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Database: PDB
Entry: 5JUV
LinkDB: 5JUV
Original site: 5JUV 
HEADER    HYDROLASE                               10-MAY-16   5JUV              
TITLE     STRUCTURE OF E298Q-BETA-GALACTOSIDASE FROM ASPERGILLUS NIGER IN       
TITLE    2 COMPLEX WITH 6-B-GALACTOPYRANOSYL GALACTOSE                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE BETA-GALACTOSIDASE A;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LACTASE A;                                                  
COMPND   5 EC: 3.2.1.23;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER CBS 513.88;                   
SOURCE   3 ORGANISM_TAXID: 425011;                                              
SOURCE   4 GENE: LACA, AN01G12150;                                              
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BJ3505                                     
KEYWDS    TIM BARREL, GH35, GLYCOSIDE HYDROLASE, KINETICS, PROTEIN              
KEYWDS   2 CONFORMATION, CARBOHYDRATE METABOLISM, B-GALACTOSIDASE, ASPERGILLUS  
KEYWDS   3 NIGER, FUNGAL PROTEIN, SUBSTRATE SPECIFICITY, PREBIOTICS,            
KEYWDS   4 GALACTOOLIGOSACCHARIDES, GOS, RECOMBINANT, 6-O-BETA-D-               
KEYWDS   5 GALACTOPYRANOSYL-D-GALACTOSE, 6-B-GALACTOPYRANOSYL GALACTOSE, 6-GAL- 
KEYWDS   6 GAL, HYDROLASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.RICO-DIAZ,M.RAMIREZ-ESCUDERO,A.VIZOSO VAZQUEZ,M.E.CERDAN,M.BECERRA, 
AUTHOR   2 J.SANZ-APARICIO                                                      
REVDAT   2   28-JUN-17 5JUV    1       JRNL                                     
REVDAT   1   19-APR-17 5JUV    0                                                
JRNL        AUTH   A.RICO-DIAZ,M.RAMIREZ-ESCUDERO,A.VIZOSO-VAZQUEZ,M.E.CERDAN,  
JRNL        AUTH 2 M.BECERRA,J.SANZ-APARICIO                                    
JRNL        TITL   STRUCTURAL FEATURES OF ASPERGILLUS NIGER BETA-GALACTOSIDASE  
JRNL        TITL 2 DEFINE ITS ACTIVITY AGAINST GLYCOSIDE LINKAGES.              
JRNL        REF    FEBS J.                       V. 284  1815 2017              
JRNL        REFN                   ISSN 1742-4658                               
JRNL        PMID   28391618                                                     
JRNL        DOI    10.1111/FEBS.14083                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.27 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.27                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 82.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 44046                          
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2413                            
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) : 2.27                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.33                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3281                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.80                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 185                          
REMARK   3   BIN FREE R VALUE                    : 0.3070                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7482                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 392                                     
REMARK   3   SOLVENT ATOMS            : 224                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.48000                                              
REMARK   3    B22 (A**2) : -1.57000                                             
REMARK   3    B33 (A**2) : -1.32000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.51000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.345         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.230         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.174         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.225         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.903                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8123 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  7264 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11120 ; 1.310 ; 2.011       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 16705 ; 0.746 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   967 ; 6.415 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   338 ;38.382 ;24.527       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1159 ;12.635 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;16.926 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1295 ; 0.070 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8955 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1792 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  3871 ; 0.946 ; 2.265       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3870 ; 0.941 ; 2.264       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4837 ; 1.600 ; 3.395       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  4838 ; 1.601 ; 3.395       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4252 ; 1.327 ; 2.523       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4253 ; 1.327 ; 2.523       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6284 ; 2.198 ; 3.736       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  8932 ; 3.162 ;18.451       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  8875 ; 3.136 ;18.456       
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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5JUV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221248.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5-6.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALBA                               
REMARK 200  BEAMLINE                       : XALOC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : KBMIRRORS                          
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.21                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46487                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.270                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 82.650                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.800                              
REMARK 200  R MERGE                    (I) : 0.15700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP 11.4.04                                        
REMARK 200 STARTING MODEL: 5IFP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: ROD-SHAPED CRYSTALS                                          
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% (W/V) PEG 3350, 0.1M BIS-TRIS        
REMARK 280  BUFFER PH 6.0 , 0.2M LITHIUM SULPHATE, THEN SOACKED IN 30MM 6-O-    
REMARK 280  BETA-D-GALACTOPYRANOSYL-D-GALACTOSE, AND CRYOPROTECTED WITH 20%     
REMARK 280  (W/V) PEG 400, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K      
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       53.19650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 111.0 KCAL/MOL                        
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 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     MET A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     CYS A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ILE A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     GLN A    15                                                      
REMARK 465     ALA A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     ILE A    21                                                      
REMARK 465     LYS A    22                                                      
REMARK 465     HIS A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     ILE A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     PHE A    28                                                      
REMARK 465     THR A    29                                                      
REMARK 465     LEU A    30                                                      
REMARK 465     THR A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     HIS A    33                                                      
REMARK 465     SER A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     PRO A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     LYS A    38                                                      
REMARK 465     ARG A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     HIS A  1009                                                      
REMARK 465     HIS A  1010                                                      
REMARK 465     HIS A  1011                                                      
REMARK 465     HIS A  1012                                                      
REMARK 465     HIS A  1013                                                      
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   OE2  GLU A   861     OH   TYR A   926              2.18            
REMARK 500   O2   MAN A  1376     O5   MAN A  1377              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 198   CD    GLU A 198   OE2    -0.073                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  49     -158.41   -141.14                                   
REMARK 500    LEU A  72       77.13   -157.01                                   
REMARK 500    PRO A  73       51.12    -90.80                                   
REMARK 500    GLU A 103       55.10   -141.23                                   
REMARK 500    ASN A 140     -100.00     60.70                                   
REMARK 500    GLU A 198     -166.31     64.46                                   
REMARK 500    THR A 202      -36.79   -139.24                                   
REMARK 500    ASN A 268       72.07   -119.73                                   
REMARK 500    SER A 289       61.48   -162.84                                   
REMARK 500    LEU A 319       54.42    -97.25                                   
REMARK 500    TYR A 359     -164.00   -116.43                                   
REMARK 500    ASN A 422     -104.15    -88.21                                   
REMARK 500    ALA A 451       30.90    -95.66                                   
REMARK 500    SER A 480       64.03     39.57                                   
REMARK 500    ASP A 499       60.26   -108.67                                   
REMARK 500    ALA A 601     -132.46   -150.50                                   
REMARK 500    ASN A 760     -111.39     47.13                                   
REMARK 500    ASP A 899       58.42   -142.20                                   
REMARK 500    ASN A 914       50.41   -149.66                                   
REMARK 500    LEU A 967       46.94    -94.10                                   
REMARK 500    THR A 983      115.48    -38.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1156        
REMARK 800  bound to ASN A 156                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  1373 through MAN A 1380 bound to ASN A 373                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1478        
REMARK 800  bound to ASN A 478                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  1622 through MAN A 1631 bound to ASN A 622                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1739        
REMARK 800  bound to ASN A 739                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1760        
REMARK 800  bound to ASN A 760                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 1777        
REMARK 800  bound to ASN A 777                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  1914 through MAN A 1919 bound to ASN A 914                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GAL A    
REMARK 800  4001 through GAL A 4002                                             
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5IFP   RELATED DB: PDB                                   
REMARK 900 5IFP CONTAINS THE SAME PROTEIN, NATIVE FORM                          
REMARK 900 RELATED ID: 5IFT   RELATED DB: PDB                                   
REMARK 900 5IFT CONTAINS THE SAME PROTEIN, IN COMPLEX WITH 3-B-                 
REMARK 900 GALACTOPYRANOSYL GLUCOSE                                             
REMARK 900 RELATED ID: 5IHR   RELATED DB: PDB                                   
REMARK 900 5IHR CONTAINS THE SAME PROTEIN, IN COMPLEX WITH ALLOLACTOSE          
DBREF  5JUV A    1  1007  UNP    A2QAN3   BGALA_ASPNC      1   1007             
SEQADV 5JUV GLN A  298  UNP  A2QAN3    GLU   298 ENGINEERED MUTATION            
SEQADV 5JUV HIS A 1008  UNP  A2QAN3              EXPRESSION TAG                 
SEQADV 5JUV HIS A 1009  UNP  A2QAN3              EXPRESSION TAG                 
SEQADV 5JUV HIS A 1010  UNP  A2QAN3              EXPRESSION TAG                 
SEQADV 5JUV HIS A 1011  UNP  A2QAN3              EXPRESSION TAG                 
SEQADV 5JUV HIS A 1012  UNP  A2QAN3              EXPRESSION TAG                 
SEQADV 5JUV HIS A 1013  UNP  A2QAN3              EXPRESSION TAG                 
SEQRES   1 A 1013  MET LYS LEU SER SER ALA CYS ALA ILE ALA LEU LEU ALA          
SEQRES   2 A 1013  ALA GLN ALA ALA GLY ALA SER ILE LYS HIS ARG ILE ASN          
SEQRES   3 A 1013  GLY PHE THR LEU THR GLU HIS SER ASP PRO ALA LYS ARG          
SEQRES   4 A 1013  GLU LEU LEU GLN LYS TYR VAL THR TRP ASP ASP LYS SER          
SEQRES   5 A 1013  LEU PHE ILE ASN GLY GLU ARG ILE MET ILE PHE SER GLY          
SEQRES   6 A 1013  GLU PHE HIS PRO PHE ARG LEU PRO VAL LYS GLU LEU GLN          
SEQRES   7 A 1013  LEU ASP ILE PHE GLN LYS VAL LYS ALA LEU GLY PHE ASN          
SEQRES   8 A 1013  CYS VAL SER PHE TYR VAL ASP TRP ALA LEU VAL GLU GLY          
SEQRES   9 A 1013  LYS PRO GLY GLU TYR ARG ALA ASP GLY ILE PHE ASP LEU          
SEQRES  10 A 1013  GLU PRO PHE PHE ASP ALA ALA SER GLU ALA GLY ILE TYR          
SEQRES  11 A 1013  LEU LEU ALA ARG PRO GLY PRO TYR ILE ASN ALA GLU SER          
SEQRES  12 A 1013  SER GLY GLY GLY PHE PRO GLY TRP LEU GLN ARG VAL ASN          
SEQRES  13 A 1013  GLY THR LEU ARG SER SER ASP LYS ALA TYR LEU ASP ALA          
SEQRES  14 A 1013  THR ASP ASN TYR VAL SER HIS VAL ALA ALA THR ILE ALA          
SEQRES  15 A 1013  LYS TYR GLN ILE THR ASN GLY GLY PRO ILE ILE LEU TYR          
SEQRES  16 A 1013  GLN PRO GLU ASN GLU TYR THR SER GLY CYS CYS GLY VAL          
SEQRES  17 A 1013  GLU PHE PRO ASP PRO VAL TYR MET GLN TYR VAL GLU ASP          
SEQRES  18 A 1013  GLN ALA ARG ASN ALA GLY VAL VAL ILE PRO LEU ILE ASN          
SEQRES  19 A 1013  ASN ASP ALA SER ALA SER GLY ASN ASN ALA PRO GLY THR          
SEQRES  20 A 1013  GLY LYS GLY ALA VAL ASP ILE TYR GLY HIS ASP SER TYR          
SEQRES  21 A 1013  PRO LEU GLY PHE ASP CYS ALA ASN PRO THR VAL TRP PRO          
SEQRES  22 A 1013  SER GLY ASP LEU PRO THR ASN PHE ARG THR LEU HIS LEU          
SEQRES  23 A 1013  GLU GLN SER PRO THR THR PRO TYR ALA ILE VAL GLN PHE          
SEQRES  24 A 1013  GLN GLY GLY SER TYR ASP PRO TRP GLY GLY PRO GLY PHE          
SEQRES  25 A 1013  ALA ALA CYS SER GLU LEU LEU ASN ASN GLU PHE GLU ARG          
SEQRES  26 A 1013  VAL PHE TYR LYS ASN ASP PHE SER PHE GLN ILE ALA ILE          
SEQRES  27 A 1013  MET ASN LEU TYR MET ILE PHE GLY GLY THR ASN TRP GLY          
SEQRES  28 A 1013  ASN LEU GLY TYR PRO ASN GLY TYR THR SER TYR ASP TYR          
SEQRES  29 A 1013  GLY SER ALA VAL THR GLU SER ARG ASN ILE THR ARG GLU          
SEQRES  30 A 1013  LYS TYR SER GLU LEU LYS LEU LEU GLY ASN PHE ALA LYS          
SEQRES  31 A 1013  VAL SER PRO GLY TYR LEU THR ALA SER PRO GLY ASN LEU          
SEQRES  32 A 1013  THR THR SER GLY TYR ALA ASP THR THR ASP LEU THR VAL          
SEQRES  33 A 1013  THR PRO LEU LEU GLY ASN SER THR GLY SER PHE PHE VAL          
SEQRES  34 A 1013  VAL ARG HIS SER ASP TYR SER SER GLU GLU SER THR SER          
SEQRES  35 A 1013  TYR LYS LEU ARG LEU PRO THR SER ALA GLY SER VAL THR          
SEQRES  36 A 1013  ILE PRO GLN LEU GLY GLY THR LEU THR LEU ASN GLY ARG          
SEQRES  37 A 1013  ASP SER LYS ILE HIS VAL THR ASP TYR ASN VAL SER GLY          
SEQRES  38 A 1013  THR ASN ILE ILE TYR SER THR ALA GLU VAL PHE THR TRP          
SEQRES  39 A 1013  LYS LYS PHE ALA ASP GLY LYS VAL LEU VAL LEU TYR GLY          
SEQRES  40 A 1013  GLY ALA GLY GLU HIS HIS GLU LEU ALA ILE SER THR LYS          
SEQRES  41 A 1013  SER ASN VAL THR VAL ILE GLU GLY SER GLU SER GLY ILE          
SEQRES  42 A 1013  SER SER LYS GLN THR SER SER SER VAL VAL VAL GLY TRP          
SEQRES  43 A 1013  ASP VAL SER THR THR ARG ARG ILE ILE GLN VAL GLY ASP          
SEQRES  44 A 1013  LEU LYS ILE LEU LEU LEU ASP ARG ASN SER ALA TYR ASN          
SEQRES  45 A 1013  TYR TRP VAL PRO GLN LEU ALA THR ASP GLY THR SER PRO          
SEQRES  46 A 1013  GLY PHE SER THR PRO GLU LYS VAL ALA SER SER ILE ILE          
SEQRES  47 A 1013  VAL LYS ALA GLY TYR LEU VAL ARG THR ALA TYR LEU LYS          
SEQRES  48 A 1013  GLY SER GLY LEU TYR LEU THR ALA ASP PHE ASN ALA THR          
SEQRES  49 A 1013  THR SER VAL GLU VAL ILE GLY VAL PRO SER THR ALA LYS          
SEQRES  50 A 1013  ASN LEU PHE ILE ASN GLY ASP LYS THR SER HIS THR VAL          
SEQRES  51 A 1013  ASP LYS ASN GLY ILE TRP SER ALA THR VAL ASP TYR ASN          
SEQRES  52 A 1013  ALA PRO ASP ILE SER LEU PRO SER LEU LYS ASP LEU ASP          
SEQRES  53 A 1013  TRP LYS TYR VAL ASP THR LEU PRO GLU ILE GLN SER SER          
SEQRES  54 A 1013  TYR ASP ASP SER LEU TRP PRO ALA ALA ASP LEU LYS GLN          
SEQRES  55 A 1013  THR LYS ASN THR LEU ARG SER LEU THR THR PRO THR SER          
SEQRES  56 A 1013  LEU TYR SER SER ASP TYR GLY PHE HIS THR GLY TYR LEU          
SEQRES  57 A 1013  LEU TYR ARG GLY HIS PHE THR ALA THR GLY ASN GLU SER          
SEQRES  58 A 1013  THR PHE ALA ILE ASP THR GLN GLY GLY SER ALA PHE GLY          
SEQRES  59 A 1013  SER SER VAL TRP LEU ASN GLY THR TYR LEU GLY SER TRP          
SEQRES  60 A 1013  THR GLY LEU TYR ALA ASN SER ASP TYR ASN ALA THR TYR          
SEQRES  61 A 1013  ASN LEU PRO GLN LEU GLN ALA GLY LYS THR TYR VAL ILE          
SEQRES  62 A 1013  THR VAL VAL ILE ASP ASN MET GLY LEU GLU GLU ASN TRP          
SEQRES  63 A 1013  THR VAL GLY GLU ASP LEU MET LYS THR PRO ARG GLY ILE          
SEQRES  64 A 1013  LEU ASN PHE LEU LEU ALA GLY ARG PRO SER SER ALA ILE          
SEQRES  65 A 1013  SER TRP LYS LEU THR GLY ASN LEU GLY GLY GLU ASP TYR          
SEQRES  66 A 1013  GLU ASP LYS VAL ARG GLY PRO LEU ASN GLU GLY GLY LEU          
SEQRES  67 A 1013  TYR ALA GLU ARG GLN GLY PHE HIS GLN PRO GLU PRO PRO          
SEQRES  68 A 1013  SER GLN ASN TRP LYS SER SER SER PRO LEU GLU GLY LEU          
SEQRES  69 A 1013  SER GLU ALA GLY ILE GLY PHE TYR SER ALA SER PHE ASP          
SEQRES  70 A 1013  LEU ASP LEU PRO LYS GLY TRP ASP VAL PRO LEU PHE LEU          
SEQRES  71 A 1013  ASN ILE GLY ASN SER THR THR PRO SER PRO TYR ARG VAL          
SEQRES  72 A 1013  GLN VAL TYR VAL ASN GLY TYR GLN TYR ALA LYS TYR ILE          
SEQRES  73 A 1013  SER ASN ILE GLY PRO GLN THR SER PHE PRO VAL PRO GLU          
SEQRES  74 A 1013  GLY ILE LEU ASN TYR ARG GLY THR ASN TRP LEU ALA VAL          
SEQRES  75 A 1013  THR LEU TRP ALA LEU ASP SER ALA GLY GLY LYS LEU GLU          
SEQRES  76 A 1013  SER LEU GLU LEU SER TYR THR THR PRO VAL LEU THR ALA          
SEQRES  77 A 1013  LEU GLY GLU VAL GLU SER VAL ASP GLN PRO LYS TYR LYS          
SEQRES  78 A 1013  LYS ARG LYS GLY ALA TYR HIS HIS HIS HIS HIS HIS              
HET    NAG  A1156      14                                                       
HET    NAG  A1373      14                                                       
HET    NAG  A1374      14                                                       
HET    BMA  A1375      11                                                       
HET    MAN  A1376      11                                                       
HET    MAN  A1377      11                                                       
HET    MAN  A1378      11                                                       
HET    MAN  A1379      11                                                       
HET    MAN  A1380      11                                                       
HET    NAG  A1478      14                                                       
HET    NAG  A1622      14                                                       
HET    NAG  A1623      14                                                       
HET    BMA  A1624      11                                                       
HET    MAN  A1625      11                                                       
HET    MAN  A1626      11                                                       
HET    MAN  A1627      11                                                       
HET    MAN  A1628      11                                                       
HET    MAN  A1629      11                                                       
HET    MAN  A1630      11                                                       
HET    MAN  A1631      11                                                       
HET    NAG  A1739      14                                                       
HET    NAG  A1760      14                                                       
HET    NAG  A1777      14                                                       
HET    NAG  A1914      14                                                       
HET    NAG  A1915      14                                                       
HET    BMA  A1916      11                                                       
HET    MAN  A1917      11                                                       
HET    MAN  A1918      11                                                       
HET    MAN  A1919      11                                                       
HET     CL  A2001       1                                                       
HET    1PE  A3001      16                                                       
HET    GAL  A4001      12                                                       
HET    GAL  A4002      11                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      CL CHLORIDE ION                                                     
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETSYN     1PE PEG400                                                           
FORMUL   2  NAG    11(C8 H15 N O6)                                              
FORMUL   3  BMA    3(C6 H12 O6)                                                 
FORMUL   3  MAN    15(C6 H12 O6)                                                
FORMUL  10   CL    CL 1-                                                        
FORMUL  11  1PE    C10 H22 O6                                                   
FORMUL  12  GAL    2(C6 H12 O6)                                                 
FORMUL  13  HOH   *224(H2 O)                                                    
HELIX    1 AA1 HIS A   68  LEU A   72  5                                   5    
HELIX    2 AA2 VAL A   74  ALA A   87  1                                  14    
HELIX    3 AA3 ASP A   98  GLU A  103  1                                   6    
HELIX    4 AA4 ASP A  112  PHE A  115  5                                   4    
HELIX    5 AA5 ASP A  116  GLY A  128  1                                  13    
HELIX    6 AA6 SER A  143  PHE A  148  5                                   6    
HELIX    7 AA7 PRO A  149  VAL A  155  5                                   7    
HELIX    8 AA8 ASP A  163  TYR A  184  1                                  22    
HELIX    9 AA9 GLN A  185  GLY A  189  5                                   5    
HELIX   10 AB1 ASP A  212  ALA A  226  1                                  15    
HELIX   11 AB2 ASN A  280  SER A  289  1                                  10    
HELIX   12 AB3 GLY A  311  LEU A  319  1                                   9    
HELIX   13 AB4 ASN A  320  SER A  333  1                                  14    
HELIX   14 AB5 ARG A  376  VAL A  391  1                                  16    
HELIX   15 AB6 PRO A  393  ALA A  398  1                                   6    
HELIX   16 AB7 ARG A  567  TYR A  571  1                                   5    
HELIX   17 AB8 THR A  589  SER A  595  1                                   7    
HELIX   18 AB9 SER A  671  LEU A  675  5                                   5    
HELIX   19 AC1 LEU A  683  GLN A  687  5                                   5    
HELIX   20 AC2 TYR A  717  GLY A  722  5                                   6    
HELIX   21 AC3 ASP A  811  THR A  815  5                                   5    
HELIX   22 AC4 PRO A  828  ILE A  832  5                                   5    
HELIX   23 AC5 LEU A  858  GLN A  863  1                                   6    
SHEET    1 AA1 3 VAL A  46  TRP A  48  0                                        
SHEET    2 AA1 3 LEU A  53  ILE A  55 -1  O  PHE A  54   N  THR A  47           
SHEET    3 AA1 3 GLU A  58  ILE A  60 -1  O  GLU A  58   N  ILE A  55           
SHEET    1 AA2 7 ILE A 192  TYR A 195  0                                        
SHEET    2 AA2 7 TYR A 130  ARG A 134  1  N  LEU A 131   O  ILE A 193           
SHEET    3 AA2 7 CYS A  92  TYR A  96  1  N  VAL A  93   O  LEU A 132           
SHEET    4 AA2 7 ILE A  62  GLU A  66  1  N  GLY A  65   O  SER A  94           
SHEET    5 AA2 7 ILE A 338  TYR A 342  1  O  MET A 339   N  SER A  64           
SHEET    6 AA2 7 ALA A 295  GLN A 300  1  N  PHE A 299   O  ASN A 340           
SHEET    7 AA2 7 HIS A 257  SER A 259  1  N  SER A 259   O  GLN A 298           
SHEET    1 AA3 8 SER A 399  PRO A 400  0                                        
SHEET    2 AA3 8 LEU A 414  LEU A 420 -1  O  LEU A 420   N  SER A 399           
SHEET    3 AA3 8 SER A 426  HIS A 432 -1  O  ARG A 431   N  THR A 415           
SHEET    4 AA3 8 LYS A 471  VAL A 479 -1  O  HIS A 473   N  PHE A 428           
SHEET    5 AA3 8 THR A 482  SER A 487 -1  O  THR A 482   N  VAL A 479           
SHEET    6 AA3 8 HIS A 512  SER A 518 -1  O  SER A 518   N  ASN A 483           
SHEET    7 AA3 8 SER A 541  ASP A 547 -1  O  TRP A 546   N  HIS A 513           
SHEET    8 AA3 8 SER A 534  GLN A 537 -1  N  LYS A 536   O  VAL A 543           
SHEET    1 AA4 2 SER A 440  TYR A 443  0                                        
SHEET    2 AA4 2 LEU A 463  ASN A 466 -1  O  LEU A 463   N  TYR A 443           
SHEET    1 AA5 2 LEU A 445  LEU A 447  0                                        
SHEET    2 AA5 2 VAL A 454  ILE A 456 -1  O  ILE A 456   N  LEU A 445           
SHEET    1 AA6 5 GLU A 490  PHE A 497  0                                        
SHEET    2 AA6 5 GLY A 500  GLY A 507 -1  O  VAL A 504   N  PHE A 492           
SHEET    3 AA6 5 LEU A 560  ASP A 566  1  O  LEU A 563   N  LEU A 503           
SHEET    4 AA6 5 ARG A 553  VAL A 557 -1  N  ILE A 555   O  ILE A 562           
SHEET    5 AA6 5 VAL A 523  GLU A 527 -1  N  THR A 524   O  GLN A 556           
SHEET    1 AA7 5 TYR A 573  TRP A 574  0                                        
SHEET    2 AA7 5 ILE A 598  LYS A 600 -1  O  VAL A 599   N  TRP A 574           
SHEET    3 AA7 5 THR A 625  ILE A 630 -1  O  ILE A 630   N  ILE A 598           
SHEET    4 AA7 5 TRP A 656  VAL A 660 -1  O  ALA A 658   N  VAL A 627           
SHEET    5 AA7 5 THR A 649  VAL A 650 -1  N  THR A 649   O  SER A 657           
SHEET    1 AA8 5 LEU A 578  ALA A 579  0                                        
SHEET    2 AA8 5 LEU A 604  LYS A 611  1  O  LEU A 610   N  ALA A 579           
SHEET    3 AA8 5 GLY A 614  ASP A 620 -1  O  TYR A 616   N  TYR A 609           
SHEET    4 AA8 5 ASN A 638  ILE A 641  1  O  PHE A 640   N  LEU A 615           
SHEET    5 AA8 5 ASP A 644  THR A 646 -1  O  THR A 646   N  LEU A 639           
SHEET    1 AA9 6 LYS A 876  SER A 877  0                                        
SHEET    2 AA9 6 LYS A 678  ASP A 681 -1  N  TYR A 679   O  LYS A 876           
SHEET    3 AA9 6 GLY A 888  ASP A 897 -1  O  SER A 893   N  LYS A 678           
SHEET    4 AA9 6 THR A 957  ALA A 966 -1  O  LEU A 960   N  ALA A 894           
SHEET    5 AA9 6 TYR A 921  VAL A 927 -1  N  ARG A 922   O  TRP A 965           
SHEET    6 AA9 6 TYR A 930  ILE A 936 -1  O  TYR A 930   N  VAL A 927           
SHEET    1 AB1 5 THR A 762  TRP A 767  0                                        
SHEET    2 AB1 5 SER A 755  LEU A 759 -1  N  LEU A 759   O  THR A 762           
SHEET    3 AB1 5 THR A 790  ASP A 798 -1  O  VAL A 796   N  SER A 756           
SHEET    4 AB1 5 TYR A 727  THR A 735 -1  N  PHE A 734   O  TYR A 791           
SHEET    5 AB1 5 SER A 833  THR A 837 -1  O  LYS A 835   N  ARG A 731           
SHEET    1 AB2 3 ASP A 775  ASN A 781  0                                        
SHEET    2 AB2 3 THR A 742  GLN A 748 -1  N  ILE A 745   O  ALA A 778           
SHEET    3 AB2 3 GLY A 818  LEU A 824 -1  O  LEU A 823   N  ALA A 744           
SHEET    1 AB3 2 TRP A 904  ASP A 905  0                                        
SHEET    2 AB3 2 VAL A 985  LEU A 986 -1  O  VAL A 985   N  ASP A 905           
SHEET    1 AB4 3 SER A 944  VAL A 947  0                                        
SHEET    2 AB4 3 LEU A 908  ILE A 912 -1  N  LEU A 910   O  PHE A 945           
SHEET    3 AB4 3 LEU A 977  TYR A 981 -1  O  GLU A 978   N  ASN A 911           
SSBOND   1 CYS A  205    CYS A  206                          1555   1555  2.95  
SSBOND   2 CYS A  266    CYS A  315                          1555   1555  2.10  
LINK         ND2 ASN A 156                 C1  NAG A1156     1555   1555  1.44  
LINK         ND2 ASN A 373                 C1  NAG A1373     1555   1555  1.44  
LINK         ND2 ASN A 478                 C1  NAG A1478     1555   1555  1.46  
LINK         ND2 ASN A 622                 C1  NAG A1622     1555   1555  1.45  
LINK         ND2 ASN A 739                 C1  NAG A1739     1555   1555  1.45  
LINK         ND2 ASN A 760                 C1  NAG A1760     1555   1555  1.46  
LINK         ND2 ASN A 777                 C1  NAG A1777     1555   1555  1.43  
LINK         ND2 ASN A 914                 C1  NAG A1914     1555   1555  1.45  
LINK         O4  NAG A1373                 C1  NAG A1374     1555   1555  1.43  
LINK         O4  NAG A1374                 C1  BMA A1375     1555   1555  1.42  
LINK         O3  BMA A1375                 C1  MAN A1376     1555   1555  1.39  
LINK         O6  BMA A1375                 C1  MAN A1379     1555   1555  1.43  
LINK         O2  MAN A1376                 C1  MAN A1377     1555   1555  1.39  
LINK         O2  MAN A1377                 C1  MAN A1378     1555   1555  1.43  
LINK         O3  MAN A1379                 C1  MAN A1380     1555   1555  1.43  
LINK         O4  NAG A1622                 C1  NAG A1623     1555   1555  1.44  
LINK         O4  NAG A1623                 C1  BMA A1624     1555   1555  1.44  
LINK         O3  BMA A1624                 C1  MAN A1627     1555   1555  1.44  
LINK         O6  BMA A1624                 C1  MAN A1625     1555   1555  1.43  
LINK         O3  MAN A1625                 C1  MAN A1626     1555   1555  1.45  
LINK         O6  MAN A1625                 C1  MAN A1630     1555   1555  1.43  
LINK         O2  MAN A1627                 C1  MAN A1628     1555   1555  1.45  
LINK         O2  MAN A1628                 C1  MAN A1629     1555   1555  1.45  
LINK         O2  MAN A1630                 C1  MAN A1631     1555   1555  1.44  
LINK         O4  NAG A1914                 C1  NAG A1915     1555   1555  1.43  
LINK         O4  NAG A1915                 C1  BMA A1916     1555   1555  1.44  
LINK         O3  BMA A1916                 C1  MAN A1917     1555   1555  1.44  
LINK         O2  MAN A1917                 C1  MAN A1918     1555   1555  1.40  
LINK         O2  MAN A1918                 C1  MAN A1919     1555   1555  1.47  
LINK         O1  GAL A4001                 C6  GAL A4002     1555   1555  1.35  
CISPEP   1 GLY A  136    PRO A  137          0        15.40                     
CISPEP   2 PHE A  210    PRO A  211          0         0.81                     
CISPEP   3 TYR A  342    MET A  343          0        -0.69                     
CISPEP   4 ILE A  456    PRO A  457          0        10.34                     
CISPEP   5 GLY A  940    PRO A  941          0         3.32                     
SITE     1 AC1  3 ARG A 862  GLN A 863  TYR A1007                               
SITE     1 AC2  5 ASN A 140  GLU A 142  GLU A 804  TRP A 806                    
SITE     2 AC2  5 GAL A4001                                                     
SITE     1 AC3  1 ASN A 156                                                     
SITE     1 AC4 19 ALA A 313  GLU A 317  THR A 369  SER A 371                    
SITE     2 AC4 19 ASN A 373  ASN A 911  SER A 915  THR A 943                    
SITE     3 AC4 19 SER A 944  GLU A 978  THR A 982  THR A 983                    
SITE     4 AC4 19 NAG A1622  MAN A1627  MAN A1628  HOH A5028                    
SITE     5 AC4 19 HOH A5053  HOH A5079  HOH A5093                               
SITE     1 AC5  3 SER A 423  ASN A 478  SER A 480                               
SITE     1 AC6 20 LEU A  42  VAL A 229  GLU A 317  ASN A 320                    
SITE     2 AC6 20 ASN A 321  GLU A 322  ARG A 325  THR A 375                    
SITE     3 AC6 20 GLU A 377  ASN A 568  TYR A 603  ASN A 622                    
SITE     4 AC6 20 THR A 983  NAG A1373  MAN A1380  HOH A5011                    
SITE     5 AC6 20 HOH A5069  HOH A5123  HOH A5148  HOH A5149                    
SITE     1 AC7  1 ASN A 739                                                     
SITE     1 AC8  6 SER A 688  ARG A 731  ASN A 760  THR A 790                    
SITE     2 AC8  6 TYR A 791  VAL A 792                                          
SITE     1 AC9  3 ASN A 773  ASP A 775  ASN A 777                               
SITE     1 AD1 13 TRP A 307  GLY A 308  TYR A 771  ALA A 772                    
SITE     2 AD1 13 ASN A 914  TYR A 935  ILE A 936  SER A 937                    
SITE     3 AD1 13 ILE A 939  GLY A 940  PRO A 941  HOH A5074                    
SITE     4 AD1 13 HOH A5092                                                     
SITE     1 AD2 16 TYR A  96  ILE A 139  ASN A 140  ALA A 141                    
SITE     2 AD2 16 GLU A 142  ASN A 199  GLU A 200  ALA A 237                    
SITE     3 AD2 16 ASP A 258  SER A 259  TYR A 260  GLN A 298                    
SITE     4 AD2 16 TYR A 304  TYR A 342  TYR A 364  1PE A3001                    
CRYST1   58.100  106.393   83.723  90.00  99.18  90.00 P 1 21 1      2          
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      0.017212  0.000000  0.002782        0.00000                         
SCALE2      0.000000  0.009399  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012099        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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