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Database: PDB
Entry: 1QPK
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Original site: 1QPK 
HEADER    HYDROLASE                               26-MAY-99   1QPK              
TITLE     MUTANT (D193G) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX           
TITLE    2 WITH MALTOTETRAOSE                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (MALTOTETRAOSE-FORMING AMYLASE);                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS STUTZERI;                           
SOURCE   3 ORGANISM_TAXID: 316;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR: PUC18                                      
KEYWDS    BETA-ALPHA-BARRELS, HYDROLASE                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.YOSHIOKA,K.HASEGAWA,Y.MATSUURA,Y.KATSUBE,M.KUBOTA                   
REVDAT   2   24-FEB-09 1QPK    1       VERSN                                    
REVDAT   1   17-NOV-99 1QPK    0                                                
JRNL        AUTH   K.HASEGAWA,M.KUBOTA,Y.MATSUURA                               
JRNL        TITL   ROLES OF CATALYTIC RESIDUES IN ALPHA-AMYLASES AS             
JRNL        TITL 2 EVIDENCED BY THE STRUCTURES OF THE                           
JRNL        TITL 3 PRODUCT-COMPLEXED MUTANTS OF A                               
JRNL        TITL 4 MALTOTETRAOSE-FORMING AMYLASE.                               
JRNL        REF    PROTEIN ENG.                  V.  12   819 1999              
JRNL        REFN                   ISSN 0269-2139                               
JRNL        PMID   10556241                                                     
JRNL        DOI    10.1093/PROTEIN/12.10.819                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Y.YOSHIOKA,K.HASEGAWA,Y.MATSUURA,Y.KATSUBE,M.KUBOTA          
REMARK   1  TITL   CRYSTAL STRUCTURES OF A MUTANT                               
REMARK   1  TITL 2 MALTOTETRAOSE-FORMING EXO-AMYLASE COCRYSTALLIZED             
REMARK   1  TITL 3 WITH MALTOPENTAOSE                                           
REMARK   1  REF    J.MOL.BIOL.                   V. 271   619 1997              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  DOI    10.1006/JMBI.1997.1222                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   Y.MORISHITA,K.HASEGAWA,Y.MATSUURA,Y.KATSUBE,                 
REMARK   1  AUTH 2 M.KUBOTA                                                     
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   1  DOI    10.1006/JMBI.1996.0887                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROFFT                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON,FINZEL                           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
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             : NULL                           
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) : 0.178                           
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            : 3293                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
REMARK   3   SOLVENT ATOMS            : 173                                     
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) : 0.014 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.034 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
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) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN BOND               (A**2) : NULL  ; NULL                
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1QPK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAY-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB009117.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 7.5                                
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                  : 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 : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : R-AXIS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31354                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08200                            
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AUTOMR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS-HCL, PH 7.5       
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       31.60500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.36000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       83.75000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       23.36000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.60500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       83.75000            
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 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   334     OD1  ASP A   338              1.93            
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      0.153                       
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. =   5.0 DEGREES          
REMARK 500    ASP A  16   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP A  82   CB  -  CA  -  C   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    ASP A  82   CA  -  CB  -  CG  ANGL. DEV. = -17.3 DEGREES          
REMARK 500    ASP A  82   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP A  82   CB  -  CG  -  OD2 ANGL. DEV. = -14.5 DEGREES          
REMARK 500    ARG A  88   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    TYR A 122   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A 137   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A 137   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    CYS A 140   CA  -  CB  -  SG  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ASP A 152   CB  -  CG  -  OD1 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ASP A 152   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG A 155   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG A 155   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP A 160   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG A 175   NE  -  CZ  -  NH1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG A 191   NE  -  CZ  -  NH1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP A 212   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    TYR A 227   CB  -  CG  -  CD1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A 233   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 248   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ASP A 279   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 279   CB  -  CG  -  OD2 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    ARG A 281   NE  -  CZ  -  NH2 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    ASP A 343   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG A 346   CD  -  NE  -  CZ  ANGL. DEV. =  56.3 DEGREES          
REMARK 500    ARG A 346   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG A 352   NE  -  CZ  -  NH1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG A 352   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG A 353   CD  -  NE  -  CZ  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    ARG A 358   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ARG A 358   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ASP A 360   CB  -  CG  -  OD1 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG A 417   NE  -  CZ  -  NH1 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ARG A 417   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.3 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    HIS A  13       70.37     36.63                                   
REMARK 500    ASN A  33       17.86     51.54                                   
REMARK 500    ASN A 148     -169.83   -129.43                                   
REMARK 500    ASP A 151      108.95   -168.97                                   
REMARK 500    ILE A 157     -111.95     57.39                                   
REMARK 500    ALA A 211       63.26   -168.67                                   
REMARK 500    LYS A 222      113.76   -161.47                                   
REMARK 500    GLN A 301      119.32    -38.86                                   
REMARK 500    TRP A 308       64.36   -159.12                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 776        DISTANCE =  5.01 ANGSTROMS                       
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 154   O                                                      
REMARK 620 2 ASN A 116   OD1 103.5                                              
REMARK 620 3 ASP A 151   OD1  82.8 164.5                                        
REMARK 620 4 ASP A 151   OD2 104.3 139.3  49.0                                  
REMARK 620 5 GLY A 197   O    86.9  78.4 116.4  74.1                            
REMARK 620 6 HOH A 553   O   175.4  75.4  97.1  78.9  97.2                      
REMARK 620 7 ASP A 162   OD1  84.1  85.4  81.1 126.5 159.1  91.4                
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   OD2                                                    
REMARK 620 2 GLN A   2   O    75.9                                              
REMARK 620 3 HIS A  13   O   160.2  84.4                                        
REMARK 620 4 ASP A  16   OD2  99.6  89.2  82.3                                  
REMARK 620 5 GLU A  17   OE1  98.6 164.5  99.8 106.1                            
REMARK 620 6 HIS A  13   ND1  95.9  87.1  80.5 162.7  79.0                      
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 CA A 451                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 452                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MTT A 460                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QI3   RELATED DB: PDB                                   
REMARK 900 MUTANT (D193N) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX          
REMARK 900 WITH MALTOTETRAOSE                                                   
REMARK 900 RELATED ID: 1QI4   RELATED DB: PDB                                   
REMARK 900 MUTANT (E219G) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX          
REMARK 900 WITH MALTOTETRAOSE                                                   
REMARK 900 RELATED ID: 1QI5   RELATED DB: PDB                                   
REMARK 900 MUTANT (D294N) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX          
REMARK 900 WITH MALTOTETRAOSE                                                   
REMARK 900 RELATED ID: 2AMG   RELATED DB: PDB                                   
REMARK 900 MALTOTETRAOSE-FORMING EXO-AMYLASE                                    
REMARK 900 RELATED ID: 1JDA   RELATED DB: PDB                                   
REMARK 900 MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE                     
REMARK 900 RELATED ID: 1JDC   RELATED DB: PDB                                   
REMARK 900 MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX          
REMARK 900 WITH MALTOTETRAOSE (CRYSTAL TYPE 1)                                  
REMARK 900 RELATED ID: 1JDD   RELATED DB: PDB                                   
REMARK 900 MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX          
REMARK 900 WITH MALTOTETRAOSE (CRYSTAL TYPE 2)                                  
DBREF  1QPK A    1   418  UNP    P13507   AMT4_PSEST      22    439             
SEQADV 1QPK GLY A  193  UNP  P13507    ASP   214 ENGINEERED                     
SEQRES   1 A  418  ASP GLN ALA GLY LYS SER PRO ASN ALA VAL ARG TYR HIS          
SEQRES   2 A  418  GLY GLY ASP GLU ILE ILE LEU GLN GLY PHE HIS TRP ASN          
SEQRES   3 A  418  VAL VAL ARG GLU ALA PRO ASN ASP TRP TYR ASN ILE LEU          
SEQRES   4 A  418  ARG GLN GLN ALA ALA THR ILE ALA ALA ASP GLY PHE SER          
SEQRES   5 A  418  ALA ILE TRP MET PRO VAL PRO TRP ARG ASP PHE SER SER          
SEQRES   6 A  418  TRP SER ASP GLY SER LYS SER GLY GLY GLY GLU GLY TYR          
SEQRES   7 A  418  PHE TRP HIS ASP PHE ASN LYS ASN GLY ARG TYR GLY SER          
SEQRES   8 A  418  ASP ALA GLN LEU ARG GLN ALA ALA SER ALA LEU GLY GLY          
SEQRES   9 A  418  ALA GLY VAL LYS VAL LEU TYR ASP VAL VAL PRO ASN HIS          
SEQRES  10 A  418  MET ASN ARG GLY TYR PRO ASP LYS GLU ILE ASN LEU PRO          
SEQRES  11 A  418  ALA GLY GLN GLY PHE TRP ARG ASN ASP CYS ALA ASP PRO          
SEQRES  12 A  418  GLY ASN TYR PRO ASN ASP CYS ASP ASP GLY ASP ARG PHE          
SEQRES  13 A  418  ILE GLY GLY ASP ALA ASP LEU ASN THR GLY HIS PRO GLN          
SEQRES  14 A  418  VAL TYR GLY MET PHE ARG ASP GLU PHE THR ASN LEU ARG          
SEQRES  15 A  418  SER GLN TYR GLY ALA GLY GLY PHE ARG PHE GLY PHE VAL          
SEQRES  16 A  418  ARG GLY TYR ALA PRO GLU ARG VAL ASN SER TRP MET THR          
SEQRES  17 A  418  ASP SER ALA ASP ASN SER PHE CYS VAL GLY GLU LEU TRP          
SEQRES  18 A  418  LYS GLY PRO SER GLU TYR PRO ASN TRP ASP TRP ARG ASN          
SEQRES  19 A  418  THR ALA SER TRP GLN GLN ILE ILE LYS ASP TRP SER ASP          
SEQRES  20 A  418  ARG ALA LYS CYS PRO VAL PHE ASP PHE ALA LEU LYS GLU          
SEQRES  21 A  418  ARG MET GLN ASN GLY SER ILE ALA ASP TRP LYS HIS GLY          
SEQRES  22 A  418  LEU ASN GLY ASN PRO ASP PRO ARG TRP ARG GLU VAL ALA          
SEQRES  23 A  418  VAL THR PHE VAL ASP ASN HIS ASP THR GLY TYR SER PRO          
SEQRES  24 A  418  GLY GLN ASN GLY GLY GLN HIS HIS TRP ALA LEU GLN ASP          
SEQRES  25 A  418  GLY LEU ILE ARG GLN ALA TYR ALA TYR ILE LEU THR SER          
SEQRES  26 A  418  PRO GLY THR PRO VAL VAL TYR TRP ASP HIS MET TYR ASP          
SEQRES  27 A  418  TRP GLY TYR GLY ASP PHE ILE ARG GLN LEU ILE GLN VAL          
SEQRES  28 A  418  ARG ARG ALA ALA GLY VAL ARG ALA ASP SER ALA ILE SER          
SEQRES  29 A  418  PHE HIS SER GLY TYR SER GLY LEU VAL ALA THR VAL SER          
SEQRES  30 A  418  GLY SER GLN GLN THR LEU VAL VAL ALA LEU ASN SER ASP          
SEQRES  31 A  418  LEU GLY ASN PRO GLY GLN VAL ALA SER GLY SER PHE SER          
SEQRES  32 A  418  GLU ALA VAL ASN ALA SER ASN GLY GLN VAL ARG VAL TRP          
SEQRES  33 A  418  ARG SER                                                      
HET     CA  A 451       1                                                       
HET     CA  A 452       1                                                       
HET    MTT  A 460      45                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     MTT MALTOTETRAOSE                                                    
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4  MTT    C24 H42 O21                                                  
FORMUL   5  HOH   *173(H2 O)                                                    
HELIX    1   1 TYR A   12  ASP A   16  5                                   5    
HELIX    2   2 ASN A   26  ALA A   31  1                                   6    
HELIX    3   3 ASP A   34  GLY A   50  1                                  17    
HELIX    4   4 SER A   91  ALA A  105  1                                  15    
HELIX    5   5 ARG A  137  CYS A  140  5                                   4    
HELIX    6   6 HIS A  167  TYR A  185  1                                  19    
HELIX    7   7 PHE A  194  TYR A  198  5                                   5    
HELIX    8   8 ALA A  199  ALA A  211  1                                  13    
HELIX    9   9 GLY A  223  TYR A  227  5                                   5    
HELIX   10  10 ASP A  231  ALA A  236  5                                   6    
HELIX   11  11 SER A  237  LYS A  250  1                                  14    
HELIX   12  12 ASP A  255  GLY A  265  1                                  11    
HELIX   13  13 SER A  266  GLY A  273  5                                   8    
HELIX   14  14 GLY A  273  ASN A  277  5                                   5    
HELIX   15  15 ASP A  279  GLU A  284  1                                   6    
HELIX   16  16 GLY A  300  GLY A  304  5                                   5    
HELIX   17  17 GLN A  311  GLY A  313  5                                   3    
HELIX   18  18 LEU A  314  SER A  325  1                                  12    
HELIX   19  19 TRP A  333  ASP A  338  1                                   6    
HELIX   20  20 TYR A  341  GLY A  356  1                                  16    
HELIX   21  21 ASN A  393  VAL A  397  5                                   5    
HELIX   22  22 SER A  409  GLY A  411  5                                   3    
SHEET    1   A 9 ILE A  19  GLN A  21  0                                        
SHEET    2   A 9 ALA A  53  MET A  56  1  O  ALA A  53   N  LEU A  20           
SHEET    3   A 9 ILE A  19  GLN A  21  1  O  LEU A  20   N  TRP A  55           
SHEET    4   A 9 THR A 328  TYR A 332  1  O  PRO A 329   N  ILE A  19           
SHEET    5   A 9 ALA A 286  THR A 288  1  O  ALA A 286   N  THR A 328           
SHEET    6   A 9 VAL A 253  PHE A 254  1  O  VAL A 253   N  VAL A 287           
SHEET    7   A 9 PHE A 215  GLY A 218  1  O  GLY A 218   N  PHE A 254           
SHEET    8   A 9 ALA A 187  PHE A 192  1  O  GLY A 188   N  PHE A 215           
SHEET    9   A 9 LYS A 108  VAL A 113  1  O  VAL A 109   N  GLY A 188           
SHEET    1   B 2 TRP A  66  ASP A  68  0                                        
SHEET    2   B 2 LYS A  71  GLY A  73 -1  O  LYS A  71   N  ASP A  68           
SHEET    1   C 5 ALA A 362  HIS A 366  0                                        
SHEET    2   C 5 LEU A 372  SER A 377 -1  O  VAL A 373   N  HIS A 366           
SHEET    3   C 5 THR A 382  LEU A 387 -1  N  LEU A 383   O  VAL A 376           
SHEET    4   C 5 VAL A 413  ARG A 417 -1  O  ARG A 414   N  ALA A 386           
SHEET    5   C 5 SER A 403  ALA A 408 -1  N  SER A 403   O  ARG A 417           
SSBOND   1 CYS A  140    CYS A  150                          1555   1555  2.01  
SSBOND   2 CYS A  216    CYS A  251                          1555   1555  2.03  
LINK        CA    CA A 451                 O   ASP A 154     1555   1555  2.35  
LINK        CA    CA A 451                 OD1 ASN A 116     1555   1555  2.47  
LINK        CA    CA A 451                 OD1 ASP A 151     1555   1555  2.51  
LINK        CA    CA A 451                 OD2 ASP A 151     1555   1555  2.70  
LINK        CA    CA A 451                 O   GLY A 197     1555   1555  2.39  
LINK        CA    CA A 451                 O   HOH A 553     1555   1555  2.45  
LINK        CA    CA A 451                 OD1 ASP A 162     1555   1555  2.57  
LINK        CA    CA A 452                 OD2 ASP A   1     1555   1555  1.99  
LINK        CA    CA A 452                 O   GLN A   2     1555   1555  2.31  
LINK        CA    CA A 452                 O   HIS A  13     1555   1555  2.19  
LINK        CA    CA A 452                 OD2 ASP A  16     1555   1555  2.27  
LINK        CA    CA A 452                 OE1 GLU A  17     1555   1555  2.20  
LINK        CA    CA A 452                 ND1 HIS A  13     1555   1555  2.45  
SITE     1 AC1  6 ASN A 116  ASP A 151  ASP A 154  ASP A 162                    
SITE     2 AC1  6 GLY A 197  HOH A 553                                          
SITE     1 AC2  5 ASP A   1  GLN A   2  HIS A  13  ASP A  16                    
SITE     2 AC2  5 GLU A  17                                                     
SITE     1 AC3 21 TRP A  25  TRP A  66  TYR A  78  PHE A  79                    
SITE     2 AC3 21 HIS A 117  PHE A 156  ILE A 157  GLY A 158                    
SITE     3 AC3 21 ASP A 160  ARG A 191  GLY A 193  PHE A 194                    
SITE     4 AC3 21 GLU A 219  HIS A 293  ASP A 294  GLN A 305                    
SITE     5 AC3 21 HOH A 515  HOH A 665  HOH A 666  HOH A 718                    
SITE     6 AC3 21 HOH A 730                                                     
CRYST1   63.210  167.500   46.720  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      0.015820  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005970  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021404        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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