GenomeNet

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                
TITLE    2 COMPLEX WITH 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            
KEYWDS   2 BINDING, CARBOHYDRATE BINDING, GLYCOSIDE HYDROLASE,                  
KEYWDS   3 AMYLOSE, AMYLOPECTIN, MALTO-OLIGOSACCHARIDE, CARBOHYDRATE-           
KEYWDS   4 BINDING MODULE                                                       
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 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-               
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.    1.81 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) : 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            : 2965                                    
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   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1625 ; 3.200 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1819 ; 5.072 ; 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 2C3W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-OCT-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-25973.                                       
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 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 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                                     
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 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                                     
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 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                                     
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                                                                      
REMARK 500   O    HOH C  2056     O    HOH B  2151     1655      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 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    ASP C  81      168.62     64.54                                   
REMARK 500    THR D  10      -63.94   -123.00                                   
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 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 GLC A1103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1106                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1107                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1108                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1109                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1110                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A1111                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B1103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B1104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B1105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B1106                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B1109                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B1107                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B1108                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC C1103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC C1104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC C1105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC C1106                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1106                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1107                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1108                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1109                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1110                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1111                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1112                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D1113                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1112                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1110                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1110                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1114                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2C3G   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CBM26 FROM BACILLUS HALODURANS                         
REMARK 900  AMYLASE                                                             
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: 2C3X   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF IODINATED CBM25 FROM BACILLUS                          
REMARK 900  HALODURANS AMYLASE IN COMPLEX WITH                                  
REMARK 900  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  A1103      12                                                       
HET    GLC  A1104      11                                                       
HET    GLC  A1105      11                                                       
HET    GLC  A1106      11                                                       
HET    GLC  A1107      12                                                       
HET    GLC  A1101      11                                                       
HET    GLC  A1102      11                                                       
HET    GLC  A1108      11                                                       
HET    GLC  A1109      12                                                       
HET    GLC  A1110      11                                                       
HET    GLC  A1111      11                                                       
HET    GLC  B1103      12                                                       
HET    GLC  B1104      11                                                       
HET    GLC  B1105      11                                                       
HET    GLC  B1106      11                                                       
HET    GLC  B1102      11                                                       
HET    GLC  B1109      12                                                       
HET    GLC  B1107      11                                                       
HET    GLC  B1108      11                                                       
HET    GLC  C1103      12                                                       
HET    GLC  C1104      11                                                       
HET    GLC  C1105      11                                                       
HET    GLC  C1106      11                                                       
HET    GLC  D1102      12                                                       
HET    GLC  D1103      11                                                       
HET    GLC  D1104      11                                                       
HET    GLC  D1105      11                                                       
HET    GLC  D1106      12                                                       
HET    GLC  D1107      11                                                       
HET    GLC  D1108      11                                                       
HET    GLC  D1109      11                                                       
HET    GLC  D1110      12                                                       
HET    GLC  D1111      11                                                       
HET    GLC  D1112      11                                                       
HET    GLC  D1113      11                                                       
HET    SO4  A1112       5                                                       
HET    SO4  B1110       5                                                       
HET    SO4  C1110       5                                                       
HET    SO4  D1114       5                                                       
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5  GLC    35(C6 H12 O6)                                                
FORMUL  14  SO4    4(O4 S 2-)                                                   
FORMUL  18  HOH   *783(H2 O1)                                                   
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         C1  GLC A1101                 O4  GLC A1108     1555   1555  1.44  
LINK         O4  GLC A1101                 C1  GLC A1102     1555   1555  1.45  
LINK         O4  GLC A1103                 C1  GLC A1104     1555   1555  1.47  
LINK         O4  GLC A1104                 C1  GLC A1105     1555   1555  1.43  
LINK         O4  GLC A1105                 C1  GLC A1106     1555   1555  1.46  
LINK         O4  GLC A1107                 C1  GLC A1108     1555   1555  1.44  
LINK         O4  GLC A1109                 C1  GLC A1110     1555   1555  1.46  
LINK         O4  GLC A1110                 C1  GLC A1111     1555   1555  1.45  
LINK         C1  GLC B1102                 O4  GLC B1108     1555   1555  1.46  
LINK         O4  GLC B1103                 C1  GLC B1104     1555   1555  1.47  
LINK         O4  GLC B1104                 C1  GLC B1105     1555   1555  1.42  
LINK         O4  GLC B1105                 C1  GLC B1106     1555   1555  1.48  
LINK         C1  GLC B1107                 O4  GLC B1109     1555   1555  1.45  
LINK         O4  GLC B1107                 C1  GLC B1108     1555   1555  1.45  
LINK         O4  GLC C1103                 C1  GLC C1104     1555   1555  1.43  
LINK         O4  GLC C1104                 C1  GLC C1105     1555   1555  1.44  
LINK         O4  GLC C1105                 C1  GLC C1106     1555   1555  1.47  
LINK         O4  GLC D1102                 C1  GLC D1103     1555   1555  1.43  
LINK         O4  GLC D1103                 C1  GLC D1104     1555   1555  1.43  
LINK         O4  GLC D1104                 C1  GLC D1105     1555   1555  1.42  
LINK         O4  GLC D1106                 C1  GLC D1107     1555   1555  1.44  
LINK         O4  GLC D1107                 C1  GLC D1108     1555   1555  1.43  
LINK         O4  GLC D1108                 C1  GLC D1109     1555   1555  1.46  
LINK         O4  GLC D1110                 C1  GLC D1111     1555   1555  1.43  
LINK         O4  GLC D1111                 C1  GLC D1112     1555   1555  1.43  
LINK         O4  GLC D1112                 C1  GLC D1113     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                     
SITE     1 AC1 11 ASP A  75  GLN A  78  ASP A  93  GLY A  94                    
SITE     2 AC1 11 GLC A1104  HOH A2182  HOH A2183  HOH A2184                    
SITE     3 AC1 11 GLN D  78  GLC D1106  GLC D1107                               
SITE     1 AC2 11 TYR A  16  LYS A  17  THR A  18  TRP A  20                    
SITE     2 AC2 11 ASP A  75  GLC A1103  GLC A1105  HOH A2136                    
SITE     3 AC2 11 HOH A2190  GLN D  78  GLC D1106                               
SITE     1 AC3  9 THR A  18  GLY A  19  TRP A  20  GLC A1104                    
SITE     2 AC3  9 GLC A1106  HOH A2087  HOH A2193  HOH A2194                    
SITE     3 AC3  9 HOH A2196                                                     
SITE     1 AC4  4 GLC A1105  HOH A2199  HOH A2201  HOH A2203                    
SITE     1 AC5  8 GLY A  70  GLC A1108  HOH A2205  HOH A2206                    
SITE     2 AC5  8 HOH A2207  HOH A2208  HOH B2112  ARG C  80                    
SITE     1 AC6  6 GLC A1102  GLC A1108  HOH A2179  HOH A2180                    
SITE     2 AC6  6 HIS B  26  ASP B  81                                          
SITE     1 AC7  2 GLC A1101  TRP B  34                                          
SITE     1 AC8  8 GLC A1101  GLC A1107  HOH A2206  HOH A2209                    
SITE     2 AC8  8 HOH A2210  HOH A2211  TRP B  74  ASN B  76                    
SITE     1 AC9 11 TRP A  34  THR A  35  THR A  36  LEU A  37                    
SITE     2 AC9 11 GLC A1110  HOH A2064  HOH A2065  HOH A2212                    
SITE     3 AC9 11 HOH A2213  HOH A2214  GLC D1105                               
SITE     1 BC1  9 LEU A  37  GLC A1109  GLC A1111  HOH A2216                    
SITE     2 BC1  9 HOH A2217  PRO B  38  GLY B  70  GLC D1104                    
SITE     3 BC1  9 GLC D1105                                                     
SITE     1 BC2  5 GLC A1110  HOH A2219  HIS B  22  HIS B  24                    
SITE     2 BC2  5 GLC D1103                                                     
SITE     1 BC3 12 ASP B  75  GLN B  78  ASP B  93  GLY B  94                    
SITE     2 BC3 12 GLC B1104  HOH B2157  HOH B2158  HOH B2159                    
SITE     3 BC3 12 GLN C  78  GLC C1103  GLC C1104  HOH C2184                    
SITE     1 BC4 11 TYR B  16  LYS B  17  THR B  18  TRP B  20                    
SITE     2 BC4 11 GLN B  73  ASP B  75  GLC B1103  GLC B1105                    
SITE     3 BC4 11 HOH B2117  GLN C  78  GLC C1103                               
SITE     1 BC5  9 THR B  18  GLY B  19  TRP B  20  GLC B1104                    
SITE     2 BC5  9 GLC B1106  HOH B2083  HOH B2165  HOH B2166                    
SITE     3 BC5  9 HOH B2167                                                     
SITE     1 BC6  3 GLC B1105  HOH B2170  HOH B2173                               
SITE     1 BC7  4 GLC B1108  TRP C  34  SO4 C1110  HOH C2192                    
SITE     1 BC8  6 ARG B  80  GLC B1107  HOH B2178  HOH B2180                    
SITE     2 BC8  6 HOH B2181  HOH B2182                                          
SITE     1 BC9  7 GLC B1108  GLC B1109  HOH B2120  HOH B2175                    
SITE     2 BC9  7 HOH B2180  TRP C  74  ASN C  76                               
SITE     1 CC1  6 GLC B1102  GLC B1107  HOH B2176  HOH B2177                    
SITE     2 CC1  6 HIS C  26  ASP C  81                                          
SITE     1 CC2 11 GLN B  78  GLC B1103  GLC B1104  HOH B2121                    
SITE     2 CC2 11 ASP C  75  GLN C  78  ASP C  93  GLY C  94                    
SITE     3 CC2 11 GLC C1104  HOH C2180  HOH C2181                               
SITE     1 CC3 11 GLN B  78  GLC B1103  TYR C  16  LYS C  17                    
SITE     2 CC3 11 THR C  18  TRP C  20  ASP C  75  GLC C1103                    
SITE     3 CC3 11 GLC C1105  HOH C2141  HOH C2184                               
SITE     1 CC4  9 THR C  18  GLY C  19  TRP C  20  GLC C1104                    
SITE     2 CC4  9 GLC C1106  HOH C2098  HOH C2185  HOH C2186                    
SITE     3 CC4  9 HOH C2187                                                     
SITE     1 CC5  3 GLC C1105  HOH C2188  HOH C2189                               
SITE     1 CC6  7 HIS B  22  SO4 B1110  HOH B2026  ARG D  80                    
SITE     2 CC6  7 GLC D1103  HOH D2151  HOH D2152                               
SITE     1 CC7 10 GLC A1111  HOH A2129  HIS B  22  SER B  71                    
SITE     2 CC7 10 SO4 B1110  HOH B2186  ARG D  80  GLC D1102                    
SITE     3 CC7 10 GLC D1104  HOH D2156                                          
SITE     1 CC8  9 LEU A  37  TRP A  74  ASN A  76  GLC A1110                    
SITE     2 CC8  9 SER B  71  GLC D1103  GLC D1105  HOH D2117                    
SITE     3 CC8  9 HOH D2156                                                     
SITE     1 CC9  9 HIS A  26  ASP A  81  GLC A1109  GLC A1110                    
SITE     2 CC9  9 HOH A2220  GLC D1104  HOH D2158  HOH D2159                    
SITE     3 CC9  9 HOH D2161                                                     
SITE     1 DC1 11 GLN A  78  GLC A1103  GLC A1104  ASP D  75                    
SITE     2 DC1 11 GLN D  78  ASP D  93  GLY D  94  GLC D1107                    
SITE     3 DC1 11 HOH D2116  HOH D2162  HOH D2163                               
SITE     1 DC2 12 GLN A  78  GLC A1103  HOH A2158  TYR D  16                    
SITE     2 DC2 12 LYS D  17  THR D  18  TRP D  20  ASP D  75                    
SITE     3 DC2 12 GLC D1106  GLC D1108  HOH D2164  HOH D2165                    
SITE     1 DC3  8 THR D  18  GLY D  19  TRP D  20  GLC D1107                    
SITE     2 DC3  8 GLC D1109  HOH D2166  HOH D2167  HOH D2168                    
SITE     1 DC4  2 GLC D1108  HOH D2169                                          
SITE     1 DC5  4 ARG A  80  GLC D1111  HOH D2172  HOH D2173                    
SITE     1 DC6  8 GLN A  78  HOH A2139  TRP D  74  ASN D  76                    
SITE     2 DC6  8 GLC D1110  GLC D1112  HOH D2172  HOH D2175                    
SITE     1 DC7  9 HIS D  26  TRP D  34  ASP D  81  GLC D1111                    
SITE     2 DC7  9 GLC D1113  HOH D2176  HOH D2177  HOH D2178                    
SITE     3 DC7  9 HOH D2179                                                     
SITE     1 DC8  3 GLC D1112  SO4 D1114  HOH D2181                               
SITE     1 DC9  5 TRP A  34  ARG A  64  HOH A2220  HOH A2221                    
SITE     2 DC9  5 HOH D2161                                                     
SITE     1 EC1  9 TRP B  20  THR B  21  ASN B  69  HOH B2183                    
SITE     2 EC1  9 HOH B2184  HOH B2185  HOH B2186  GLC D1102                    
SITE     3 EC1  9 GLC D1103                                                     
SITE     1 EC2  7 GLC B1102  TRP C  34  ARG C  64  HOH C2190                    
SITE     2 EC2  7 HOH C2191  HOH C2192  HOH C2193                               
SITE     1 EC3  5 TRP D  34  ARG D  64  GLC D1113  HOH D2181                    
SITE     2 EC3  5 HOH D2182                                                     
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                                                                             
DBGET integrated database retrieval system