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Database: PDB
Entry: 1OB0
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Original site: 1OB0 
HEADER    HYDROLASE                               21-JAN-03   1OB0              
TITLE     KINETIC STABILIZATION OF BACILLUS LICHENIFORMIS ALPHA-AMYLASE         
TITLE    2 THROUGH INTRODUCTION OF HYDROPHOBIC RESIDUES AT THE SURFACE          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 1,4-ALPHA-D-GLUCAN-4-GLUCANOHYDROLASE;                      
COMPND   5 EC: 3.2.1.1;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;                         
SOURCE   3 ORGANISM_TAXID: 1402;                                                
SOURCE   4 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;                                
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 1423                                        
KEYWDS    HYDROLASE, GLYCOSYLTRANSFERASE, STARCH DEGRADATION,                   
KEYWDS   2 THERMOSTABILITY, CALCIUM, SODIUM                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MACHIUS,N.DECLERCK,R.HUBER,G.WIEGAND                                
REVDAT   4   22-JAN-14 1OB0    1       TITLE  KEYWDS REMARK VERSN               
REVDAT   4 2                           FORMUL ATOM                              
REVDAT   3   24-FEB-09 1OB0    1       VERSN                                    
REVDAT   2   03-APR-03 1OB0    1       JRNL                                     
REVDAT   1   30-JAN-03 1OB0    0                                                
JRNL        AUTH   M.MACHIUS,N.DECLERCK,R.HUBER,G.WIEGAND                       
JRNL        TITL   KINETIC STABILIZATION OF BACILLUS LICHENIFORMIS              
JRNL        TITL 2 ALPHA-AMYLASE THROUGH INTRODUCTION OF HYDROPHOBIC            
JRNL        TITL 3 RESIDUES AT THE SURFACE                                      
JRNL        REF    J.BIOL.CHEM.                  V. 278 11546 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12540849                                                     
JRNL        DOI    10.1074/JBC.M212618200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.Y.HWANG,H.K.SONG,C.CHANG,J.LEE,S.Y.LEE,K.K.KIM,            
REMARK   1  AUTH 2 S.CHOE,R.M.SWEET,S.W.SUH                                     
REMARK   1  TITL   CRYSTAL STRUCTURE OF THERMOSTABLE ALPHA-AMYLASE              
REMARK   1  TITL 2 FROM BACILLUS LICHENIFORMIS REFINED AT 1.7 A                 
REMARK   1  TITL 3 RESOLUTION                                                   
REMARK   1  REF    MOL.CELLS                     V.   7   251 1997              
REMARK   1  REFN                   ISSN 1016-8478                               
REMARK   1  PMID   9163741                                                      
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.MACHIUS,N.DECLERCK,R.HUBER,G.WIEGAND                       
REMARK   1  TITL   ACTIVATION OF BACILLUS LICHENIFORMIS ALPHA-AMYLASE           
REMARK   1  TITL 2 THROUGH A DISORDER-->ORDER TRANSITION OF THE                 
REMARK   1  TITL 3 SUBSTRATE-BINDING SITE MEDIATED BY A                         
REMARK   1  TITL 4 CALCIUM-SODIUM-CALCIUM METAL TRIAD                           
REMARK   1  REF    STRUCTURE                     V.   6   281 1998              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1  PMID   9551551                                                      
REMARK   1  DOI    10.1016/S0969-2126(98)00032-X                                
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.MACHIUS,G.WIEGAND,R.HUBER                                  
REMARK   1  TITL   CRYSTAL STRUCTURE OF CALCIUM-DEPLETED BACILLUS               
REMARK   1  TITL 2 LICHENIFORMIS ALPHA-AMYLASE AT 2.2 A RESOLUTION              
REMARK   1  REF    J.MOL.BIOL.                   V. 246   545 1995              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   7877175                                                      
REMARK   1  DOI    10.1006/JMBI.1994.0106                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.83 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 987507.06                      
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.000000                       
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 93.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 53205                          
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) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.154                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.7                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1448                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.83                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.94                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.1                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 8072                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.228                        
REMARK   3   BIN FREE R VALUE                    : 0.223                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 2.6                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 215                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4101                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 324                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.7                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.7                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.34                                                
REMARK   3    B22 (A**2) : -0.34                                                
REMARK   3    B33 (A**2) : 0.69                                                 
REMARK   3    B12 (A**2) : 0.23                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.14                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.16                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.15                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.4                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.0                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.84                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.15  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.66  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.04  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.14  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.357256                                             
REMARK   3   BSOL        : 48.3911                                              
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_REP.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 1OB0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JAN-03.                  
REMARK 100 THE PDBE ID CODE IS EBI-11966.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 278.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : BEAM FOCUSSING MIRROR SYSTEM       
REMARK 200                                   (MSC, USA)                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55286                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.830                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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 1BPL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 59                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.0                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED BY              
REMARK 280  VAPOR DIFFUSION FROM DROPS CONTAINING 4 UL OF PROTEIN               
REMARK 280  SOLUTION (10 MG/ML IN 50 MM TRIS/HCL, PH 8.0) PLUS 4 UL             
REMARK 280  OF RESERVOIR SOLUTION (50 MM HEPES, 1 M AMMONIUM SULFATE,           
REMARK 280  1% (V/V) PEG 500, PH 7.0) EQUILIBRATED AGAINST 1 ML OF              
REMARK 280  RESERVOIR SOLUTION.                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.82200            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       91.64400            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       68.73300            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      114.55500            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       22.91100            
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  CATALYSES ENDOHYDROLYSIS OF 1,4-ALPHA-GLUCOSIDIC                    
REMARK 400  LINKAGES IN OLIGOSACCHARIDES AND POLYSACCHARIDES.                   
REMARK 400  PRIMARILY USED IN THE FOOD INDUSTRY FOR HIGH TEMPERATURE            
REMARK 400  LIQUEFACTION OF STARCH-CONTAINING MASHES AND IN THE                 
REMARK 400  DETERGENT INDUSTRY TO REMOVE STARCH.                                
REMARK 400  ACTIVE AT RELATIVELY HIGH PH VALUES (UP TO PH 11)                   
REMARK 400  AND AT HIGH TEMPERATURES (UP TO 100 DEGREE                          
REMARK 400  CELSIUS).                                                           
REMARK 400  ENGINEERED RESIDUES  HIS (133) VAL                                  
REMARK 400                       ASN (190) PHE                                  
REMARK 400                       ALA (209) VAL                                  
REMARK 400                       GLN (264) SER                                  
REMARK 400                       ASN (265) TYR                                  
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     ALA A     1                                                      
REMARK 465     ASN A     2                                                      
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    GLU A 185   C     VAL A 186   N       0.188                       
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    HIS A 140   CB  -  CG  -  ND1 ANGL. DEV. =   9.5 DEGREES          
REMARK 500    HIS A 159   CB  -  CG  -  ND1 ANGL. DEV. =   9.9 DEGREES          
REMARK 500    HIS A 293   CB  -  CG  -  ND1 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    HIS A 450   CB  -  CG  -  ND1 ANGL. DEV. =   9.8 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  11      162.71    178.61                                   
REMARK 500    ALA A  58       87.95     30.89                                   
REMARK 500    LEU A  64       42.24    -91.96                                   
REMARK 500    TYR A 150      -34.24     75.64                                   
REMARK 500    TYR A 198     -147.96     52.09                                   
REMARK 500    SER A 337       53.81   -166.88                                   
REMARK 500    PHE A 403       64.46   -118.41                                   
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 A 195         0.09    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLU A 465        -16.47                                           
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 501  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 194   OD1                                                    
REMARK 620 2 ASP A 194   O    80.8                                              
REMARK 620 3 ASP A 200   OD1 112.7  78.3                                        
REMARK 620 4 ASP A 200   OD2  69.3  84.8  45.7                                  
REMARK 620 5 HOH A2060   O    98.4 161.3  84.9  77.6                            
REMARK 620 6 HIS A 235   O    80.3  90.7 161.0 149.6 107.6                      
REMARK 620 7 ASN A 104   OD1 161.7 102.4  85.6 128.8  84.3  81.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 502  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 161   OD1                                                    
REMARK 620 2 ALA A 181   O    87.5                                              
REMARK 620 3 ASP A 183   OD1  81.0 109.5                                        
REMARK 620 4 ASP A 204   OD1 157.8  93.8  77.7                                  
REMARK 620 5 HOH A2122   O   124.9  82.6 152.8  77.2                            
REMARK 620 6 ASP A 161   OD2  50.3  83.1 129.8 151.8  74.6                      
REMARK 620 7 ASP A 202   OD2  91.2 160.2  89.7  94.8  82.0  80.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 503  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2204   O                                                      
REMARK 620 2 TYR A 302   O    76.4                                              
REMARK 620 3 HIS A 406   O    81.5  78.8                                        
REMARK 620 4 ASP A 430   OD1 165.7 117.1  96.1                                  
REMARK 620 5 GLY A 300   O    77.9 105.2 157.3 101.6                            
REMARK 620 6 ASP A 430   OD2 142.0  81.6 124.1  49.9  78.5                      
REMARK 620 7 ASP A 407   OD2  80.1 150.5  80.2  85.6  86.9 127.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 504  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 161   OD1                                                    
REMARK 620 2 ASP A 194   OD2  87.2                                              
REMARK 620 3 ASP A 200   OD2 115.5  87.8                                        
REMARK 620 4 ASP A 183   OD2  92.9  89.9 151.3                                  
REMARK 620 5 ILE A 201   O   108.0 164.4  88.5  86.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  9-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BLI   RELATED DB: PDB                                   
REMARK 900  BACILLUS LICHENIFORMIS ALPHA-AMYLASE                                
REMARK 900 RELATED ID: 1BPL   RELATED DB: PDB                                   
REMARK 900  GLYCOSYLTRANSFERASE                                                 
REMARK 900 RELATED ID: 1E3X   RELATED DB: PDB                                   
REMARK 900  NATIVE STRUCTURE OF CHIMAERIC AMYLASE FROM B.                       
REMARK 900  AMYLOLIQUEFACIENS AND B. LICHENIFORMIS AT 1.92A                     
REMARK 900 RELATED ID: 1E3Z   RELATED DB: PDB                                   
REMARK 900  ACARBOSE COMPLEX OF CHIMAERIC AMYLASE FROM B.                       
REMARK 900  AMYLOLIQUEFACIENS AND B. LICHENIFORMIS AT 1.93A                     
REMARK 900 RELATED ID: 1E40   RELATED DB: PDB                                   
REMARK 900  TRIS/MALTOTRIOSE COMPLEX OF CHIMAERIC AMYLASE                       
REMARK 900   FROM B. AMYLOLIQUEFACIENS AND B.                                   
REMARK 900  LICHENIFORMIS AT 2.2A                                               
REMARK 900 RELATED ID: 1E43   RELATED DB: PDB                                   
REMARK 900  NATIVE STRUCTURE OF CHIMAERIC AMYLASE FROM B.                       
REMARK 900  AMYLOLIQUEFACIENS AND B. LICHENIFORMIS AT 1.7A                      
REMARK 900 RELATED ID: 1VJS   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF ALPHA-AMYLASE PRECURSOR                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 DATABASE ENTRY SWS P06278 CONTAINS A 29 RESIDUE PRECURSOR.           
REMARK 999 NUMBERING IN THE PDB ENTRY STARTS WITH 1 WHICH CORRESPONDS           
REMARK 999 TO RESIDUE 30 IN THE DATABASE ENTRY.                                 
DBREF  1OB0 A    1   483  UNP    P06278   AMY_BACLI       30    512             
SEQADV 1OB0 VAL A  133  UNP  P06278    HIS   162 ENGINEERED MUTATION            
SEQADV 1OB0 LEU A  134  UNP  P06278    ARG   163 CONFLICT                       
SEQADV 1OB0 PHE A  190  UNP  P06278    ASN   219 ENGINEERED MUTATION            
SEQADV 1OB0 VAL A  209  UNP  P06278    ALA   238 ENGINEERED MUTATION            
SEQADV 1OB0 SER A  264  UNP  P06278    GLN   293 ENGINEERED MUTATION            
SEQADV 1OB0 TYR A  265  UNP  P06278    ASN   294 ENGINEERED MUTATION            
SEQADV 1OB0 GLY A  310  UNP  P06278    SER   339 CONFLICT                       
SEQADV 1OB0 SER A  320  UNP  P06278    ALA   349 CONFLICT                       
SEQRES   1 A  483  ALA ASN LEU ASN GLY THR LEU MET GLN TYR PHE GLU TRP          
SEQRES   2 A  483  TYR MET PRO ASN ASP GLY GLN HIS TRP LYS ARG LEU GLN          
SEQRES   3 A  483  ASN ASP SER ALA TYR LEU ALA GLU HIS GLY ILE THR ALA          
SEQRES   4 A  483  VAL TRP ILE PRO PRO ALA TYR LYS GLY THR SER GLN ALA          
SEQRES   5 A  483  ASP VAL GLY TYR GLY ALA TYR ASP LEU TYR ASP LEU GLY          
SEQRES   6 A  483  GLU PHE HIS GLN LYS GLY THR VAL ARG THR LYS TYR GLY          
SEQRES   7 A  483  THR LYS GLY GLU LEU GLN SER ALA ILE LYS SER LEU HIS          
SEQRES   8 A  483  SER ARG ASP ILE ASN VAL TYR GLY ASP VAL VAL ILE ASN          
SEQRES   9 A  483  HIS LYS GLY GLY ALA ASP ALA THR GLU ASP VAL THR ALA          
SEQRES  10 A  483  VAL GLU VAL ASP PRO ALA ASP ARG ASN ARG VAL ILE SER          
SEQRES  11 A  483  GLY GLU VAL LEU ILE LYS ALA TRP THR HIS PHE HIS PHE          
SEQRES  12 A  483  PRO GLY ARG GLY SER THR TYR SER ASP PHE LYS TRP HIS          
SEQRES  13 A  483  TRP TYR HIS PHE ASP GLY THR ASP TRP ASP GLU SER ARG          
SEQRES  14 A  483  LYS LEU ASN ARG ILE TYR LYS PHE GLN GLY LYS ALA TRP          
SEQRES  15 A  483  ASP TRP GLU VAL SER ASN GLU PHE GLY ASN TYR ASP TYR          
SEQRES  16 A  483  LEU MET TYR ALA ASP ILE ASP TYR ASP HIS PRO ASP VAL          
SEQRES  17 A  483  VAL ALA GLU ILE LYS ARG TRP GLY THR TRP TYR ALA ASN          
SEQRES  18 A  483  GLU LEU GLN LEU ASP GLY PHE ARG LEU ASP ALA VAL LYS          
SEQRES  19 A  483  HIS ILE LYS PHE SER PHE LEU ARG ASP TRP VAL ASN HIS          
SEQRES  20 A  483  VAL ARG GLU LYS THR GLY LYS GLU MET PHE THR VAL ALA          
SEQRES  21 A  483  GLU TYR TRP SER TYR ASP LEU GLY ALA LEU GLU ASN TYR          
SEQRES  22 A  483  LEU ASN LYS THR ASN PHE ASN HIS SER VAL PHE ASP VAL          
SEQRES  23 A  483  PRO LEU HIS TYR GLN PHE HIS ALA ALA SER THR GLN GLY          
SEQRES  24 A  483  GLY GLY TYR ASP MET ARG LYS LEU LEU ASN GLY THR VAL          
SEQRES  25 A  483  VAL SER LYS HIS PRO LEU LYS SER VAL THR PHE VAL ASP          
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 ASP SER GLN ARG GLU ILE          
SEQRES  30 A  483  PRO ALA LEU LYS HIS LYS ILE GLU PRO ILE LEU LYS ALA          
SEQRES  31 A  483  ARG LYS GLN TYR ALA TYR GLY ALA GLN HIS ASP TYR PHE          
SEQRES  32 A  483  ASP HIS HIS ASP ILE VAL GLY TRP THR ARG GLU GLY ASP          
SEQRES  33 A  483  SER SER VAL ALA ASN SER GLY LEU ALA ALA LEU ILE THR          
SEQRES  34 A  483  ASP GLY PRO GLY GLY ALA LYS ARG MET TYR VAL GLY ARG          
SEQRES  35 A  483  GLN ASN ALA GLY GLU THR TRP HIS ASP ILE THR GLY ASN          
SEQRES  36 A  483  ARG SER GLU PRO VAL VAL ILE ASN SER GLU GLY TRP GLY          
SEQRES  37 A  483  GLU PHE HIS VAL ASN GLY GLY SER VAL SER ILE TYR VAL          
SEQRES  38 A  483  GLN ARG                                                      
HET     CA  A 501       1                                                       
HET     CA  A 502       1                                                       
HET     CA  A 503       1                                                       
HET     NA  A 504       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
FORMUL   2   CA    3(CA 2+)                                                     
FORMUL   5   NA    NA 1+                                                        
FORMUL   6  HOH   *324(H2 O)                                                    
HELIX    1   1 GLN A   20  HIS A   35  1                                  16    
HELIX    2   2 THR A   79  ARG A   93  1                                  15    
HELIX    3   3 HIS A  156  TYR A  158  5                                   3    
HELIX    4   4 HIS A  205  GLN A  224  1                                  20    
HELIX    5   5 ALA A  232  ILE A  236  5                                   5    
HELIX    6   6 LYS A  237  GLY A  253  1                                  17    
HELIX    7   7 ASP A  266  THR A  277  1                                  12    
HELIX    8   8 ASP A  285  GLN A  298  1                                  14    
HELIX    9   9 ASP A  303  ASN A  309  5                                   7    
HELIX   10  10 THR A  311  HIS A  316  1                                   6    
HELIX   11  11 PHE A  343  ARG A  354  1                                  12    
HELIX   12  12 TYR A  363  GLY A  368  1                                   6    
HELIX   13  13 LEU A  380  TYR A  394  1                                  15    
HELIX   14  14 GLY A  441  ALA A  445  5                                   5    
SHEET    1  AA10 LEU A   7  GLN A   9  0                                        
SHEET    2  AA10 ALA A  39  ILE A  42  1  O  ALA A  39   N  MET A   8           
SHEET    3  AA10 ASN A  96  VAL A 101  1  O  ASN A  96   N  VAL A  40           
SHEET    4  AA10 GLY A 227  LEU A 230  1  O  GLY A 227   N  GLY A  99           
SHEET    5  AA10 PHE A 257  ALA A 260  1  O  PHE A 257   N  PHE A 228           
SHEET    6  AA10 SER A 282  PHE A 284  1  O  SER A 282   N  ALA A 260           
SHEET    7  AA10 SER A 320  PHE A 323  1  N  VAL A 321   O  VAL A 283           
SHEET    8  AA10 TYR A 358  PHE A 362  1  O  TYR A 358   N  THR A 322           
SHEET    9  AA10 LEU A   7  GLN A   9  1  O  LEU A   7   N  VAL A 361           
SHEET   10  AA10 LEU A   7  GLN A   9                                           
SHEET    1  AB 9 HIS A 105  LYS A 106  0                                        
SHEET    2  AB 9 ALA A 199  ILE A 201 -1  O  ALA A 199   N  LYS A 106           
SHEET    3  AB 9 PHE A 160  THR A 163 -1  N  ASP A 161   O  ASP A 200           
SHEET    4  AB 9 TYR A 175  PHE A 177 -1  O  TYR A 175   N  THR A 163           
SHEET    5  AB 9 ALA A 111  ASP A 121 -1  O  VAL A 118   N  LYS A 176           
SHEET    6  AB 9 ASP A 124  VAL A 128 -1  N  ASP A 124   O  ASP A 121           
SHEET    7  AB 9 ALA A 111  ASP A 121 -1  O  ASP A 121   N  ASP A 124           
SHEET    8  AB 9 VAL A 133  HIS A 140 -1  O  VAL A 133   N  ALA A 117           
SHEET    9  AB 9 ALA A 111  ASP A 121 -1  O  ALA A 111   N  HIS A 140           
SHEET    1  AC 6 GLN A 399  TYR A 402  0                                        
SHEET    2  AC 6 ILE A 408  ARG A 413 -1  O  GLY A 410   N  TYR A 402           
SHEET    3  AC 6 LEU A 424  THR A 429 -1  O  LEU A 424   N  ARG A 413           
SHEET    4  AC 6 VAL A 477  GLN A 482 -1  O  SER A 478   N  LEU A 427           
SHEET    5  AC 6 THR A 448  ASP A 451 -1  O  HIS A 450   N  VAL A 481           
SHEET    6  AC 6 VAL A 460  VAL A 461 -1  O  VAL A 460   N  TRP A 449           
SHEET    1  AD 2 GLY A 434  TYR A 439  0                                        
SHEET    2  AD 2 TRP A 467  VAL A 472 -1  O  GLY A 468   N  MET A 438           
LINK        CA    CA A 501                 OD1 ASP A 194     1555   1555  2.41  
LINK        CA    CA A 501                 O   ASP A 194     1555   1555  2.43  
LINK        CA    CA A 501                 OD1 ASP A 200     1555   1555  2.42  
LINK        CA    CA A 501                 OD2 ASP A 200     1555   1555  3.04  
LINK        CA    CA A 501                 O   HOH A2060     1555   1555  2.48  
LINK        CA    CA A 501                 O   HIS A 235     1555   1555  2.36  
LINK        CA    CA A 501                 OD1 ASN A 104     1555   1555  2.38  
LINK        CA    CA A 502                 OD1 ASP A 161     1555   1555  2.55  
LINK        CA    CA A 502                 O   ALA A 181     1555   1555  2.42  
LINK        CA    CA A 502                 OD1 ASP A 183     1555   1555  2.38  
LINK        CA    CA A 502                 OD1 ASP A 204     1555   1555  2.46  
LINK        CA    CA A 502                 O   HOH A2122     1555   1555  2.59  
LINK        CA    CA A 502                 OD2 ASP A 161     1555   1555  2.60  
LINK        CA    CA A 502                 OD2 ASP A 202     1555   1555  2.46  
LINK        CA    CA A 503                 O   TYR A 302     1555   1555  2.35  
LINK        CA    CA A 503                 O   HIS A 406     1555   1555  2.57  
LINK        CA    CA A 503                 OD1 ASP A 430     1555   1555  2.57  
LINK        CA    CA A 503                 O   GLY A 300     1555   1555  2.57  
LINK        CA    CA A 503                 OD2 ASP A 430     1555   1555  2.63  
LINK        CA    CA A 503                 OD2 ASP A 407     1555   1555  2.39  
LINK        CA    CA A 503                 O   HOH A2204     1555   1555  2.70  
LINK        NA    NA A 504                 OD2 ASP A 194     1555   1555  2.47  
LINK        NA    NA A 504                 OD2 ASP A 200     1555   1555  2.50  
LINK        NA    NA A 504                 OD2 ASP A 183     1555   1555  2.59  
LINK        NA    NA A 504                 O   ILE A 201     1555   1555  2.55  
LINK        NA    NA A 504                 OD1 ASP A 161     1555   1555  2.43  
CISPEP   1 TRP A  184    GLU A  185          0         1.38                     
SITE     1 AC1  5 ASN A 104  ASP A 194  ASP A 200  HIS A 235                    
SITE     2 AC1  5 HOH A2060                                                     
SITE     1 AC2  6 ASP A 161  ALA A 181  ASP A 183  ASP A 202                    
SITE     2 AC2  6 ASP A 204  HOH A2122                                          
SITE     1 AC3  6 GLY A 300  TYR A 302  HIS A 406  ASP A 407                    
SITE     2 AC3  6 ASP A 430  HOH A2204                                          
SITE     1 AC4  5 ASP A 161  ASP A 183  ASP A 194  ASP A 200                    
SITE     2 AC4  5 ILE A 201                                                     
CRYST1   91.292   91.292  137.466  90.00  90.00 120.00 P 61          6          
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      0.010954  0.006324  0.000000        0.00000                         
SCALE2      0.000000  0.012648  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007274        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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