GenomeNet

Database: PDB
Entry: 2C3H
LinkDB: 2C3H
Original site: 2C3H 
HEADER    CARBOHYDRATE-BINDING MODULE             07-OCT-05   2C3H              
TITLE     STRUCTURE OF CBM26 FROM BACILLUS HALODURANS AMYLASE IN                
TITLE    2 COMPLEX WITH MALTOSE                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE G-6;                                         
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: CARBOHYDRATE-BINDING MODULE, RESIDUES 771-863;             
COMPND   5 SYNONYM: FAMILY 26 CARBOHYDRATE-BINDING MODULE;                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS HALODURANS;                            
SOURCE   3 ORGANISM_TAXID: 272558;                                              
SOURCE   4 STRAIN: C-125;                                                       
SOURCE   5 ATCC: BAA-125;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET 28A;                                   
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET-BHCBM6                                
KEYWDS    CARBOHYDRATE-BINDING MODULE, STARCH BINDING, CARBOHYDRATE             
KEYWDS   2 BINDING, GLYCOSIDE HYDROLASE, AMYLOSE, AMYLOPECTIN,                  
KEYWDS   3 MALTO-OLIGOSACCHARIDE, 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 2C3H    1       VERSN                                    
REVDAT   2   18-JAN-06 2C3H    1       JRNL                                     
REVDAT   1   17-OCT-05 2C3H    0                                                
JRNL        AUTH   A.B.BORASTON,M.HEALEY,J.KLASSEN,E.FICKO-BLEAN,               
JRNL        AUTH 2 A.LAMMERTS VAN BUEREN,V.LAW                                  
JRNL        TITL   A STRUCTURAL AND FUNCTIONAL ANALYSIS OF ALPHA-               
JRNL        TITL 2 GLUCAN RECOGNITION BY FAMILY 25 AND 26                       
JRNL        TITL 3 CARBOHYDRATE-BINDING MODULES REVEALS A CONSERVED             
JRNL        TITL 4 MODE OF STARCH RECOGNITION                                   
JRNL        REF    J.BIOL.CHEM.                  V. 281   587 2006              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   16230347                                                     
JRNL        DOI    10.1074/JBC.M509958200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.24 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 55701                          
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) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2964                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.24                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.29                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3482                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2900                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 182                          
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6219                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 241                                     
REMARK   3   SOLVENT ATOMS            : 804                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.14000                                              
REMARK   3    B22 (A**2) : 1.14000                                              
REMARK   3    B33 (A**2) : -1.71000                                             
REMARK   3    B12 (A**2) : 0.57000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.243         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.230         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.172         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.129         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6736 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9235 ; 1.993 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   729 ; 8.999 ; 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):   877 ; 0.171 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5396 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3535 ; 0.239 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   737 ; 0.192 ; 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):    82 ; 0.274 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    43 ; 0.232 ; 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):  3667 ; 0.892 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5937 ; 1.670 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3069 ; 2.521 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3298 ; 3.837 ; 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 2C3H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-OCT-05.                  
REMARK 100 THE PDBE ID CODE IS EBI-25914.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 113.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 55701                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.240                              
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     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.0000                             
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   (%): 58.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      120.32867            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       60.16433            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       60.16433            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      120.32867            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8                                  
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 350 BIOMOLECULE:  5                                                      
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: E                                     
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:  6                                                      
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: F                                     
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:  7                                                      
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: G                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 BIOMOLECULE:  8                                                      
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: H                                     
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     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     MET A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     GLY A    97                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     MET B     2                                                      
REMARK 465     GLY B    97                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     HIS C     1                                                      
REMARK 465     MET C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     PRO C    96                                                      
REMARK 465     GLY C    97                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     HIS D     1                                                      
REMARK 465     MET D     2                                                      
REMARK 465     ALA D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     GLY D    97                                                      
REMARK 465     GLY E     0                                                      
REMARK 465     HIS E     1                                                      
REMARK 465     MET E     2                                                      
REMARK 465     ALA E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     GLY E    97                                                      
REMARK 465     GLY F     0                                                      
REMARK 465     HIS F     1                                                      
REMARK 465     MET F     2                                                      
REMARK 465     ALA F     3                                                      
REMARK 465     SER F     4                                                      
REMARK 465     PRO F    96                                                      
REMARK 465     GLY F    97                                                      
REMARK 465     GLY G     0                                                      
REMARK 465     HIS G     1                                                      
REMARK 465     MET G     2                                                      
REMARK 465     ALA G     3                                                      
REMARK 465     SER G     4                                                      
REMARK 465     GLY G    97                                                      
REMARK 465     GLY H     0                                                      
REMARK 465     HIS H     1                                                      
REMARK 465     MET H     2                                                      
REMARK 465     ALA H     3                                                      
REMARK 465     SER H     4                                                      
REMARK 465     GLY H    97                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A    82  -  O    HOH A  2079              2.16            
REMARK 500   OD2  ASP D    82  -  OE1  GLU E    90              2.00            
REMARK 500   OE1  GLU D    90  -  OD2  ASP E    82              2.19            
REMARK 500   NE   ARG E    66  -  O    HOH E  2059              2.18            
REMARK 500   CZ   ARG E    66  -  O    HOH E  2059              2.13            
REMARK 500   OD2  ASP F    82  -  OE2  GLU H    90              2.16            
REMARK 500   O    ARG F    95  -  O    HOH F  2082              2.13            
REMARK 500   O4   SO4 A  1097  -  O    HOH A  2098              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   O    HOH F  2055     O    HOH F  2084     4556      2.11           
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  31   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A  82   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP A  82   C   -  N   -  CA  ANGL. DEV. =  18.4 DEGREES          
REMARK 500    ASP A  84   CB  -  CG  -  OD2 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG A  95   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A  95   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP B  14   CB  -  CG  -  OD2 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ASP B  25   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP B  84   CB  -  CG  -  OD2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ASP B  88   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ARG B  95   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ASP C  14   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP C  31   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP C  65   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP C  82   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG C  81   CA  -  C   -  N   ANGL. DEV. =  13.7 DEGREES          
REMARK 500    ARG C  81   O   -  C   -  N   ANGL. DEV. = -10.1 DEGREES          
REMARK 500    ASP C  82   C   -  N   -  CA  ANGL. DEV. =  21.7 DEGREES          
REMARK 500    ASP C  84   CB  -  CG  -  OD2 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG C  95   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP D  25   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP D  84   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP D  88   CB  -  CG  -  OD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP E  47   CB  -  CG  -  OD2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ASP E  82   C   -  N   -  CA  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    ASP E  84   CB  -  CG  -  OD2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ASP E  88   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP F  31   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    LEU F  61   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
REMARK 500    ARG F  81   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ASP F  84   CB  -  CG  -  OD2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    ASP F  88   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    ARG G  81   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG G  81   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP G  84   CB  -  CG  -  OD2 ANGL. DEV. =   7.7 DEGREES          
REMARK 500    ARG H  81   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP H  84   CB  -  CG  -  OD2 ANGL. DEV. =   7.8 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    TYR A  44      -77.48   -104.43                                   
REMARK 500    ASP A  82      -76.22     80.75                                   
REMARK 500    THR B  34      150.26    -47.74                                   
REMARK 500    TYR B  44      -67.87   -102.62                                   
REMARK 500    ASP B  82      -70.96    117.26                                   
REMARK 500    ARG B  95      110.47    115.27                                   
REMARK 500    TYR C  44      -68.62   -107.53                                   
REMARK 500    ASP C  82      -37.94     95.19                                   
REMARK 500    THR D  34      156.42    -43.35                                   
REMARK 500    TYR D  44      -61.03   -109.05                                   
REMARK 500    ASP D  65     -163.25   -108.50                                   
REMARK 500    ASP D  82      -57.57    127.28                                   
REMARK 500    ASP E  82      -68.97    109.98                                   
REMARK 500    ASN F  27      114.92   -165.52                                   
REMARK 500    ASP F  65     -165.31   -100.37                                   
REMARK 500    ASP F  82      -61.30    117.15                                   
REMARK 500    TYR G  44      -62.63   -109.31                                   
REMARK 500    ASP G  65     -169.37   -114.04                                   
REMARK 500    ASP G  82      -50.16    133.15                                   
REMARK 500    ASP H  65     -169.24   -101.17                                   
REMARK 500    ASP H  82      -44.26    108.77                                   
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 ARG D   81     ASP D   82                  -43.49                    
REMARK 500 ARG F   81     ASP F   82                  -30.99                    
REMARK 500 ARG G   81     ASP G   82                  -56.81                    
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    ASP A  82        13.4      L          L   OUTSIDE RANGE           
REMARK 500    ASP B  82        22.5      L          L   OUTSIDE RANGE           
REMARK 500    ASP C  82         0.7      L          D   EXPECTING SP3           
REMARK 500    TRP C  86        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ASP D  82        23.8      L          L   OUTSIDE RANGE           
REMARK 500    TRP D  86        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ASP E  82        20.1      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 GLC A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC C 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC D 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC E 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC F 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC F 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC G 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC G 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC H 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLC H 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1097                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1098                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1099                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1100                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1096                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1097                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F1096                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G1097                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G1098                 
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: 2C3V   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF IODINATED CBM25 FROM BACILLUS                          
REMARK 900  HALODURANS AMYLASE                                                  
REMARK 900 RELATED ID: 2C3W   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CBM25 FROM BACILLUS HALODURANS                         
REMARK 900  AMYLASE IN COMPLEX WITH MALTOTETRAOSE                               
REMARK 900 RELATED ID: 2C3X   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF IODINATED CBM25 FROM BACILLUS                          
REMARK 900  HALODURANS AMYLASE IN COMPLEX WITH                                  
REMARK 900  MALTOTETRAOSE                                                       
DBREF  2C3H A    0     4  PDB    2C3H     2C3H             0      4             
DBREF  2C3H A    5    97  UNP    Q9KFR4   Q9KFR4_BACHD   771    863             
DBREF  2C3H B    0     4  PDB    2C3H     2C3H             0      4             
DBREF  2C3H B    5    97  UNP    Q9KFR4   Q9KFR4_BACHD   771    863             
DBREF  2C3H C    0     4  PDB    2C3H     2C3H             0      4             
DBREF  2C3H C    5    97  UNP    Q9KFR4   Q9KFR4_BACHD   771    863             
DBREF  2C3H D    0     4  PDB    2C3H     2C3H             0      4             
DBREF  2C3H D    5    97  UNP    Q9KFR4   Q9KFR4_BACHD   771    863             
DBREF  2C3H E    0     4  PDB    2C3H     2C3H             0      4             
DBREF  2C3H E    5    97  UNP    Q9KFR4   Q9KFR4_BACHD   771    863             
DBREF  2C3H F    0     4  PDB    2C3H     2C3H             0      4             
DBREF  2C3H F    5    97  UNP    Q9KFR4   Q9KFR4_BACHD   771    863             
DBREF  2C3H G    0     4  PDB    2C3H     2C3H             0      4             
DBREF  2C3H G    5    97  UNP    Q9KFR4   Q9KFR4_BACHD   771    863             
DBREF  2C3H H    0     4  PDB    2C3H     2C3H             0      4             
DBREF  2C3H H    5    97  UNP    Q9KFR4   Q9KFR4_BACHD   771    863             
SEQRES   1 A   98  GLY HIS MET ALA SER GLY LEU THR ILE TYR PHE LYS LYS          
SEQRES   2 A   98  PRO ASP SER TRP GLY THR PRO HIS LEU TYR TYR TYR ASP          
SEQRES   3 A   98  THR ASN PRO LYS VAL ASP GLU PRO THR TRP SER GLU ALA          
SEQRES   4 A   98  PRO GLU MET GLU HIS TYR GLU GLY ASP TRP TYR THR HIS          
SEQRES   5 A   98  THR ILE GLU GLY VAL GLU SER VAL ARG LEU LEU PHE LYS          
SEQRES   6 A   98  ASP ARG GLY THR ASN GLN TRP PRO GLY PRO GLY GLU PRO          
SEQRES   7 A   98  GLY PHE PHE ARG ASP GLN ASP GLY TRP PHE ASP GLY GLU          
SEQRES   8 A   98  TRP HIS VAL ASP ARG PRO GLY                                  
SEQRES   1 B   98  GLY HIS MET ALA SER GLY LEU THR ILE TYR PHE LYS LYS          
SEQRES   2 B   98  PRO ASP SER TRP GLY THR PRO HIS LEU TYR TYR TYR ASP          
SEQRES   3 B   98  THR ASN PRO LYS VAL ASP GLU PRO THR TRP SER GLU ALA          
SEQRES   4 B   98  PRO GLU MET GLU HIS TYR GLU GLY ASP TRP TYR THR HIS          
SEQRES   5 B   98  THR ILE GLU GLY VAL GLU SER VAL ARG LEU LEU PHE LYS          
SEQRES   6 B   98  ASP ARG GLY THR ASN GLN TRP PRO GLY PRO GLY GLU PRO          
SEQRES   7 B   98  GLY PHE PHE ARG ASP GLN ASP GLY TRP PHE ASP GLY GLU          
SEQRES   8 B   98  TRP HIS VAL ASP ARG PRO GLY                                  
SEQRES   1 C   98  GLY HIS MET ALA SER GLY LEU THR ILE TYR PHE LYS LYS          
SEQRES   2 C   98  PRO ASP SER TRP GLY THR PRO HIS LEU TYR TYR TYR ASP          
SEQRES   3 C   98  THR ASN PRO LYS VAL ASP GLU PRO THR TRP SER GLU ALA          
SEQRES   4 C   98  PRO GLU MET GLU HIS TYR GLU GLY ASP TRP TYR THR HIS          
SEQRES   5 C   98  THR ILE GLU GLY VAL GLU SER VAL ARG LEU LEU PHE LYS          
SEQRES   6 C   98  ASP ARG GLY THR ASN GLN TRP PRO GLY PRO GLY GLU PRO          
SEQRES   7 C   98  GLY PHE PHE ARG ASP GLN ASP GLY TRP PHE ASP GLY GLU          
SEQRES   8 C   98  TRP HIS VAL ASP ARG PRO GLY                                  
SEQRES   1 D   98  GLY HIS MET ALA SER GLY LEU THR ILE TYR PHE LYS LYS          
SEQRES   2 D   98  PRO ASP SER TRP GLY THR PRO HIS LEU TYR TYR TYR ASP          
SEQRES   3 D   98  THR ASN PRO LYS VAL ASP GLU PRO THR TRP SER GLU ALA          
SEQRES   4 D   98  PRO GLU MET GLU HIS TYR GLU GLY ASP TRP TYR THR HIS          
SEQRES   5 D   98  THR ILE GLU GLY VAL GLU SER VAL ARG LEU LEU PHE LYS          
SEQRES   6 D   98  ASP ARG GLY THR ASN GLN TRP PRO GLY PRO GLY GLU PRO          
SEQRES   7 D   98  GLY PHE PHE ARG ASP GLN ASP GLY TRP PHE ASP GLY GLU          
SEQRES   8 D   98  TRP HIS VAL ASP ARG PRO GLY                                  
SEQRES   1 E   98  GLY HIS MET ALA SER GLY LEU THR ILE TYR PHE LYS LYS          
SEQRES   2 E   98  PRO ASP SER TRP GLY THR PRO HIS LEU TYR TYR TYR ASP          
SEQRES   3 E   98  THR ASN PRO LYS VAL ASP GLU PRO THR TRP SER GLU ALA          
SEQRES   4 E   98  PRO GLU MET GLU HIS TYR GLU GLY ASP TRP TYR THR HIS          
SEQRES   5 E   98  THR ILE GLU GLY VAL GLU SER VAL ARG LEU LEU PHE LYS          
SEQRES   6 E   98  ASP ARG GLY THR ASN GLN TRP PRO GLY PRO GLY GLU PRO          
SEQRES   7 E   98  GLY PHE PHE ARG ASP GLN ASP GLY TRP PHE ASP GLY GLU          
SEQRES   8 E   98  TRP HIS VAL ASP ARG PRO GLY                                  
SEQRES   1 F   98  GLY HIS MET ALA SER GLY LEU THR ILE TYR PHE LYS LYS          
SEQRES   2 F   98  PRO ASP SER TRP GLY THR PRO HIS LEU TYR TYR TYR ASP          
SEQRES   3 F   98  THR ASN PRO LYS VAL ASP GLU PRO THR TRP SER GLU ALA          
SEQRES   4 F   98  PRO GLU MET GLU HIS TYR GLU GLY ASP TRP TYR THR HIS          
SEQRES   5 F   98  THR ILE GLU GLY VAL GLU SER VAL ARG LEU LEU PHE LYS          
SEQRES   6 F   98  ASP ARG GLY THR ASN GLN TRP PRO GLY PRO GLY GLU PRO          
SEQRES   7 F   98  GLY PHE PHE ARG ASP GLN ASP GLY TRP PHE ASP GLY GLU          
SEQRES   8 F   98  TRP HIS VAL ASP ARG PRO GLY                                  
SEQRES   1 G   98  GLY HIS MET ALA SER GLY LEU THR ILE TYR PHE LYS LYS          
SEQRES   2 G   98  PRO ASP SER TRP GLY THR PRO HIS LEU TYR TYR TYR ASP          
SEQRES   3 G   98  THR ASN PRO LYS VAL ASP GLU PRO THR TRP SER GLU ALA          
SEQRES   4 G   98  PRO GLU MET GLU HIS TYR GLU GLY ASP TRP TYR THR HIS          
SEQRES   5 G   98  THR ILE GLU GLY VAL GLU SER VAL ARG LEU LEU PHE LYS          
SEQRES   6 G   98  ASP ARG GLY THR ASN GLN TRP PRO GLY PRO GLY GLU PRO          
SEQRES   7 G   98  GLY PHE PHE ARG ASP GLN ASP GLY TRP PHE ASP GLY GLU          
SEQRES   8 G   98  TRP HIS VAL ASP ARG PRO GLY                                  
SEQRES   1 H   98  GLY HIS MET ALA SER GLY LEU THR ILE TYR PHE LYS LYS          
SEQRES   2 H   98  PRO ASP SER TRP GLY THR PRO HIS LEU TYR TYR TYR ASP          
SEQRES   3 H   98  THR ASN PRO LYS VAL ASP GLU PRO THR TRP SER GLU ALA          
SEQRES   4 H   98  PRO GLU MET GLU HIS TYR GLU GLY ASP TRP TYR THR HIS          
SEQRES   5 H   98  THR ILE GLU GLY VAL GLU SER VAL ARG LEU LEU PHE LYS          
SEQRES   6 H   98  ASP ARG GLY THR ASN GLN TRP PRO GLY PRO GLY GLU PRO          
SEQRES   7 H   98  GLY PHE PHE ARG ASP GLN ASP GLY TRP PHE ASP GLY GLU          
SEQRES   8 H   98  TRP HIS VAL ASP ARG PRO GLY                                  
HET    GLC  A 201      12                                                       
HET    GLC  A 202      11                                                       
HET    GLC  B 201      12                                                       
HET    GLC  B 202      11                                                       
HET    GLC  C 201      12                                                       
HET    GLC  C 202      11                                                       
HET    GLC  D 201      12                                                       
HET    GLC  D 202      11                                                       
HET    GLC  D 300      12                                                       
HET    GLC  E 201      12                                                       
HET    GLC  E 202      11                                                       
HET    GLC  F 201      12                                                       
HET    GLC  F 202      11                                                       
HET    GLC  G 201      12                                                       
HET    GLC  G 202      11                                                       
HET    GLC  H 201      12                                                       
HET    GLC  H 202      11                                                       
HET    SO4  A1097       5                                                       
HET    SO4  A1098       5                                                       
HET    SO4  A1099       5                                                       
HET    SO4  A1100       5                                                       
HET    SO4  C1096       5                                                       
HET    SO4  C1097       5                                                       
HET    SO4  F1096       5                                                       
HET    SO4  G1097       5                                                       
HET    SO4  G1098       5                                                       
HETNAM     GLC ALPHA-D-GLUCOSE                                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   9  GLC    17(C6 H12 O6)                                                
FORMUL  19  SO4    9(O4 S 2-)                                                   
FORMUL  28  HOH   *804(H2 O1)                                                   
HELIX    1   1 THR A   34  ALA A   38  5                                   5    
HELIX    2   2 THR B   34  ALA B   38  5                                   5    
HELIX    3   3 THR D   34  ALA D   38  5                                   5    
HELIX    4   4 THR G   34  ALA G   38  5                                   5    
SHEET    1  AA 5 GLU A  42  GLU A  45  0                                        
SHEET    2  AA 5 TRP A  48  ILE A  53 -1  O  TRP A  48   N  TYR A  44           
SHEET    3  AA 5 LEU A   6  LYS A  11 -1  O  LEU A   6   N  ILE A  53           
SHEET    4  AA 5 TRP A  86  PHE A  87  1  O  PHE A  87   N  LYS A  11           
SHEET    5  AA 5 TRP A  91  HIS A  92 -1  O  HIS A  92   N  TRP A  86           
SHEET    1  AB 3 HIS A  20  ASN A  27  0                                        
SHEET    2  AB 3 SER A  58  LYS A  64 -1  O  SER A  58   N  ASN A  27           
SHEET    3  AB 3 PHE A  79  ARG A  81 -1  O  PHE A  79   N  LEU A  61           
SHEET    1  AC 3 HIS A  20  ASN A  27  0                                        
SHEET    2  AC 3 SER A  58  LYS A  64 -1  O  SER A  58   N  ASN A  27           
SHEET    3  AC 3 GLN A  70  TRP A  71 -1  O  TRP A  71   N  PHE A  63           
SHEET    1  BA 5 GLU B  42  GLU B  45  0                                        
SHEET    2  BA 5 TRP B  48  ILE B  53 -1  O  TRP B  48   N  TYR B  44           
SHEET    3  BA 5 LEU B   6  LYS B  11 -1  O  LEU B   6   N  ILE B  53           
SHEET    4  BA 5 GLY B  85  PHE B  87  1  O  GLY B  85   N  TYR B   9           
SHEET    5  BA 5 TRP B  91  HIS B  92 -1  O  HIS B  92   N  TRP B  86           
SHEET    1  BB 3 HIS B  20  ASN B  27  0                                        
SHEET    2  BB 3 SER B  58  LYS B  64 -1  O  SER B  58   N  ASN B  27           
SHEET    3  BB 3 PHE B  79  ARG B  81 -1  O  PHE B  79   N  LEU B  61           
SHEET    1  BC 3 HIS B  20  ASN B  27  0                                        
SHEET    2  BC 3 SER B  58  LYS B  64 -1  O  SER B  58   N  ASN B  27           
SHEET    3  BC 3 GLN B  70  TRP B  71 -1  O  TRP B  71   N  PHE B  63           
SHEET    1  CA 5 GLU C  42  GLU C  45  0                                        
SHEET    2  CA 5 TRP C  48  ILE C  53 -1  O  TRP C  48   N  TYR C  44           
SHEET    3  CA 5 LEU C   6  LYS C  11 -1  O  LEU C   6   N  ILE C  53           
SHEET    4  CA 5 GLY C  85  PHE C  87  1  O  GLY C  85   N  TYR C   9           
SHEET    5  CA 5 TRP C  91  HIS C  92 -1  O  HIS C  92   N  TRP C  86           
SHEET    1  CB 3 HIS C  20  ASN C  27  0                                        
SHEET    2  CB 3 SER C  58  LYS C  64 -1  O  SER C  58   N  ASN C  27           
SHEET    3  CB 3 PHE C  79  ARG C  81 -1  O  PHE C  79   N  LEU C  61           
SHEET    1  CC 3 HIS C  20  ASN C  27  0                                        
SHEET    2  CC 3 SER C  58  LYS C  64 -1  O  SER C  58   N  ASN C  27           
SHEET    3  CC 3 GLN C  70  TRP C  71 -1  O  TRP C  71   N  PHE C  63           
SHEET    1  DA 5 GLU D  42  GLU D  45  0                                        
SHEET    2  DA 5 TRP D  48  ILE D  53 -1  O  TRP D  48   N  TYR D  44           
SHEET    3  DA 5 LEU D   6  LYS D  11 -1  O  LEU D   6   N  ILE D  53           
SHEET    4  DA 5 GLY D  85  PHE D  87  1  O  GLY D  85   N  TYR D   9           
SHEET    5  DA 5 TRP D  91  HIS D  92 -1  O  HIS D  92   N  TRP D  86           
SHEET    1  DB 6 HIS D  20  ASN D  27  0                                        
SHEET    2  DB 6 SER D  58  LYS D  64 -1  O  SER D  58   N  ASN D  27           
SHEET    3  DB 6 GLN D  70  TRP D  71 -1  O  TRP D  71   N  PHE D  63           
SHEET    4  DB 6 SER D  58  LYS D  64 -1  O  PHE D  63   N  TRP D  71           
SHEET    5  DB 6 PHE D  79  ARG D  81 -1  O  PHE D  79   N  LEU D  61           
SHEET    6  DB 6 SER D  58  LYS D  64 -1  O  VAL D  59   N  ARG D  81           
SHEET    1  EA 5 GLU E  42  GLU E  45  0                                        
SHEET    2  EA 5 TRP E  48  ILE E  53 -1  O  TRP E  48   N  TYR E  44           
SHEET    3  EA 5 LEU E   6  LYS E  11 -1  O  LEU E   6   N  ILE E  53           
SHEET    4  EA 5 GLY E  85  PHE E  87  1  O  GLY E  85   N  TYR E   9           
SHEET    5  EA 5 TRP E  91  HIS E  92 -1  O  HIS E  92   N  TRP E  86           
SHEET    1  EB 6 HIS E  20  ASN E  27  0                                        
SHEET    2  EB 6 SER E  58  LYS E  64 -1  O  SER E  58   N  ASN E  27           
SHEET    3  EB 6 GLN E  70  TRP E  71 -1  O  TRP E  71   N  PHE E  63           
SHEET    4  EB 6 SER E  58  LYS E  64 -1  O  PHE E  63   N  TRP E  71           
SHEET    5  EB 6 PHE E  79  ARG E  81 -1  O  PHE E  79   N  LEU E  61           
SHEET    6  EB 6 SER E  58  LYS E  64 -1  O  VAL E  59   N  ARG E  81           
SHEET    1  FA 5 GLU F  42  GLU F  45  0                                        
SHEET    2  FA 5 TRP F  48  ILE F  53 -1  O  TRP F  48   N  TYR F  44           
SHEET    3  FA 5 LEU F   6  LYS F  11 -1  O  LEU F   6   N  ILE F  53           
SHEET    4  FA 5 GLY F  85  PHE F  87  1  O  GLY F  85   N  TYR F   9           
SHEET    5  FA 5 TRP F  91  HIS F  92 -1  O  HIS F  92   N  TRP F  86           
SHEET    1  FB 6 HIS F  20  ASN F  27  0                                        
SHEET    2  FB 6 SER F  58  LYS F  64 -1  O  SER F  58   N  ASN F  27           
SHEET    3  FB 6 GLN F  70  TRP F  71 -1  O  TRP F  71   N  PHE F  63           
SHEET    4  FB 6 SER F  58  LYS F  64 -1  O  PHE F  63   N  TRP F  71           
SHEET    5  FB 6 PHE F  79  ARG F  81 -1  O  PHE F  79   N  LEU F  61           
SHEET    6  FB 6 SER F  58  LYS F  64 -1  O  VAL F  59   N  ARG F  81           
SHEET    1  GA 5 GLU G  42  GLU G  45  0                                        
SHEET    2  GA 5 TRP G  48  ILE G  53 -1  O  TRP G  48   N  TYR G  44           
SHEET    3  GA 5 LEU G   6  LYS G  11 -1  O  LEU G   6   N  ILE G  53           
SHEET    4  GA 5 TRP G  86  PHE G  87  1  O  PHE G  87   N  LYS G  11           
SHEET    5  GA 5 TRP G  91  HIS G  92 -1  O  HIS G  92   N  TRP G  86           
SHEET    1  GB 6 HIS G  20  ASN G  27  0                                        
SHEET    2  GB 6 SER G  58  LYS G  64 -1  O  SER G  58   N  ASN G  27           
SHEET    3  GB 6 GLN G  70  TRP G  71 -1  O  TRP G  71   N  PHE G  63           
SHEET    4  GB 6 SER G  58  LYS G  64 -1  O  PHE G  63   N  TRP G  71           
SHEET    5  GB 6 PHE G  79  ARG G  81 -1  O  PHE G  79   N  LEU G  61           
SHEET    6  GB 6 SER G  58  LYS G  64 -1  O  VAL G  59   N  ARG G  81           
SHEET    1  HA 5 GLU H  42  TYR H  44  0                                        
SHEET    2  HA 5 TRP H  48  ILE H  53 -1  O  TRP H  48   N  TYR H  44           
SHEET    3  HA 5 LEU H   6  LYS H  11 -1  O  LEU H   6   N  ILE H  53           
SHEET    4  HA 5 GLY H  85  PHE H  87  1  O  GLY H  85   N  TYR H   9           
SHEET    5  HA 5 TRP H  91  HIS H  92 -1  O  HIS H  92   N  TRP H  86           
SHEET    1  HB 6 HIS H  20  ASN H  27  0                                        
SHEET    2  HB 6 SER H  58  LYS H  64 -1  O  SER H  58   N  ASN H  27           
SHEET    3  HB 6 GLN H  70  TRP H  71 -1  O  TRP H  71   N  PHE H  63           
SHEET    4  HB 6 SER H  58  LYS H  64 -1  O  PHE H  63   N  TRP H  71           
SHEET    5  HB 6 PHE H  79  ARG H  81 -1  O  PHE H  79   N  LEU H  61           
SHEET    6  HB 6 SER H  58  LYS H  64 -1  O  VAL H  59   N  ARG H  81           
LINK         O4  GLC A 201                 C1  GLC A 202     1555   1555  1.65  
LINK         O4  GLC B 201                 C1  GLC B 202     1555   1555  1.42  
LINK         O4  GLC C 201                 C1  GLC C 202     1555   1555  1.44  
LINK         O4  GLC D 201                 C1  GLC D 202     1555   1555  1.42  
LINK         O4  GLC E 201                 C1  GLC E 202     1555   1555  1.42  
LINK         O4  GLC F 201                 C1  GLC F 202     1555   1555  1.44  
LINK         O4  GLC G 201                 C1  GLC G 202     1555   1555  1.44  
LINK         O4  GLC H 201                 C1  GLC H 202     1555   1555  1.44  
CISPEP   1 ASN A   27    PRO A   28          0        -3.38                     
CISPEP   2 TRP A   71    PRO A   72          0         1.99                     
CISPEP   3 ARG A   81    ASP A   82          0        21.47                     
CISPEP   4 ASP A   84    GLY A   85          0         1.80                     
CISPEP   5 ASN B   27    PRO B   28          0        -6.19                     
CISPEP   6 TRP B   71    PRO B   72          0        -2.76                     
CISPEP   7 ARG B   81    ASP B   82          0       -29.02                     
CISPEP   8 ASP B   84    GLY B   85          0        22.67                     
CISPEP   9 ASN C   27    PRO C   28          0        -7.65                     
CISPEP  10 TRP C   71    PRO C   72          0        -0.20                     
CISPEP  11 ARG C   81    ASP C   82          0       -28.26                     
CISPEP  12 ASP C   84    GLY C   85          0        -2.84                     
CISPEP  13 ASN D   27    PRO D   28          0         0.47                     
CISPEP  14 TRP D   71    PRO D   72          0         2.65                     
CISPEP  15 ASP D   84    GLY D   85          0        21.25                     
CISPEP  16 ASN E   27    PRO E   28          0        -7.71                     
CISPEP  17 TRP E   71    PRO E   72          0        -2.75                     
CISPEP  18 ARG E   81    ASP E   82          0       -10.92                     
CISPEP  19 ASP E   84    GLY E   85          0        -2.62                     
CISPEP  20 ASN F   27    PRO F   28          0        -3.57                     
CISPEP  21 TRP F   71    PRO F   72          0        -0.54                     
CISPEP  22 ASP F   84    GLY F   85          0        -5.70                     
CISPEP  23 ASN G   27    PRO G   28          0       -11.79                     
CISPEP  24 TRP G   71    PRO G   72          0        -2.10                     
CISPEP  25 ASP G   84    GLY G   85          0        -4.24                     
CISPEP  26 ASN H   27    PRO H   28          0        -2.24                     
CISPEP  27 TRP H   71    PRO H   72          0         2.05                     
CISPEP  28 ARG H   81    ASP H   82          0       -27.78                     
CISPEP  29 ASP H   84    GLY H   85          0       -25.36                     
SITE     1 AC1 11 TYR A  22  TRP A  35  GLN A  70  PRO A  74                    
SITE     2 AC1 11 GLY A  75  GLC A 202  HOH A2093  HOH A2095                    
SITE     3 AC1 11 HOH A2096  HOH A2097  PRO E  74                               
SITE     1 AC2  8 TYR A  22  TYR A  24  GLY A  75  GLU A  76                    
SITE     2 AC2  8 PRO A  77  GLC A 201  PRO E  74  GLY E  75                    
SITE     1 AC3 10 TYR B  22  TRP B  35  GLN B  70  GLY B  75                    
SITE     2 AC3 10 GLC B 202  HOH B2098  HOH B2099  PRO H  74                    
SITE     3 AC3 10 GLY H  75  GLU H  76                                          
SITE     1 AC4  9 TYR B  22  GLY B  75  GLU B  76  GLC B 201                    
SITE     2 AC4  9 HOH B2099  HOH B2100  HOH B2101  GLC F 202                    
SITE     3 AC4  9 HOH F2020                                                     
SITE     1 AC5 10 TYR C  22  TRP C  35  GLN C  70  GLY C  75                    
SITE     2 AC5 10 GLC C 202  HOH C2099  HOH C2100  PRO D  74                    
SITE     3 AC5 10 GLY D  75  GLU D  76                                          
SITE     1 AC6 10 TYR C  22  TYR C  24  LEU C  62  GLY C  75                    
SITE     2 AC6 10 GLU C  76  PRO C  77  GLC C 201  HOH C2101                    
SITE     3 AC6 10 HOH C2102  GLC E 202                                          
SITE     1 AC7  9 PRO C  74  TYR D  22  TRP D  35  GLN D  70                    
SITE     2 AC7  9 PRO D  74  GLY D  75  GLC D 202  HOH D2100                    
SITE     3 AC7  9 HOH D2101                                                     
SITE     1 AC8  9 PRO C  74  GLY C  75  TYR D  22  GLY D  75                    
SITE     2 AC8  9 GLU D  76  PRO D  77  GLC D 201  HOH D2102                    
SITE     3 AC8  9 HOH D2103                                                     
SITE     1 AC9  2 GLN D  70  TRP D  71                                          
SITE     1 BC1 11 PRO A  74  GLY A  75  GLU A  76  HOH A2075                    
SITE     2 BC1 11 HOH C2023  TYR E  22  TRP E  35  GLN E  70                    
SITE     3 BC1 11 GLY E  75  GLC E 202  HOH E2102                               
SITE     1 BC2  9 GLC C 202  HOH C2023  TYR E  22  TYR E  24                    
SITE     2 BC2  9 GLY E  75  GLU E  76  PRO E  77  GLC E 201                    
SITE     3 BC2  9 HOH E2103                                                     
SITE     1 BC3 10 HOH B2022  TYR F  22  TRP F  35  GLN F  70                    
SITE     2 BC3 10 GLY F  75  GLC F 202  HOH F2083  PRO G  74                    
SITE     3 BC3 10 GLY G  75  GLU G  76                                          
SITE     1 BC4 11 GLC B 202  HOH B2021  HOH B2022  HOH B2101                    
SITE     2 BC4 11 TYR F  22  TYR F  24  GLY F  75  GLU F  76                    
SITE     3 BC4 11 PRO F  77  GLC F 201  HOH F2085                               
SITE     1 BC5  8 PRO F  74  TYR G  22  TRP G  35  GLN G  70                    
SITE     2 BC5  8 PRO G  74  GLY G  75  GLC G 202  HOH G2083                    
SITE     1 BC6  9 PRO F  74  GLY F  75  TYR G  22  GLY G  75                    
SITE     2 BC6  9 GLU G  76  PRO G  77  GLC G 201  HOH G2084                    
SITE     3 BC6  9 HOH G2085                                                     
SITE     1 BC7  9 PRO B  74  TYR H  22  TRP H  35  GLN H  70                    
SITE     2 BC7  9 GLY H  75  GLC H 202  HOH H2113  HOH H2114                    
SITE     3 BC7  9 HOH H2116                                                     
SITE     1 BC8 10 PRO B  74  GLY B  75  TYR H  22  TYR H  24                    
SITE     2 BC8 10 GLY H  75  GLU H  76  PRO H  77  GLC H 201                    
SITE     3 BC8 10 HOH H2117  HOH H2118                                          
SITE     1 BC9  5 HIS A  92  VAL A  93  ASP A  94  HOH A2090                    
SITE     2 BC9  5 HOH A2098                                                     
SITE     1 CC1  7 PRO A  13  ASP A  14  SER A  15  HOH A2099                    
SITE     2 CC1  7 HOH A2100  HOH A2101  PRO E  13                               
SITE     1 CC2  4 GLY A  17  THR A  18  HOH A2038  HOH A2064                    
SITE     1 CC3  7 LYS A  11  ASP A  47  TRP A  48  ARG A  95                    
SITE     2 CC3  7 HOH A2008  PRO B  39  GLU B  40                               
SITE     1 CC4  8 PHE A  79  PHE A  80  PHE C  79  PHE C  80                    
SITE     2 CC4  8 HOH C2075  HOH C2076  HOH C2103  HOH C2104                    
SITE     1 CC5  6 THR C  34  TRP C  35  SER C  36  HOH C2099                    
SITE     2 CC5  6 HOH C2100  HOH C2106                                          
SITE     1 CC6  7 PHE F  79  PHE F  80  HOH F2086  PHE H  79                    
SITE     2 CC6  7 PHE H  80  HOH H2070  HOH H2087                               
SITE     1 CC7  6 PHE B  79  PHE B  80  HOH B2074  PHE G  79                    
SITE     2 CC7  6 PHE G  80  HOH G2061                                          
SITE     1 CC8  4 GLY G  17  THR G  18  ARG G  66  HOH G2086                    
CRYST1  108.204  108.204  180.493  90.00  90.00 120.00 P 32 2 1     48          
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      0.009242  0.005336  0.000000        0.00000                         
SCALE2      0.000000  0.010672  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005540        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system