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Database: PDB
Entry: 2C3G
LinkDB: 2C3G
Original site: 2C3G 
HEADER    CARBOHYDRATE-BINDING MODULE             07-OCT-05   2C3G              
TITLE     STRUCTURE OF CBM26 FROM BACILLUS HALODURANS AMYLASE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE G-6;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CARBOHYDRATE-BINDING MODULE, RESIDUES 771-863;             
COMPND   5 SYNONYM: FAMILY 26 CARBOHYDRATE-BINDING MODULE;                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS HALODURANS;                            
SOURCE   3 ORGANISM_TAXID: 272558;                                              
SOURCE   4 STRAIN: C-125;                                                       
SOURCE   5 ATCC: BAA-125;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET 28A;                                   
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-BHCBM6                                
KEYWDS    CARBOHYDRATE-BINDING MODULE, STARCH BINDING, CARBOHYDRATE             
KEYWDS   2 BINDING, GLYCOSIDE HYDROLASE, AMYLOSE, AMYLOPECTIN,                  
KEYWDS   3 MALTO-OLIGOSACCHARIDE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.B.BORASTON,M.HEALEY,J.KLASSEN,E.FICKO-BLEAN,                        
AUTHOR   2 A.LAMMERTS VAN BUEREN,V.LAW                                          
REVDAT   3   24-FEB-09 2C3G    1       VERSN                                    
REVDAT   2   18-JAN-06 2C3G    1       JRNL                                     
REVDAT   1   17-OCT-05 2C3G    0                                                
JRNL        AUTH   A.B.BORASTON,M.HEALEY,J.KLASSEN,E.FICKO-BLEAN,               
JRNL        AUTH 2 A.LAMMERTS VAN BUEREN,V.LAW                                  
JRNL        TITL   A STRUCTURAL AND FUNCTIONAL ANALYSIS OF ALPHA-               
JRNL        TITL 2 GLUCAN RECOGNITION BY FAMILY 25 AND 26                       
JRNL        TITL 3 CARBOHYDRATE-BINDING MODULES REVEALS A CONSERVED             
JRNL        TITL 4 MODE OF STARCH RECOGNITION                                   
JRNL        REF    J.BIOL.CHEM.                  V. 281   587 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16230347                                                     
JRNL        DOI    10.1074/JBC.M509958200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.0  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 7356                           
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) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.302                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 354                             
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 543                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 19                           
REMARK   3   BIN FREE R VALUE                    : 0.2860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 819                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 86                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.99000                                             
REMARK   3    B22 (A**2) : -0.99000                                             
REMARK   3    B33 (A**2) : 1.97000                                              
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): 0.227         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.215         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.185         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.016         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.871                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   855 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1169 ; 1.870 ; 1.901       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):    99 ;10.690 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   104 ; 0.195 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   709 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   401 ; 0.227 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    61 ; 0.239 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    28 ; 0.329 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    11 ; 0.222 ; 0.200       
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):   488 ; 0.748 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   787 ; 1.323 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   367 ; 1.863 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   381 ; 2.688 ; 4.500       
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  : NULL                                       
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   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2C3G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-25901.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 113.0                              
REMARK 200  PH                             : NULL                               
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          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7536                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.4000                             
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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  0.000000 -1.000000  0.000000       24.64300            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       24.64300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.38000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       24.64300            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       24.64300            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       43.38000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       24.64300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       24.64300            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       43.38000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       24.64300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       24.64300            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       43.38000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  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 GENERATING THE BIOMOLECULE                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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      HOH A2025  LIES ON A SPECIAL POSITION.                          
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     THR A  69     O                                                  
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   CD2  HIS A     2  -  O    HOH A  2004              2.10            
REMARK 500   OE1  GLU A    43  -  O    HOH A  2041              1.93            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ASP A  15   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    GLY A  74   N   -  CA  -  C   ANGL. DEV. = -15.1 DEGREES          
REMARK 500    ASP A  85   CB  -  CG  -  OD2 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP A  89   CB  -  CG  -  OD2 ANGL. DEV. =   8.3 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 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   2      137.02    112.90                                   
REMARK 500    ASP A  26       74.89      4.83                                   
REMARK 500    TYR A  45      -62.19   -108.73                                   
REMARK 500    ASP A  83      -32.02    117.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A    1     HIS A    2                  132.38                    
REMARK 500 PRO A   73     GLY A   74                   40.56                    
REMARK 500 ARG A   82     ASP A   83                  -44.85                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR A  69        -25.55                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    HIS A   2        20.7      L          L   OUTSIDE RANGE           
REMARK 500    ASP A  26        21.8      L          L   OUTSIDE RANGE           
REMARK 500    ASP A  83        18.2      L          L   OUTSIDE RANGE           
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 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                              CD A1099  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY A   6   O                                                      
REMARK 620 2 ASP A  48   OD1  83.7                                              
REMARK 620 3 ASP A  48   OD2  77.3  51.2                                        
REMARK 620 4 ASP A  15   OD2 161.3 102.5  92.7                                  
REMARK 620 5 ASP A  85   OD2  84.6  92.6 140.6 112.4                            
REMARK 620 6 HOH A2015   O    83.2 162.4 114.0  86.6  97.9                      
REMARK 620 7 ASP A  85   OD1 127.9  78.9 123.0  70.8  48.1 118.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1100  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2001   O                                                      
REMARK 620 2 HOH A2004   O    81.6                                              
REMARK 620 3 ASP A  89   OD1 157.4  96.4                                        
REMARK 620 4 HIS A  93   NE2  94.5 149.7  98.1                                  
REMARK 620 5 HOH A2079   O    98.3  61.6 100.5  89.6                            
REMARK 620 6 ASP A  89   OD2 100.5 109.2  58.7 101.1 157.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1101  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2043   O                                                      
REMARK 620 2 HIS A  52   ND1  93.0                                              
REMARK 620 3 GLU A  55   OE1  82.9  90.0                                        
REMARK 620 4 GLU A  55   OE2 102.5 131.3  47.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1102  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  44   ND1                                                    
REMARK 620 2 HOH A2002   O   172.4                                              
REMARK 620 3 HOH A2003   O   100.5  72.5                                        
REMARK 620 4 HOH A2071   O    95.7  80.9  83.7                                  
REMARK 620 5 GLY A   1   O    88.9  92.5  79.9 163.6                            
REMARK 620 6 HOH A2070   O    89.4  97.0 165.0  84.1 111.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CD A1099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CD A1100                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CD A1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CD A1102                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C3H   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CBM26 FROM BACILLUS HALODURANS                         
REMARK 900  AMYLASE IN COMPLEX WITH MALTOSE                                     
REMARK 900 RELATED ID: 2C3V   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF IODINATED CBM25 FROM BACILLUS                          
REMARK 900  HALODURANS AMYLASE                                                  
REMARK 900 RELATED ID: 2C3W   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CBM25 FROM BACILLUS HALODURANS                         
REMARK 900  AMYLASE IN COMPLEX WITH MALTOTETRAOSE                               
REMARK 900 RELATED ID: 2C3X   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF IODINATED CBM25 FROM BACILLUS                          
REMARK 900  HALODURANS AMYLASE IN COMPLEX WITH                                  
REMARK 900  MALTOTETRAOSE                                                       
DBREF  2C3G A    1     5  PDB    2C3G     2C3G             1      5             
DBREF  2C3G A    6    98  UNP    Q9KFR4   Q9KFR4_BACHD   771    863             
SEQRES   1 A   98  GLY HIS MET ALA SER GLY LEU THR ILE TYR PHE LYS LYS          
SEQRES   2 A   98  PRO ASP SER TRP GLY THR PRO HIS LEU TYR TYR TYR ASP          
SEQRES   3 A   98  THR ASN PRO LYS VAL ASP GLU PRO THR TRP SER GLU ALA          
SEQRES   4 A   98  PRO GLU MET GLU HIS TYR GLU GLY ASP TRP TYR THR HIS          
SEQRES   5 A   98  THR ILE GLU GLY VAL GLU SER VAL ARG LEU LEU PHE LYS          
SEQRES   6 A   98  ASP ARG GLY THR ASN GLN TRP PRO GLY PRO GLY GLU PRO          
SEQRES   7 A   98  GLY PHE PHE ARG ASP GLN ASP GLY TRP PHE ASP GLY GLU          
SEQRES   8 A   98  TRP HIS VAL ASP ARG PRO GLY                                  
HET     CD  A1099       1                                                       
HET     CD  A1100       1                                                       
HET     CD  A1101       1                                                       
HET     CD  A1102       1                                                       
HETNAM      CD CADMIUM ION                                                      
FORMUL   2   CD    4(CD 2+)                                                     
FORMUL   6  HOH   *86(H2 O1)                                                    
SHEET    1  AA 5 GLU A  43  GLU A  46  0                                        
SHEET    2  AA 5 TRP A  49  GLU A  55 -1  O  TRP A  49   N  TYR A  45           
SHEET    3  AA 5 GLY A   6  LYS A  12 -1  O  LEU A   7   N  ILE A  54           
SHEET    4  AA 5 GLY A  86  PHE A  88  1  O  GLY A  86   N  TYR A  10           
SHEET    5  AA 5 TRP A  92  HIS A  93 -1  O  HIS A  93   N  TRP A  87           
SHEET    1  AB 3 PRO A  20  ASN A  28  0                                        
SHEET    2  AB 3 SER A  59  ASP A  66 -1  O  SER A  59   N  ASN A  28           
SHEET    3  AB 3 PHE A  80  ARG A  82 -1  O  PHE A  80   N  LEU A  62           
SHEET    1  AC 3 PRO A  20  ASN A  28  0                                        
SHEET    2  AC 3 SER A  59  ASP A  66 -1  O  SER A  59   N  ASN A  28           
SHEET    3  AC 3 GLN A  71  TRP A  72 -1  O  TRP A  72   N  PHE A  64           
LINK        CD    CD A1099                 O   GLY A   6     1555   5555  2.44  
LINK        CD    CD A1099                 OD1 ASP A  48     1555   1555  2.33  
LINK        CD    CD A1099                 OD2 ASP A  48     1555   1555  2.53  
LINK        CD    CD A1099                 OD2 ASP A  15     1555   1555  2.21  
LINK        CD    CD A1099                 OD2 ASP A  85     1555   5555  2.49  
LINK        CD    CD A1099                 O   HOH A2015     1555   1555  1.97  
LINK        CD    CD A1099                 OD1 ASP A  85     1555   5555  2.68  
LINK        CD    CD A1100                 O   HOH A2001     1555   5555  2.34  
LINK        CD    CD A1100                 O   HOH A2004     1555   5555  2.84  
LINK        CD    CD A1100                 OD1 ASP A  89     1555   1555  2.13  
LINK        CD    CD A1100                 NE2 HIS A  93     1555   1555  2.33  
LINK        CD    CD A1100                 O   HOH A2079     1555   1555  2.28  
LINK        CD    CD A1100                 OD2 ASP A  89     1555   1555  2.36  
LINK        CD    CD A1101                 ND1 HIS A  52     1555   1555  2.42  
LINK        CD    CD A1101                 OE1 GLU A  55     1555   2655  2.86  
LINK        CD    CD A1101                 OE2 GLU A  55     1555   2655  2.42  
LINK        CD    CD A1101                 O   HOH A2043     1555   1555  2.32  
LINK        CD    CD A1102                 O   HOH A2002     1555   2655  2.24  
LINK        CD    CD A1102                 O   HOH A2003     1555   2655  2.23  
LINK        CD    CD A1102                 O   HOH A2071     1555   5555  2.33  
LINK        CD    CD A1102                 O   GLY A   1     1555   2655  2.11  
LINK        CD    CD A1102                 O   HOH A2070     1555   5555  2.31  
LINK        CD    CD A1102                 ND1 HIS A  44     1555   1555  2.40  
CISPEP   1 ASN A   28    PRO A   29          0        -1.44                     
CISPEP   2 TRP A   72    PRO A   73          0        -8.84                     
CISPEP   3 ASP A   85    GLY A   86          0       -23.40                     
SITE     1 AC1  5 GLY A   6  ASP A  15  ASP A  48  ASP A  85                    
SITE     2 AC1  5 HOH A2015                                                     
SITE     1 AC2  5 ASP A  89  HIS A  93  HOH A2001  HOH A2004                    
SITE     2 AC2  5 HOH A2079                                                     
SITE     1 AC3  4 GLU A  43  HIS A  52  GLU A  55  HOH A2043                    
SITE     1 AC4  6 GLY A   1  HIS A  44  HOH A2002  HOH A2003                    
SITE     2 AC4  6 HOH A2070  HOH A2071                                          
CRYST1   49.286   49.286   86.760  90.00  90.00  90.00 P 42 21 2     8          
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      0.020290  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.020290  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011526        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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