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Database: PDB
Entry: 1QI3
LinkDB: 1QI3
Original site: 1QI3 
HEADER    HYDROLASE                               01-JUN-99   1QI3              
TITLE     MUTANT (D193N) MALTOTETRAOSE-FORMING EXO-AMYLASE IN COMPLEX           
TITLE    2 WITH MALTOTETRAOSE                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (EXO-MALTOTETRAOHYDROLASE);                        
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                                                        
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    K.HASEGAWA,M.KUBOTA,Y.MATSUURA                                        
REVDAT   3   24-FEB-09 1QI3    1       VERSN                                    
REVDAT   2   01-APR-03 1QI3    1       JRNL                                     
REVDAT   1   24-NOV-99 1QI3    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,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   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) : 0.186                           
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            : 3297                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
REMARK   3   SOLVENT ATOMS            : 157                                     
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 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.032 ; 0.030               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.038 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.012 ; 0.020               
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.172 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.185 ; 0.400               
REMARK   3    MULTIPLE TORSION                (A) : 0.191 ; 0.400               
REMARK   3    H-BOND (X...Y)                  (A) : 0.154 ; 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) : 2.500 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 18.500; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : 33.200; 20.000              
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND               (A**2) : 0.708 ; 1.000               
REMARK   3   MAIN-CHAIN ANGLE              (A**2) : 1.252 ; 1.500               
REMARK   3   SIDE-CHAIN BOND               (A**2) : 1.320 ; 1.500               
REMARK   3   SIDE-CHAIN ANGLE              (A**2) : 2.113 ; 2.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1QI3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB001147.                                      
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                                
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   : 33736                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 62.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06200                            
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: OTHER                        
REMARK 200 SOFTWARE USED: AUTOMR                                                
REMARK 200 STARTING MODEL: 1JDD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 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       32.88500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.39000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       85.40000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       23.39000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.88500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       85.40000            
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: 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 219   CD    GLU A 219   OE2     0.081                       
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. =   5.1 DEGREES          
REMARK 500    ARG A  29   NE  -  CZ  -  NH2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ASP A  82   CB  -  CG  -  OD2 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG A  96   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG A  96   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 137   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG A 137   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    CYS A 140   CA  -  CB  -  SG  ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ASP A 162   CB  -  CG  -  OD1 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG A 175   CD  -  NE  -  CZ  ANGL. DEV. =  23.7 DEGREES          
REMARK 500    ARG A 175   NE  -  CZ  -  NH1 ANGL. DEV. =   9.1 DEGREES          
REMARK 500    ARG A 175   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A 191   NE  -  CZ  -  NH1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 212   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG A 233   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG A 233   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG A 248   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG A 248   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP A 279   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    TYR A 319   CB  -  CG  -  CD1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    TYR A 321   CB  -  CG  -  CD1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ASP A 334   CA  -  CB  -  CG  ANGL. DEV. = -15.1 DEGREES          
REMARK 500    ARG A 346   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    GLN A 347   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    ARG A 353   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG A 358   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ASP A 390   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG A 414   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 417   CD  -  NE  -  CZ  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG A 417   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 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       14.33     58.63                                   
REMARK 500    PHE A  79       55.53   -140.39                                   
REMARK 500    VAL A 114       77.69   -116.88                                   
REMARK 500    ASN A 148     -167.50   -119.36                                   
REMARK 500    ASP A 151      108.87   -171.59                                   
REMARK 500    ILE A 157     -109.42     56.09                                   
REMARK 500    PHE A 194       58.03     39.09                                   
REMARK 500    ALA A 211       57.62   -160.72                                   
REMARK 500    HIS A 306       61.77     38.76                                   
REMARK 500    TRP A 308       59.98   -162.82                                   
REMARK 500    PRO A 326      172.30    -56.49                                   
REMARK 500    SER A 409       62.87     39.57                                   
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         0.10    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 452  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A   2   O                                                      
REMARK 620 2 HIS A  13   O    84.3                                              
REMARK 620 3 HIS A  13   ND1  87.4  76.5                                        
REMARK 620 4 ASP A  16   OD1  95.3  90.8 166.7                                  
REMARK 620 5 GLU A  17   OE2 161.8 104.9  79.8 100.1                            
REMARK 620 6 ASP A   1   OD1  73.8 158.0 100.4  92.9  95.8                      
REMARK 620 N                    1     2     3     4     5                       
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 ASN A 116   OD1                                                    
REMARK 620 2 ASP A 151   OD1 137.1                                              
REMARK 620 3 ASP A 151   OD2 160.0  51.2                                        
REMARK 620 4 ASP A 154   O    98.9 112.2  90.7                                  
REMARK 620 5 ASP A 162   OD2  81.1 127.2  81.8  87.7                            
REMARK 620 6 GLY A 197   O    72.9  78.9 125.2  88.7 152.8                      
REMARK 620 7 HOH A 553   O    69.7  81.7  97.8 166.1  82.7  95.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: NUL                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: NULL                                               
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 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 1QI3       SWS     P13507       1 -    21 NOT IN ATOMS LIST          
REMARK 999 1QI3       SWS     P13507     440 -   548 NOT IN ATOMS LIST          
DBREF  1QI3 A    1   429  UNP    P13507   AMT4_PSEST      22    450             
SEQADV 1QI3 ASN A  193  UNP  P13507    ASP   214 ENGINEERED                     
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 ASN 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 GLU 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     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   *157(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  2.04  
LINK         O   GLN A   2                CA    CA A 452     1555   1555  2.43  
LINK         O   HIS A  13                CA    CA A 452     1555   1555  2.22  
LINK         ND1 HIS A  13                CA    CA A 452     1555   1555  2.36  
LINK         OD1 ASP A  16                CA    CA A 452     1555   1555  2.31  
LINK         OE2 GLU A  17                CA    CA A 452     1555   1555  2.00  
LINK         OD1 ASN A 116                CA    CA A 451     1555   1555  2.57  
LINK         OD1 ASP A 151                CA    CA A 451     1555   1555  2.63  
LINK         OD2 ASP A 151                CA    CA A 451     1555   1555  2.52  
LINK         O   ASP A 154                CA    CA A 451     1555   1555  2.41  
LINK         OD2 ASP A 162                CA    CA A 451     1555   1555  2.21  
LINK         O   GLY A 197                CA    CA A 451     1555   1555  2.35  
LINK        CA    CA A 451                 O   HOH A 553     1555   1555  2.45  
LINK        CA    CA A 452                 OD1 ASP A   1     1555   1555  1.94  
SITE     1 NUL  3 ASN A 193  GLU A 219  ASP A 294                               
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 20 TRP A  66  TYR A  78  PHE A  79  HIS A 117                    
SITE     2 AC3 20 PHE A 156  ILE A 157  GLY A 158  ASP A 160                    
SITE     3 AC3 20 ALA A 161  ASN A 193  PHE A 194  GLU A 219                    
SITE     4 AC3 20 ASP A 294  GLN A 305  HOH A 515  HOH A 665                    
SITE     5 AC3 20 HOH A 666  HOH A 685  HOH A 725  HOH A 731                    
CRYST1   65.770  170.800   46.780  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      0.015204  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005855  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021377        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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