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Database: PDB
Entry: 2C3W
LinkDB: 2C3W
Original site: 2C3W 
HEADER    SUGAR BINDING PROTEIN                   12-OCT-05   2C3W              
TITLE     STRUCTURE OF CBM25 FROM BACILLUS HALODURANS AMYLASE IN COMPLEX WITH   
TITLE    2 MALTOTETRAOSE                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE G-6;                                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: CARBOHYDRATE-BINDING MODULE, RESIDUES 863-958;             
COMPND   5 SYNONYM: FAMILY 25 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    SUGAR-BINDING PROTEIN, CARBOHYDRATE-BINDING MODULE, STARCH BINDING,   
KEYWDS   2 CARBOHYDRATE BINDING, GLYCOSIDE HYDROLASE, AMYLOSE, AMYLOPECTIN,     
KEYWDS   3 MALTO-OLIGOSACCHARIDE, SUGAR BINDING PROTEIN                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.B.BORASTON,M.HEALEY,J.KLASSEN,E.FICKO-BLEAN,A.LAMMERTS VAN BUEREN,  
AUTHOR   2 V.LAW                                                                
REVDAT   4   29-JUL-20 2C3W    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE   ATOM                              
REVDAT   3   24-FEB-09 2C3W    1       VERSN                                    
REVDAT   2   18-JAN-06 2C3W    1       JRNL                                     
REVDAT   1   17-OCT-05 2C3W    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-GLUCAN         
JRNL        TITL 2 RECOGNITION BY FAMILY 25 AND 26 CARBOHYDRATE-BINDING MODULES 
JRNL        TITL 3 REVEALS A CONSERVED 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.    1.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 47599                          
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) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.158                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2544                            
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) : 1.81                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.86                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3517                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 182                          
REMARK   3   BIN FREE R VALUE                    : 0.2790                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2959                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 414                                     
REMARK   3   SOLVENT ATOMS            : 783                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.29000                                             
REMARK   3    B22 (A**2) : -1.24000                                             
REMARK   3    B33 (A**2) : 1.10000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.86000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.107         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.110         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.073         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.368         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3486 ; 0.020 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2764 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4806 ; 1.975 ; 2.056       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6412 ; 1.375 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   376 ; 7.036 ; 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):   610 ; 0.149 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3485 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   635 ; 0.006 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   578 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3358 ; 0.273 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1865 ; 0.095 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   532 ; 0.170 ; 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):     7 ; 0.228 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    35 ; 0.358 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    52 ; 0.161 ; 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):  1861 ; 1.184 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2986 ; 2.105 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1625 ; 3.200 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1819 ; 5.072 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2C3W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-OCT-05.                  
REMARK 100 THE DEPOSITION ID IS D_1290025973.                                   
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        : NULL                               
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   : 47599                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.810                              
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     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.3000                            
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   (%): 48.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       47.27650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, F, G                            
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: B, H, I                               
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: C, J                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: D, K, L, M                            
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     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     GLY C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     MET C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     GLY C     7                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     MET D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     GLY D     7                                                      
REMARK 465     ASP D     8                                                      
REMARK 465     LYS D   102                                                      
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 B  2151     O    HOH C  2056     2645     2.18            
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   8   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    ASP A  11   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B  11   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 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    THR A  10      -78.78   -121.60                                   
REMARK 500    ASP A  81      166.60     69.55                                   
REMARK 500    THR B  10      -70.97   -116.14                                   
REMARK 500    ASP B  81      162.60     64.59                                   
REMARK 500    THR C  10      -74.94   -118.86                                   
REMARK 500    GLN C  31       18.97     59.61                                   
REMARK 500    ASP C  81      168.62     64.54                                   
REMARK 500    THR D  10      -63.94   -123.00                                   
REMARK 500    GLN D  31       19.72     59.76                                   
REMARK 500    ASP D  81      165.41     65.87                                   
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 A2021        DISTANCE =  6.36 ANGSTROMS                       
REMARK 525    HOH A2029        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH A2173        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH B2007        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH C2016        DISTANCE =  7.11 ANGSTROMS                       
REMARK 525    HOH C2026        DISTANCE =  6.04 ANGSTROMS                       
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 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C3G   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CBM26 FROM BACILLUS HALODURANS AMYLASE                  
REMARK 900 RELATED ID: 2C3H   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF CBM26 FROM BACILLUS HALODURANS AMYLASE IN COMPLEX WITH  
REMARK 900 MALTOSE                                                              
REMARK 900 RELATED ID: 2C3V   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF IODINATED CBM25 FROM BACILLUS HALODURANS AMYLASE        
REMARK 900 RELATED ID: 2C3X   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF IODINATED CBM25 FROM BACILLUS HALODURANS AMYLASE IN     
REMARK 900 COMPLEX WITH MALTOTETRAOSE                                           
DBREF  2C3W A    1     6  PDB    2C3W     2C3W             1      6             
DBREF  2C3W A    7   102  UNP    Q9KFR4   Q9KFR4_BACHD   863    958             
DBREF  2C3W B    1     6  PDB    2C3W     2C3W             1      6             
DBREF  2C3W B    7   102  UNP    Q9KFR4   Q9KFR4_BACHD   863    958             
DBREF  2C3W C    1     6  PDB    2C3W     2C3W             1      6             
DBREF  2C3W C    7   102  UNP    Q9KFR4   Q9KFR4_BACHD   863    958             
DBREF  2C3W D    1     6  PDB    2C3W     2C3W             1      6             
DBREF  2C3W D    7   102  UNP    Q9KFR4   Q9KFR4_BACHD   863    958             
SEQRES   1 A  102  GLY SER HIS MET ALA SER GLY ASP ALA THR ASP ILE THR          
SEQRES   2 A  102  ILE TYR TYR LYS THR GLY TRP THR HIS PRO HIS ILE HIS          
SEQRES   3 A  102  TYR SER LEU ASN GLN GLY ALA TRP THR THR LEU PRO GLY          
SEQRES   4 A  102  VAL PRO LEU THR LYS SER GLU TYR GLU GLY TYR VAL LYS          
SEQRES   5 A  102  VAL THR ILE GLU ALA GLU GLU GLY SER GLN LEU ARG ALA          
SEQRES   6 A  102  ALA PHE ASN ASN GLY SER GLY GLN TRP ASP ASN ASN GLN          
SEQRES   7 A  102  GLY ARG ASP TYR ASP PHE SER SER GLY VAL HIS THR LEU          
SEQRES   8 A  102  ALA ASP GLY ARG ILE LEU SER GLY THR PRO LYS                  
SEQRES   1 B  102  GLY SER HIS MET ALA SER GLY ASP ALA THR ASP ILE THR          
SEQRES   2 B  102  ILE TYR TYR LYS THR GLY TRP THR HIS PRO HIS ILE HIS          
SEQRES   3 B  102  TYR SER LEU ASN GLN GLY ALA TRP THR THR LEU PRO GLY          
SEQRES   4 B  102  VAL PRO LEU THR LYS SER GLU TYR GLU GLY TYR VAL LYS          
SEQRES   5 B  102  VAL THR ILE GLU ALA GLU GLU GLY SER GLN LEU ARG ALA          
SEQRES   6 B  102  ALA PHE ASN ASN GLY SER GLY GLN TRP ASP ASN ASN GLN          
SEQRES   7 B  102  GLY ARG ASP TYR ASP PHE SER SER GLY VAL HIS THR LEU          
SEQRES   8 B  102  ALA ASP GLY ARG ILE LEU SER GLY THR PRO LYS                  
SEQRES   1 C  102  GLY SER HIS MET ALA SER GLY ASP ALA THR ASP ILE THR          
SEQRES   2 C  102  ILE TYR TYR LYS THR GLY TRP THR HIS PRO HIS ILE HIS          
SEQRES   3 C  102  TYR SER LEU ASN GLN GLY ALA TRP THR THR LEU PRO GLY          
SEQRES   4 C  102  VAL PRO LEU THR LYS SER GLU TYR GLU GLY TYR VAL LYS          
SEQRES   5 C  102  VAL THR ILE GLU ALA GLU GLU GLY SER GLN LEU ARG ALA          
SEQRES   6 C  102  ALA PHE ASN ASN GLY SER GLY GLN TRP ASP ASN ASN GLN          
SEQRES   7 C  102  GLY ARG ASP TYR ASP PHE SER SER GLY VAL HIS THR LEU          
SEQRES   8 C  102  ALA ASP GLY ARG ILE LEU SER GLY THR PRO LYS                  
SEQRES   1 D  102  GLY SER HIS MET ALA SER GLY ASP ALA THR ASP ILE THR          
SEQRES   2 D  102  ILE TYR TYR LYS THR GLY TRP THR HIS PRO HIS ILE HIS          
SEQRES   3 D  102  TYR SER LEU ASN GLN GLY ALA TRP THR THR LEU PRO GLY          
SEQRES   4 D  102  VAL PRO LEU THR LYS SER GLU TYR GLU GLY TYR VAL LYS          
SEQRES   5 D  102  VAL THR ILE GLU ALA GLU GLU GLY SER GLN LEU ARG ALA          
SEQRES   6 D  102  ALA PHE ASN ASN GLY SER GLY GLN TRP ASP ASN ASN GLN          
SEQRES   7 D  102  GLY ARG ASP TYR ASP PHE SER SER GLY VAL HIS THR LEU          
SEQRES   8 D  102  ALA ASP GLY ARG ILE LEU SER GLY THR PRO LYS                  
HET    GLC  E   1      12                                                       
HET    GLC  E   2      11                                                       
HET    GLC  E   3      11                                                       
HET    GLC  E   4      11                                                       
HET    GLC  F   1      12                                                       
HET    GLC  F   2      11                                                       
HET    GLC  F   3      11                                                       
HET    GLC  F   4      11                                                       
HET    GLC  G   1      12                                                       
HET    GLC  G   2      11                                                       
HET    GLC  G   3      11                                                       
HET    GLC  H   1      12                                                       
HET    GLC  H   2      11                                                       
HET    GLC  H   3      11                                                       
HET    GLC  H   4      11                                                       
HET    GLC  I   1      12                                                       
HET    GLC  I   2      11                                                       
HET    GLC  I   3      11                                                       
HET    GLC  I   4      11                                                       
HET    GLC  J   1      12                                                       
HET    GLC  J   2      11                                                       
HET    GLC  J   3      11                                                       
HET    GLC  J   4      11                                                       
HET    GLC  K   1      12                                                       
HET    GLC  K   2      11                                                       
HET    GLC  K   3      11                                                       
HET    GLC  K   4      11                                                       
HET    GLC  L   1      12                                                       
HET    GLC  L   2      11                                                       
HET    GLC  L   3      11                                                       
HET    GLC  L   4      11                                                       
HET    GLC  M   1      12                                                       
HET    GLC  M   2      11                                                       
HET    GLC  M   3      11                                                       
HET    GLC  M   4      11                                                       
HET    SO4  A1112       5                                                       
HET    SO4  B1110       5                                                       
HET    SO4  C1110       5                                                       
HET    SO4  D1114       5                                                       
HETNAM     GLC ALPHA-D-GLUCOPYRANOSE                                            
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  GLC    35(C6 H12 O6)                                                
FORMUL  14  SO4    4(O4 S 2-)                                                   
FORMUL  18  HOH   *783(H2 O)                                                    
SHEET    1  AA 5 THR A  43  LYS A  44  0                                        
SHEET    2  AA 5 TYR A  50  ILE A  55 -1  O  LYS A  52   N  THR A  43           
SHEET    3  AA 5 ILE A  12  LYS A  17 -1  O  ILE A  12   N  ILE A  55           
SHEET    4  AA 5 GLY A  87  ALA A  92  1  O  GLY A  87   N  THR A  13           
SHEET    5  AA 5 ARG A  95  SER A  98 -1  O  ARG A  95   N  ALA A  92           
SHEET    1  AB 4 VAL A  40  PRO A  41  0                                        
SHEET    2  AB 4 HIS A  24  LEU A  29 -1  O  ILE A  25   N  VAL A  40           
SHEET    3  AB 4 GLN A  62  ASN A  68 -1  O  ARG A  64   N  SER A  28           
SHEET    4  AB 4 TYR A  82  SER A  85 -1  O  TYR A  82   N  ALA A  65           
SHEET    1  AC 4 VAL A  40  PRO A  41  0                                        
SHEET    2  AC 4 HIS A  24  LEU A  29 -1  O  ILE A  25   N  VAL A  40           
SHEET    3  AC 4 GLN A  62  ASN A  68 -1  O  ARG A  64   N  SER A  28           
SHEET    4  AC 4 TRP A  74  ASP A  75 -1  O  ASP A  75   N  PHE A  67           
SHEET    1  BA 5 THR B  43  LYS B  44  0                                        
SHEET    2  BA 5 TYR B  50  ILE B  55 -1  O  LYS B  52   N  THR B  43           
SHEET    3  BA 5 ILE B  12  LYS B  17 -1  O  ILE B  12   N  ILE B  55           
SHEET    4  BA 5 GLY B  87  ALA B  92  1  O  GLY B  87   N  THR B  13           
SHEET    5  BA 5 ARG B  95  SER B  98 -1  O  ARG B  95   N  ALA B  92           
SHEET    1  BB 4 VAL B  40  PRO B  41  0                                        
SHEET    2  BB 4 HIS B  24  LEU B  29 -1  O  ILE B  25   N  VAL B  40           
SHEET    3  BB 4 GLN B  62  ASN B  68 -1  O  ARG B  64   N  SER B  28           
SHEET    4  BB 4 TYR B  82  SER B  85 -1  O  TYR B  82   N  ALA B  65           
SHEET    1  BC 4 VAL B  40  PRO B  41  0                                        
SHEET    2  BC 4 HIS B  24  LEU B  29 -1  O  ILE B  25   N  VAL B  40           
SHEET    3  BC 4 GLN B  62  ASN B  68 -1  O  ARG B  64   N  SER B  28           
SHEET    4  BC 4 TRP B  74  ASP B  75 -1  O  ASP B  75   N  PHE B  67           
SHEET    1  CA 5 THR C  43  LYS C  44  0                                        
SHEET    2  CA 5 TYR C  50  ILE C  55 -1  O  LYS C  52   N  THR C  43           
SHEET    3  CA 5 ILE C  12  LYS C  17 -1  O  ILE C  12   N  ILE C  55           
SHEET    4  CA 5 GLY C  87  ALA C  92  1  O  GLY C  87   N  THR C  13           
SHEET    5  CA 5 ARG C  95  SER C  98 -1  O  ARG C  95   N  ALA C  92           
SHEET    1  CB 4 VAL C  40  PRO C  41  0                                        
SHEET    2  CB 4 HIS C  24  LEU C  29 -1  O  ILE C  25   N  VAL C  40           
SHEET    3  CB 4 GLN C  62  ASN C  68 -1  O  ARG C  64   N  SER C  28           
SHEET    4  CB 4 TYR C  82  SER C  85 -1  O  TYR C  82   N  ALA C  65           
SHEET    1  CC 4 VAL C  40  PRO C  41  0                                        
SHEET    2  CC 4 HIS C  24  LEU C  29 -1  O  ILE C  25   N  VAL C  40           
SHEET    3  CC 4 GLN C  62  ASN C  68 -1  O  ARG C  64   N  SER C  28           
SHEET    4  CC 4 TRP C  74  ASP C  75 -1  O  ASP C  75   N  PHE C  67           
SHEET    1  DA 5 THR D  43  LYS D  44  0                                        
SHEET    2  DA 5 TYR D  50  ILE D  55 -1  O  LYS D  52   N  THR D  43           
SHEET    3  DA 5 ILE D  12  LYS D  17 -1  O  ILE D  12   N  ILE D  55           
SHEET    4  DA 5 GLY D  87  ALA D  92  1  O  GLY D  87   N  THR D  13           
SHEET    5  DA 5 ARG D  95  SER D  98 -1  O  ARG D  95   N  ALA D  92           
SHEET    1  DB 7 VAL D  40  PRO D  41  0                                        
SHEET    2  DB 7 HIS D  24  LEU D  29 -1  O  ILE D  25   N  VAL D  40           
SHEET    3  DB 7 GLN D  62  ASN D  68 -1  O  ARG D  64   N  SER D  28           
SHEET    4  DB 7 TRP D  74  ASP D  75 -1  O  ASP D  75   N  PHE D  67           
SHEET    5  DB 7 GLN D  62  ASN D  68 -1  O  PHE D  67   N  ASP D  75           
SHEET    6  DB 7 TYR D  82  SER D  85 -1  O  TYR D  82   N  ALA D  65           
SHEET    7  DB 7 GLN D  62  ASN D  68 -1  O  LEU D  63   N  PHE D  84           
LINK         O4  GLC E   1                 C1  GLC E   2     1555   1555  1.44  
LINK         O4  GLC E   2                 C1  GLC E   3     1555   1555  1.44  
LINK         O4  GLC E   3                 C1  GLC E   4     1555   1555  1.45  
LINK         O4  GLC F   1                 C1  GLC F   2     1555   1555  1.47  
LINK         O4  GLC F   2                 C1  GLC F   3     1555   1555  1.43  
LINK         O4  GLC F   3                 C1  GLC F   4     1555   1555  1.46  
LINK         O4  GLC G   1                 C1  GLC G   2     1555   1555  1.46  
LINK         O4  GLC G   2                 C1  GLC G   3     1555   1555  1.45  
LINK         O4  GLC H   1                 C1  GLC H   2     1555   1555  1.45  
LINK         O4  GLC H   2                 C1  GLC H   3     1555   1555  1.45  
LINK         O4  GLC H   3                 C1  GLC H   4     1555   1555  1.46  
LINK         O4  GLC I   1                 C1  GLC I   2     1555   1555  1.47  
LINK         O4  GLC I   2                 C1  GLC I   3     1555   1555  1.42  
LINK         O4  GLC I   3                 C1  GLC I   4     1555   1555  1.48  
LINK         O4  GLC J   1                 C1  GLC J   2     1555   1555  1.43  
LINK         O4  GLC J   2                 C1  GLC J   3     1555   1555  1.44  
LINK         O4  GLC J   3                 C1  GLC J   4     1555   1555  1.47  
LINK         O4  GLC K   1                 C1  GLC K   2     1555   1555  1.43  
LINK         O4  GLC K   2                 C1  GLC K   3     1555   1555  1.43  
LINK         O4  GLC K   3                 C1  GLC K   4     1555   1555  1.42  
LINK         O4  GLC L   1                 C1  GLC L   2     1555   1555  1.44  
LINK         O4  GLC L   2                 C1  GLC L   3     1555   1555  1.43  
LINK         O4  GLC L   3                 C1  GLC L   4     1555   1555  1.46  
LINK         O4  GLC M   1                 C1  GLC M   2     1555   1555  1.43  
LINK         O4  GLC M   2                 C1  GLC M   3     1555   1555  1.43  
LINK         O4  GLC M   3                 C1  GLC M   4     1555   1555  1.47  
CISPEP   1 LEU A   37    PRO A   38          0        10.49                     
CISPEP   2 LEU B   37    PRO B   38          0        -0.88                     
CISPEP   3 LEU C   37    PRO C   38          0         1.61                     
CISPEP   4 LEU D   37    PRO D   38          0        -0.98                     
CRYST1   47.533   94.553   64.868  90.00 104.65  90.00 P 1 21 1      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      0.021038  0.000000  0.005500        0.00000                         
SCALE2      0.000000  0.010576  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015934        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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