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Database: PDB
Entry: 2C3V
LinkDB: 2C3V
Original site: 2C3V 
HEADER    CARBOHYDRATE-BINDING MODULE             12-OCT-05   2C3V              
TITLE     STRUCTURE OF IODINATED CBM25 FROM BACILLUS HALODURANS                 
TITLE    2 AMYLASE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE G-6;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CARBOHYDRATE-BINDING MODULE, RESIDUES 863-958;             
COMPND   5 SYNONYM: FAMILY 25 CARBOHYDRATE-BINDING MODULE;                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ALPHA-AMYLASE G-6;                                         
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: CARBOHYDRATE-BINDING MODULE, RESIDUES 863-958;             
COMPND  11 SYNONYM: FAMILY 25 CARBOHYDRATE-BINDING MODULE;                      
COMPND  12 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;                               
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: BACILLUS HALODURANS;                            
SOURCE  13 ORGANISM_TAXID: 272558;                                              
SOURCE  14 STRAIN: C-125;                                                       
SOURCE  15 ATCC: BAA-125;                                                       
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR: PET 28A;                                   
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET-BHCBM6                                
KEYWDS    CARBOHYDRATE-BINDING MODULE, STARCH BINDING, CARBOHYDRATE             
KEYWDS   2 BINDING, GLYCOSIDE HYDROLASE, AMYLOSE, AMYLOPECTIN,                  
KEYWDS   3 MALTO-OLIGOSACCHARIDE, CARBOHYDRATE- 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 2C3V    1       VERSN                                    
REVDAT   2   18-JAN-06 2C3V    1       JRNL                                     
REVDAT   1   17-OCT-05 2C3V    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.    1.39 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) : 1.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 67.42                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 28505                          
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) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.250                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1542                            
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) : 1.39                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.43                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1149                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.5190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 56                           
REMARK   3   BIN FREE R VALUE                    : 0.4180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1438                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 212                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.10000                                             
REMARK   3    B22 (A**2) : 0.68000                                              
REMARK   3    B33 (A**2) : -0.50000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.33000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.106         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.090         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.062         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.607         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1519 ; 0.019 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1251 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2078 ; 1.893 ; 1.935       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2923 ; 0.981 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   190 ; 7.439 ; 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):   218 ; 0.124 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1734 ; 0.014 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   316 ; 0.021 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   288 ; 0.250 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1482 ; 0.268 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   892 ; 0.091 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   136 ; 0.168 ; 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):    25 ; 0.195 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    93 ; 0.313 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    20 ; 0.122 ; 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):   931 ; 1.715 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1492 ; 2.762 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   588 ; 4.365 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   583 ; 7.195 ; 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 2C3V 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-25969.                                       
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   : 28505                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.390                              
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     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : 0.07000                            
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: SAD                          
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   (%): 31.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.80                     
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       20.90950            
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                                                    
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 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    78                                                      
REMARK 465     SER A    79                                                      
REMARK 465     HIS A    80                                                      
REMARK 465     MET A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     SER A    83                                                      
REMARK 465     GLY A    84                                                      
REMARK 465     LYS A   179                                                      
REMARK 465     GLY B    78                                                      
REMARK 465     SER B    79                                                      
REMARK 465     HIS B    80                                                      
REMARK 465     GLU B   123                                                      
REMARK 465     TYR B   124                                                      
REMARK 465     GLU B   125                                                      
REMARK 465     GLY B   126                                                      
REMARK 465     LYS B   179                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS B 121    CB   CG   CD   CE   NZ                              
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 B 170   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  87      -79.16   -127.02                                   
REMARK 500    ASP A 158      167.93     62.51                                   
REMARK 500    HIS B  99       74.09   -110.77                                   
REMARK 500    ASP B 158      169.28     62.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR B  113     LEU B  114                 -136.58                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU B 114        23.6      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 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 IOD B   1                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B   2                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B   3                 
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: 2C3W   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CBM25 FROM BACILLUS HALODURANS                         
REMARK 900  AMYLASE IN COMPLEX WITH MALTOTETRAOSE                               
REMARK 900 RELATED ID: 2C3X   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF IODINATED CBM25 FROM BACILLUS                          
REMARK 900  HALODURANS AMYLASE IN COMPLEX WITH                                  
REMARK 900  MALTOTETRAOSE                                                       
DBREF  2C3V A   78    83  PDB    2C3V     2C3V            78     83             
DBREF  2C3V A   84   179  UNP    Q9KFR4   Q9KFR4_BACHD   863    958             
DBREF  2C3V B   78    83  PDB    2C3V     2C3V            78     83             
DBREF  2C3V B   84   179  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 TYI GLU GLY TYI 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                  
MODRES 2C3V TYI A  124  TYR  OSINE  3,5 DIIODOTYROSINE                          
MODRES 2C3V TYI A  127  TYR  OSINE  3,5 DIIODOTYROSINE                          
HET    TYI  A 124      14                                                       
HET    TYI  A 127      23                                                       
HET    IOD  B   1       3                                                       
HET    IOD  B   2       3                                                       
HET    IOD  B   3       2                                                       
HETNAM     TYI 3,5-DIIODOTYROSINE                                               
HETNAM     IOD IODIDE ION                                                       
FORMUL   1  TYI    2(C9 H9 I2 N O3)                                             
FORMUL   3  IOD    3(I 1-)                                                      
FORMUL   6  HOH   *212(H2 O1)                                                   
HELIX    1   1 ASN A  153  ARG A  157  5                                   5    
HELIX    2   2 ASN B  153  ARG B  157  5                                   5    
SHEET    1  AA 9 THR A 120  LYS A 121  0                                        
SHEET    2  AA 9 TYI A 127  ILE A 132 -1  O  LYS A 129   N  THR A 120           
SHEET    3  AA 9 ILE A  89  LYS A  94 -1  O  ILE A  89   N  ILE A 132           
SHEET    4  AA 9 GLY A 164  ALA A 169  1  O  GLY A 164   N  THR A  90           
SHEET    5  AA 9 ARG A 172  SER A 175 -1  O  ARG A 172   N  ALA A 169           
SHEET    6  AA 9 VAL B 128  GLU B 133 -1  O  THR B 131   N  SER A 175           
SHEET    7  AA 9 ILE B  89  TYR B  93 -1  O  ILE B  89   N  ILE B 132           
SHEET    8  AA 9 GLY B 164  ALA B 169  1  O  GLY B 164   N  THR B  90           
SHEET    9  AA 9 ARG B 172  SER B 175 -1  O  ARG B 172   N  ALA B 169           
SHEET    1  AB 7 THR A 120  LYS A 121  0                                        
SHEET    2  AB 7 TYI A 127  ILE A 132 -1  O  LYS A 129   N  THR A 120           
SHEET    3  AB 7 ILE A  89  LYS A  94 -1  O  ILE A  89   N  ILE A 132           
SHEET    4  AB 7 GLY A 164  ALA A 169  1  O  GLY A 164   N  THR A  90           
SHEET    5  AB 7 ARG A 172  SER A 175 -1  O  ARG A 172   N  ALA A 169           
SHEET    6  AB 7 VAL B 128  GLU B 133 -1  O  THR B 131   N  SER A 175           
SHEET    7  AB 7 THR B 120  LYS B 121 -1  O  THR B 120   N  LYS B 129           
SHEET    1  AC 4 VAL A 117  PRO A 118  0                                        
SHEET    2  AC 4 HIS A 101  LEU A 106 -1  O  ILE A 102   N  VAL A 117           
SHEET    3  AC 4 GLN A 139  ASN A 145 -1  O  ARG A 141   N  SER A 105           
SHEET    4  AC 4 TYR A 159  SER A 162 -1  O  TYR A 159   N  ALA A 142           
SHEET    1  AD 4 VAL A 117  PRO A 118  0                                        
SHEET    2  AD 4 HIS A 101  LEU A 106 -1  O  ILE A 102   N  VAL A 117           
SHEET    3  AD 4 GLN A 139  ASN A 145 -1  O  ARG A 141   N  SER A 105           
SHEET    4  AD 4 TRP A 151  ASP A 152 -1  O  ASP A 152   N  PHE A 144           
SHEET    1  BA 4 VAL B 117  PRO B 118  0                                        
SHEET    2  BA 4 HIS B 101  LEU B 106 -1  O  ILE B 102   N  VAL B 117           
SHEET    3  BA 4 GLN B 139  ASN B 145 -1  O  ARG B 141   N  SER B 105           
SHEET    4  BA 4 TYR B 159  SER B 162 -1  O  TYR B 159   N  ALA B 142           
SHEET    1  BB 4 VAL B 117  PRO B 118  0                                        
SHEET    2  BB 4 HIS B 101  LEU B 106 -1  O  ILE B 102   N  VAL B 117           
SHEET    3  BB 4 GLN B 139  ASN B 145 -1  O  ARG B 141   N  SER B 105           
SHEET    4  BB 4 TRP B 151  ASP B 152 -1  O  ASP B 152   N  PHE B 144           
LINK         C   GLU A 123                 N   TYI A 124     1555   1555  1.35  
LINK         C   TYI A 124                 N   GLU A 125     1555   1555  1.32  
LINK         C   GLY A 126                 N   TYI A 127     1555   1555  1.34  
LINK         C   TYI A 127                 N   VAL A 128     1555   1555  1.33  
CISPEP   1 LEU A  114    PRO A  115          0         5.61                     
SITE     1 AC1  5 HOH A2019  HOH A2020  HOH A2022  PRO B 178                    
SITE     2 AC1  5 HOH B2079                                                     
SITE     1 AC2  5 GLN A 150  TYR B  92  THR B 177  HOH B2038                    
SITE     2 AC2  5 HOH B2079                                                     
SITE     1 AC3  1 TYR B 127                                                     
CRYST1   30.198   41.819   68.183  90.00  97.18  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.033115  0.000000  0.004172        0.00000                         
SCALE2      0.000000  0.023913  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014782        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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