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Database: PDB
Entry: 1JDD
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HEADER    HYDROLASE                               16-JUN-97   1JDD              
TITLE     MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE                      
TITLE    2 COCRYSTALLIZED WITH MALTOTETRAOSE (CRYSTAL TYPE 2)                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 1,4-ALPHA MALTOTETRAHYDROLASE;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MALTOTETRAOSE-FORMING EXO-AMYLASE;                          
COMPND   5 EC: 3.2.1.60;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: CRYSTAL TYPE 2                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS STUTZERI;                           
SOURCE   3 ORGANISM_TAXID: 316;                                                 
SOURCE   4 STRAIN: MO-19;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: HB101;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PUC18                                      
KEYWDS    HYDROLASE, MALTOTETRAOSE-FORMING EXO AMYLASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.YOSHIOKA,K.HASEGAWA,Y.MATSUURA,Y.KATSUBE,M.KUBOTA                   
REVDAT   2   24-FEB-09 1JDD    1       VERSN                                    
REVDAT   1   15-OCT-97 1JDD    0                                                
JRNL        AUTH   Y.YOSHIOKA,K.HASEGAWA,Y.MATSUURA,Y.KATSUBE,M.KUBOTA          
JRNL        TITL   CRYSTAL STRUCTURES OF A MUTANT                               
JRNL        TITL 2 MALTOTETRAOSE-FORMING EXO-AMYLASE COCRYSTALLIZED             
JRNL        TITL 3 WITH MALTOPENTAOSE.                                          
JRNL        REF    J.MOL.BIOL.                   V. 271   619 1997              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9281429                                                      
JRNL        DOI    10.1006/JMBI.1997.1222                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Y.MORISHITA,K.HASEGAWA,Y.MATSUURA,Y.KATSUBE,                 
REMARK   1  AUTH 2 M.KUBOTA,S.SAKAI                                             
REMARK   1  TITL   CRYSTAL STRUCTURE OF A MALTOTETRAOSE-FORMING                 
REMARK   1  TITL 2 EXO-AMYLASE FROM PSEUDOMONAS STUTZERI                        
REMARK   1  REF    J.MOL.BIOL.                   V. 267   661 1997              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROFFT, X-PLOR                                       
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,FINZEL                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 35190                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
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            : 3297                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 46                                      
REMARK   3   SOLVENT ATOMS            : 227                                     
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) : 0.18                            
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) : 0.015 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.035 ; 0.030               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.042 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.013 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.187 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.187 ; 0.400               
REMARK   3    MULTIPLE TORSION                (A) : 0.202 ; 0.400               
REMARK   3    H-BOND (X...Y)                  (A) : 0.181 ; 0.400               
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 2.600 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 19.100; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : 32.700; 20.000              
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 0.725 ; 1.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 1.266 ; 1.500               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.352 ; 1.500               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 2.145 ; 2.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: X-PLOR WAS ALSO USED.                     
REMARK   4                                                                      
REMARK   4 1JDD 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        : 27-NOV-92                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35190                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08900                            
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: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76                     
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       32.80000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.40000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       85.35000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       23.40000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.80000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       85.35000            
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     GLY A   419                                                      
REMARK 465     THR A   420                                                      
REMARK 465     GLY A   421                                                      
REMARK 465     SER A   422                                                      
REMARK 465     GLY A   423                                                      
REMARK 465     GLY A   424                                                      
REMARK 465     GLY A   425                                                      
REMARK 465     GLU A   426                                                      
REMARK 465     PRO A   427                                                      
REMARK 465     GLY A   428                                                      
REMARK 465     ALA A   429                                                      
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   NH1  ARG A    61     OD2  ASP A    82              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    ASP A  82   CA    ASP A  82   CB      0.149                       
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  11   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG A  61   CD  -  NE  -  CZ  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    ARG A  61   NE  -  CZ  -  NH1 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ARG A  61   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    ASP A  68   N   -  CA  -  CB  ANGL. DEV. =  12.3 DEGREES          
REMARK 500    ASP A  82   CB  -  CA  -  C   ANGL. DEV. = -16.5 DEGREES          
REMARK 500    ASP A  82   CA  -  CB  -  CG  ANGL. DEV. = -14.1 DEGREES          
REMARK 500    ASP A  82   CB  -  CG  -  OD1 ANGL. DEV. = -15.4 DEGREES          
REMARK 500    ASP A  82   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG A  96   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A 137   NE  -  CZ  -  NH1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ARG A 137   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP A 139   CB  -  CG  -  OD1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP A 139   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    CYS A 140   CA  -  CB  -  SG  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ASP A 152   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ARG A 175   CD  -  NE  -  CZ  ANGL. DEV. =  13.2 DEGREES          
REMARK 500    ARG A 175   NE  -  CZ  -  NH1 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG A 175   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG A 182   CD  -  NE  -  CZ  ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    ASP A 231   CB  -  CG  -  OD1 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ARG A 233   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG A 233   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ASP A 244   CB  -  CG  -  OD1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG A 248   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    CYS A 251   CA  -  CB  -  SG  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ASP A 279   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG A 283   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 283   NE  -  CZ  -  NH2 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    TYR A 319   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG A 346   CD  -  NE  -  CZ  ANGL. DEV. =  40.0 DEGREES          
REMARK 500    ARG A 346   NH1 -  CZ  -  NH2 ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    ARG A 346   NE  -  CZ  -  NH1 ANGL. DEV. =  12.0 DEGREES          
REMARK 500    GLN A 347   CA  -  CB  -  CG  ANGL. DEV. =  18.7 DEGREES          
REMARK 500    ARG A 352   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 353   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 358   CD  -  NE  -  CZ  ANGL. DEV. =  56.2 DEGREES          
REMARK 500    ARG A 358   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG A 358   NE  -  CZ  -  NH2 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    VAL A 373   CA  -  CB  -  CG1 ANGL. DEV. =   9.2 DEGREES          
REMARK 500    ASP A 390   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    VAL A 397   N   -  CA  -  CB  ANGL. DEV. = -13.7 DEGREES          
REMARK 500    ARG A 414   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG A 414   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG A 417   CB  -  CA  -  C   ANGL. DEV. = -12.2 DEGREES          
REMARK 500    ARG A 417   CD  -  NE  -  CZ  ANGL. DEV. = -13.0 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    ASN A  33       17.57     57.36                                   
REMARK 500    ASN A 148     -165.29   -113.08                                   
REMARK 500    ASP A 151      109.46   -172.00                                   
REMARK 500    ILE A 157     -112.43     55.86                                   
REMARK 500    PHE A 194       62.54     34.16                                   
REMARK 500    ALA A 211       54.99   -158.65                                   
REMARK 500    TRP A 308       60.79   -166.18                                   
REMARK 500    PRO A 326      172.73    -55.00                                   
REMARK 500    SER A 409       66.09     39.13                                   
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    ARG A 417         0.12    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 451  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 162   OD2                                                    
REMARK 620 2 GLY A 197   O   153.2                                              
REMARK 620 3 ASP A 154   O    85.8  90.1                                        
REMARK 620 4 ASN A 116   OD1  85.4  69.2 100.0                                  
REMARK 620 5 ASP A 151   OD1 129.2  76.9 109.9 134.4                            
REMARK 620 6 ASP A 151   OD2  82.0 124.5  90.4 163.0  51.2                      
REMARK 620 7 HOH A 594   O    85.8  94.8 169.8  73.6  79.9  94.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 452  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A   1   OD1                                                    
REMARK 620 2 GLU A  17   OE2  94.0                                              
REMARK 620 3 HIS A  13   O   152.3 104.7                                        
REMARK 620 4 GLN A   2   O    75.1 154.7  79.5                                  
REMARK 620 5 ASP A  16   OD1 100.4 108.5  93.0  96.0                            
REMARK 620 6 HIS A  13   ND1  96.8  72.0  70.5  86.5 162.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 460                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 461                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 462                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 463                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 451                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 452                  
DBREF  1JDD A    1   429  UNP    P13507   AMT4_PSEST      22    450             
SEQADV 1JDD GLN A  219  UNP  P13507    GLU   240 ENGINEERED                     
SEQADV 1JDD ASP A  334  UNP  P13507    SER   355 CONFLICT                       
SEQRES   1 A  429  ASP GLN ALA GLY LYS SER PRO ASN ALA VAL ARG TYR HIS          
SEQRES   2 A  429  GLY GLY ASP GLU ILE ILE LEU GLN GLY PHE HIS TRP ASN          
SEQRES   3 A  429  VAL VAL ARG GLU ALA PRO ASN ASP TRP TYR ASN ILE LEU          
SEQRES   4 A  429  ARG GLN GLN ALA ALA THR ILE ALA ALA ASP GLY PHE SER          
SEQRES   5 A  429  ALA ILE TRP MET PRO VAL PRO TRP ARG ASP PHE SER SER          
SEQRES   6 A  429  TRP SER ASP GLY SER LYS SER GLY GLY GLY GLU GLY TYR          
SEQRES   7 A  429  PHE TRP HIS ASP PHE ASN LYS ASN GLY ARG TYR GLY SER          
SEQRES   8 A  429  ASP ALA GLN LEU ARG GLN ALA ALA SER ALA LEU GLY GLY          
SEQRES   9 A  429  ALA GLY VAL LYS VAL LEU TYR ASP VAL VAL PRO ASN HIS          
SEQRES  10 A  429  MET ASN ARG GLY TYR PRO ASP LYS GLU ILE ASN LEU PRO          
SEQRES  11 A  429  ALA GLY GLN GLY PHE TRP ARG ASN ASP CYS ALA ASP PRO          
SEQRES  12 A  429  GLY ASN TYR PRO ASN ASP CYS ASP ASP GLY ASP ARG PHE          
SEQRES  13 A  429  ILE GLY GLY ASP ALA ASP LEU ASN THR GLY HIS PRO GLN          
SEQRES  14 A  429  VAL TYR GLY MET PHE ARG ASP GLU PHE THR ASN LEU ARG          
SEQRES  15 A  429  SER GLN TYR GLY ALA GLY GLY PHE ARG PHE ASP PHE VAL          
SEQRES  16 A  429  ARG GLY TYR ALA PRO GLU ARG VAL ASN SER TRP MET THR          
SEQRES  17 A  429  ASP SER ALA ASP ASN SER PHE CYS VAL GLY GLN LEU TRP          
SEQRES  18 A  429  LYS GLY PRO SER GLU TYR PRO ASN TRP ASP TRP ARG ASN          
SEQRES  19 A  429  THR ALA SER TRP GLN GLN ILE ILE LYS ASP TRP SER ASP          
SEQRES  20 A  429  ARG ALA LYS CYS PRO VAL PHE ASP PHE ALA LEU LYS GLU          
SEQRES  21 A  429  ARG MET GLN ASN GLY SER ILE ALA ASP TRP LYS HIS GLY          
SEQRES  22 A  429  LEU ASN GLY ASN PRO ASP PRO ARG TRP ARG GLU VAL ALA          
SEQRES  23 A  429  VAL THR PHE VAL ASP ASN HIS ASP THR GLY TYR SER PRO          
SEQRES  24 A  429  GLY GLN ASN GLY GLY GLN HIS HIS TRP ALA LEU GLN ASP          
SEQRES  25 A  429  GLY LEU ILE ARG GLN ALA TYR ALA TYR ILE LEU THR SER          
SEQRES  26 A  429  PRO GLY THR PRO VAL VAL TYR TRP ASP HIS MET TYR ASP          
SEQRES  27 A  429  TRP GLY TYR GLY ASP PHE ILE ARG GLN LEU ILE GLN VAL          
SEQRES  28 A  429  ARG ARG ALA ALA GLY VAL ARG ALA ASP SER ALA ILE SER          
SEQRES  29 A  429  PHE HIS SER GLY TYR SER GLY LEU VAL ALA THR VAL SER          
SEQRES  30 A  429  GLY SER GLN GLN THR LEU VAL VAL ALA LEU ASN SER ASP          
SEQRES  31 A  429  LEU GLY ASN PRO GLY GLN VAL ALA SER GLY SER PHE SER          
SEQRES  32 A  429  GLU ALA VAL ASN ALA SER ASN GLY GLN VAL ARG VAL TRP          
SEQRES  33 A  429  ARG SER GLY THR GLY SER GLY GLY GLY GLU PRO GLY ALA          
HET    GLC  A 460      11                                                       
HET    GLC  A 461      11                                                       
HET    GLC  A 462      11                                                       
HET    GLC  A 463      12                                                       
HET     CA  A 451       1                                                       
HET     CA  A 452       1                                                       
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  GLC    4(C6 H12 O6)                                                 
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   5  HOH   *152(H2 O)                                                    
HELIX    1   1 HIS A   13  GLY A   15  5                                   3    
HELIX    2   2 VAL A   27  GLU A   30  1                                   4    
HELIX    3   3 TRP A   35  ASP A   49  1                                  15    
HELIX    4   4 ASP A   92  GLY A  104  1                                  13    
HELIX    5   5 ARG A  137  ASP A  139  5                                   3    
HELIX    6   6 PRO A  168  GLN A  184  1                                  17    
HELIX    7   7 VAL A  195  GLY A  197  5                                   3    
HELIX    8   8 PRO A  200  SER A  210  1                                  11    
HELIX    9   9 PRO A  224  GLU A  226  5                                   3    
HELIX   10  10 TRP A  232  THR A  235  5                                   4    
HELIX   11  11 TRP A  238  ALA A  249  1                                  12    
HELIX   12  12 PHE A  256  ASN A  264  1                                   9    
HELIX   13  13 ILE A  267  HIS A  272  5                                   6    
HELIX   14  14 LEU A  274  GLY A  276  5                                   3    
HELIX   15  15 PRO A  280  VAL A  285  1                                   6    
HELIX   16  16 GLN A  301  GLY A  303  5                                   3    
HELIX   17  17 ASP A  312  THR A  324  5                                  13    
HELIX   18  18 TRP A  333  TYR A  337  1                                   5    
HELIX   19  19 GLY A  342  ALA A  355  1                                  14    
HELIX   20  20 PRO A  394  GLN A  396  5                                   3    
SHEET    1   A 6 VAL A 330  TYR A 332  0                                        
SHEET    2   A 6 ILE A  19  GLN A  21  1  N  ILE A  19   O  VAL A 331           
SHEET    3   A 6 ALA A  53  MET A  56  1  N  ALA A  53   O  LEU A  20           
SHEET    4   A 6 LYS A 108  VAL A 113  1  N  LYS A 108   O  ILE A  54           
SHEET    5   A 6 ALA A 187  PHE A 192  1  N  GLY A 188   O  VAL A 109           
SHEET    6   A 6 PHE A 215  GLY A 218  1  N  PHE A 215   O  PHE A 190           
SHEET    1   B 2 TRP A  66  ASP A  68  0                                        
SHEET    2   B 2 LYS A  71  GLY A  73 -1  N  GLY A  73   O  TRP A  66           
SHEET    1   C 5 ALA A 362  PHE A 365  0                                        
SHEET    2   C 5 LEU A 372  SER A 377 -1  N  SER A 377   O  ALA A 362           
SHEET    3   C 5 THR A 382  LEU A 387 -1  N  LEU A 387   O  LEU A 372           
SHEET    4   C 5 VAL A 413  ARG A 417 -1  N  TRP A 416   O  VAL A 384           
SHEET    5   C 5 SER A 403  ALA A 408 -1  N  ALA A 408   O  VAL A 413           
SSBOND   1 CYS A  140    CYS A  150                          1555   1555  2.04  
SSBOND   2 CYS A  216    CYS A  251                          1555   1555  2.03  
LINK        CA    CA A 451                 OD2 ASP A 162     1555   1555  2.28  
LINK        CA    CA A 451                 O   GLY A 197     1555   1555  2.34  
LINK        CA    CA A 452                 OD1 ASP A   1     1555   1555  1.93  
LINK        CA    CA A 452                 OE2 GLU A  17     1555   1555  2.16  
LINK         C1  GLC A 460                 O4  GLC A 461     1555   1555  1.45  
LINK         C1  GLC A 461                 O4  GLC A 462     1555   1555  1.40  
LINK         C1  GLC A 462                 O4  GLC A 463     1555   1555  1.38  
LINK        CA    CA A 451                 O   ASP A 154     1555   1555  2.41  
LINK        CA    CA A 451                 OD1 ASN A 116     1555   1555  2.57  
LINK        CA    CA A 451                 OD1 ASP A 151     1555   1555  2.69  
LINK        CA    CA A 451                 OD2 ASP A 151     1555   1555  2.47  
LINK        CA    CA A 451                 O   HOH A 594     1555   1555  2.51  
LINK        CA    CA A 452                 O   HIS A  13     1555   1555  2.45  
LINK        CA    CA A 452                 O   GLN A   2     1555   1555  2.43  
LINK        CA    CA A 452                 OD1 ASP A  16     1555   1555  2.56  
LINK        CA    CA A 452                 ND1 HIS A  13     1555   1555  2.73  
SITE     1 AC1  7 PHE A  79  ILE A 157  GLY A 158  ASP A 160                    
SITE     2 AC1  7 ALA A 161  GLC A 461  HOH A 649                               
SITE     1 AC2  7 TRP A  66  PHE A  79  ILE A 157  GLC A 460                    
SITE     2 AC2  7 GLC A 462  HOH A 560  HOH A 591                               
SITE     1 AC3  8 TRP A  25  TYR A  78  GLN A 305  GLC A 461                    
SITE     2 AC3  8 GLC A 463  HOH A 576  HOH A 627  HOH A 630                    
SITE     1 AC4 11 TYR A  78  HIS A 117  PHE A 156  ARG A 191                    
SITE     2 AC4 11 ASP A 193  PHE A 194  GLN A 219  HIS A 293                    
SITE     3 AC4 11 ASP A 294  GLC A 462  HOH A 561                               
SITE     1 AC5  6 ASN A 116  ASP A 151  ASP A 154  ASP A 162                    
SITE     2 AC5  6 GLY A 197  HOH A 594                                          
SITE     1 AC6  5 ASP A   1  GLN A   2  HIS A  13  ASP A  16                    
SITE     2 AC6  5 GLU A  17                                                     
CRYST1   65.600  170.700   46.800  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      0.015244  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005858  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021368        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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