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Database: PDB
Entry: 3BH4
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Original site: 3BH4 
HEADER    HYDROLASE                               28-NOV-07   3BH4              
TITLE     HIGH RESOLUTION CRYSTAL STRUCTURE OF BACILLUS                         
TITLE    2 AMYLOLIQUEFACIENS ALPHA-AMYLASE                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN GLUCANOHYDROLASE;                        
COMPND   5 EC: 3.2.1.1;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS AMYLOLIQUEFACIENS;                     
SOURCE   3 ORGANISM_TAXID: 1390                                                 
KEYWDS    CRYSTAL STRUCTURE ALPHA-AMYLASE, CALCIUM, CARBOHYDRATE                
KEYWDS   2 METABOLISM, GLYCOSIDASE, HYDROLASE, METAL-BINDING, SECRETED          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ALIKHAJEH,K.KHAJEH,B.RANJBAR,H.NADERI-MANESH,Y.H.LIN,               
AUTHOR   2 M.Y.LIU,C.J.CHEN                                                     
REVDAT   3   02-MAR-10 3BH4    1       JRNL                                     
REVDAT   2   13-JAN-09 3BH4    1       AUTHOR                                   
REVDAT   1   09-DEC-08 3BH4    0                                                
JRNL        AUTH   J.ALIKHAJEH,K.KHAJEH,B.RANJBAR,H.NADERI-MANESH,              
JRNL        AUTH 2 Y.H.LIN,E.LIU,H.H.GUAN,Y.C.HSIEH,P.CHUANKHAYAN,              
JRNL        AUTH 3 Y.C.HUANG,J.JEYARAMAN,M.Y.LIU,C.J.CHEN                       
JRNL        TITL   STRUCTURE OF BACILLUS AMYLOLIQUEFACIENS                      
JRNL        TITL 2 ALPHA-AMYLASE AT HIGH RESOLUTION: IMPLICATIONS FOR           
JRNL        TITL 3 THERMAL STABILITY.                                           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  66   121 2010              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   20124706                                                     
JRNL        DOI    10.1107/S1744309109051938                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 196849                         
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 SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 19548                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.0900                       
REMARK   3   BIN FREE R VALUE                    : 0.1000                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 1.220                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7778                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 647                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.33                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.40300                                              
REMARK   3    B22 (A**2) : -4.25100                                             
REMARK   3    B33 (A**2) : 2.84700                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 53.10                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3BH4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-DEC-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB045513.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-AUG-07                          
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               : NSRRC                              
REMARK 200  BEAMLINE                       : BL13B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 196849                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2677.6000                          
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) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.46000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 167.400                            
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1E43                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL, PH7.5, 24% PEG3350,      
REMARK 280  3.5MM CACL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       44.88000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       74.33800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       44.88000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       74.33800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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  215   CD    CE    NZ                                      
REMARK 480     LEU A  443   CG                                                  
REMARK 480     LYS B  215   CD    CE    NZ                                      
REMARK 480     LEU B  443   CG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   796     O    HOH B   796     2765     1.58            
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  10      164.26    175.28                                   
REMARK 500    LEU A  63       40.54    -87.95                                   
REMARK 500    ASN A 123       86.05   -160.03                                   
REMARK 500    TYR A 149      -32.43     73.99                                   
REMARK 500    GLU A 186       63.79     88.40                                   
REMARK 500    LEU A 197      -55.86   -129.69                                   
REMARK 500    TYR A 199     -141.99     48.20                                   
REMARK 500    LYS A 238      115.42    -37.59                                   
REMARK 500    SER A 338       62.99   -167.14                                   
REMARK 500    LYS A 371       40.38   -100.97                                   
REMARK 500    PHE B  10      160.27    177.31                                   
REMARK 500    LEU B  63       44.85    -87.49                                   
REMARK 500    ASN B 123       85.08   -159.26                                   
REMARK 500    TYR B 149      -32.48     76.21                                   
REMARK 500    GLU B 179       46.85     31.48                                   
REMARK 500    LEU B 197      -57.09   -128.06                                   
REMARK 500    TYR B 199     -143.84     48.21                                   
REMARK 500    LYS B 238      113.80    -36.90                                   
REMARK 500    SER B 338       60.79   -169.44                                   
REMARK 500    LYS B 371       35.74    -99.26                                   
REMARK 500    ILE B 404       67.18   -106.33                                   
REMARK 500    SER B 418       46.75    -79.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR B 196         0.07    SIDE CHAIN                              
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 486  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 103   OD1                                                    
REMARK 620 2 ASP A 195   O    96.8                                              
REMARK 620 3 ASP A 195   OD1 162.0  82.4                                        
REMARK 620 4 ASP A 201   OD1  89.0  78.9 108.3                                  
REMARK 620 5 HIS A 236   O    84.0  88.9  78.0 165.2                            
REMARK 620 6 HOH A 506   O    88.0 162.4  98.1  84.3 108.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 488  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 160   OD1                                                    
REMARK 620 2 ASP A 160   OD2  50.0                                              
REMARK 620 3 ALA A 182   O    77.1  92.5                                        
REMARK 620 4 ASP A 184   OD1 132.3  83.0 117.7                                  
REMARK 620 5 ASP A 203   OD1  85.6  86.8 157.7  84.4                            
REMARK 620 6 ASP A 205   OD2 154.5 155.5  94.1  73.0  95.7                      
REMARK 620 7 HOH A 566   O    72.4 120.3  87.9 145.8  73.4  83.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 489  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 160   OD2                                                    
REMARK 620 2 ASP A 184   OD2  87.9                                              
REMARK 620 3 ASP A 195   OD1 132.4  88.3                                        
REMARK 620 4 ASP A 195   OD2  86.1  95.0  47.1                                  
REMARK 620 5 ASP A 201   OD2 111.0 161.1  78.0  85.2                            
REMARK 620 6 VAL A 202   O   104.4  87.7 122.8 169.3  88.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 485  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A 301   O                                                      
REMARK 620 2 TYR A 303   O   107.4                                              
REMARK 620 3 PRO A 407   O   164.4  77.8                                        
REMARK 620 4 ASP A 408   OD2  90.2 152.6  80.1                                  
REMARK 620 5 ASP A 431   OD1 102.8 112.5  88.2  82.7                            
REMARK 620 6 ASP A 431   OD2  80.6  77.4 114.9 127.2  50.1                      
REMARK 620 7 HOH A 505   O    77.7  80.1  89.0  83.4 166.1 142.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 487  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 445   OD1                                                    
REMARK 620 2 GLU A 448   OE1  87.1                                              
REMARK 620 3 GLU A 448   OE2  92.7  49.9                                        
REMARK 620 4 GLN A 483   OE1 152.2  75.7  92.8                                  
REMARK 620 5 HOH A 550   O   135.7 119.3  81.8  72.1                            
REMARK 620 6 HOH A 539   O    71.7  83.5 132.0  84.5 140.4                      
REMARK 620 7 HOH A 525   O    66.4 123.1  80.7 141.4  69.3 127.5                
REMARK 620 8 HOH A 500   O    91.2 157.6 152.4  96.4  76.5  74.9  76.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B   1  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 103   OD1                                                    
REMARK 620 2 ASP B 195   O    98.2                                              
REMARK 620 3 ASP B 195   OD1 162.6  81.3                                        
REMARK 620 4 ASP B 201   OD1  88.7  78.2 108.2                                  
REMARK 620 5 HIS B 236   O    83.5  88.6  79.1 163.5                            
REMARK 620 6 HOH B 492   O    86.5 164.2  98.7  86.9 107.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 486  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 160   OD1                                                    
REMARK 620 2 ASP B 160   OD2  50.2                                              
REMARK 620 3 ALA B 182   O    81.3  96.6                                        
REMARK 620 4 ASP B 184   OD1 130.7  81.1 116.1                                  
REMARK 620 5 ASP B 203   OD1  83.9  86.4 157.8  86.1                            
REMARK 620 6 ASP B 205   OD2 155.0 154.8  90.8  74.0  95.7                      
REMARK 620 7 HOH B 511   O    74.4 123.6  83.1 148.3  77.0  81.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 488  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 160   OD2                                                    
REMARK 620 2 ASP B 184   OD2  88.2                                              
REMARK 620 3 ASP B 195   OD1 132.0  89.6                                        
REMARK 620 4 ASP B 195   OD2  84.4  94.3  48.0                                  
REMARK 620 5 ASP B 201   OD2 110.9 160.9  77.2  87.0                            
REMARK 620 6 VAL B 202   O   104.8  88.2 123.1 170.6  87.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 485  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 301   O                                                      
REMARK 620 2 TYR B 303   O   107.3                                              
REMARK 620 3 PRO B 407   O   164.9  78.4                                        
REMARK 620 4 ASP B 408   OD1  87.7 154.2  82.3                                  
REMARK 620 5 ASP B 431   OD1  82.9  77.0 112.2 126.7                            
REMARK 620 6 ASP B 431   OD2 100.8 115.3  88.8  81.0  50.2                      
REMARK 620 7 HOH B 516   O    78.2  79.6  89.3  83.3 143.8 164.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 487  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 445   OD1                                                    
REMARK 620 2 GLU B 448   OE1  84.5                                              
REMARK 620 3 GLU B 448   OE2  90.1  49.3                                        
REMARK 620 4 GLN B 483   NE2 152.3  76.3  92.2                                  
REMARK 620 5 HOH B 573   O   132.4 121.2  81.8  75.2                            
REMARK 620 6 HOH B 558   O    65.1 124.1  83.4 142.5  67.4                      
REMARK 620 7 HOH B 546   O    94.9 156.9 153.7  95.2  75.8  75.4                
REMARK 620 8 HOH B 523   O    71.6  81.1 129.0  85.7 144.7 125.4  76.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 485                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 486                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 487                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 488                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 489                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 485                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 486                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 487                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 488                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BLI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1E43   RELATED DB: PDB                                   
DBREF  3BH4 A    2   484  UNP    P00692   AMY_BACAM       32    514             
DBREF  3BH4 B    2   484  UNP    P00692   AMY_BACAM       32    514             
SEQRES   1 A  483  VAL ASN GLY THR LEU MET GLN TYR PHE GLU TRP TYR THR          
SEQRES   2 A  483  PRO ASN ASP GLY GLN HIS TRP LYS ARG LEU GLN ASN ASP          
SEQRES   3 A  483  ALA GLU HIS LEU SER ASP ILE GLY ILE THR ALA VAL TRP          
SEQRES   4 A  483  ILE PRO PRO ALA TYR LYS GLY LEU SER GLN SER ASP ASN          
SEQRES   5 A  483  GLY TYR GLY PRO TYR ASP LEU TYR ASP LEU GLY GLU PHE          
SEQRES   6 A  483  GLN GLN LYS GLY THR VAL ARG THR LYS TYR GLY THR LYS          
SEQRES   7 A  483  SER GLU LEU GLN ASP ALA ILE GLY SER LEU HIS SER ARG          
SEQRES   8 A  483  ASN VAL GLN VAL TYR GLY ASP VAL VAL LEU ASN HIS LYS          
SEQRES   9 A  483  ALA GLY ALA ASP ALA THR GLU ASP VAL THR ALA VAL GLU          
SEQRES  10 A  483  VAL ASN PRO ALA ASN ARG ASN GLN GLU THR SER GLU GLU          
SEQRES  11 A  483  TYR GLN ILE LYS ALA TRP THR ASP PHE ARG PHE PRO GLY          
SEQRES  12 A  483  ARG GLY ASN THR TYR SER ASP PHE LYS TRP HIS TRP TYR          
SEQRES  13 A  483  HIS PHE ASP GLY ALA ASP TRP ASP GLU SER ARG LYS ILE          
SEQRES  14 A  483  SER ARG ILE PHE LYS PHE ARG GLY GLU GLY LYS ALA TRP          
SEQRES  15 A  483  ASP TRP GLU VAL SER SER GLU ASN GLY ASN TYR ASP TYR          
SEQRES  16 A  483  LEU MET TYR ALA ASP VAL ASP TYR ASP HIS PRO ASP VAL          
SEQRES  17 A  483  VAL ALA GLU THR LYS LYS TRP GLY ILE TRP TYR ALA ASN          
SEQRES  18 A  483  GLU LEU SER LEU ASP GLY PHE ARG ILE ASP ALA ALA LYS          
SEQRES  19 A  483  HIS ILE LYS PHE SER PHE LEU ARG ASP TRP VAL GLN ALA          
SEQRES  20 A  483  VAL ARG GLN ALA THR GLY LYS GLU MET PHE THR VAL ALA          
SEQRES  21 A  483  GLU TYR TRP GLN ASN ASN ALA GLY LYS LEU GLU ASN TYR          
SEQRES  22 A  483  LEU ASN LYS THR SER PHE ASN GLN SER VAL PHE ASP VAL          
SEQRES  23 A  483  PRO LEU HIS PHE ASN LEU GLN ALA ALA SER SER GLN GLY          
SEQRES  24 A  483  GLY GLY TYR ASP MET ARG ARG LEU LEU ASP GLY THR VAL          
SEQRES  25 A  483  VAL SER ARG HIS PRO GLU LYS ALA VAL THR PHE VAL GLU          
SEQRES  26 A  483  ASN HIS ASP THR GLN PRO GLY GLN SER LEU GLU SER THR          
SEQRES  27 A  483  VAL GLN THR TRP PHE LYS PRO LEU ALA TYR ALA PHE ILE          
SEQRES  28 A  483  LEU THR ARG GLU SER GLY TYR PRO GLN VAL PHE TYR GLY          
SEQRES  29 A  483  ASP MET TYR GLY THR LYS GLY THR SER PRO LYS GLU ILE          
SEQRES  30 A  483  PRO SER LEU LYS ASP ASN ILE GLU PRO ILE LEU LYS ALA          
SEQRES  31 A  483  ARG LYS GLU TYR ALA TYR GLY PRO GLN HIS ASP TYR ILE          
SEQRES  32 A  483  ASP HIS PRO ASP VAL ILE GLY TRP THR ARG GLU GLY ASP          
SEQRES  33 A  483  SER SER ALA ALA LYS SER GLY LEU ALA ALA LEU ILE THR          
SEQRES  34 A  483  ASP GLY PRO GLY GLY SER LYS ARG MET TYR ALA GLY LEU          
SEQRES  35 A  483  LYS ASN ALA GLY GLU THR TRP TYR ASP ILE THR GLY ASN          
SEQRES  36 A  483  ARG SER ASP THR VAL LYS ILE GLY SER ASP GLY TRP GLY          
SEQRES  37 A  483  GLU PHE HIS VAL ASN ASP GLY SER VAL SER ILE TYR VAL          
SEQRES  38 A  483  GLN LYS                                                      
SEQRES   1 B  483  VAL ASN GLY THR LEU MET GLN TYR PHE GLU TRP TYR THR          
SEQRES   2 B  483  PRO ASN ASP GLY GLN HIS TRP LYS ARG LEU GLN ASN ASP          
SEQRES   3 B  483  ALA GLU HIS LEU SER ASP ILE GLY ILE THR ALA VAL TRP          
SEQRES   4 B  483  ILE PRO PRO ALA TYR LYS GLY LEU SER GLN SER ASP ASN          
SEQRES   5 B  483  GLY TYR GLY PRO TYR ASP LEU TYR ASP LEU GLY GLU PHE          
SEQRES   6 B  483  GLN GLN LYS GLY THR VAL ARG THR LYS TYR GLY THR LYS          
SEQRES   7 B  483  SER GLU LEU GLN ASP ALA ILE GLY SER LEU HIS SER ARG          
SEQRES   8 B  483  ASN VAL GLN VAL TYR GLY ASP VAL VAL LEU ASN HIS LYS          
SEQRES   9 B  483  ALA GLY ALA ASP ALA THR GLU ASP VAL THR ALA VAL GLU          
SEQRES  10 B  483  VAL ASN PRO ALA ASN ARG ASN GLN GLU THR SER GLU GLU          
SEQRES  11 B  483  TYR GLN ILE LYS ALA TRP THR ASP PHE ARG PHE PRO GLY          
SEQRES  12 B  483  ARG GLY ASN THR TYR SER ASP PHE LYS TRP HIS TRP TYR          
SEQRES  13 B  483  HIS PHE ASP GLY ALA ASP TRP ASP GLU SER ARG LYS ILE          
SEQRES  14 B  483  SER ARG ILE PHE LYS PHE ARG GLY GLU GLY LYS ALA TRP          
SEQRES  15 B  483  ASP TRP GLU VAL SER SER GLU ASN GLY ASN TYR ASP TYR          
SEQRES  16 B  483  LEU MET TYR ALA ASP VAL ASP TYR ASP HIS PRO ASP VAL          
SEQRES  17 B  483  VAL ALA GLU THR LYS LYS TRP GLY ILE TRP TYR ALA ASN          
SEQRES  18 B  483  GLU LEU SER LEU ASP GLY PHE ARG ILE ASP ALA ALA LYS          
SEQRES  19 B  483  HIS ILE LYS PHE SER PHE LEU ARG ASP TRP VAL GLN ALA          
SEQRES  20 B  483  VAL ARG GLN ALA THR GLY LYS GLU MET PHE THR VAL ALA          
SEQRES  21 B  483  GLU TYR TRP GLN ASN ASN ALA GLY LYS LEU GLU ASN TYR          
SEQRES  22 B  483  LEU ASN LYS THR SER PHE ASN GLN SER VAL PHE ASP VAL          
SEQRES  23 B  483  PRO LEU HIS PHE ASN LEU GLN ALA ALA SER SER GLN GLY          
SEQRES  24 B  483  GLY GLY TYR ASP MET ARG ARG LEU LEU ASP GLY THR VAL          
SEQRES  25 B  483  VAL SER ARG HIS PRO GLU LYS ALA VAL THR PHE VAL GLU          
SEQRES  26 B  483  ASN HIS ASP THR GLN PRO GLY GLN SER LEU GLU SER THR          
SEQRES  27 B  483  VAL GLN THR TRP PHE LYS PRO LEU ALA TYR ALA PHE ILE          
SEQRES  28 B  483  LEU THR ARG GLU SER GLY TYR PRO GLN VAL PHE TYR GLY          
SEQRES  29 B  483  ASP MET TYR GLY THR LYS GLY THR SER PRO LYS GLU ILE          
SEQRES  30 B  483  PRO SER LEU LYS ASP ASN ILE GLU PRO ILE LEU LYS ALA          
SEQRES  31 B  483  ARG LYS GLU TYR ALA TYR GLY PRO GLN HIS ASP TYR ILE          
SEQRES  32 B  483  ASP HIS PRO ASP VAL ILE GLY TRP THR ARG GLU GLY ASP          
SEQRES  33 B  483  SER SER ALA ALA LYS SER GLY LEU ALA ALA LEU ILE THR          
SEQRES  34 B  483  ASP GLY PRO GLY GLY SER LYS ARG MET TYR ALA GLY LEU          
SEQRES  35 B  483  LYS ASN ALA GLY GLU THR TRP TYR ASP ILE THR GLY ASN          
SEQRES  36 B  483  ARG SER ASP THR VAL LYS ILE GLY SER ASP GLY TRP GLY          
SEQRES  37 B  483  GLU PHE HIS VAL ASN ASP GLY SER VAL SER ILE TYR VAL          
SEQRES  38 B  483  GLN LYS                                                      
HET     CA  A 485       1                                                       
HET     CA  A 486       1                                                       
HET     CA  A 487       1                                                       
HET     CA  A 488       1                                                       
HET     NA  A 489       1                                                       
HET     CA  B   1       1                                                       
HET     CA  B 485       1                                                       
HET     CA  B 486       1                                                       
HET     CA  B 487       1                                                       
HET     NA  B 488       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
FORMUL   3   CA    8(CA 2+)                                                     
FORMUL   7   NA    2(NA 1+)                                                     
FORMUL  13  HOH   *647(H2 O)                                                    
HELIX    1   1 GLN A   19  GLY A   35  1                                  17    
HELIX    2   2 THR A   78  ARG A   92  1                                  15    
HELIX    3   3 HIS A  155  TYR A  157  5                                   3    
HELIX    4   4 HIS A  206  SER A  225  1                                  20    
HELIX    5   5 ALA A  233  ILE A  237  5                                   5    
HELIX    6   6 LYS A  238  GLY A  254  1                                  17    
HELIX    7   7 ASN A  267  THR A  278  1                                  12    
HELIX    8   8 ASP A  286  GLN A  299  1                                  14    
HELIX    9   9 ASP A  304  LEU A  308  5                                   5    
HELIX   10  10 THR A  312  HIS A  317  1                                   6    
HELIX   11  11 PHE A  344  THR A  354  1                                  11    
HELIX   12  12 TYR A  364  GLY A  369  1                                   6    
HELIX   13  13 LEU A  381  TYR A  395  1                                  15    
HELIX   14  14 GLY A  442  ALA A  446  5                                   5    
HELIX   15  15 GLN B   19  GLY B   35  1                                  17    
HELIX   16  16 THR B   78  ARG B   92  1                                  15    
HELIX   17  17 HIS B  155  TYR B  157  5                                   3    
HELIX   18  18 HIS B  206  SER B  225  1                                  20    
HELIX   19  19 ALA B  233  ILE B  237  5                                   5    
HELIX   20  20 LYS B  238  GLY B  254  1                                  17    
HELIX   21  21 ASN B  267  THR B  278  1                                  12    
HELIX   22  22 ASP B  286  GLN B  299  1                                  14    
HELIX   23  23 ASP B  304  LEU B  308  5                                   5    
HELIX   24  24 THR B  312  HIS B  317  1                                   6    
HELIX   25  25 PHE B  344  THR B  354  1                                  11    
HELIX   26  26 TYR B  364  GLY B  369  1                                   6    
HELIX   27  27 LEU B  381  TYR B  395  1                                  15    
HELIX   28  28 GLY B  442  ALA B  446  5                                   5    
SHEET    1   A 9 LEU A   6  GLN A   8  0                                        
SHEET    2   A 9 ALA A  38  ILE A  41  1  O  TRP A  40   N  MET A   7           
SHEET    3   A 9 GLN A  95  VAL A 100  1  O  TYR A  97   N  VAL A  39           
SHEET    4   A 9 GLY A 228  ILE A 231  1  O  ARG A 230   N  VAL A 100           
SHEET    5   A 9 PHE A 258  ALA A 261  1  O  VAL A 260   N  ILE A 231           
SHEET    6   A 9 SER A 283  PHE A 285  1  O  SER A 283   N  ALA A 261           
SHEET    7   A 9 ALA A 321  PHE A 324  1  O  VAL A 322   N  VAL A 284           
SHEET    8   A 9 TYR A 359  PHE A 363  1  O  TYR A 359   N  ALA A 321           
SHEET    9   A 9 LEU A   6  GLN A   8  1  N  LEU A   6   O  VAL A 362           
SHEET    1   B 2 LYS A  46  GLY A  47  0                                        
SHEET    2   B 2 PRO A  57  ASP A  59 -1  O  TYR A  58   N  LYS A  46           
SHEET    1   C 6 HIS A 104  LYS A 105  0                                        
SHEET    2   C 6 ALA A 200  VAL A 202 -1  O  ALA A 200   N  LYS A 105           
SHEET    3   C 6 PHE A 159  ASP A 165 -1  N  ASP A 160   O  ASP A 201           
SHEET    4   C 6 ILE A 170  PHE A 176 -1  O  PHE A 174   N  ALA A 162           
SHEET    5   C 6 ALA A 110  ASN A 120 -1  N  VAL A 117   O  LYS A 175           
SHEET    6   C 6 ASN A 123  GLU A 127 -1  O  GLN A 126   N  ASN A 120           
SHEET    1   D 6 HIS A 104  LYS A 105  0                                        
SHEET    2   D 6 ALA A 200  VAL A 202 -1  O  ALA A 200   N  LYS A 105           
SHEET    3   D 6 PHE A 159  ASP A 165 -1  N  ASP A 160   O  ASP A 201           
SHEET    4   D 6 ILE A 170  PHE A 176 -1  O  PHE A 174   N  ALA A 162           
SHEET    5   D 6 ALA A 110  ASN A 120 -1  N  VAL A 117   O  LYS A 175           
SHEET    6   D 6 TYR A 132  ASP A 139 -1  O  ILE A 134   N  VAL A 114           
SHEET    1   E 6 GLN A 400  TYR A 403  0                                        
SHEET    2   E 6 VAL A 409  ARG A 414 -1  O  GLY A 411   N  TYR A 403           
SHEET    3   E 6 LEU A 425  THR A 430 -1  O  ALA A 427   N  TRP A 412           
SHEET    4   E 6 VAL A 478  GLN A 483 -1  O  TYR A 481   N  ALA A 426           
SHEET    5   E 6 THR A 449  ASP A 452 -1  N  TYR A 451   O  VAL A 482           
SHEET    6   E 6 THR A 460  LYS A 462 -1  O  VAL A 461   N  TRP A 450           
SHEET    1   F 2 GLY A 435  TYR A 440  0                                        
SHEET    2   F 2 TRP A 468  VAL A 473 -1  O  PHE A 471   N  LYS A 437           
SHEET    1   G 9 LEU B   6  GLN B   8  0                                        
SHEET    2   G 9 ALA B  38  ILE B  41  1  O  TRP B  40   N  MET B   7           
SHEET    3   G 9 GLN B  95  VAL B 100  1  O  TYR B  97   N  VAL B  39           
SHEET    4   G 9 GLY B 228  ILE B 231  1  O  ARG B 230   N  VAL B 100           
SHEET    5   G 9 PHE B 258  ALA B 261  1  O  VAL B 260   N  ILE B 231           
SHEET    6   G 9 SER B 283  PHE B 285  1  O  SER B 283   N  THR B 259           
SHEET    7   G 9 ALA B 321  PHE B 324  1  O  VAL B 322   N  VAL B 284           
SHEET    8   G 9 TYR B 359  PHE B 363  1  O  TYR B 359   N  ALA B 321           
SHEET    9   G 9 LEU B   6  GLN B   8  1  N  LEU B   6   O  VAL B 362           
SHEET    1   H 2 LYS B  46  GLY B  47  0                                        
SHEET    2   H 2 PRO B  57  ASP B  59 -1  O  TYR B  58   N  LYS B  46           
SHEET    1   I 6 HIS B 104  LYS B 105  0                                        
SHEET    2   I 6 ALA B 200  VAL B 202 -1  O  ALA B 200   N  LYS B 105           
SHEET    3   I 6 PHE B 159  ASP B 165 -1  N  ASP B 160   O  ASP B 201           
SHEET    4   I 6 ILE B 170  PHE B 176 -1  O  PHE B 174   N  ALA B 162           
SHEET    5   I 6 ALA B 110  ASN B 120 -1  N  VAL B 117   O  LYS B 175           
SHEET    6   I 6 ASN B 123  GLU B 127 -1  O  GLN B 126   N  ASN B 120           
SHEET    1   J 6 HIS B 104  LYS B 105  0                                        
SHEET    2   J 6 ALA B 200  VAL B 202 -1  O  ALA B 200   N  LYS B 105           
SHEET    3   J 6 PHE B 159  ASP B 165 -1  N  ASP B 160   O  ASP B 201           
SHEET    4   J 6 ILE B 170  PHE B 176 -1  O  PHE B 174   N  ALA B 162           
SHEET    5   J 6 ALA B 110  ASN B 120 -1  N  VAL B 117   O  LYS B 175           
SHEET    6   J 6 TYR B 132  ASP B 139 -1  O  ILE B 134   N  VAL B 114           
SHEET    1   K 6 GLN B 400  TYR B 403  0                                        
SHEET    2   K 6 VAL B 409  ARG B 414 -1  O  GLY B 411   N  TYR B 403           
SHEET    3   K 6 LEU B 425  THR B 430 -1  O  ALA B 427   N  TRP B 412           
SHEET    4   K 6 VAL B 478  GLN B 483 -1  O  TYR B 481   N  ALA B 426           
SHEET    5   K 6 THR B 449  ASP B 452 -1  N  TYR B 451   O  VAL B 482           
SHEET    6   K 6 VAL B 461  LYS B 462 -1  O  VAL B 461   N  TRP B 450           
SHEET    1   L 2 GLY B 435  TYR B 440  0                                        
SHEET    2   L 2 TRP B 468  VAL B 473 -1  O  PHE B 471   N  LYS B 437           
LINK         OD1 ASN A 103                CA    CA A 486     1555   1555  2.43  
LINK         OD1 ASP A 160                CA    CA A 488     1555   1555  2.61  
LINK         OD2 ASP A 160                NA    NA A 489     1555   1555  2.43  
LINK         OD2 ASP A 160                CA    CA A 488     1555   1555  2.58  
LINK         O   ALA A 182                CA    CA A 488     1555   1555  2.45  
LINK         OD1 ASP A 184                CA    CA A 488     1555   1555  2.48  
LINK         OD2 ASP A 184                NA    NA A 489     1555   1555  2.54  
LINK         O   ASP A 195                CA    CA A 486     1555   1555  2.46  
LINK         OD1 ASP A 195                CA    CA A 486     1555   1555  2.51  
LINK         OD1 ASP A 195                NA    NA A 489     1555   1555  2.89  
LINK         OD2 ASP A 195                NA    NA A 489     1555   1555  2.50  
LINK         OD1 ASP A 201                CA    CA A 486     1555   1555  2.47  
LINK         OD2 ASP A 201                NA    NA A 489     1555   1555  2.44  
LINK         O   VAL A 202                NA    NA A 489     1555   1555  2.52  
LINK         OD1 ASP A 203                CA    CA A 488     1555   1555  2.59  
LINK         OD2 ASP A 205                CA    CA A 488     1555   1555  2.59  
LINK         O   HIS A 236                CA    CA A 486     1555   1555  2.43  
LINK         O   GLY A 301                CA    CA A 485     1555   1555  2.50  
LINK         O   TYR A 303                CA    CA A 485     1555   1555  2.40  
LINK         O   PRO A 407                CA    CA A 485     1555   1555  2.51  
LINK         OD2 ASP A 408                CA    CA A 485     1555   1555  2.39  
LINK         OD1 ASP A 431                CA    CA A 485     1555   1555  2.58  
LINK         OD2 ASP A 431                CA    CA A 485     1555   1555  2.62  
LINK         OD1 ASN A 445                CA    CA A 487     1555   1555  2.48  
LINK         OE1 GLU A 448                CA    CA A 487     1555   1555  2.68  
LINK         OE2 GLU A 448                CA    CA A 487     1555   1555  2.55  
LINK         OE1 GLN A 483                CA    CA A 487     1555   1555  2.65  
LINK         OD1 ASN B 103                CA    CA B   1     1555   1555  2.40  
LINK         OD1 ASP B 160                CA    CA B 486     1555   1555  2.59  
LINK         OD2 ASP B 160                NA    NA B 488     1555   1555  2.37  
LINK         OD2 ASP B 160                CA    CA B 486     1555   1555  2.57  
LINK         O   ALA B 182                CA    CA B 486     1555   1555  2.41  
LINK         OD1 ASP B 184                CA    CA B 486     1555   1555  2.42  
LINK         OD2 ASP B 184                NA    NA B 488     1555   1555  2.54  
LINK         O   ASP B 195                CA    CA B   1     1555   1555  2.42  
LINK         OD1 ASP B 195                CA    CA B   1     1555   1555  2.47  
LINK         OD1 ASP B 195                NA    NA B 488     1555   1555  2.83  
LINK         OD2 ASP B 195                NA    NA B 488     1555   1555  2.46  
LINK         OD1 ASP B 201                CA    CA B   1     1555   1555  2.45  
LINK         OD2 ASP B 201                NA    NA B 488     1555   1555  2.46  
LINK         O   VAL B 202                NA    NA B 488     1555   1555  2.53  
LINK         OD1 ASP B 203                CA    CA B 486     1555   1555  2.51  
LINK         OD2 ASP B 205                CA    CA B 486     1555   1555  2.53  
LINK         O   HIS B 236                CA    CA B   1     1555   1555  2.42  
LINK         O   GLY B 301                CA    CA B 485     1555   1555  2.48  
LINK         O   TYR B 303                CA    CA B 485     1555   1555  2.40  
LINK         O   PRO B 407                CA    CA B 485     1555   1555  2.49  
LINK         OD1 ASP B 408                CA    CA B 485     1555   1555  2.42  
LINK         OD1 ASP B 431                CA    CA B 485     1555   1555  2.58  
LINK         OD2 ASP B 431                CA    CA B 485     1555   1555  2.60  
LINK         OD1 ASN B 445                CA    CA B 487     1555   1555  2.52  
LINK         OE1 GLU B 448                CA    CA B 487     1555   1555  2.69  
LINK         OE2 GLU B 448                CA    CA B 487     1555   1555  2.59  
LINK         NE2 GLN B 483                CA    CA B 487     1555   1555  2.62  
LINK        CA    CA A 485                 O   HOH A 505     1555   1555  2.80  
LINK        CA    CA A 486                 O   HOH A 506     1555   1555  2.73  
LINK        CA    CA A 487                 O   HOH A 550     1555   1555  2.94  
LINK        CA    CA A 487                 O   HOH A 539     1555   1555  2.72  
LINK        CA    CA A 487                 O   HOH A 525     1555   1555  2.86  
LINK        CA    CA A 487                 O   HOH A 500     1555   1555  2.73  
LINK        CA    CA A 488                 O   HOH A 566     1555   1555  2.95  
LINK        CA    CA B   1                 O   HOH B 492     1555   1555  2.70  
LINK        CA    CA B 485                 O   HOH B 516     1555   1555  2.79  
LINK        CA    CA B 486                 O   HOH B 511     1555   1555  2.78  
LINK        CA    CA B 487                 O   HOH B 573     1555   1555  2.99  
LINK        CA    CA B 487                 O   HOH B 558     1555   1555  2.93  
LINK        CA    CA B 487                 O   HOH B 546     1555   1555  2.82  
LINK        CA    CA B 487                 O   HOH B 523     1555   1555  2.78  
SITE     1 AC1  5 GLY A 301  TYR A 303  PRO A 407  ASP A 408                    
SITE     2 AC1  5 ASP A 431                                                     
SITE     1 AC2  4 ASN A 103  ASP A 195  ASP A 201  HIS A 236                    
SITE     1 AC3  3 ASN A 445  GLU A 448  GLN A 483                               
SITE     1 AC4  5 ASP A 160  ALA A 182  ASP A 184  ASP A 203                    
SITE     2 AC4  5 ASP A 205                                                     
SITE     1 AC5  4 ASP A 160  ASP A 184  ASP A 195  ASP A 201                    
SITE     1 AC6  5 ASN B 103  ASP B 195  ASP B 201  HIS B 236                    
SITE     2 AC6  5 ILE B 237                                                     
SITE     1 AC7  5 GLY B 301  TYR B 303  PRO B 407  ASP B 408                    
SITE     2 AC7  5 ASP B 431                                                     
SITE     1 AC8  5 ASP B 160  ALA B 182  ASP B 184  ASP B 203                    
SITE     2 AC8  5 ASP B 205                                                     
SITE     1 AC9  3 ASN B 445  GLU B 448  GLN B 483                               
SITE     1 BC1  4 ASP B 160  ASP B 184  ASP B 195  ASP B 201                    
CRYST1   89.760  148.676   76.197  90.00  90.00  90.00 P 21 21 2     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      0.011141  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006726  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013124        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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