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Database: PDB
Entry: 6TAA
LinkDB: 6TAA
Original site: 6TAA 
HEADER    HYDROLASE(O-GLYCOSYL)                   21-AUG-92   6TAA              
TITLE     STRUCTURE AND MOLECULAR MODEL REFINEMENT OF ASPERGILLUS               
TITLE    2 ORYZAE (TAKA) ALPHA-AMYLASE: AN APPLICATION OF THE                   
TITLE    3 SIMULATED-ANNEALING METHOD                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.2.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;                             
SOURCE   3 ORGANISM_TAXID: 5062                                                 
KEYWDS    HYDROLASE(O-GLYCOSYL)                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.J.SWIFT,L.BRADY,Z.S.DEREWENDA,E.J.DODSON,J.P.TURKENBURG,            
AUTHOR   2 A.J.WILKINSON                                                        
REVDAT   2   24-FEB-09 6TAA    1       VERSN                                    
REVDAT   1   31-OCT-93 6TAA    0                                                
JRNL        AUTH   H.J.SWIFT,L.BRADY,Z.S.DEREWENDA,E.J.DODSON,                  
JRNL        AUTH 2 G.G.DODSON,J.P.TURKENBURG,A.J.WILKINSON                      
JRNL        TITL   STRUCTURE AND MOLECULAR MODEL REFINEMENT OF                  
JRNL        TITL 2 ASPERGILLUS ORYZAE (TAKA) ALPHA-AMYLASE: AN                  
JRNL        TITL 3 APPLICATION OF THE SIMULATED-ANNEALING METHOD.               
JRNL        REF    ACTA CRYSTALLOGR.,SECT.B      V.  47   535 1991              
JRNL        REFN                   ISSN 0108-7681                               
JRNL        PMID   1930835                                                      
JRNL        DOI    10.1107/S0108768191001970                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.BOEL,L.BRADY,A.M.BRZOZOWSKI,Z.DEREWENDA,                   
REMARK   1  AUTH 2 G.G.DODSON,V.J.JENSEN,S.B.PETERSEN,H.SWIFT,L.THIM,           
REMARK   1  AUTH 3 H.F.WOLDIKE                                                  
REMARK   1  TITL   CALCIUM BINDING IN ALPHA-AMYLASES: AN X-RAY                  
REMARK   1  TITL 2 DIFFRACTION STUDY AT 2.1 ANGSTROMS RESOLUTION OF             
REMARK   1  TITL 3 TWO ENZYMES FROM ASPERGILLUS                                 
REMARK   1  REF    BIOCHEMISTRY                  V.  29  6244 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.70                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 23482                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3686                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 239                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.022 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.063 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.080 ; 0.060               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.020 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.161 ; 0.120               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.220 ; 0.500               
REMARK   3    MULTIPLE TORSION                (A) : 0.268 ; 0.500               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : 0.250 ; 0.500               
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 3.912 ; 20.000              
REMARK   3    STAGGERED                 (DEGREES) : 22.909; 20.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 1.009 ; 1.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 1.602 ; 1.500               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.943 ; 1.500               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 2.703 ; 2.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:  SIDE CHAINS OF RESIDUES ALA 1, ASP       
REMARK   3  5, AND LYS 36 ARE NOT CLEARLY VISIBLE IN ELECTRON DENSITY           
REMARK   3  MAPS, AND ATOMS HAVE BEEN INCLUDED WITH OCCUPANCY ZERO, GIVING      
REMARK   3  RISE TO NON-IDEAL INTERMOLECULAR DISTANCES AFTER REFINEMENT.        
REMARK   4                                                                      
REMARK   4 6TAA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.52000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.78000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.59150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.78000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.52000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.59150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   477                                                      
REMARK 465     SER A   478                                                      
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     ALA A    1   CB                                                  
REMARK 480     ASP A    5   CG    OD1   OD2                                     
REMARK 480     ALA A   33   CB                                                  
REMARK 480     LYS A   36   CG    CD    CE    NZ                                
REMARK 480     GLU A   92   OE1   OE2                                           
REMARK 480     SER A  130   OG                                                  
REMARK 480     LYS A  138   CG    CD    CE    NZ                                
REMARK 480     GLN A  153   CG    CD    OE1   NE2                               
REMARK 480     ASN A  169   OD1   ND2                                           
REMARK 480     ASP A  181   CG    OD1   OD2                                     
REMARK 480     GLN A  433   CD    OE1   NE2                                     
REMARK 480     LYS A  473   CD    CE    NZ                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A     5     OH   TYR A   113              1.48            
REMARK 500   CE   LYS A    36     O    HOH A   584              1.58            
REMARK 500   CB   ALA A     1     O    HOH A   529              1.77            
REMARK 500   OD2  ASP A    77     O    HOH A   585              2.00            
REMARK 500   O    PRO A    70     O    HOH A   589              2.01            
REMARK 500   O    CYS A    38     O    HOH A   579              2.11            
REMARK 500   OE1  GLU A   156     O    HOH A   606              2.17            
REMARK 500   OH   TYR A    88     OE2  GLU A   186              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  92   CD    GLU A  92   OE1     0.172                       
REMARK 500    GLU A  92   CD    GLU A  92   OE2    -0.140                       
REMARK 500    LYS A 138   CE    LYS A 138   NZ     -0.315                       
REMARK 500    ASN A 169   CG    ASN A 169   OD1     0.192                       
REMARK 500    ASP A 181   CB    ASP A 181   CG      0.176                       
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    ARG A   7   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A   7   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    TYR A  12   CB  -  CG  -  CD2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    TYR A  12   CB  -  CG  -  CD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A  17   CB  -  CG  -  OD2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG A  18   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ALA A  33   CB  -  CA  -  C   ANGL. DEV. =  11.4 DEGREES          
REMARK 500    ASP A  34   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A  34   CB  -  CG  -  OD2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500    TYR A  37   CB  -  CG  -  CD1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    THR A  41   CA  -  CB  -  OG1 ANGL. DEV. = -15.2 DEGREES          
REMARK 500    ILE A  60   CA  -  CB  -  CG1 ANGL. DEV. = -12.4 DEGREES          
REMARK 500    ILE A  60   CA  -  CB  -  CG2 ANGL. DEV. =  15.3 DEGREES          
REMARK 500    THR A  63   CA  -  CB  -  CG2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    VAL A  65   N   -  CA  -  CB  ANGL. DEV. = -17.6 DEGREES          
REMARK 500    GLN A  68   CG  -  CD  -  OE1 ANGL. DEV. =  15.9 DEGREES          
REMARK 500    TYR A  75   CB  -  CG  -  CD1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500    TYR A  88   CB  -  CG  -  CD2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    TYR A  88   CB  -  CG  -  CD1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    TYR A  94   CB  -  CG  -  CD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TYR A  94   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    THR A  96   N   -  CA  -  CB  ANGL. DEV. = -13.3 DEGREES          
REMARK 500    LEU A 103   CB  -  CA  -  C   ANGL. DEV. =  12.0 DEGREES          
REMARK 500    SER A 105   O   -  C   -  N   ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG A 110   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ASP A 117   CB  -  CG  -  OD1 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    TYR A 125   CB  -  CG  -  CD1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ALA A 128   CB  -  CA  -  C   ANGL. DEV. =  10.6 DEGREES          
REMARK 500    VAL A 132   CG1 -  CB  -  CG2 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ASP A 133   CB  -  CG  -  OD1 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    VAL A 132   O   -  C   -  N   ANGL. DEV. =  10.0 DEGREES          
REMARK 500    LYS A 138   CD  -  CE  -  NZ  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    PRO A 139   N   -  CA  -  CB  ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    SER A 141   C   -  N   -  CA  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    GLN A 153   CB  -  CA  -  C   ANGL. DEV. =  12.9 DEGREES          
REMARK 500    TYR A 155   CB  -  CG  -  CD1 ANGL. DEV. =  -4.7 DEGREES          
REMARK 500    ASP A 157   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A 157   CB  -  CG  -  OD2 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    ASP A 163   CA  -  CB  -  CG  ANGL. DEV. =  13.6 DEGREES          
REMARK 500    ASN A 169   OD1 -  CG  -  ND2 ANGL. DEV. = -17.5 DEGREES          
REMARK 500    VAL A 171   CG1 -  CB  -  CG2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    ASP A 177   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP A 177   CA  -  C   -  O   ANGL. DEV. =  15.3 DEGREES          
REMARK 500    ASP A 181   CA  -  CB  -  CG  ANGL. DEV. = -13.5 DEGREES          
REMARK 500    VAL A 182   CG1 -  CB  -  CG2 ANGL. DEV. =  10.1 DEGREES          
REMARK 500    VAL A 183   CB  -  CA  -  C   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    GLU A 186   CG  -  CD  -  OE1 ANGL. DEV. =  14.8 DEGREES          
REMARK 500    ASP A 189   CB  -  CG  -  OD2 ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ASP A 201   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     128 ANGLE DEVIATIONS.                             
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    ALA A  78       39.38    -86.64                                   
REMARK 500    ASP A 181      -19.69    -49.69                                   
REMARK 500    SER A 199       69.26     60.13                                   
REMARK 500    THR A 207       39.18     37.28                                   
REMARK 500    ASN A 251       63.44    -68.06                                   
REMARK 500    ALA A 329      123.10    -33.69                                   
REMARK 500    SER A 415     -105.27    -84.65                                   
REMARK 500    SER A 447      -35.79    148.42                                   
REMARK 500    ALA A 470      -78.03   -142.15                                   
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    GLU A  92         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 479  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 162   O                                                      
REMARK 620 2 HIS A 210   O    72.7                                              
REMARK 620 3 HOH A 553   O    76.2  86.1                                        
REMARK 620 4 ASP A 175   OD2  82.8 155.4  89.8                                  
REMARK 620 5 HOH A 525   O    62.6  73.3 137.7  94.1                            
REMARK 620 6 HOH A 550   O   122.1 119.8 150.8  72.0  68.2                      
REMARK 620 7 ASN A 121   OD1 152.5  81.6  92.9 122.8 119.2  79.0                
REMARK 620 8 ASP A 175   OD1 121.5 147.8  71.5  50.3 138.5  79.3  76.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 480  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 230   OE2                                                    
REMARK 620 2 HOH A 556   O    73.3                                              
REMARK 620 3 ASP A 206   OD1 104.2  86.8                                        
REMARK 620 4 GLU A 230   OE1  44.4 103.3  74.1                                  
REMARK 620 N                    1     2     3                                   
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 479                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 480                  
DBREF  6TAA A    1   478  UNP    P10529   AMYA_ASPOR      22    499             
SEQRES   1 A  478  ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE          
SEQRES   2 A  478  LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR          
SEQRES   3 A  478  THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY          
SEQRES   4 A  478  GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE          
SEQRES   5 A  478  GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL          
SEQRES   6 A  478  THR ALA GLN LEU PRO GLN THR THR ALA TYR GLY ASP ALA          
SEQRES   7 A  478  TYR HIS GLY TYR TRP GLN GLN ASP ILE TYR SER LEU ASN          
SEQRES   8 A  478  GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER          
SEQRES   9 A  478  SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP          
SEQRES  10 A  478  VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER          
SEQRES  11 A  478  SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN          
SEQRES  12 A  478  ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU          
SEQRES  13 A  478  ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN          
SEQRES  14 A  478  THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL          
SEQRES  15 A  478  VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL          
SEQRES  16 A  478  SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL          
SEQRES  17 A  478  LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS          
SEQRES  18 A  478  ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY          
SEQRES  19 A  478  ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP          
SEQRES  20 A  478  GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN          
SEQRES  21 A  478  ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR          
SEQRES  22 A  478  ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER          
SEQRES  23 A  478  THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO          
SEQRES  24 A  478  ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS          
SEQRES  25 A  478  ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY ILE PRO          
SEQRES  26 A  478  ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY          
SEQRES  27 A  478  ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY          
SEQRES  28 A  478  TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER          
SEQRES  29 A  478  ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR          
SEQRES  30 A  478  GLY PHE VAL THR TYR LYS ASN TRP PRO ILE TYR LYS ASP          
SEQRES  31 A  478  ASP THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER          
SEQRES  32 A  478  GLN ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY          
SEQRES  33 A  478  ASP SER TYR THR LEU SER LEU SER GLY ALA GLY TYR THR          
SEQRES  34 A  478  ALA GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR          
SEQRES  35 A  478  VAL THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET          
SEQRES  36 A  478  ALA GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS          
SEQRES  37 A  478  LEU ALA GLY SER LYS ILE CYS SER SER SER                      
HET     CA  A 479       1                                                       
HET     CA  A 480       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4  HOH   *239(H2 O)                                                    
HELIX    1   1 THR A    2  ARG A    7  1                                   6    
HELIX    2   2 LEU A   15  ALA A   20  1                                   6    
HELIX    3   3 ASN A   31  GLN A   35  5                                   5    
HELIX    4   4 THR A   41  ASP A   47  1                                   7    
HELIX    5   5 LYS A   48  GLY A   54  1                                   7    
HELIX    6   6 ASP A   98  ARG A  110  1                                  13    
HELIX    7   7 ALA A  128  VAL A  132  5                                   5    
HELIX    8   8 SER A  142  TYR A  145  5                                   4    
HELIX    9   9 ASP A  157  CYS A  164  1                                   8    
HELIX   10  10 LYS A  180  SER A  199  1                                  20    
HELIX   11  11 THR A  207  VAL A  211  5                                   5    
HELIX   12  12 GLN A  212  ASP A  214  5                                   3    
HELIX   13  13 PHE A  215  GLY A  224  1                                  10    
HELIX   14  14 ASP A  235  CYS A  240  1                                   6    
HELIX   15  15 PRO A  241  VAL A  245  5                                   5    
HELIX   16  16 ASN A  251  LYS A  263  1                                  13    
HELIX   17  17 SER A  268  CYS A  283  1                                  16    
HELIX   18  18 ASP A  285  LEU A  288  5                                   4    
HELIX   19  19 ARG A  300  THR A  305  1                                   6    
HELIX   20  20 ASP A  307  ASN A  321  1                                  15    
HELIX   21  21 GLY A  330  HIS A  334  5                                   5    
HELIX   22  22 ALA A  346  GLY A  351  5                                   6    
HELIX   23  23 SER A  356  ASP A  376  1                                  21    
HELIX   24  24 GLY A  378  TYR A  382  5                                   5    
SHEET    1   A 8 GLY A 248  VAL A 249  0                                        
SHEET    2   A 8 TYR A 226  GLY A 229  1  O  CYS A 227   N  GLY A 248           
SHEET    3   A 8 GLY A 202  ILE A 205  1  O  LEU A 203   N  ILE A 228           
SHEET    4   A 8 TYR A 113  VAL A 118  1  O  LEU A 114   N  GLY A 202           
SHEET    5   A 8 ALA A  59  ILE A  62  1  O  ILE A  60   N  MET A 115           
SHEET    6   A 8 ILE A  11  LEU A  14  1  N  TYR A  12   O  ALA A  59           
SHEET    7   A 8 ILE A 324  TYR A 328  1  O  PRO A 325   N  ILE A  11           
SHEET    8   A 8 GLY A 290  THR A 291  1  N  THR A 291   O  ILE A 324           
SHEET    1   B 2 THR A  66  GLN A  68  0                                        
SHEET    2   B 2 GLN A  84  LEU A  90 -1  N  GLN A  85   O  ALA A  67           
SHEET    1   C 2 LEU A 166  GLY A 167  0                                        
SHEET    2   C 2 SER A 172  LEU A 173 -1  N  LEU A 173   O  LEU A 166           
SHEET    1   D 6 TRP A 385  ASP A 390  0                                        
SHEET    2   D 6 THR A 393  LYS A 398 -1  O  THR A 393   N  ASP A 390           
SHEET    3   D 6 ILE A 405  SER A 410 -1  N  ILE A 405   O  LYS A 398           
SHEET    4   D 6 ARG A 461  PRO A 465 -1  O  ARG A 461   N  ILE A 408           
SHEET    5   D 6 GLN A 433  GLU A 436 -1  N  THR A 435   O  TYR A 464           
SHEET    6   D 6 THR A 441  THR A 444 -1  O  THR A 441   N  GLU A 436           
SHEET    1   E 2 TYR A 419  LEU A 423  0                                        
SHEET    2   E 2 VAL A 451  MET A 455 -1  O  VAL A 451   N  LEU A 423           
SSBOND   1 CYS A   30    CYS A   38                          1555   1555  1.99  
SSBOND   2 CYS A  150    CYS A  164                          1555   1555  2.10  
SSBOND   3 CYS A  240    CYS A  283                          1555   1555  1.94  
SSBOND   4 CYS A  440    CYS A  475                          1555   1555  1.98  
LINK        CA    CA A 479                 O   GLU A 162     1555   1555  2.55  
LINK        CA    CA A 479                 O   HIS A 210     1555   1555  2.64  
LINK        CA    CA A 479                 O   HOH A 553     1555   1555  2.43  
LINK        CA    CA A 479                 OD2 ASP A 175     1555   1555  2.74  
LINK        CA    CA A 479                 O   HOH A 525     1555   1555  2.67  
LINK        CA    CA A 479                 O   HOH A 550     1555   1555  2.36  
LINK        CA    CA A 479                 OD1 ASN A 121     1555   1555  2.44  
LINK        CA    CA A 479                 OD1 ASP A 175     1555   1555  2.66  
LINK        CA    CA A 480                 OE2 GLU A 230     1555   1555  2.85  
LINK        CA    CA A 480                 O   HOH A 556     1555   1555  2.31  
LINK        CA    CA A 480                 OD1 ASP A 206     1555   1555  2.56  
LINK        CA    CA A 480                 OE1 GLU A 230     1555   1555  2.71  
CISPEP   1 LYS A  138    PRO A  139          0         5.52                     
CISPEP   2 ASP A  340    PRO A  341          0         0.06                     
SITE     1 AC1  7 ASN A 121  GLU A 162  ASP A 175  HIS A 210                    
SITE     2 AC1  7 HOH A 525  HOH A 550  HOH A 553                               
SITE     1 AC2  3 ASP A 206  GLU A 230  HOH A 556                               
CRYST1   51.040   67.183  133.560  90.00  90.00  90.00 P 21 21 21    4          
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      0.019592  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014885  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007487        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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