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Database: PDB
Entry: 2GUY
LinkDB: 2GUY
Original site: 2GUY 
HEADER    HYDROLASE                               02-MAY-06   2GUY              
TITLE     ORTHORHOMBIC CRYSTAL STRUCTURE (SPACE GROUP P21212) OF ASPERGILLUS    
TITLE    2 NIGER ALPHA-AMYLASE AT 1.6 A RESOLUTION                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE A;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TAKA-AMYLASE A, TAA, 1,4- ALPHA-D-GLUCAN GLUCANOHYDROLASE;  
COMPND   5 EC: 3.2.1.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;                             
SOURCE   3 ORGANISM_TAXID: 5062                                                 
KEYWDS    (BETA-ALPHA) 8 BARREL, HYDROLASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.VUJICIC ZAGAR                                                       
REVDAT   3   13-JUL-11 2GUY    1       VERSN                                    
REVDAT   2   24-FEB-09 2GUY    1       VERSN                                    
REVDAT   1   15-AUG-06 2GUY    0                                                
JRNL        AUTH   A.VUJICIC-ZAGAR,B.W.DIJKSTRA                                 
JRNL        TITL   MONOCLINIC CRYSTAL FORM OF ASPERGILLUS NIGER ALPHA-AMYLASE   
JRNL        TITL 2 IN COMPLEX WITH MALTOSE AT 1.8 ANGSTROMS RESOLUTION.         
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  62   716 2006              
JRNL        REFN                   ESSN 1744-3091                               
JRNL        PMID   16880540                                                     
JRNL        DOI    10.1107/S1744309106024729                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.59 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.59                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 60711                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.196                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3245                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.59                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.63                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3418                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 183                          
REMARK   3   BIN FREE R VALUE                    : 0.2720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3686                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 564                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.31                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.79000                                             
REMARK   3    B22 (A**2) : 1.08000                                              
REMARK   3    B33 (A**2) : -0.29000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.084         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.085         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.059         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.205         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3828 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5234 ; 1.483 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   475 ; 5.772 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   174 ;35.711 ;25.115       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   567 ;13.725 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;10.104 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   579 ; 0.110 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2950 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1903 ; 0.217 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2703 ; 0.324 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   815 ; 0.172 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.030 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    48 ; 0.235 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    98 ; 0.279 ; 0.500       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2394 ; 1.158 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3805 ; 1.726 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1659 ; 1.482 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1429 ; 2.129 ; 3.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   476                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.5739   6.5953  18.7641              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0168 T22:  -0.0169                                     
REMARK   3      T33:  -0.0373 T12:   0.0354                                     
REMARK   3      T13:   0.0160 T23:  -0.0221                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0247 L22:   0.8174                                     
REMARK   3      L33:   0.6026 L12:  -0.3997                                     
REMARK   3      L13:   0.0484 L23:  -0.2453                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1099 S12:   0.1992 S13:   0.0083                       
REMARK   3      S21:  -0.0613 S22:  -0.1166 S23:  -0.0204                       
REMARK   3      S31:  -0.0035 S32:  -0.0366 S33:   0.0068                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2GUY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB037580.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-AUG-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91835                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : PRODC                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 65130                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.590                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07900                            
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) : 1.59                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55600                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 7TAA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 0.2M NA-ACETATE, 0.1M NA   
REMARK 280  -CACODYLATE, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  296K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       51.39950            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.61400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.39950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.61400            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1252  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   477                                                      
REMARK 465     SER A   478                                                      
REMARK 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   NZ   LYS A   412     CE1  TYR A   419              2.02            
REMARK 500   O    HOH A  1147     O    HOH A  1521              2.09            
REMARK 500   O    HOH A  1177     O    HOH A  1443              2.12            
REMARK 500   O    HOH A  1311     O    HOH A  1375              2.12            
REMARK 500   OE1  GLU A   109     O    HOH A  1452              2.13            
REMARK 500   O    HOH A  1112     O    HOH A  1446              2.17            
REMARK 500   OG   SER A   422     ND2  ASN A   450              2.17            
REMARK 500   O    HOH A  1134     O    HOH A  1566              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1227     O    HOH A  1302     2555     2.03            
REMARK 500   O    HOH A  1428     O    HOH A  1441     3556     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  78       45.81    -79.57                                   
REMARK 500    TRP A  83       61.50   -119.95                                   
REMARK 500    GLN A  85      -34.80   -130.64                                   
REMARK 500    ALA A 329      121.60    -36.03                                   
REMARK 500    ASP A 340      126.94    -33.64                                   
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 A1123        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH A1444        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH A1470        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH A1540        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A1555        DISTANCE =  5.04 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 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1050   O                                                      
REMARK 620 2 GLU A 162   O    73.9                                              
REMARK 620 3 ASP A 175   OD2  88.7  78.1                                        
REMARK 620 4 HOH A1026   O   144.2  72.5  96.4                                  
REMARK 620 5 HOH A1194   O   144.7 132.4  77.4  70.4                            
REMARK 620 6 ASP A 175   OD1  68.3 115.7  51.7 139.5  77.8                      
REMARK 620 7 ASN A 121   OD1  88.7 152.1 124.0 116.4  73.4  75.8                
REMARK 620 8 HIS A 210   O    80.1  81.7 159.0  83.0 121.4 136.1  73.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 601                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 7TAA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FAMILY 13 ALPHA AMYLASE FROM                    
REMARK 900 ASPERGILLUS ORYZAE IN COMPLEX WITH ACARBOSE                          
REMARK 900 RELATED ID: 6TAA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN IN A DIFFERENT                 
REMARK 900 CRYSTAL FORM                                                         
REMARK 900 RELATED ID: 2TAA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN IN A DIFFERENT                 
REMARK 900 CRYSTAL FORM                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 CURRENTLY THERE IS NO AMINOACID SEQUENCE DATABASE REFERENCE          
REMARK 999 AVAILABLE FOR THE PROTEIN                                            
DBREF  2GUY A    1   478  UNP    P0C1B3   AMYA1_ASPOR     22    499             
SEQRES   1 A  478  ALA THR PRO ALA ASP TRP ARG SER GLN SER ILE TYR PHE          
SEQRES   2 A  478  LEU LEU THR ASP ARG PHE ALA ARG THR ASP GLY SER THR          
SEQRES   3 A  478  THR ALA THR CYS ASN THR ALA ASP GLN LYS TYR CYS GLY          
SEQRES   4 A  478  GLY THR TRP GLN GLY ILE ILE ASP LYS LEU ASP TYR ILE          
SEQRES   5 A  478  GLN GLY MET GLY PHE THR ALA ILE TRP ILE THR PRO VAL          
SEQRES   6 A  478  THR ALA GLN LEU PRO GLN THR THR ALA TYR GLY ASP ALA          
SEQRES   7 A  478  TYR HIS GLY TYR TRP GLN GLN ASP ILE TYR SER LEU ASN          
SEQRES   8 A  478  GLU ASN TYR GLY THR ALA ASP ASP LEU LYS ALA LEU SER          
SEQRES   9 A  478  SER ALA LEU HIS GLU ARG GLY MET TYR LEU MET VAL ASP          
SEQRES  10 A  478  VAL VAL ALA ASN HIS MET GLY TYR ASP GLY ALA GLY SER          
SEQRES  11 A  478  SER VAL ASP TYR SER VAL PHE LYS PRO PHE SER SER GLN          
SEQRES  12 A  478  ASP TYR PHE HIS PRO PHE CYS PHE ILE GLN ASN TYR GLU          
SEQRES  13 A  478  ASP GLN THR GLN VAL GLU ASP CYS TRP LEU GLY ASP ASN          
SEQRES  14 A  478  THR VAL SER LEU PRO ASP LEU ASP THR THR LYS ASP VAL          
SEQRES  15 A  478  VAL LYS ASN GLU TRP TYR ASP TRP VAL GLY SER LEU VAL          
SEQRES  16 A  478  SER ASN TYR SER ILE ASP GLY LEU ARG ILE ASP THR VAL          
SEQRES  17 A  478  LYS HIS VAL GLN LYS ASP PHE TRP PRO GLY TYR ASN LYS          
SEQRES  18 A  478  ALA ALA GLY VAL TYR CYS ILE GLY GLU VAL LEU ASP GLY          
SEQRES  19 A  478  ASP PRO ALA TYR THR CYS PRO TYR GLN ASN VAL MET ASP          
SEQRES  20 A  478  GLY VAL LEU ASN TYR PRO ILE TYR TYR PRO LEU LEU ASN          
SEQRES  21 A  478  ALA PHE LYS SER THR SER GLY SER MET ASP ASP LEU TYR          
SEQRES  22 A  478  ASN MET ILE ASN THR VAL LYS SER ASP CYS PRO ASP SER          
SEQRES  23 A  478  THR LEU LEU GLY THR PHE VAL GLU ASN HIS ASP ASN PRO          
SEQRES  24 A  478  ARG PHE ALA SER TYR THR ASN ASP ILE ALA LEU ALA LYS          
SEQRES  25 A  478  ASN VAL ALA ALA PHE ILE ILE LEU ASN ASP GLY ILE PRO          
SEQRES  26 A  478  ILE ILE TYR ALA GLY GLN GLU GLN HIS TYR ALA GLY GLY          
SEQRES  27 A  478  ASN ASP PRO ALA ASN ARG GLU ALA THR TRP LEU SER GLY          
SEQRES  28 A  478  TYR PRO THR ASP SER GLU LEU TYR LYS LEU ILE ALA SER          
SEQRES  29 A  478  ALA ASN ALA ILE ARG ASN TYR ALA ILE SER LYS ASP THR          
SEQRES  30 A  478  GLY PHE VAL THR TYR LYS ASN TRP PRO ILE TYR LYS ASP          
SEQRES  31 A  478  ASP THR THR ILE ALA MET ARG LYS GLY THR ASP GLY SER          
SEQRES  32 A  478  GLN ILE VAL THR ILE LEU SER ASN LYS GLY ALA SER GLY          
SEQRES  33 A  478  ASP SER TYR THR LEU SER LEU SER GLY ALA GLY TYR THR          
SEQRES  34 A  478  ALA GLY GLN GLN LEU THR GLU VAL ILE GLY CYS THR THR          
SEQRES  35 A  478  VAL THR VAL GLY SER ASP GLY ASN VAL PRO VAL PRO MET          
SEQRES  36 A  478  ALA GLY GLY LEU PRO ARG VAL LEU TYR PRO THR GLU LYS          
SEQRES  37 A  478  LEU ALA GLY SER LYS ILE CYS SER SER SER                      
MODRES 2GUY ASN A  197  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A1000      14                                                       
HET    NAG  A1001      14                                                       
HET    BMA  A1002      11                                                       
HET     CA  A 601       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM      CA CALCIUM ION                                                      
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   2  BMA    C6 H12 O6                                                    
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *564(H2 O)                                                    
HELIX    1   1 THR A    2  ARG A    7  1                                   6    
HELIX    2   2 LEU A   15  ALA A   20  1                                   6    
HELIX    3   3 ASN A   31  GLN A   35  5                                   5    
HELIX    4   4 THR A   41  LYS A   48  1                                   8    
HELIX    5   5 LYS A   48  GLY A   54  1                                   7    
HELIX    6   6 THR A   96  ARG A  110  1                                  15    
HELIX    7   7 ALA A  128  VAL A  132  5                                   5    
HELIX    8   8 ASP A  133  PHE A  137  5                                   5    
HELIX    9   9 SER A  142  PHE A  146  5                                   5    
HELIX   10  10 ASP A  157  CYS A  164  1                                   8    
HELIX   11  11 LYS A  180  SER A  199  1                                  20    
HELIX   12  12 THR A  207  VAL A  211  5                                   5    
HELIX   13  13 GLN A  212  ASP A  214  5                                   3    
HELIX   14  14 PHE A  215  GLY A  224  1                                  10    
HELIX   15  15 ASP A  235  CYS A  240  1                                   6    
HELIX   16  16 PRO A  241  VAL A  245  5                                   5    
HELIX   17  17 ASN A  251  LYS A  263  1                                  13    
HELIX   18  18 SER A  268  CYS A  283  1                                  16    
HELIX   19  19 ASP A  285  LEU A  288  5                                   4    
HELIX   20  20 ARG A  300  TYR A  304  5                                   5    
HELIX   21  21 ASP A  307  ASN A  321  1                                  15    
HELIX   22  22 GLY A  330  HIS A  334  5                                   5    
HELIX   23  23 ALA A  346  GLY A  351  5                                   6    
HELIX   24  24 SER A  356  ASP A  376  1                                  21    
HELIX   25  25 GLU A  467  ALA A  470  5                                   4    
SHEET    1   A 8 GLY A 248  VAL A 249  0                                        
SHEET    2   A 8 TYR A 226  GLY A 229  1  N  GLY A 229   O  GLY A 248           
SHEET    3   A 8 GLY A 202  ILE A 205  1  N  ILE A 205   O  ILE A 228           
SHEET    4   A 8 TYR A 113  VAL A 118  1  N  VAL A 118   O  ARG A 204           
SHEET    5   A 8 ALA A  59  ILE A  62  1  N  ILE A  60   O  MET A 115           
SHEET    6   A 8 ILE A  11  LEU A  14  1  N  LEU A  14   O  TRP A  61           
SHEET    7   A 8 ILE A 324  TYR A 328  1  O  PRO A 325   N  ILE A  11           
SHEET    8   A 8 GLY A 290  THR A 291  1  N  THR A 291   O  ILE A 326           
SHEET    1   B 2 THR A  66  GLN A  68  0                                        
SHEET    2   B 2 GLN A  84  LEU A  90 -1  O  GLN A  85   N  ALA A  67           
SHEET    1   C 3 TYR A 125  ASP A 126  0                                        
SHEET    2   C 3 VAL A 171  LEU A 173 -1  O  SER A 172   N  TYR A 125           
SHEET    3   C 3 LEU A 166  GLY A 167 -1  N  LEU A 166   O  LEU A 173           
SHEET    1   D 6 TRP A 385  ASP A 390  0                                        
SHEET    2   D 6 THR A 393  LYS A 398 -1  O  ALA A 395   N  TYR A 388           
SHEET    3   D 6 ILE A 405  SER A 410 -1  O  LEU A 409   N  ILE A 394           
SHEET    4   D 6 ARG A 461  PRO A 465 -1  O  LEU A 463   N  VAL A 406           
SHEET    5   D 6 GLN A 433  GLU A 436 -1  N  THR A 435   O  TYR A 464           
SHEET    6   D 6 THR A 441  THR A 444 -1  O  VAL A 443   N  LEU A 434           
SHEET    1   E 2 TYR A 419  LEU A 423  0                                        
SHEET    2   E 2 VAL A 451  MET A 455 -1  O  MET A 455   N  TYR A 419           
SSBOND   1 CYS A   30    CYS A   38                          1555   1555  2.13  
SSBOND   2 CYS A  150    CYS A  164                          1555   1555  2.49  
SSBOND   3 CYS A  240    CYS A  283                          1555   1555  2.04  
SSBOND   4 CYS A  440    CYS A  475                          1555   1555  2.05  
LINK         ND2 ASN A 197                 C1  NAG A1000     1555   1555  1.45  
LINK         O4  NAG A1000                 C1  NAG A1001     1555   1555  1.44  
LINK         O4  NAG A1001                 C1  BMA A1002     1555   1555  1.46  
LINK        CA    CA A 601                 O   HOH A1050     1555   1555  2.51  
LINK        CA    CA A 601                 O   GLU A 162     1555   1555  2.44  
LINK        CA    CA A 601                 OD2 ASP A 175     1555   1555  2.50  
LINK        CA    CA A 601                 O   HOH A1026     1555   1555  2.48  
LINK        CA    CA A 601                 O   HOH A1194     1555   1555  2.43  
LINK        CA    CA A 601                 OD1 ASP A 175     1555   1555  2.61  
LINK        CA    CA A 601                 OD1 ASN A 121     1555   1555  2.38  
LINK        CA    CA A 601                 O   HIS A 210     1555   1555  2.41  
CISPEP   1 LYS A  138    PRO A  139          0         4.88                     
CISPEP   2 ASP A  340    PRO A  341          0         5.20                     
SITE     1 AC1  7 TYR A  88  TRP A 190  SER A 193  ASN A 197                    
SITE     2 AC1  7 NAG A1001  HOH A1080  HOH A1246                               
SITE     1 AC2  3 NAG A1000  BMA A1002  HOH A1367                               
SITE     1 AC3  1 NAG A1001                                                     
SITE     1 AC4  7 ASN A 121  GLU A 162  ASP A 175  HIS A 210                    
SITE     2 AC4  7 HOH A1026  HOH A1050  HOH A1194                               
CRYST1  102.799   63.228   74.456  90.00  90.00  90.00 P 21 21 2     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      0.009728  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015816  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013431        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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