.4113 S33:  -0.3245                       
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 :   A   544        A   559                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.1211  13.2525  -2.8565              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1286 T22:   0.0710                                     
REMARK   3      T33:   0.1203 T12:  -0.0084                                     
REMARK   3      T13:   0.0065 T23:   0.0256                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8262 L22:   3.1558                                     
REMARK   3      L33:   7.2201 L12:  -0.4559                                     
REMARK   3      L13:  -1.0246 L23:   4.7392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0096 S12:   0.2110 S13:   0.0146                       
REMARK   3      S21:  -0.2193 S22:   0.1434 S23:  -0.0507                       
REMARK   3      S31:  -0.2893 S32:   0.1543 S33:  -0.1338                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES: WITH TLS ADDED                                  
REMARK   4                                                                      
REMARK   4 4MB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000081689.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-SEP-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.1.27                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 104533                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.992                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.08100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.3.0                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 7.5, 24% (W/V) PEG        
REMARK 280  4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       50.53500            
REMARK 290   SMTRY3   2  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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 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     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLU A   541                                                      
REMARK 465     ARG A   542                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 153    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 214    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 216    CB   CG   OD1  OD2                                  
REMARK 470     LYS A 517    CE   NZ                                             
REMARK 470     GLN A 540    CG   CD   OE1  NE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A  345   NZ                                                  
REMARK 480     LYS A  411   CD   CE   NZ                                        
REMARK 480     LYS A  478   CD   CE   NZ                                        
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   OD1  ASP A    85     O    HOH A  1013              1.86            
REMARK 500   OE1  GLU A   400     O    HOH A  1185              2.13            
REMARK 500   NE   ARG A   395     O    HOH A  1172              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 179   CZ    ARG A 179   NH1     0.096                       
REMARK 500    LYS A 345   CE    LYS A 345   NZ     -0.239                       
REMARK 500    GLN A 489   CD    GLN A 489   OE1     0.141                       
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    GLU A 112   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ASP A 123   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG A 179   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG A 179   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ASP A 209   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG A 225   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP A 285   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG A 313   CD  -  NE  -  CZ  ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG A 313   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 339   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 344   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    LYS A 345   CD  -  CE  -  NZ  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ASP A 379   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 386   CB  -  CG  -  OD1 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ARG A 395   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A 395   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    GLU A 396   OE1 -  CD  -  OE2 ANGL. DEV. =  11.1 DEGREES          
REMARK 500    LYS A 411   CG  -  CD  -  CE  ANGL. DEV. = -19.2 DEGREES          
REMARK 500    ASP A 428   CB  -  CG  -  OD1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ASP A 450   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 450   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ARG A 474   NE  -  CZ  -  NH1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    LYS A 478   CB  -  CG  -  CD  ANGL. DEV. =  16.7 DEGREES          
REMARK 500    ARG A 500   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    GLU A 516   CG  -  CD  -  OE1 ANGL. DEV. = -15.1 DEGREES          
REMARK 500    MET A 557   CG  -  SD  -  CE  ANGL. DEV. = -10.2 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                                                                      
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  18      -69.50    -94.55                                   
REMARK 500    SER A  55      141.63   -171.04                                   
REMARK 500    ASP A  66      113.79   -161.75                                   
REMARK 500    SER A 145      154.39     80.96                                   
REMARK 500    PHE A 163     -134.29   -103.98                                   
REMARK 500    VAL A 200       53.73     30.52                                   
REMARK 500    HIS A 217      -13.63    101.57                                   
REMARK 500    VAL A 244      -64.26   -132.36                                   
REMARK 500    GLU A 274     -103.29   -116.80                                   
REMARK 500    ASN A 291       53.47   -159.00                                   
REMARK 500    ARG A 344     -106.41   -124.65                                   
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                              CA A 602  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  20   OD1                                                    
REMARK 620 2 ASN A  22   OD1  85.6                                              
REMARK 620 3 ASP A  24   OD1  88.7  82.9                                        
REMARK 620 4 PHE A  26   O    86.8 169.3  89.4                                  
REMARK 620 5 ASP A  28   OD2  89.7  84.8 167.7 102.6                            
REMARK 620 6 HOH A 822   O   167.4  87.6  79.9  98.3 100.3                      
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 TRS A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 602                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4MAZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4M8U   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4M56   RELATED DB: PDB                                   
DBREF  4MB1 A    1   561  UNP    O06994   O16G1_BACSU      1    561             
SEQADV 4MB1 PRO A  202  UNP  O06994    GLY   202 ENGINEERED MUTATION            
SEQRES   1 A  561  MET SER GLU TRP TRP LYS GLU ALA VAL VAL TYR GLN ILE          
SEQRES   2 A  561  TYR PRO ARG SER PHE TYR ASP ALA ASN GLY ASP GLY PHE          
SEQRES   3 A  561  GLY ASP LEU GLN GLY VAL ILE GLN LYS LEU ASP TYR ILE          
SEQRES   4 A  561  LYS ASN LEU GLY ALA ASP VAL ILE TRP LEU SER PRO VAL          
SEQRES   5 A  561  PHE ASP SER PRO GLN ASP ASP ASN GLY TYR ASP ILE SER          
SEQRES   6 A  561  ASP TYR LYS ASN MET TYR GLU LYS PHE GLY THR ASN GLU          
SEQRES   7 A  561  ASP MET PHE GLN LEU ILE ASP GLU VAL HIS LYS ARG GLY          
SEQRES   8 A  561  MET LYS ILE VAL MET ASP LEU VAL VAL ASN HIS THR SER          
SEQRES   9 A  561  ASP GLU HIS ALA TRP PHE ALA GLU SER ARG LYS SER LYS          
SEQRES  10 A  561  ASP ASN PRO TYR ARG ASP TYR TYR LEU TRP LYS ASP PRO          
SEQRES  11 A  561  LYS PRO ASP GLY SER GLU PRO ASN ASN TRP GLY SER ILE          
SEQRES  12 A  561  PHE SER GLY SER ALA TRP THR TYR ASP GLU GLY THR GLY          
SEQRES  13 A  561  GLN TYR TYR LEU HIS TYR PHE SER LYS LYS GLN PRO ASP          
SEQRES  14 A  561  LEU ASN TRP GLU ASN GLU ALA VAL ARG ARG GLU VAL TYR          
SEQRES  15 A  561  ASP VAL MET ARG PHE TRP MET ASP ARG GLY VAL ASP GLY          
SEQRES  16 A  561  TRP ARG MET ASP VAL ILE PRO SER ILE SER LYS TYR THR          
SEQRES  17 A  561  ASP PHE PRO ASP TYR GLU THR ASP HIS SER ARG SER TYR          
SEQRES  18 A  561  ILE VAL GLY ARG TYR HIS SER ASN GLY PRO ARG LEU HIS          
SEQRES  19 A  561  GLU PHE ILE GLN GLU MET ASN ARG GLU VAL LEU SER HIS          
SEQRES  20 A  561  TYR ASP CYS MET THR VAL GLY GLU ALA ASN GLY SER ASP          
SEQRES  21 A  561  ILE GLU GLU ALA LYS LYS TYR THR ASP ALA SER ARG GLN          
SEQRES  22 A  561  GLU LEU ASN MET ILE PHE THR PHE GLU HIS MET ASP ILE          
SEQRES  23 A  561  ASP LYS GLU GLN ASN SER PRO ASN GLY LYS TRP GLN ILE          
SEQRES  24 A  561  LYS PRO PHE ASP LEU ILE ALA LEU LYS LYS THR MET THR          
SEQRES  25 A  561  ARG TRP GLN THR GLY LEU MET ASN VAL GLY TRP ASN THR          
SEQRES  26 A  561  LEU TYR PHE GLU ASN HIS ASP GLN PRO ARG VAL ILE SER          
SEQRES  27 A  561  ARG TRP GLY ASN ASP ARG LYS LEU ARG LYS GLU CYS ALA          
SEQRES  28 A  561  LYS ALA PHE ALA THR VAL LEU HIS GLY MET LYS GLY THR          
SEQRES  29 A  561  PRO PHE ILE TYR GLN GLY GLU GLU ILE GLY MET VAL ASN          
SEQRES  30 A  561  SER ASP MET PRO LEU GLU MET TYR ASP ASP LEU GLU ILE          
SEQRES  31 A  561  LYS ASN ALA TYR ARG GLU LEU VAL VAL GLU ASN LYS THR          
SEQRES  32 A  561  MET SER GLU LYS GLU PHE VAL LYS ALA VAL MET ILE LYS          
SEQRES  33 A  561  GLY ARG ASP HIS ALA ARG THR PRO MET GLN TRP ASP ALA          
SEQRES  34 A  561  GLY LYS HIS ALA GLY PHE THR ALA GLY ASP PRO TRP ILE          
SEQRES  35 A  561  PRO VAL ASN SER ARG TYR GLN ASP ILE ASN VAL LYS GLU          
SEQRES  36 A  561  SER LEU GLU ASP GLN ASP SER ILE PHE PHE TYR TYR GLN          
SEQRES  37 A  561  LYS LEU ILE GLN LEU ARG LYS GLN TYR LYS ILE MET ILE          
SEQRES  38 A  561  TYR GLY ASP TYR GLN LEU LEU GLN GLU ASN ASP PRO GLN          
SEQRES  39 A  561  VAL PHE SER TYR LEU ARG GLU TYR ARG GLY GLU LYS LEU          
SEQRES  40 A  561  LEU VAL VAL VAL ASN LEU SER GLU GLU LYS ALA LEU PHE          
SEQRES  41 A  561  GLU ALA PRO PRO GLU LEU ILE HIS GLU ARG TRP LYS VAL          
SEQRES  42 A  561  LEU ILE SER ASN TYR PRO GLN GLU ARG ALA ASP LEU LYS          
SEQRES  43 A  561  SER ILE SER LEU LYS PRO TYR GLU ALA VAL MET GLY ILE          
SEQRES  44 A  561  SER ILE                                                      
HET    TRS  A 601       8                                                       
HET     CA  A 602       1                                                       
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETNAM      CA CALCIUM ION                                                      
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   2  TRS    C4 H12 N O3 1+                                               
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *498(H2 O)                                                    
HELIX    1   1 TYR A   14  PHE A   18  5                                   5    
HELIX    2   2 ASP A   28  GLY A   43  1                                  16    
HELIX    3   3 THR A   76  ARG A   90  1                                  15    
HELIX    4   4 HIS A  107  ARG A  114  1                                   8    
HELIX    5   5 TYR A  121  TYR A  125  5                                   5    
HELIX    6   6 ASN A  174  ARG A  191  1                                  18    
HELIX    7   7 VAL A  200  ILE A  204  5                                   5    
HELIX    8   8 GLY A  224  SER A  228  5                                   5    
HELIX    9   9 ARG A  232  VAL A  244  1                                  13    
HELIX   10  10 LEU A  245  TYR A  248  5                                   4    
HELIX   11  11 ASP A  260  ASP A  269  1                                  10    
HELIX   12  12 ALA A  270  GLN A  273  5                                   4    
HELIX   13  13 ASN A  294  GLN A  298  5                                   5    
HELIX   14  14 ASP A  303  LEU A  318  1                                  16    
HELIX   15  15 ARG A  335  GLY A  341  1                                   7    
HELIX   16  16 LEU A  346  GLY A  360  1                                  15    
HELIX   17  17 GLY A  370  GLY A  374  5                                   5    
HELIX   18  18 PRO A  381  TYR A  385  5                                   5    
HELIX   19  19 ASP A  387  VAL A  398  1                                  12    
HELIX   20  20 SER A  405  GLY A  417  1                                  13    
HELIX   21  21 ARG A  418  ARG A  422  5                                   5    
HELIX   22  22 GLY A  430  PHE A  435  5                                   6    
HELIX   23  23 ASN A  452  ASP A  459  1                                   8    
HELIX   24  24 SER A  462  TYR A  477  1                                  16    
HELIX   25  25 LYS A  478  GLY A  483  1                                   6    
HELIX   26  26 PRO A  523  ILE A  527  5                                   5    
SHEET    1   A 8 MET A 277  PHE A 279  0                                        
SHEET    2   A 8 MET A 251  GLU A 255  1  N  GLY A 254   O  PHE A 279           
SHEET    3   A 8 GLY A 195  MET A 198  1  N  MET A 198   O  VAL A 253           
SHEET    4   A 8 LYS A  93  LEU A  98  1  N  LEU A  98   O  ARG A 197           
SHEET    5   A 8 VAL A  46  LEU A  49  1  N  ILE A  47   O  VAL A  95           
SHEET    6   A 8 VAL A  10  ILE A  13  1  N  TYR A  11   O  VAL A  46           
SHEET    7   A 8 THR A 364  TYR A 368  1  O  ILE A 367   N  VAL A  10           
SHEET    8   A 8 THR A 325  LEU A 326  1  N  LEU A 326   O  PHE A 366           
SHEET    1   B 2 PHE A  53  ASP A  54  0                                        
SHEET    2   B 2 ASP A  66  MET A  70 -1  O  ASN A  69   N  ASP A  54           
SHEET    1   C 3 TRP A 127  LYS A 128  0                                        
SHEET    2   C 3 GLN A 157  LEU A 160 -1  O  TYR A 158   N  LYS A 128           
SHEET    3   C 3 TRP A 149  ASP A 152 -1  N  ASP A 152   O  GLN A 157           
SHEET    1   D 5 GLN A 486  LEU A 488  0                                        
SHEET    2   D 5 VAL A 495  TYR A 502 -1  O  SER A 497   N  LEU A 488           
SHEET    3   D 5 GLU A 505  ASN A 512 -1  O  VAL A 511   N  PHE A 496           
SHEET    4   D 5 ALA A 555  SER A 560 -1  O  VAL A 556   N  VAL A 510           
SHEET    5   D 5 TRP A 531  SER A 536 -1  N  LYS A 532   O  ILE A 559           
SHEET    1   E 2 ALA A 518  GLU A 521  0                                        
SHEET    2   E 2 SER A 547  LEU A 550 -1  O  ILE A 548   N  PHE A 520           
LINK         OD1 ASP A  20                CA    CA A 602     1555   1555  2.27  
LINK         OD1 ASN A  22                CA    CA A 602     1555   1555  2.32  
LINK         OD1 ASP A  24                CA    CA A 602     1555   1555  2.38  
LINK         O   PHE A  26                CA    CA A 602     1555   1555  2.27  
LINK         OD2 ASP A  28                CA    CA A 602     1555   1555  2.31  
LINK        CA    CA A 602                 O   HOH A 822     1555   1555  2.31  
SITE     1 AC1 11 ASP A  59  TYR A  62  HIS A 102  PHE A 144                    
SITE     2 AC1 11 PHE A 163  ASP A 199  GLU A 255  ARG A 418                    
SITE     3 AC1 11 HOH A 717  HOH A 719  HOH A1179                               
SITE     1 AC2  6 ASP A  20  ASN A  22  ASP A  24  PHE A  26                    
SITE     2 AC2  6 ASP A  28  HOH A 822                                          
CRYST1   48.500  101.070   61.850  90.00 112.86  90.00 P 1 21 1      2          
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      0.020619  0.000000  0.008693        0.00000                         
SCALE2      0.000000  0.009894  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017546        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system